AU2003223469A1 - Nucleic acid and corresponding protein entitled 98p4b6 useful in treatment and detection of cancer - Google Patents

Description

WO 03/087306 PCT/US03/10462 NUCLEIC ACID AND CORRESPONDING PROTEIN ENTITLED 98P4B6 USEFUL IN TREATMENT AND DETECTION OF CANCER CROSS-REFERENCE TO RELATED APPLICATIONS This application is a continuation-in-part of pending United States patent application USSN 09/455,486, filed 06 December-1999, and claims priority from United States patent application USSN 091323,873, now United States patent number 6,329, 503 filed 01-June-1999, and this application claims priority from United States provisional application USSN not yet assigned, filed 20-December-2002 and United States provisional patent application number 60/317,840, filed September 6, 2001 and United States provisional patent application number 60/370,387 filed April 5, 2002. This application relates to United States provisional patent application number 60/087,520, filed June 1, 1998 and United States provisional patent application number 60/091,183, filed June 30, 1998 and United States Patent application number 10/011,095, filed December 6, 2001 and United States patent application number 10/010,667, filed December 6, 2001 and United States provisional patent application number 60/296,656, filed June 6, 2001, and United States patent application number 101165,044, filed June 6, 2002. The contents of the applications listed in this paragraph are fully incorporated by reference herein. STATEMENT OF RIGHTS TO INVENTIONS MADE UNDER FEDERALLY SPONSORED RESEARCH Not applicable. FIELD OF THE INVENTION The invention described herein relates to genes and their encoded proteins, termed 98P486 or STEAP-2, expressed in certain cancers, and to diagnostic and therapeutic methods and compositions useful in the management of cancers that express 98P4B6. BACKGROUND OF THE INVENTION Cancer is the second leading cause of human death next to coronary disease. Worldwide, millions of people die from cancer every year. In the United States alone, as reported by the American Cancer Society, cancer causes the death of well over a half-million people annually, with over 1.2 million new cases diagnosed per year. While deaths from heart disease have been declining significantly, those resulting from cancer generally are on the rise. In the early part of the next century, cancer is predicted to become the leading cause of death. Worldwide, several cancers stand out as the leading killers. In particular, carcinomas of the lung, prostate, breast, colon, pancreas, and ovary represent the primary causes of cancer death. These and virtually all other carcinomas share a common lethal feature. With very few exceptions, metastatic disease from a carcinoma is fatal. Moreover, even for those cancer patients who initially survive their primary cancers, common experience has shown that their lives are dramatically altered. Many cancer patients experience strong anxieties driven by the awareness of the potential for recurrence or treatment failure. Many cancer patients experience physical debilitations following treatment. Furthermore, many cancer patients experience a recurrence. Worldwide, prostate cancer is the fourth most prevalent cancer in men. In North America and Northern Europe, it is by far the most common cancer in males and is the second leading cause of cancer death in men. In the United States alone, well over 30,000 men die annually of this disease - second only to lung cancer. Despite the magnitude of these figures, there is still no effective treatment for metastatic prostate cancer. Surgical prostatectomy, radiation therapy, WO 03/087306 PCT/US03/10462 hormone ablation therapy, surgical castration and chemotherapy continue to be the main treatment modalities. Unfortunately, these treatments are ineffective for many and are often associated with undesirable consequences. On the diagnostic front, the lack of a prostate tumor marker that can accurately detect early-stage, localized tumors remains a significant limitation in the diagnosis and management of this disease. Although the serum prostate specific antigen (PSA) assay has been a very useful tool, however its specificity and general utility is widely regarded as lacking in several important respects. Progress in identifying additional specific markers for prostate cancer has been improved by the generation of prostate cancer xenografts that can recapitulate different stages of the disease in mice. The LAPC (Los Angeles Prostate Cancer) xenografts are prostate cancer xenografts that have survived passage in severe combined immune deficient (SCID) mice and have exhibited the capacity to mimic the transition from androgen dependence to androgen independence (Klein et al, 1997, Nat. Med. 3:402). More recently identified prostate cancer markers include PCTA-1 (Su et aL, 1996, Proc. Natl. Acad. Sci. USA 93: 7252), prostate-specific membrane (PSM) antigen (Pinto etal., Clin Cancer Res 1996 Sep 2 (9): 1445 51), STEAP (Hubert, et al., Proc Natl Acad Sci U S A. 1999 Dec 7; 96(25): 14523-8) and prostate stem cell antigen (PSCA) (Reiter et at., 1998, Proc. Natl. Acad. Sci. USA 95: 1735). While previously identified markers such as PSA, PSM, PCTA and PSCA have facilitated efforts to diagnose and treat prostate cancer, there is need for the identification of additional markers and therapeutic targets for prostate and related cancers in order to further improve diagnosis and therapy. Renal cell carcinoma (RCC) accounts for approximately 3 percent of adult malignancies. Once adenomas reach a diameter of 2 to 3 cm, malignant potential exists. In the adult, the two principal malignant renal tumors are renal cell adenocarcinoma and transitional cell carcinoma of the renal pelvis or ureter. The incidence of renal cell adenocarcinoma is estimated at more than 29,000 cases in the United States, and more than 11,600 patients died of this disease in 1998. Transitional cell carcinoma is less frequent, with an incidence of approximately 500 cases per year in the United States. Surgery has been the primary therapy for renal cell adenocarcinoma for many decades. Until recently, metastatic disease has been refractory to any systemic therapy. With recent developments in systemic therapies, particularly immunotherapies, metastatic renal cell carcinoma may be approached aggressively in appropriate patients with a possibility of durable responses. Nevertheless, there is a remaining need for effective therapies for these patients. Of all new cases of cancer in the United States, bladder cancer represents approximately 5 percent in men (fifth most common neoplasm) and 3 percent in women (eighth most common neoplasm). The incidence is increasing slowly, concurrent with an increasing older population. In 1998, there was an estimated 54,500 cases, including 39,500 in men and 15,000 in women. The age-adjusted incidence in the United States is 32 per 100,000 for men and eight per 100,000 in women. The historic male/female ratio of 3:1 may be decreasing related to smoking patterns in women. There were an estimated 11,000 deaths from bladder cancer in 1998 (7,800 in men and 3,900 in women). Bladder cancer incidence and mortality strongly increase with age and will be an increasing problem as the population becomes more elderly. Most bladder cancers recur in the bladder. Bladder cancer is managed with a combination of transurethral resection of the bladder (TUR) and intravesical chemotherapy or immunotherapy. The multifocal and recurrent nature of bladder cancer points out the limitations of TUR. Most muscle-invasive cancers are not cured by TUR alone. Radical cystectomy and urinary diversion is the most effective means to eliminate the cancer but carry an undeniable impact on urinary and sexual function. There continues to be a significant need for treatment modalities that are beneficial for bladder cancer patients. An estimated 130,200 cases of colorectal cancer occurred in 2000 in the United States, including 93,800 cases of colon cancer and 36,400 of rectal cancer. Colorectal cancers are the third most common cancers in men and women. Incidence rates declined significantly during 1992-1996 (-2.1% per year). Research suggests that these declines have been 2 WO 03/087306 PCT/USO3/10462 due to increased screening and polyp removal, preventing progression of polyps to invasive cancers. There were an estimated 56,300 deaths (47,700 from colon cancer, 8,600 from rectal cancer) in 2000, accounting for about 11% of all U.S. cancer deaths. At present, surgery is the most common form of therapy for colorectal cancer, and for cancers that have not spread, it is frequently curative. Chemotherapy, or chemotherapy plus radiation, is given before or after surgery to most patients whose cancer has deeply perforated the bowel wall or has spread to the lymph nodes. A permanent colostomy (creation of an abdominal opening for elimination of body wastes) is occasionally needed for colon cancer and is infrequently required for rectal cancer. There continues to be a need for effective diagnostic and treatment modalities for colorectal cancer. There were an estimated 164,100 new cases of lung and bronchial cancer in 2000, accounting for 14% of all U.S. cancer diagnoses. The incidence rate of lung and bronchial cancer is declining significantly in men, from a high of 86.5 per 100,000 in 1984 to 70.0 in 1996. In the 1990s, the rate of increase among women began to slow. In 1996, the incidence rate in women was 42.3 per 100,000. Lung and bronchial cancer caused an estimated 156,900 deaths in 2000, accounting for 28% of all cancer deaths. During 1992-1996, mortality from lung cancer declined significantly among men (-1.7% per year) while rates for women were still significantly increasing (0.9% per year). Since 1987, more women have died each year of lung cancer than breast cancer, which, for over 40 years, was the major cause of cancer death in women. Decreasing lung cancer incidence and mortality rates most likely resulted from decreased smoking rates over the previous 30 years; however, decreasing smoking patterns among women lag behind those of men. Of concern, although the declines in adult tobacco use have slowed, tobacco use in youth is increasing again. Treatment options for lung and bronchial cancer are determined by the type and stage of the cancer and include surgery, radiation therapy, and chemotherapy. For many localized cancers, surgery is usually the treatment of choice. Because the disease has usually spread by the time it is discovered, radiation therapy and chemotherapy are often needed in combination with surgery. Chemotherapy alone or combined with radiation is the treatment of choice for small cell lung cancer; on this regimen, a large percentage of patients experience remission, which in some cases is long lasting. There is however, an ongoing need for effective treatment and diagnostic approaches for lung and bronchial cancers. An estimated 182,800 new invasive cases of breast cancer were expected to occur among women in the United States during 2000. Additionally, about 1,400 new cases of breast cancer were expected to be diagnosed in men in 2000. After increasing about 4% per year in the 1980s, breast cancer incidence rates in women have leveled off in the 1990s to about 110.6 cases per 100,000. In the U.S. alone, there were an estimated 41,200 deaths (40,800 women, 400 men) in 2000 due to breast cancer. Breast cancer ranks second among cancer deaths in women. According to the most recent data, mortality rates declined significantly during 1992-1996 with the largest decreases in younger women, both white and black. These decreases were probably the result of earlier detection and improved treatment. Taking into account the medical circumstances and the patient's preferences, treatment of breast cancer may involve lumpectomy (local removal of the tumor) and removal of the lymph nodes under the arm; mastectomy (surgical removal of the breast) and removal of the lymph nodes under the arm; radiation therapy; chemotherapy; or hormone therapy. Often, two or more methods are used in combination. Numerous studies have shown that, for early stage disease, long-term survival rates after lumpectomy plus radiotherapy are similar to survival rates after modified radical mastectomy. Significant advances in reconstruction techniques provide several options for breast reconstruction after mastectomy. Recently, such reconstruction has been done at the same time as the mastectomy. 3 WO 03/087306 PCT/US03/10462 Local excision of ductal carcinoma in situ (DCIS) with adequate amounts of surrounding normal breast tissue may prevent the local recurrence of the DCIS. Radiation to the breast and/or tamoxifen may reduce the chance of DCIS occurring in the remaining breast tissue. This is important because DCIS, if left untreated, may develop into invasive breast cancer. Nevertheless, there are serious side effects or sequelae to these treatments. There is, therefore, a need for efficacious breast cancer treatments. There were an estimated 23,100 new cases of ovarian cancer in the United States in 2000. It accounts for 4% of all cancers among women and ranks second among gynecologic cancers. During 1992-1996, ovarian cancer incidence rates were significantly declining. Consequent to ovarian cancer, there were an estimated 14,000 deaths in 2000. Ovarian cancer causes more deaths than any other cancer of the female reproductive system. Surgery, radiation therapy, and chemotherapy are treatment options for ovarian cancer. Surgery usually includes the removal of one or both ovaries, the fallopian tubes (salpingo-oophorectomy), and the uterus (hysterectomy). In some very early tumors, only the involved ovary will be removed, especially in young women who wish to have children. In advanced disease, an attempt is made to remove all intra-abdominal disease to enhance the effect of chemotherapy. There continues to be an important need for effective treatment options for ovarian cancer. There were an estimated 28,300 new cases of pancreatic cancer in the United States in 2000. Over the past 20 years, rates of pancreatic cancer have declined in men. Rates among women have remained approximately constant but may be beginning to decline. Pancreatic cancer caused an estimated 28,200 deaths in 2000 in the United States. Over the past 20 years, there has been a slight but significant decrease in mortality rates among men (about -0.9% per year) while rates have increased slightly among women. Surgery, radiation therapy, and chemotherapy are treatment options for pancreatic cancer. These treatment options can extend survival and/or relieve symptoms in many patients but are not likely to produce a cure for most. There is a significant need for additional therapeutic and diagnostic options for pancreatic cancer. SUMMARY OF THE INVENTION The present invention relates to a gene, designated 98P4B6, that has now been found to be over-expressed in the cancer(s) listed in Table I. Northern blot expression analysis of 98P4B6 gene expression in normal tissues shows a restricted expression pattern in adult tissues. The nucleotide (Figure 2) and amino acid (Figure 2, and Figure 3) sequences of 98P4B6 are provided. The tissue-related profile of 98P4B6 in normal adult tissues, combined with the over-expression observed in the tissues listed in Table I, shows that 98P4B6 is aberrantly over-expressed in at least some cancers, and thus serves as a useful diagnostic, prophylactic, prognostic, and/or therapeutic target for cancers of the tissue(s) such as those listed in Table I. The invention provides polynucleotides corresponding or complementary to all or part of the 98P4B6 genes, mRNAs, and/or coding sequences, preferably in isolated form, including polynucleotides encoding 98P4B6-related proteins and fragments of4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more than 25 contiguous amino acids; at least 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100 or more than 100 contiguous amino acids of a 98P4B6-related protein, as well as the peptides/proteins themselves; DNA, RNA, DNNARNA hybrids, and related molecules, polynucleotides or oligonucleotides complementary or having at least a 90% homology to the 98P4B6 genes or mRNA sequences or parts thereof, and polynucleotides or oligonucleotides that hybridize to the 98P4B6 genes, mRNAs, or to 98P4B6-encoding polynucleotides. Also provided are means for isolating cDNAs and the genes encoding 98P4B6. Recombinant DNA molecules containing 98P4B6 polynucleotides, cells transformed or transduced with such molecules, and host vector systems for the expression of 98P4B6 gene products are also provided. The invention further provides antibodies that bind to 98P4B6 proteins and polypeptide fragments thereof, including polyclonal and monoclonal antibodies, murine arid 4 WO 03/087306 PCT/USO3/10462 other mammalian antibodies, chimeric antibodies, humanized and fully human antibodies, and antibodies labeled with a detectable marker or therapeutic agent. In certain embodiments, there is a proviso that the entire nucleic acid sequence of Figure 2 is not encoded and/or the entire amino acid sequence of Figure 2 is not prepared. In certain embodiments, the entire nucleic acid sequence of Figure 2 is encoded and/or the entire amino acid sequence of Figure 2 is prepared, either of which are in respective human unit dose forms. The invention further provides methods for detecting the presence and status of 98P4B6 polynucleotides and proteins in various biological samples, as well as methods for identifying cells that express 98P4B6. A typical embodiment of this invention provides methods for monitoring 98P4B6 gene products in a tissue or hematology sample having or suspected of having some form of growth dysregulation such as cancer. The invention further provides various immunogenic or therapeutic compositions and strategies for treating cancers that express 98P4B6 such as cancers of tissues listed in Table I, including therapies aimed at inhibiting the transcription, translation, processing or function of 98P4B6 as well as cancer vaccines. In one aspect, the invention provides compositions, and methods comprising them, for treating a cancer that expresses 98P4B6 in a human subject wherein the composition comprises a carrier suitable for human use and a human unit dose of one or more than one agent that inhibits the production or function of 98P4B6. Preferably, the carrier is a uniquely human carrier. In another aspect of the invention, the agent is a moiety that is immunoreactive with 98P4B6 protein. Non-limiting examples of such moieties include, but are not limited to, antibodies (such as single chain, monoclonal, polyclonal, humanized, chimeric, or human antibodies), functional equivalents thereof (whether naturally occurring or synthetic), and combinations thereof. The antibodies can be conjugated to a diagnostic or therapeutic moiety. In another aspect, the agent is a small molecule as defined herein. In another aspect, the agent comprises one or more than one peptide which comprises a cytotoxic T lymphocyte (CTL) epitope that binds an HLA class I molecule in a human to elicit a CTL response to 98P4B6 and/or one or more than one peptide which comprises a helper T lymphocyte (HTL) epitope which binds an HLA class II molecule in a human to elicit an HTL response. The peptides of the invention may be on the same or on one or more separate polypeptide molecules. In a further aspect of the invention, the agent comprises one or more than one nucleic acid molecule that expresses one or more than one of the CTL or HTL response stimulating peptides as described above. In yet another aspect of the invention, the one or more than one nucleic acid molecule may express a moiety that is immunologically reactive with 98P4B6 as described above. The one or more than one nucleic acid molecule may also be, or encodes, a molecule that inhibits production of 98P4B6. Non-limiting examples of such molecules include, but are not limited to, those complementary to a nucleotide sequence essential for production of 98P4B6 (e.g. antisense sequences or molecules that form a triple helix with a nucleotide double helix essential for 98P4B6 production) or a ribozyme effective to lyse 98P4B6 mRNA. Note that to determine the starting position of any peptide set forth in Tables VIII-XXI and XXII to XLIX (collectively HLA Peptide Tables) respective to its parental protein, e.g., variant 1, variant 2, etc., reference is made to three factors: the particular variant, the length of the peptide in an HLA Peptide Table, and the Search Peptides in Table VII. Generally, a unique Search Peptide is used to obtain HLA peptides of a particular for a particular variant. The position of each Search Peptide relative to its respective parent molecule is listed in Table VII. Accordingly, if a Search Peptide begins at position "X", one must add the value "X - 1" to each position in Tables VIII-XXI and XXII to XLIX to obtain the actual position of the HLA peptides in their parental molecule. For example, if a particular Search Peptide begins at position 150 of its parental molecule, one must add 150 - 1, i.e., 149 to each HLA peptide amino acid position to calculate the position of that amino acid in the parent molecule. One embodiment of the invention comprises an HLA peptide, that occurs at least twice in Tables VIII-XXI and XXII to XLIX collectively, or an oligonucleotide that encodes the HLA peptide. Another embodiment of the invention comprises an 5 WO 03/087306 PCT/USO3/10462 HLA peptide that occurs at least once in Tables VIII-XXI and at least once in tables XXII to XLIX, or an oligonucleotide that encodes the HLA peptide. Another embodiment of the invention is antibody epitopes, which comprise a peptide regions, or an oligonucleotide encoding the peptide region, that has one two, three, four, or five of the following characteristics: i) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Hydrophilicity profile of Figure 5; ii) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or less than 0.5, 0.4, 0.3, 0.2, 0.1, or having a value equal to 0.0, in the Hydropathicity profile of Figure 6; iii) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Percent Accessible Residues profile of Figure 7; iv) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0,8, 0.9, or having a value equal to 1.0, in the Average Flexibility profile of Figure 8; or v) a peptide region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Beta-turn profile of Figure 9. BRIEF DESCRIPTION OF THE FIGURES Figure 1. The 98P4B6 SSH sequence of 183 nucleotides. Figure 2. A) The cDNA and amino acid sequence of 98P4B6 variant 1 (also called "98P4B6 v.1" or "98P4B6 variant 1") is shown in Figure 2A. The start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. B) The cDNA and amino acid sequence of 98P4B6 variant 2 (also called "98P4B6 v.2") is shown in Figure 2B. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 4-138 including the stop codon. C) The cDNA and amino acid sequence of 98P486 variant 3 (also called "98P4B6 v.3") is shown in Figure 2C. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 188-1552 including the stop codon. 0) The cDNA and amino acid sequence of 98P486 variant 4 (also called "98P486 v.4") is shown in Figure 2D. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 318-1682 including the stop codon. E) The cDNA and amino acid sequence of 98P4B6 variant 5 (also called "98P4B6 v.5") is shown in Figure 2E. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 318-1577 including the stop codon. F) The cDNA and amino acid sequence of 98P4B6 variant 6 (also called "98P4B6 v.6") is shown in Figure 2F. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 318-1790 including the stop codon. G) The cDNA and amino acid sequence of 98P4B6 variant 7 (also called "98P4B6 v.7") is shown in Figure 2G. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. 6 WO 03/087306 PCT/USO3/10462 H) The cDNA and amino acid sequence of 98P4B6 variant 8 (also called "98P4B6 v.8") is shown in Figure 2H. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. I) The cDNA and amino acid sequence of 98P4B6 variant 9 (also called "98P4B6 v.9") is shown in Figure 21. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. J) The cDNA and amino acid sequence of 98P4B6 variant 10 (also called "98P4B6 v.10") is shown in Figure 2J. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. K) The cDNA and amino acid sequence of 98P4B6 variant 11 (also called "98P4B6 v.11") is shown in Figure 2K. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. L) The cDNA and amino acid sequence of 98P4B6 variant 12 (also called "98P4B6 v.12") is shown in Figure 2L. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. M) The cDNA and amino acid sequence of 98P4B6 variant 13 (also called '98P4B6 v.13") is shown in Figure 2M. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. N) The cDNA and amino acid sequence of 98P4B6 variant 14 (also called '98P4B6 v.14") is shown in Figure 2N. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. 0) The cDNA and amino acid sequence of 98P4B6 variant 15 (also called "98P4B6 v.15") is shown in Figure 20. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. P) The cDNA and amino acid sequence of 98P4B6 variant 16 (also called '98P4B6 v.16") is shown in Figure 2P. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. Q) The cDNA and amino acid sequence of 98P4B6 variant 17 (also called "98P4B6 v.17") is shown in Figure 2Q. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. R) The cDNA and amino acid sequence of 98P4B6 variant 18 (also called '98P4B6 v.18") is shown in Figure 2R. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. S) The cDNA and amino acid sequence of 98P4B6 variant 19 (also called '98P4B6 v.19") is shown in Figure 2S. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 355-1719 including the stop codon. T) The cDNA and amino acid sequence of 98P4B6 variant 20 (also called "98P4B6 v.20") is shown in Figure 2T. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. U) The cDNA and amino acid sequence of 98P4B6 variant 21 (also called "98P4B6 v.21") is shown in Figure 2U. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. 7 WO 03/087306 PCT/USO3/10462 V) The cDNA and amino acid sequence of 98P4B6 variant 22 (also called "98P4B6 v.22") is shown in Figure 2V. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. W) The cDNA and amino acid sequence of 98P4B6 variant 23 (also called "98P4B6 v.23") is shown in Figure 2W. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. X) The cDNA and amino acid sequence of 98P4B6 variant 24 (also called "98P4B6 v.24") is shown in Figure 2X. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 295-2025 including the stop codon. Y) The cDNA and amino acid sequence of 98P4B6 variant 25 (also called "98P4B6 v.25") is shown in Figure 2Y. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. Z) The cDNA and amino acid sequence of 98P4B6 variant 26 (also called "98P4B6 v.26") is shown in Figure 2Z. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AA) The cDNA and amino acid sequence of 98P4B6 variant 27 (also called "98P4B6 v.27") is shown in Figure 2AA. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AB) The cDNA and amino acid sequence of 98P4B6 variant 28 (also called "98P4B6 v.28") is shown in Figure 2AB. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AC) The cDNA and amino acid sequence of 98P4B6 variant 29 (also called "98P4B6 v.29") is shown in Figure 2AC, The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AD) The cDNA and amino acid sequence of 98P4B6 variant 30 (also called "98P4B6 v.30") is shown in Figure 2AD. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AE) The cDNA and amino acid sequence of 98P4B6 variant 31 (also called '98P4B6 v.31") is shown in Figure 2AE. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AF) The cDNA and amino acid sequence of 98P4B6 variant 32 (also called "98P4B6 v.32") is shown in Figure 2AF. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AG) The cDNA and amino acid sequence of 98P4B6 variant 33 (also called "98P4B6 v.33") is shown in Figure 2AG. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AH) The cDNA and amino acid sequence of 98P4B6 variant 34 (also called "98P4B6 v.34") is shown in Figure 2AH. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. Al) The cDNA and amino acid sequence of 98P4B6 variant 35 (also called "98P4B6 v.35") is shown in Figure 2AL. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. 8 WO 03/087306 PCT/USO3/10462 AJ) The cDNA and amino acid sequence of 98P4B6 variant 36 (also called "98P4B6 v.36") is shown in Figure 2AJ. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AK) The cDNA and amino acid sequence of 98P4B6 variant 37 (also called "98P4B6 v.37") is shown in Figure 2AK. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. AL) The cDNA and amino acid sequence of 98P4B6 variant 38 (also called "98P4B6 v.38") is shown in Figure 2AL. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 394-1866 including the stop codon. Figure 3. A) The amino acid sequence of 98P4B6 v.1 is shown in Figure 3A; it has 454 amino acids. B) The amino acid sequence of 98P4B6 v.2 is shown in Figure 3B; it has 45 amino acids. C) The amino acid sequence of 98P4B6 v.5 is shown in Figure 3C; it has 419 amino acids. D) The amino acid sequence of 98P4B6 v.6 is shown in Figure 3D; it has 490 amino acids. E) The amino acid sequence of 98P4B6 v.7 is shown in Figure 3E; it has 576 amino acids. F) The amino acid sequence of 98P4B6 v.8 is shown in Figure 3F; it has 490 amino acids. G) The amino acid sequence of 98P4B6 v.13 is shown in Figure 3G; it has 454 amino acids. H) The amino acid sequence of 98P4B6 v.14 is shown in Figure 3H; it has 454 amino acids. I) The amino acid sequence of 98P4B6 v.21 is shown in Figure 31; it has 576 amino acids. J) The amino acid sequence of 98P4B6 v.25 is shown in Figure 3J; it has 490 amino acids. As used herein, a reference to 98P4B6 includes all variants thereof, including those shown in Figures 2, 3, 10, and 11, unless the context clearly indicates otherwise. Figure 4. Comparison of 98P4B6 with known genes: Human STAMP1, human six transmembrane epithelial antigen of prostate 2 and mouse six transmembrane epithelial antigen of prostate 2. Figure 4(A) Alignment of 98P4B6 variant 1 to human STAMP1 (gi 15418732). Figure 4(B) Alignment of 98P4B6 variant 1 with human STEAP2 (gi:23308593). Figure 4(C) Alignment of 98P4B6 variant 1 with mouse STEAP2 (gi 28501136). Figure 4(D): Clustal Alignment of the three 98P4B6 variants, depicting that 98P4B6 V1 B contains an additional 62 aa at its N-terminus relative to Vi, and that 98P4B6 V2 carries a Ito T point mutation at aa 225 relative to Vi. Figure 5. Hydrophilicity amino acid profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Hopp and Woods (Hopp T.P., Woods K.R., 1981. Proc. Natl. Acad. Sci. U.S.A. 78:3824-3828) accessed on the Protscale website located on the World Wide Web at (expasy.chcgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 6. Hydropathicity amino acid profile of 98P486v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Kyte and Doolittle (Kyte J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 7. Percent accessible residues amino acid profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Janin (Janin J., 1979 Nature 277:491-492) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 8. Average flexibility amino acid profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Bhaskaran and Ponnuswamy (Bhaskaran R., and Ponnuswamy P.K., 9 WO 03/087306 PCT/US03/10462 1988. Int. J. Pept. Protein Res. 32:242-255) accessed on the ProtScale website located on the World Wide Web at (.expasy.chlcgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 9. Beta-turn amino acid profile of 98P4B6v.1, v.2, v.5, v.6, and v.7 determined by computer algorithm sequence analysis using the method of Deleage and Roux (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294) accessed on the ProtScale website located on the World Wide Web at (.expasy.ch/cgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 10. Figure 10(a): Schematic alignment of SNP variants of 98P4B6 v.1. Variants 98P4B6 v.9 through v.19 were variants with single nucleotide difference from v.1. Though these SNP variants were shown separately, they could also occur in any combinations and in any transcript variants, as shown in Fig. 12, that contains the bases. SNP in regions of other transcript variants, such as v.2, v.6 and v.8, not common with v.1 were not shown here. Numbers correspond to those of 98P4B6 v.1. Black box shows the same sequence as 98P4B6 v.1. SNPs are indicated above the box. Figure 10(b): Schematic alignment of SNP variants of 98P4B6 v.7. Variants 98P4B6 v.20 through v.24 were variants with single nucleotide difference from v.7. Though these SNP variants were shown separately, they could also occur in any combinations and in any transcript variants, as shown in Fig. 12, that contains the bases. Those SNP in regions common with v.1 were not shown here. Numbers correspond to those of 98P4B6 v.7. Black box shows the same sequence as 98P4B6 v.7. SNPs are indicated above the box. Figure 10(c): Schematic alignment of SNP variants of 98P4B6 v.8. Variants 98P4B6 v.25 through v.38 were variants with single nucleotide difference from v.8. Though these SNP variants were shown separately, they could also occur in any combinations and in any transcript variants, as shown in Fig. 12, that contains the bases. Those SNP in regions of common with v.1 were not shown here. Numbers correspond to those of 98P4B6 v.8. Black box shows the same sequence as 98P4B6 v.8. SNPs are indicated above the box. Figure 11. Schematic alignment of protein variants of 98P4B6. Protein variants corresponded to nucleotide variants. Nucleotide variants 98P4B6 v.3, v.4, v.9 through v.12, and v.15 through v.19 coded for the same protein as v.1. Nucleotide variants 98P4B6 v.6 and v.8 coded the same protein except for single amino acid at 475, which is an "M" in v.8. Variants v.25 was translated from v.25, a SNP variant of v.8, with one amino acid difference at 565. Similarly, v.21 differed from v.7 by one amino acid at 565. Single amino acid differences were indicated above the boxes. Black boxes represent the same sequence as 98P4B6 v.1. Numbers underneath the box correspond to 98P4B6 v.1. Figure 12. Structure of transcript variants of 98P4B6. Variant 98P4B6 v.2 through v.8 were transcript variants of v.1. Variant v.2 was a single exon transcript whose 3' portion was the same as the last exon of v.1. The first two exons of v.3 were in intron 1 of v. 1. Variants v.4, v.5 and v.6 spliced out 224-334 in the first exon of v.1. In addition, v.5 spliced out exon 5 while v.6 spliced out exon 6 but extended exon 5 of v.1. Variant v.7 used alternative transcription start and different 3' exons. Variant v.8 extended 5' end and kept the whole intron 5 of v.1. The first 35 bases of v.1 were not in the nearby 5' region of v.1 on the current assembly of the human genome. Ends of exons in the transcripts are marked above the boxes. Potential exons of this gene are shown in order as on the human genome. Poly A tails and single nucleotide differences are not shown in the figure. Numbers in "()" underneath the boxes correspond to those of 98P4B6 v.1. Lengths of introns and exons are not proportional. Figure 13. Secondary structure and transmembrane domains prediction for 98P4B6 protein variants. 13(A), 13(B), 13(C), 13(D), 13(E): The secondary structure of 98P4B6 protein variant 1 (SEQ ID NO: 193), Variant 2 (SEQ ID NO: 194), Variant 5 (SEQ ID NO: 195), Variant 6 (SEQ ID NO: 196), and Variant 7 (SEQ ID NO: 197) were predicted using the HNN - Hierarchical Neural Network method (Guermeur, 1997, located on the World Wide Web at .pbil.ibcp.fr/cgi bin/npsaautomat.pl?page=npsa nn.html, accessed from the ExPasy molecular biology server located on the World Wide Web at.expasy.chttools.. This method predicts the presence and location of alpha helices, extended strands, and random coils from the primary protein sequence. The percent of the protein in a given secondary structure is also listed. 10 WO 03/087306 PCT/USO3/10462 13(F), 13(H), 13(J), 13(L), and 13(N): Schematic representations of the probability of existence of transmembrane regions and orientation of 98P4B6 variants 1, 2, 5-7, respectively, based on the TMpred algorithm of Hofmann and Stoffel which utilizes TMBASE (K. Hofmann, W. Stoffel. TMBASE - A database of membrane spanning protein segments Biol. Chem. Hoppe-Seyler 374:166, 1993). 13(G), 13(I), 13(K), 13(M), and 13(0): Schematic representations of the probability of the existence of transmembrane regions and the extracellular and intracellular orientation of 98P4B6 variants 1, 2, 5-7, respectively, based on the TMHMM algorithm of Sonnhammer, von Heijne, and Krogh (Erik L.L. Sonnhammer, Gunnar von Heijne, and Anders Krogh: A hidden Markov model for predicting transmembrane helices in protein sequences. In Proc. of Sixth Int. Conf. on Intelligent Systems for Molecular Biology, p 175-182 Ed J. Glasgow, T. Littlejohn, F. Major, R. Lathrop, D. Sankoff, and C. Sensen Menlo Park, CA: AAAI Press, 1998). The TMpred and TMHMM algorithms are accessed from the ExPasy molecular biology server located on the World Wide Web at.expasy.chftools/. Figure 14. 98P4B6 Expression in Human Normal and Patient Cancer Tissues. First strand cDNA was generated from normal stomach, normal brain, normal heart, normal liver, normal skeletal muscle, normal testis, normal prostate, normal bladder, normal kidney, normal colon, normal lung, normal pancreas, and a pool of cancer specimens from prostate cancer patients, bladder cancer patients, kidney cancer patients, colon cancer patients, lung cancer patients, pancreas cancer patients, and a pool of 2 patient prostate metastasis to lymph node. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers directed to 98P4B6 v.1, v.13, and v.14 (A), or directed specifically to the splice variants 98P4B6 v.6 and v.8 (B), was performed at 26 and 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Results show strong expression of 98P4B6 v.1, v.13, and v.14 and its splice variants v.6 and v.8 in normal prostate and in prostate cancer. Expression was also detected in bladder cancer, kidney cancer, colon cancer, lung cancer, pancreas cancer, breast cancer, cancer metastasis as well as in the prostate cancer metastasis to lymph node specimens, compared to all normal tissues tested. Figure 15. 98P4B6 Expression in lung, ovary, prostate, bladder, cervix, uterus and pancreas patient cancer specimens. First strand cDNA was prepared from a panel of patient cancer specimens. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers to 98P4B6 v.1, v.13, and v.14, was performed at 26 and 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Expression was recorded as absent, low, medium or strong. Results show expression of 98P4B6 in the majority of all patient cancer specimens tested. Figure 16. Expression of 98P4B6 in stomach cancer patient specimens. (A) RNA was extracted from normal stomach (N) and from 10 different stomach cancer patient specimens (T). Northern blot with 10 pg of total RNA/lane was probed with 98P4B6 sequence. Results show strong expression of 98P4B6 in the stomach tumor tissues and lower expression in normal stomach. The lower panel represents ethidium bromide staining of the blot showing quality of the RNA samples. (B) Expression of 98P4B6 was assayed in a panel of human stomach cancers (T) and their respective matched normal tissues (N) on RNA dot blots. 98P4B6 was detected in 7 out of 8 stomach tumors but not in the matched normal tissue. Figure 17. Detection of 98P4B6 expression with polyclonal antibody. 293T cells were transfected with 98P4B6.GFP.pcDNA3.1/mychis construct clone A2 or clone B12. STEAPi1.GFP vector was used as a positive control. And as a negative control an empty vector was used. Forty hours later, cell lysates were collected. Samples were run on an SDS-PAGE acrylamide gel, blotted and stained with either anti-GFP antibody (A), anti-98P486 antibody generated against amino acids 198-389 (B), or anti-98P4B6 antibody generated against amino acids 153-165. The blot was developed using the ECL chemiluminescence kit and visualized by autoradiography. Results show expression of the expected 98P4B6.GFP fusion protein as detected by the anti-GFP antibody. Also, we were able to raise 2 different polyclonal antibodies that recognized the 98P4B6.GFP fusion proteins as shown in B and C. 11 WO 03/087306 PCT/USO3/10462 Figure 18. Detection of 98P4B6 expression with polyclona antibody. 293T cells were transfected with 98P4B6.GFP.pcDNA3.1/mychis construct clone A12 or clone 812. Expression of the 98P4B6.GFP fusion protein was detected by flow cytometry (A) and by flurorescent microscopy (B). Results show strong green fluorescence in the majority of the cells. The fusion protein localized to the perinuclear area and to the cell membrane. Figure 19. STEAP-2 Characteristics. The expression of STEAP-2 in normal tissues is predominantly restricted to the prostate. STEAP-2 is expressed in several cancerous tissues. In patient-derived prostate, colon, and lung cancer specimens; and Multiple cancer cell lines, including prostate, colon, Ewing's sarcoma, lung, kidney, pancreas and testis. By ISH, STEAP-2 expression appears to be primarily limited to ductal epithelial cells. Figure 20. STEAP-2 Induces Tyrosine Phosphorylation in PC3 Cells. STEAP-2 induces the tyrosine phosphorylation of proteins at 140-150, 120, 75-80, 62 and 40 kDa. Figure 21. STEAP-2 Enhances Tyrosine Phosphorylation in NIH 3T3 Cells. STEAP-2 enhances the phosphorylation of p 1 35-140, p78-75 by STEAP-2 in NIH 3T3 cells. STEAP-2 C-Flag enhances the phosphorylation of p180, and induces the de-phosphorylation of p132, p 82 and p75. Figure 22. STEAP-2 Induces ERK Phosphorylation. STEAP-2 Induces ERK phosphorylation in PC3 and 3T3 cells in 0.5 and 10% FBS. Lack or ERK phosphorylation in 3T3-STEAP-2-cflag cells. Potential role as dominant negative. Figure 23. STEAP Enhances Calcium Flux in PC3 cells. PC-STEAP-1 and PC3-STEAP-2 exhibit enhanced calcium flux in response to LPA. PC3-STEAP-1 demonstrates susceptibility to the L type calcium channel inhibitor, conotoxin. PC3-STEAP-2 shown susceptibility to the PQ type calcium channel inhibitor, agatoxin. NDGA and TEA had no effect on the proliferation of PC3-STEAP-2 cells. Figure 24. STEAP-2 Alters the Effect of Paclitaxel on PC3 Cells. Other Chemotherapeutics Tested without yielding a differential response between STEAP-expressing and control cells were Flutamide, Genistein, Rapamycin. STEAP-2 confers partial resistance to Paclitaxel in PC3 cells. Over 8 fold increase in percent survival of PC3-STEAP-2 relative to PC3-Neo cells. Figure 25. Inhibition of Apoptosis by STEAP-2. PC3 cells were treated with paclitaxel for 60 hours and analyzed for apoptosis by annexinV-PI staining. Expression of STEAP-2 partially inhibits apoptosis by paclitaxel. Figure 26. STEAP-2 Attenuates Paclitaxel Mediated Apoptosis. PC3 cells were treated with paclitaxel for 68 hours and analyzed for apoptosis. Expression of STEAP-2, but not STEAP-2CFlag, partially inhibits apoptosis by paclitaxel. DETAILED DESCRIPTION OF THE INVENTION Outline of Sections I.) Definitions II.) 98P4B6 Polynucleotides II.A.) Uses of 98P4B6 Polynucleotides II.A.1.) Monitoring of Genetic Abnormalities 1I.A.2.) Antisense Embodiments II.A.3.) Primers and Primer Pairs II.A.4.) Isolation of 98P4B6-Encoding Nucleic Acid Molecules II.A.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems III.) 98P4B6-related Proteins III.A.) Motif-bearing Protein Embodiments IIlI.B.) Expression of 98P4B6-related Proteins III.C.) Modifications of 98P4B6-related Proteins 12 WO 03/087306 PCT/US03/10462 III.D.) Uses of 98P4B6-related Proteins IV.) 98P4B6 Antibodies V.) 98P4B6 Cellular Immune Responses VI.) 98P4B6 Transgenic Animals VII.) Methods for the Detection of 98P4B6 VIII.) Methods for Monitoring the Status of 98P4B6-related Genes and Their Products IX.) Identification of Molecules That Interact With 98P4B6 X.) Therapeutic Methods and Compositions X.A.) Anti-Cancer Vaccines X.B.) 98P4B6 as a Target for Antibody-Based Therapy X.C.) 98P4B6 as a Target for Cellular Immune Responses X.C.1. Minigene Vaccines XC.2. Combinations of CTL Peptides with Helper Peptides X.C.3. Combinations of CTL Peptides with T Cell Priming Agents X.C.4. Vaccine Compositions Comprising DC Pulsed with CTL andlor HTL Peptides X.D.) Adoptive Immunotherapy X.E.) Administration of Vaccines for Therapeutic or Prophylactic Purposes XI.) Diagnostic and Prognostic Embodiments of 98P4B6. XII.) Inhibition of 98P4B6 Protein Function XII.A.) Inhibition of 98P4B6 With Intracellular Antibodies XII.B.) Inhibition of 98P4B6 with Recombinant Proteins XII.C.) Inhibition of 98P4B6 Transcription or Translation XII.D.) General Considerations for Therapeutic Strategies XIII.) Identification, Characterization and Use of Modulators of 98P4B6 XIV.) KITSIArticles of Manufacture I.) Definitions: Unless otherwise defined, all terms of art, notations and other scientific terms or terminology used herein are intended to have the meanings commonly understood by those of skill in the art to which this invention pertains. In some cases, terms with commonly understood meanings are defined herein for clarity and/or for ready reference, and the inclusion of such definitions herein should not necessarily be construed to represent a substantial difference over what is generally understood in the art. Many of the techniques and procedures described or referenced herein are well understood and commonly employed using conventional methodology by those skilled in the art, such as, for example, the widely utilized molecular cloning methodologies described in Sambrook et al., Molecular Cloning: A Laboratory Manual 2nd. edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. As appropriate, procedures involving the use of commercially available kits and reagents are generally carried out in accordance with manufacturer defined protocols and/or parameters unless otherwise noted. The terms "advanced prostate cancer", "locally advanced prostate cancer', "advanced disease" and "locally advanced disease" mean prostate cancers that have extended through the prostate capsule, and are meant to include stage C disease under the American Urological Association (AUA) system, stage C1 - C2 disease under the Whitmore-Jewett system, and stage T3 -T4 and N+ disease under the TNM (tumor, node, metastasis) system. In general, surgery is not recommended for patients with locally advanced disease, and these patients have substantially less favorable outcomes 13 WO 03/087306 PCT/US03/10462 compared to patients having clinically localized (organ-confined) prostate cancer. Locally advanced disease is clinically identified by palpable evidence of induration beyond the lateral border of the prostate, or asymmetry or induration above the prostate base. Locally advanced prostate cancer is presently diagnosed pathologically following radical prostatectomy if the tumor invades or penetrates the prostatic capsule, extends into the surgical margin, or invades the seminal vesicles. "Altering the native glycosylation pattern" is intended for purposes herein to mean deleting one or more carbohydrate moieties found in native sequence 98P4B6 (either by removing the underlying glycosylation site or by deleting the glycosylation by chemical and/or enzymatic means), andlor adding one or more glycosylation sites that are not present in the native sequence 98P4B6. In addition, the phrase includes qualitative changes in the glycosylation of the native proteins, involving a change in the nature and proportions of the various carbohydrate moieties present. The term "analog" refers to a molecule which is structurally similar or shares similar or corresponding attributes with another molecule (e.g. a 98P4B6-related protein). For example, an analog of a 98P4B6 protein can be specifically bound by an antibody or T cell that specifically binds to 98P4B6. The term "antibody" is used in the broadest sense. Therefore, an "antibody" can be naturally occunrring or man-made such as monoclonal antibodies produced by conventional hybridoma technology. Anti-98P4B6 antibodies comprise monoclonal and polyclonal antibodies as well as fragments containing the antigen-binding domain and/or one or more complementarity determining regions of these antibodies. An "antibody fragment" is defined as at least a portion of the variable region of the immunoglobulin molecule that binds to its target, i.e., the antigen-binding region. In one embodiment it specifically covers single anti-98P4B6 antibodies and clones thereof (including agonist, antagonist and neutralizing antibodies) and anti-98P4B6 antibody compositions with polyepitopic specificity. The term "codon optimized sequences" refers to nucleotide sequences that have been optimized for a particular host species by replacing any codons having a usage frequency of less than about 20%. Nucleotide sequences that have been optimized for expression in a given host species by elimination of spurious polyadenylation sequences, elimination of exon/intron splicing signals, elimination of transposon-like repeats and/or optimization of GC content in addition to codon optimization are referred to herein as an "expression enhanced sequences." A "combinatorial library" is a collection of diverse chemical compounds generated by either chemical synthesis or biological synthesis by combining a number of chemical "building blocks" such as reagents. For example, a linear combinatorial chemical library, such as a polypeptide (e.g., mutein) library, is formed by combining a set of chemical building blocks called amino acids in every possible way for a given compound length (i.e., the number of amino acids in a polypeptide compound). Numerous chemical compounds are synthesized through such combinatorial mixing of chemical building blocks (Gallop et al., J. Med. Chem. 37(9): 1233-1251 (1994)). Preparation and screening of combinatorial libraries is well known to those of skill in the art. Such combinatorial chemical libraries include, but are not limited to, peptide libraries (see, e.g., U.S. Patent No. 5,010,175, Furka, Pept. Prot. Res. 37:487-493 (1991), Houghton et al., Nature, 354:84-88 (1991)), peptoids (PCT Publication No WO 91/19735), encoded peptides (PCT Publication WO 93/20242), random bio- oligomers (PCT Publication WO 92/00091), benzodiazepines (U.S. Pat. No. 5,288,514), diversomers such as hydantoins, benzodiazepines and dipeptides (Hobbs et al., Proc. Nat. Acad. Sci. USA 90:6909-6913 (1993)), vinylogous polypeptides (Hagihara et al., J. Amer. Chem. Soc. 114:6568 (1992)), nonpeptidal peptidomimetics with a Beta-D-Glucose scaffolding (Hirschmann et al., J. Amer. Chem. Soc. 114:9217-9218 (1992)), analogous organic syntheses of small compound libraries (Chen et al., J. Amer. Chem. Soc. 116:2661 (1994)), oligocarbarnates (Cho, et al., Science 261:1303 (1993)), and/or peptidyl phosphonates (Campbell et al., J. Org. Chem. 59:658 (1994)). See, generally, Gordon et al., J. Med. Chem. 37:1385 (1994), nucleic acid libraries (see, e.g., Stratagene, Corp.), peptide nucleic acid libraries (see, e.g., U.S. Patent 5,539,083), antibody libraries (see, e.g., Vaughn et al., Nature 14 WO 03/087306 PCT/USO3/10462 Biotechnology 14(3): 309-314 (1996), and PCT/US96/10287), carbohydrate libraries (see, e.g., Liang et al., Science 274:1520-1522 (1996), and U.S. Patent No. 5,593,853), and small organic molecule libraries (see, e.g., benzodiazepines, Baum, C&EN, Jan 18, page 33 (1993); isoprenoids, U.S. Patent No. 5,569,588; thiazolidinones and metathiazanones, U.S. Patent No. 5,549,974; pyrrolidines, U.S. Patent Nos. 5,525,735 and 5,519,134; morpholino compounds, U.S. Patent No. 5,506, 337; benzodiazepines, U.S. Patent No. 5,288,514; and the like). Devices for the preparation of combinatorial libraries are commercially available (see, e.g., 357 NIPS, 390 NIPS, Advanced Chem Tech, Louisville KY; Symphony, Rainin, Woburn, MA; 433A, Applied Biosystems, Foster City, CA; 9050, Plus, Millipore, Bedford, NIA). A number of well-known robotic systems have also been developed for solution phase chemistries. These systems include automated workstations such as the automated synthesis apparatus developed by Takeda Chemical Industries, LTD. (Osaka, Japan) and many robotic systems utilizing robotic arms (Zymate H, Zymark Corporation, Hopkinton, Mass.; Orca, Hewlett-Packard, Palo Alto, Calif.), which mimic the manual synthetic operations performed by a chemist. Any of the above devices are suitable for use with the present invention. The nature and implementation of modifications to these devices (if any) so that they can operate as discussed herein will be apparent to persons skilled in the relevant art. In addition, numerous combinatorial libraries are themselves commercially available (see, e.g., ComGenex, Princeton, NJ; Asinex, Moscow, RU; Tripos, Inc., St. Louis, MO; ChemStar, Ltd, Moscow, RU; 3D Pharmaceuticals, Exton, PA; Martek Biosciences, Columbia, MD; etc.). The term "cytotoxic agent" refers to a substance that inhibits or prevents the expression activity of cells, function of cells andlor causes destruction of cells. The term is intended to include radioactive isotopes chemotherapeutic agents, and toxins such as small molecule toxins or enzymatically active toxins of bacterial, fungal, plant or animal origin, including fragments and/or variants thereof. Examples of cytotoxic agents include, but are not limited to auristatins, auromycins, maytansinoids, yttrium, bismuth, ricin, ricin A-chain, combrestatin, duocarmycins, dolostatins, doxorubicin, daunorubicin, taxol, cisplatin, cc1065, ethidium bromide, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin dione, actinomycin, diphtheria toxin, Pseudomonas exotoxin (PE) A, PE40, abrin, abrin A chain, modeccin A chain, alpha-sarcin, gelonin, mitogellin, retstrictocin, phenomycin, enomycin, curicin, crotin, calicheamicin, Sapaonatia officinalis inhibitor, and glucocorticoid and other chemotherapeutic agents, as well as radioisotopes such as At 21 1 , 1131, 1125, y90, Re 186 , Re 188 , Sms 1 5 3 , Bi 2 12or213, p32 and radioactive isotopes of Lu including Lu 17 7 . Antibodies may also be conjugated to an anti cancer pro-drug activating enzyme capable of converting the pro-drug to its active form. The "gene product" is sometimes referred to herein as a protein or mRNA. For example, a "gene product of the invention" is sometimes referred to herein as a "cancer amino acid sequence", "cancer protein", "protein of a cancer listed in Table I", a "cancer mRNA", "mRNA of a cancer listed in Table I", etc. In one embodiment, the cancer protein is encoded by a nucleic acid of Figure 2. The cancer protein can be a fragment, or alternatively, be the full-length protein to the fragment encoded by the nucleic acids of Figure 2. In one embodiment, a cancer amino acid sequence is used to determine sequence identity or similarity. In another embodiment, the sequences are naturally occurring allelic variants of a protein encoded by a nucleic acid of Figure 2. In another embodiment, the sequences are sequence variants as further described herein. "High throughput screening" assays for the presence, absence, quantification, or other properties of particular nucleic acids or protein products are well known to those of skill in the art. Similarly, binding assays and reporter gene assays are similarly well known. Thus, e.g., U.S. Patent No. 5,559,410 discloses high throughput screening methods for proteins; U.S. Patent No. 5,585,639 discloses high throughput screening methods for nucleic acid binding (i.e., in arrays); while U.S. Patent Nos. 5,576,220 and 5,541,061 disclose high throughput methods of screening for ligandlantibody binding. In addition, high throughput screening systems are commercially available (see, e.g., Amersham Biosciences, Piscataway, NJ; Zymark Corp., Hopkinton, MA; Air Technical Industries, Mentor, OH; Beckman Instruments, Inc. Fullerton, 15 WO 03/087306 PCT/US03/10462 CA; Precision Systems, Inc., Natick, MA; etc.). These systems typically automate entire procedures, including all sample and reagent pipetting, liquid dispensing, timed incubations, and final readings of the microplate in detector(s) appropriate for the assay. These configurable systems provide high throughput and rapid start up as well as a high degree of flexibility and customization. The manufacturers of such systems provide detailed protocols for various high throughput systems. Thus, e.g., Zymark Corp. provides technical bulletins describing screening systems for detecting the modulation of gene transcription, ligand binding, and the like. The term "homolog" refers to a molecule which exhibits homology to another molecule, by for example, having sequences of chemical residues that are the same or similar at corresponding positions. "Human Leukocyte Antigen"or "HLA" is a human class I or class II Major Histocompatibility Complex (MHC) protein (see, e.g., Stites, et at., IMMUNOLOGY, 8m ED., Lange Publishing, Los Altos, CA (1994). The terms "hybridize", "hybridizing", "hybridizes" and the like, used in the context of polynucleotides, are meant to refer to conventional hybridization conditions, preferably such as hybridization in 50% formamide/6XSSC/0.1% SDS/100 tg/ml ssDNA, in which temperatures for hybridization are above 37 degrees C and temperatures for washing in 0.1XSSC/0.1% SDS are above 55 degrees C. The phrases "isolated" or "biologically pure" refer to material which is substantially or essentially free from components which normally accompany the material as it is found in its native state. Thus, isolated peptides in accordance with the invention preferably do not contain materials normally associated with the peptides in their in situ environment. For example, a polynudcleotide is said to be "isolated" when it is substantially separated from contaminant polynucleotides that correspond or are complementary to genes other than the 98P4B6 genes or that encode polypeptides other than 98P4B6 gene product or fragments thereof. A skilled artisan can readily employ nucleic acid isolation procedures to obtain an isolated 98P4B6 polynucleotide. A protein is said to be "isolated," for example, when physical, mechanical or chemical methods are employed to remove the 98P4B6 proteins from cellular constituents that are normally associated with the protein. A skilled artisan can readily employ standard purification methods to obtain an isolated 98P4B6 protein. Alternatively, an isolated protein can be prepared by chemical means. The term "mammal" refers to any organism classified as a mammal, including mice, rats, rabbits, dogs, cats, cows, horses and humans. In one embodiment of the invention, the mammal is a mouse. In another embodiment of the invention, the mammal is a human. The terms "metastatic prostate cancer" and "metastatic disease" mean prostate cancers that have spread to regional lymph nodes or to distant sites, and are meant to include stage D disease under the AUA system and stage TxNxM+ under the TNM system. As is the case with locally advanced prostate cancer, surgery is generally not indicated for patients with metastatic disease, and hormonal (androgen ablation) therapy is a preferred treatment modality. Patients with metastatic prostate cancer eventually develop an androgen-refractory state within 12 to 18 months of treatment initiation. Approximately half of these androgen-refractory patients die within 6 months after developing that status. The most common site for prostate cancer metastasis is bone. Prostate cancer bone metastases are often osteoblastic rather than osteolytic (i.e., resulting in net bone formation). Bone metastases are found most frequently in the spine, followed by the femur, pelvis, rib cage, skull and humerus. Other common sites for metastasis include lymph nodes, lung, liver and brain. Metastatic prostate cancer is typically diagnosed by open or laparoscopic pelvic lymphadenectomy, whole body radionuclide scans, skeletal radiography, and/or bone lesion biopsy. The term "modulator" or "test compound" or "drug candidate" or grammatical equivalents as used herein describe any molecule, e.g., protein, oligopeptide, small organic molecule, polysaccharide, polynucleotide, etc., to be tested for the capacity to directly or indirectly alter the cancer phenotype or the expression of a cancer sequence, e.g., a nucleic acid or protein sequences, or effects of cancer sequences (e.g., signaling, gene expression, protein interaction, etc.) In one aspect, 16 WO 03/087306 PCT/USO3/10462 a modulator will neutralize the effect of a cancer protein of the invention. By "neutralize" is meant that an activity of a protein is inhibited or blocked, along with the consequent effect on the cell. In another aspect, a modulator will neutralize the effect of a gene, and its corresponding protein, of the invention by normalizing levels of said protein. In preferred embodiments, modulators alter expression profiles, or expression profile nucleic acids or proteins provided herein, or downstream effector pathways. In one embodiment, the modulator suppresses a cancer phenotype, e.g. to a normal tissue fingerprint. In another embodiment, a modulator induced a cancer phenotype. Generally, a plurality of assay mixtures is run in parallel with different agent concentrations to obtain a differential response to the various concentrations. Typically, one of these concentrations serves as a negative control, i.e., at zero concentration or below the level of detection. Modulators, drug candidates or test compounds encompass numerous chemical classes, though typically they are organic molecules, preferably small organic compounds having a molecular weight of more than 100 and less than about 2,500 Daltons. Preferred small molecules are less than 2000, or less than 1500 or less than 1000 or less than 500 D. Candidate agents comprise functional groups necessary for structural interaction with proteins, particularly hydrogen bonding, and typically include at least an amine, carbonyl, hydroxyl or carboxyl group, preferably at least two of the functional chemical groups. The candidate agents often comprise cyclical carbon or heterocyclic structures and/or aromatic or polyaromatic structures substituted with one or more of the above functional groups. Modulators also comprise biomolecules such as peptides, saccharides, fatty acids, steroids, purines, pyrimidines, derivatives, structural analogs or combinations thereof. Particularly preferred are peptides. One class of modulators are peptides, for example of from about five to about 35 amino acids, with from about five to about 20 amino acids being preferred, and from about 7 to about 15 being particularly preferred. Preferably, the cancer modulatory protein is soluble, includes a non-transmembrane region, and/or, has an N terminal Cys to aid in solubility. In one embodiment, the C-terminus of the fragment is kept as a free acid and the N-terminus is a free amine to aid in coupling, i.e., to cysteine. In one embodiment, a cancer protein of the invention is conjugated to an immunogenic agent as discussed herein. In one embodiment, the cancer protein is conjugated to BSA. The peptides of the invention, e.g., of preferred lengths, can be linked to each other or to other amino acids to create a longer peptidelprotein. The modulatory peptides can be digests of naturally occurring proteins as is outlined above, random peptides, or "biased" random peptides. In a preferred embodiment, peptide/protein-based modulators are antibodies, and fragments thereof, as defined herein. Modulators of cancer can also be nucleic acids. Nucleic acid modulating agents can be naturally occurring nucleic acids, random nucleic acids, or "biased" random nucleic acids. For example, digests of prokaryotic or eukaryotic genomes can be used in an approach analogous to that outlined above for proteins. The term "monoclonal antibody" refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the antibodies comprising the population are identical except for possible naturally occurring mutations that are present in minor amounts. A "motif', as in biological motif of a 98P4B6-related protein, refers to any pattern of amino acids forming part of the primary sequence of a protein, that is associated with a particular function (e.g. protein-protein interaction, protein-DNA interaction, etc) or modification (e.g. that is phosphorylated, glycosylated or amidated), or localization (e.g. secretory sequence, nuclear localization sequence, etc.) or a sequence that is correlated with being immunogenic, either humorally or cellularly. A motif can be either contiguous or capable of being aligned to certain positions that are generally correlated with a certain function or property. In the context of HLA motifs, "motif" refers to the pattern of residues in a peptide of defined length, usually a peptide of from about 8 to about 13 amino acids for a class I HLA motif and from about 6 to about 25 amino acids for a class 11 HLA motif, which is recognized by a particular HLA molecule. Peptide motifs for HLA binding are typically different for each protein encoded by each human HLA allele and differ in the pattern of the primary and secondary anchor residues. 17 WO 03/087306 PCT/US03/10462 A "pharmaceutical excipient" comprises a material such as an adjuvant, a carrier, pH-adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservative, and the like. "Pharmaceutically acceptable" refers to a non-toxic, inert, and/or composition that is physiologically compatible with humans or other mammals. The term "polynucleotide" means a polymeric form of nucleotides of at least 10 bases or base pairs in length, either ribonucleotides or deoxynucleotides or a modified form of either type of nucleotide, and is meant to include single and double stranded forms of DNA and/or RNA. In the art, this term if often used interchangeably with "oligonucleotide". A polynucleotide can comprise a nucleotide sequence disclosed herein wherein thymidine (T), as shown for example in Figure 2, can also be uracil (U); this definition pertains to the differences between the chemical structures of DNA and RNA, in particular the observation that one of the four major bases in RNA is uracil (U) instead of thymidine (T). The term "polypeptide" means a polymer of at least about 4, 5, 6, 7, or 8 amino acids. Throughout the specification, standard three letter or single letter designations for amino acids are used. In the art, this term is often used interchangeably with "peptide" or "protein". An HLA "primary anchor residue" is an amino acid at a specific position along a peptide sequence which is understood to provide a contact point between the immunogenic peptide and the HLA molecule. One to three, usually two, primary anchor residues within a peptide of defined length generally defines a "motif for an immunogenic peptide. These residues are understood to fit in close contact with peptide binding groove of an HLA molecule, with their side chains buried in specific pockets of the binding groove. In one embodiment, for example, the primary anchor residues for an HLA class I molecule are located at position 2 (from the amino terminal position) and at the carboxyl terminal position of a 8, 9, 10, 11, or 12 residue peptide epitope in accordance with the invention. Alternatively, in another embodiment, the primary anchor residues of a peptide binds an HLA class 11 molecule are spaced relative to each other, rather than to the termini of a peptide, where the peptide is generally of at least 9 amino acids in length. The primary anchor positions for each motif and supermotif are set forth in Table IV. For example, analog peptides can be created by altering the presence or absence of particular residues in the primary and/or secondary anchor positions shown in Table IV. Such analogs are used to modulate the binding affinity and/or population coverage of a peptide comprising a particular HLA motif or supermotif, "Radioisotopes" include, but are not limited to the following (non-limiting exemplary uses are also set forth): Examples of Medical Isotopes: Isotope Description of use Actinium-225 (AC-225) See Thorium-229 (Th-229) Actinium-227 (AC-227) Parent of Radium-223 (Ra-223) which is an alpha emitter used to treat metastases in the skeleton resulting from cancer (i.e., breast and prostate cancers), and cancer radioimmunotherapy Bismuth-212 (Bi-212) See Thorium-228 (Th-228) Bismuth-213 (Bi-213) See Thorium-229 (Th-229) Cadmium-109 (Cd-109) Cancer detection 18 WO 03/087306 PCT/US03/10462 Cobalt-60 (Co-60) Radiation source for radiotherapy of cancer, for food irradiators, and for sterilization of medical supplies Copper-64 (Cu-64) A positron emitter used for cancer therapy and SPECT imaging Copper-67 (Cu-67) Beta/gamma emitter used in cancer radioimmunotherapy and diagnostic studies (i.e., breast and colon cancers, and lymphoma) Dysprosium-166 (Dy-166) Cancer radioimmunotherapy Erbium-169 (Er-169) Rheumatoid arthritis treatment, particularly for the small joints associated with fingers and toes Europium-152 (Eu-152) Radiation source for food irradiation and for sterilization of medical supplies Europium-154 (Eu-1 54) Radiation source for food irradiation and for sterilization of medical supplies Gadolinium-153 (Gd-153) Osteoporosis detection and nuclear medical quality assurance devices Gold-1 98 (Au-198) Implant and intracavity therapy of ovarian, prostate, and brain cancers Holmium-166 (Ho-166) Multiple myeloma treatment in targeted skeletal therapy, cancer radioimmunotherapy, bone marrow ablation, and rheumatoid arthritis treatment Iodine-125 (I-125) Osteoporosis detection, diagnostic imaging, tracer drugs, brain cancer treatment, radiolabeling, tumor imaging, mapping of receptors in the brain, interstitial radiation therapy, brachytherapy for treatment of prostate cancer, determination of glomerular filtration rate (GFR), determination of plasma volume, detection of deep vein thrombosis of the legs Iodine-131 (I-131) Thyroid function evaluation, thyroid disease detection, treatment of thyroid cancer as well as other non malignant thyroid diseases (i.e., Graves disease, goiters, and hyperthyroidism), treatment of leukemia, lymphoma, and other forms of cancer (e.g., breast cancer) using radioimmunotherapy fridium-192 (Ir-192) Brachytherapy, brain and spinal cord tumor treatment, treatment of blocked arteries (i.e., arteriosclerosis and restenosis), and implantsfor breast and prostate tumors Lutetium-177 (Lu-177) 19 WO 03/087306 PCT/USO3/10462 Cancer radioimmunotherapy and treatment of blocked arteries (i.e., arteriosclerosis and restenosis) Molybdenum-99 (Mo-99) Parent of Technetium-99m (Tc-99m) which is used for imaging the brain, liver, lungs, heart, and other organs. Currently, Tc-99m is the most widely used radioisotope used for diagnostic imaging of various cancers and diseases involving the brain, heart, liver, lungs; also used in detection of deep vein thrombosis of the legs Osmium-194 (Os-194) Cancer radioimmunotherapy Palladium-103 (Pd-103) Prostate cancer treatment Platinum-195m (Pt-195m) Studies on biodistribution and metabolism of cisplatin, a chemotherapeutic drug Phosphorus-32 (P-32) Polycythemia rubra vera (blood cell disease) and leukemia treatment, bone cancer diagnosis/treatment; colon, pancreatic, and liver cancer treatment; radiolabeling nucleic acids for in vitro research, diagnosis of superficial tumors, treatment of blocked arteries (i.e., arteriosclerosis and restenosis), and intracavity therapy Phosphorus-33 (P-33) Leukemia treatment, bone disease diagnosis/treatment, radiolabeling, and treatment of blocked arteries (i.e., arteriosclerosis and restenosis) Radium-223 (Ra-223) See Actinium-227 (Ac-227) Rhenium-186 (Re-186) Bone cancer pain relief, rheumatoid arthritis treatment, and diagnosis and treatment of lymphoma and bone, breast, colon, and liver cancers using radioimmunotherapy Rhenium-188 (Re-188) Cancer diagnosis and treatment using radioimmunotherapy, bone cancer pain relief, treatment of rheumatoid arthritis, and treatment of prostate cancer Rhodium-105 (Rh-105) Cancer radioimmunotherapy Samarium-145 (Sm-145) Ocular cancer treatment Samarium-153 (Sm-153) Cancer radicimmunotherapy and bone cancer pain relief Scandium-47 (Sc-47) Cancer radioimmunotherapy and bone cancer pain relief Selenium-75 (Se-75) 20 WO 03/087306 PCT/USO3/10462 Radiotracer used in brain studies, imaging of adrenal cortex by gamma-scintigraphy, lateral locations of steroid secreting tumors, pancreatic scanning, detection of hyperactive parathyroid glands, measure rate of bile acid loss from the endogenous pool Strontium-85 (Sr-85) Bone cancer detection and brain scans Strontium-89 (Sr-89) Bone cancer pain relief, multiple myeloma treatment, and osteoblastic therapy Technetium-99m (Tc-99m) See Molybdenum-99 (Mo-99) Thorium-228 (Th-228) Parent of Bismuth-212 (Bi-212) which is an alpha emitter used in cancer radioimmunotherapy Thorium-229 (Th-229) Parent of Actinium-225 (Ac-225) and grandparent of Bismuth-213 (Bi-213) which are alpha emitters used in cancer radioimmunotherapy Thulium-170 (Tm-170) Gamma source for blood irradiators, energy source for implanted medical devices Tin-117m (Sn-117m) Cancer immunotherapy and bone cancer pain relief Tungsten-188 (W-188) Parent for Rhenium-188 (Re-188) which is used for cancer diagnostics/treatment, bone cancer pain relief, rheumatoid arthritis treatment, and treatment of blocked arteries (i.e., arteriosclerosis and restenosis) Xenon-127 (Xe-127) Neuroimaging of brain disorders, high resolution SPECT studies, pulmonary function tests, and cerebral blood flow studies Ytterbium-175 (Yb-175) Cancer radioimmunotherapy Yttrium-90 (Y-90) Microseeds obtained from irradiating Yttrium-89 (Y-89) for liver cancer treatment Yttrium-91 (Y-91) A gamma-emitting label for Yttrium-90 (Y-90) which is used for cancer radioimmunotherapy (i.e., lymphoma, breast, colon, kidney, lung, ovarian, prostate, pancreatic, and inoperable liver cancers) 21 WO 03/087306 PCT/USO3/10462 By "randomized" or grammatical equivalents as herein applied to nucleic acids and proteins is meant that each nucleic acid and peptide consists of essentially random nucleotides and amino acids, respectively. These random peptides (or nucleic acids, discussed herein) can incorporate any nucleotide or amino acid at any position. The synthetic process can be designed to generate randomized proteins or nucleic acids, to allow the formation of all or most of the possible combinations over the length of the sequence, thus forming a library of randomized candidate bioactive proteinaceous agents. In one embodiment, a library is "fully randomized," with no sequence preferences or constants at any position. In another embodiment, the library is a "biased random" library. That is, some positions within the sequence either are held constant, or are selected from a limited number of possibilities. For example, the nucleotides or amino acid residues are randomized within a defined class, e.g., of hydrophobic amino acids, hydrophilic residues, sterically biased (either small or large) residues, towards the creation of nucleic acid binding domains, the creation of cysteines, for cross-linking, prolines for SH-3 domains, serines, threonines, tyrosines or histidines for phosphorylation sites, etc., or to purines, etc. A "recombinant" DNA or RNA molecule is a DNA or RNA molecule that has been subjected to molecular manipulation in vitro. Non-limiting examples of small molecules include compounds that bind or interact with 98P4B6, ligands including hormones, neuropeptides, chemokines, odorants, phospholipids, and functional equivalents thereof that bind and preferably inhibit 98P4B6 protein function. Such non-limiting small molecules preferably have a molecular weight of less than about 10 kDa, more preferably below about 9, about 8, about 7, about 6, about 5 or about 4 kDa. In certain embodiments, small molecules physically associate with, or bind, 98P4B6 protein; are not found in naturally occurring metabolic pathways; and/or are more soluble in aqueous than non-aqueous solutions "Stringency" of hybridization reactions is readily determinable by one of ordinary skill in the art, and generally is an empirical calculation dependent upon probe length, washing temperature, and salt concentration. In general, longer probes require higher temperatures for proper annealing, while shorter probes need lower temperatures. Hybridization generally depends on the ability of denatured nucleic acid sequences to reanneal when complementary strands are present in an environment below their melting temperature. The higher the degree of desired homology between the probe and hybridizable sequence, the higher the relative temperature that can be used. As a result, it follows that higher relative temperatures would tend to make the reaction conditions more stringent, while lower temperatures less so. For additional details and explanation of stringency of hybridization reactions, see Ausubel et aL, Current Protocols in Molecular Biology, Wiley Interscience Publishers, (1995). "Stringent conditions" or "high stringency conditions", as defined herein, are identified by, but not limited to, those that: (1) employ low ionic strength and high temperature for washing, for example 0.015 M sodium chloride/0.0015 M sodium citrate/0.1% sodium dodecyl sulfate at 50OC; (2) employ during hybridization a denaturing agent, such as formamide, for example, 50% (v/v) formamide with 0.1% bovine serum albumin/0.1% Ficoll/0.1% polyvinylpyrrolidone/50 mM sodium phosphate buffer at pH 6.5 with 750 mM sodium chloride, 75 mM sodium citrate at 42 OC; or (3) employ 50% formamide, 5 x SSC (0.75 M NaCI, 0.075 M sodium citrate), 50 mM sodium phosphate (pH 6.8), 0.1% sodium pyrophosphate, 5 x Denhardt's solution, sonicated salmon sperm DNA (50 Ig/ml), 0.1% SDS, and 10% dextran sulfate at 42 oC, with washes at 42oC in 0.2 x SSC (sodium chloride/sodium, citrate) and 50% formamide at 55 oC, followed by a high-stringency wash consisting of 0.1 x SSC containing EDTA at 55 oC. "Moderately stringent conditions" are described by, but not limited to, those in Sambrook et al., Molecular Cloning: A Laboratory Manual, New York: Cold Spring Harbor Press, 1989, and include the use of washing solution and hybridization conditions (e.g., temperature, ionic strength and %SDS) less stringent than those described above. An example of moderately stringent conditions is overnight incubation at 370C in a solution comprising: 20% formamide, 5 x SSC (150 mM NaCI, 15 mM trisodium citrate), 50 mM sodium phosphate (pH 7.6), 5 x 22 WO 03/087306 PCT/US03/10462 Denhardt's solution, 10% dextran sulfate, and 20 mg/mL denatured sheared salmon sperm DNA, followed by washing the filters in 1 x SSC at about 37-50oC. The skilled artisan will recognize how to adjust the temperature, ionic strength, etc. as necessary to accommodate factors such as probe length and the like. An HLA "supermotif" is a peptide binding specificity shared by HLA molecules encoded by two or more HLA alleles. Overall phenotypic frequencies of HLA-supertypes in different ethnic populations are set forth in Table IV (F). The non limiting constituents of various supetypes are as follows: A2. A*0201, A*0202, A*0203, A*0204, A* 0205, A*0206, A*6802, A*6901, A*0207 A3: A3, All, A31, A*3301, A*6801, A*0301, A*1101, A*3101 B7: B7, B*3501-03, B*51, 8*5301, B*5401, B*5501, B*5502, B*5601, B*6701, B*7801, B*0702, B*5101, B*5602 844: 8*3701, B*4402, B*4403, 8*60 (8*4001), 861 (B*4006) Al: A*0102, A*2604, A*3601, A*4301, A*8001 A24: A*24, A*30, A*2403, A*2404, A*3002, A*3003 B27: B*1401-02, B*1503, B*1509, B*1510, B*1518, B*3801-02, B*3901, B*3902, B*3903-04, B*4801-02, B7301, B*2701-08 B58: B*1516, 8*1517, 8*5701, 8*5702, B58 B62: B*4601, B52, B*1501 (B62), B*1502 (B75), B*1513 (B77) Calculated population coverage afforded by different HLA-supertype combinations are set forth in Table IV (G). As used herein "to treat" or "therapeutic" and grammatically related terms, refer to any improvement of any consequence of disease, such as prolonged survival, less morbidity, and/or a lessening of side effects which are the byproducts of an alternative therapeutic modality; full eradication of disease is not required. A "transgenic animal" (e.g., a mouse or rat) is an animal having cells that contain a transgene, which transgene was introduced into the animal or an ancestor of the animal at a prenatal, e.g., an embryonic stage. A "transgene" is a DNA that is integrated into the genome of a cell from which a transgenic animal develops. As used herein, an HLA or cellular immune response "vaccine" is a composition that contains or encodes one or more peptides of the invention. There are numerous embodiments of such vaccines, such as a cocktail of one or more individual peptides; one or more peptides of the invention comprised by a polyepitopic peptide; or nucleic acids that encode such individual peptides or polypeptides, e.g., a minigene that encodes a polyepitopic peptide. The "one or more peptides" can include any whole unit integer from 1-150 or more, e.g., at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, or 150 or more peptides of the invention. The peptides or polypeptides can optionally be modified, such as by lipidation, addition of targeting or other sequences. HLA class I peptides of the invention can be admixed with, or linked to, HLA class II peptides, to facilitate activation of both cytotoxic T lymphocytes and helper T lymphocytes. HLA vaccines can also comprise peptide-pulsed antigen presenting cells, e.g., dendritic cells. The term "variant" refers to a molecule that exhibits a vaiiation from a described type or norm, such as a protein that has one or more different amino acid residues in the corresponding position(s) of a specifically described protein (e.g. the 98P4B6 protein shown in Figure 2 or Figure 3. An analog is an example of a variant protein. Splice isoforms and single nucleotides polymorphisms (SNPs) are further examples of variants. The "98P4B6-related proteins" of the invention include those specifically identified herein, as well as allelic variants, conservative substitution variants, analogs and homologs that can be isolated/generated and characterized without undue experimentation following the methods outlined herein or readily available in the art. Fusion proteins that combine parts of different 98P4B6 proteins or fragments thereof, as well as fusion proteins of a 98P4B6 protein and a heterologous polypeptide are 23 WO 03/087306 PCT/USO3/10462 also included. Such 98P4B6 proteins are collectively referred to as the 98P4B6-related proteins, the proteins of the invention, or 98P4B6. The term '98P4B6-related protein" refers to a polypeptide fragment or a 98P4B6 protein sequence of 4, 5, 6,7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more than 25 amino adcids; or, at least 30, 35, 40, 45, 50, 55, 60, 65, 70, 80, 85, 90, 95, 100, 105, 110, 115, 120,125,130, 135, 140,145, 150, 155, 160,165, 170, 175, 180,185,190,195, 200, 225, 250, 275, 300, 325, 350, 375, 400, 425, 450, 475, 500, 525, 550, 575, or 576 or more amino acids. 11.) 98P4B6 Polynucleotides One aspect of the invention provides polynucleotides corresponding or complementary to all or part of a 98P4B6 gene, mRNA, and/or coding sequence, preferably in isolated form, including polynucleotides encoding a 98P4B6-related protein and fragments thereof, DNA, RNA, DNAIRNA hybrid, and related molecules, polynucleotides or oligonucleotides complementary to a 98P4B6 gene or mRNA sequence or a part thereof, and polynucleotides or oligonucleotides that hybridize to a 98P4B6 gene, mRNA, or to a 98P4B6 encoding polynucleotide (collectively, "98P4B6 polynucleotides"). In all instances when referred to in this section, T can also be U in Figure 2. Embodiments of a 98P4B6 polynucleotide include: a 98P4B6 polynucleotide having the sequence shown in Figure 2, the nucleotide sequence of 98P4B6 as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polynucleotide having the sequence as shown in Figure 2; or, at least 10 contiguous nucleotides of a polynucleotide having the sequence as shown in Figure 2 where T is U. For example, embodiments of 98P4B6 nucleotides comprise, without limitation: (I) a polynucleotide comprising, consisting essentially of, or consisting of a sequence as shown in Figure 2, wherein T can also be U; (11) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2A, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (111) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2B, from nucleotide residue number 4 through nucleotide residue number 138, including the stop codon, wherein T can also be U; (IV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2C, from nucleotide residue number 188 through nucleotide residue number 1552, including the a stop codon, wherein T can also be U; (V) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2D, from nucleotide residue number 318 through nucleotide residue number 1682, including the stop codon, wherein T can also be U; (VI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2E, from nucleotide residue number 318 through nucleotide residue number 1577, including the stop codon, wherein T can also be U; (VII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2F, from nucleotide residue number 318 through nucleotide residue number 1790, including the stop codon, wherein T can also be U; 24 WO 03/087306 PCT/USO3/10462 (VIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2G, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (IX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2H, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (X) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 21, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2J, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2K, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2L, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XIV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2M, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2N, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XVI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 20, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XVII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2P, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XVIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2Q, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; 25 WO 03/087306 PCT/USO3/10462 (XIX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2R, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2S, from nucleotide residue number 355 through nucleotide residue number 1719, including the stop codon, wherein T can also be U; (XXI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2T, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2U, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2V, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXIV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2W, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2X, from nucleotide residue number 295 through nucleotide residue number 2025, including the stop codon, wherein T can also be U; (XXVI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2Y, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXVII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2Z, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXVIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AA, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXIX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AB, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; 26 WO 03/087306 PCT/USO3/10462 (XXX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AC, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AD, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AE, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AF, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXIV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AG, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXV) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AH, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXVI) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AI, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXVII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AJ, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXVIII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AK, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XXXIX) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2AL, from nucleotide residue number 394 through nucleotide residue number 1866, including the stop codon, wherein T can also be U; (XL) a polynucleotide that encodes a 98P486-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% homologous to an entire amino acid sequence shown in Figure 2A-AL; (XLI) a polynucleotide that encodes a 98P4B6-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identical to an entire amino acid sequence shown in Figure 2A-AL; 27 WO 03/087306 PCT/USO3/10462 (XLII) a polynucleotide that encodes at least one peptide set forth in Tables VIII-XXI and XXII-XLIX; (XLIII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10,11, 12,13,14,15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (XLIV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10,11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; (XLV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XLVI) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XLVII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9,10, 11, 12,13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3A, 3G, and 3H in any whole number increment up to 454 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of Figure 9; (XLVIII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (XLIX) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; 28 WO 03/087306 PCT/USO3/10462 (L) a polynucleotide that encodes apeptide region of at least 5, 6,7,8,9,10,11,12, 13,14,15,16,17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that includes 1,2,3, 4,5,6,7, 8, 9,10,11, 12,13,14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (LI) a polynucleotide that encodes apeptide region of at least 5, 6,7,8,9,10,11,12,13,14,15,16,17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3B in any whole number increment up to 45 that includes 1,2,3,4,5,6,7, 8,9,10,11, 12,13,14,15,16, 17,18,19,20,21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (LII) a polynucleotide that encodes apeptide region of at least 5, 6,7,8,9,10,11,12,13,14,15,16,17,18, 19, 20, 21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32, 33, 34, 35 amino acids ofa peptide of Figure 3B in any whole numberincrementupto45 thatincludes 1, 2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34,35 amino acid position(s) having a value greater than 0.5 in the Beta turn profile of Figure 9 (LIII) a polynucleotide that encodes a peptide region ofat least5, 6,7,8,9,10,11, 12,13,14,15,16,17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3C in any whole number increment up to 419 that includes 1,2,3,4,5, 6,7,8,9,10,11,12,13,14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (LIV) apolynucleotide that encodes apeptide region of at least 5, 6,7,8,9,10,11,12,13,14,15,16,17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3C in any whole number increment up to 419 thatincludes 1, 2,3,4, 5,6,7, 8,9,10,11,12,13,14,15,16,17,18,19,20,21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31,32,33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; (LV) apolynucleotide that encodes apeptide region of at least 5,6,7,8,9,10,11,12,13,14,15,16,17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3C in any whole numberincrementupto419that includes 1,2,3,4,5,6,7,8, 9 , 10,11,12,13,14,15,16,17,18,19,20,21,22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (LVI) a polynucleotide that encodes a peptide region of at least 5, 6,7,8,9,10,11,12,13,14, 15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids ofa peptide of Figure 3C in any whole number increment up to 419 that includes 1, 2,3,4,5,6,7,8,9,10,11,12,13, 14,15, 16,17,18,19,20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (LVII) a polynucleotide thatencodes a peptide region of atleast 5, 6,7,8, 9,10,11, 12,13, 14,15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3C in any whole 29 WO 03/087306 PCT/USO3/10462 number increment up to 419 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9,10,11, 12, 13,14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta turn profile of Figure 9 (LVIII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (LIX) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 1, 2, 3,4, 5, 6, 7, 8, 9, 10, 11, 12,13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; (LX) a polynudeofide that encodes a peptide region of at least 5, 6, 7, 8, 9,10,11, 12, 13,14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (LXI) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (LXII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3D, 3F, and 3J in any whole number increment up to 490 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of Figure 9 (LXIII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (LXIV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids ofa peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 30 WO 03/087306 PCT/US03/10462 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; (LXV) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (LXVI) a polynucleotide that encodes a peptide region of at least 5, 6,7, 8,9,10,11,12,13,14,15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13,14,15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (LXVII) a polynucleotide that encodes a peptide region of at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a peptide of Figure 3E and 31 in any whole number increment up to 576 that includes 1, 2, 3, 4, 5, 6, 7, 8, 9,10,11, 12, 13,14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of Figure 9 (LXVIII) a polynucleotide that is fully complementary to a polynucleotide of any one of (I)-(LXVII). (LXIX) a peptide that is encoded by any of (I) to (LXVIII); and (LXX) a composition comprising a polynucleotide of any of (I)-(LXVIII) or peptide of (LXIX) together with a pharmaceutical excipient and/or in a human unit dose form. (LXXI) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to modulate a cell expressing 98P4B6, (LXXII) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6 (LXXIII) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6, said cell from a cancer of a tissue listed in Table I; (LXXIV) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or treat a a cancer; (LXX(V) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to diagnose, prophylax, prognose, or treat a a cancer of a tissue listed in Table I; and, (LXXVI) a method of using a polynucleotide of any (I)-(LXVIII) or peptide of (LXIX) or a composition of (LXX) in a method to identify or characterize a modulator of a cell expressing 98P4B6. 31 WO 03/087306 PCT/US03/10462 As used herein, a range is understood to disclose specifically all whole unit positions thereof. Typical embodiments of the invention disclosed herein include 98P4B6 polynucleotides that encode specific , portions of 98P4B6 mRNA sequences (and those which are complementary to such sequences) such as those that encode the proteins and/or fragments thereof, for example: . (a) 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17,18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105,110,115, 120,125,130,135,140,145,150,155,160,165,170,175,180,185, 1,90, 195, 200, 225, 250, 275, 300, 325, 350, 375, 400, 410, 420, 430, 440, 450 or 454 or more contiguous amino acids of 98P4B6 variant 1; the maximal lengths relevant for other variants are: variant 2, 44 amino acids; variant 5, 419 amino acids, variant 6, 490 amino acids, variant 7, 576 amino acids, variant 8, 490 amino acids, variant 13, 454 amino acids, variant 14, 454 amino acids, variant 21, 576 amino acids, and variant 25, 490 amino acids. For example, representative embodiments of the invention disclosed herein include: polynucleotides and their encoded peptides themselves encoding about amino acid 1 to about amino acid 10 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 10 to about amino acid 20 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 20 to about amino acid 30 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 30 to about amino acid 40 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 40 to about amino acid 50 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 50 to about amino acid 60 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 60 to about amino acid 70 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 70 to about amino acid 80 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 80 to about amino acid 90 of the 98P4B6 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 90 to about amino acid 100 of the 98P4B6 protein shown in Figure 2 or Figure 3, in increments of about 10 amino acids, ending at the carboxyl terminal amino acid set forth in Figure 2 or Figure 3. Accordingly, polynucleotides encoding portions of the amino acid sequence (of about 10 amino acids), of amino acids, 100 through the carboxyl terminal amino acid of the 98P4B6 protein are embodiments of the invention. Wherein it is understood that each particular amino acid position discloses that position plus or minus five amino acid residues. Polynucleotides encoding relatively long portions of a 98P4B6 protein are also within the scope of the invention. For example, polynucleotides encoding from about amino acid 1 (or 20 or 30 or 40 etc.) to about amino acid 20, (or 30, or 40 or 50 etc.) of the 98P4B6 protein "or variant" shown in Figure 2 or Figure 3 can be generated by a variety of techniques well known in the art. These polynucleotide fragments can include any portion of the 98P4B6 sequence as shown in Figure 2. Additional illustrative embodiments of the invention disclosed herein include 98P4B6 polynucleotide fragments encoding one or more of the biological motifs contained within a 98P4B6 protein 'or variant" sequence, including one or more of the motif-bearing subsequences of a 98P4B6 protein "or variant" set forth in Tables VIll-XXI and XXII-XLIX. In another embodiment, typical polynucleolide fragments of the invention encode one or more of the regions of 98P4B6 protein or variant that exhibit homology to a known molecule. In another embodiment of the invention, typical polynucleotide fragments can encode one or more of the 98P4B6 protein or variant N-glycosylation sites, cAMP and cGMP-dependent protein kinase phosphorylation sites, casein kinase II phosphorylation sites or N-myristoylation site and amidation sites. Note that to determine the starting position of any peptide set forth in Tables VIII-XXI and Tables XXII to XLIX (collectively HLA Peptide Tables) respective to its parental protein, e.g., variant 1, variant 2, etc., reference is made to three factors: the particular variant, the length of the peptide in an HLA Peptide Table, and the Search Peptides listed in Table VII. Generally, a unique Search Peptide is used to obtain HLA peptides for a particular variant The position of each Search Peptide relative to its respective parent molecule is listed in Table VII. Accordingly, if a Search Peptide begins at position "X", one must add the value "X minus 1" to each position in Tables VIII-XXI and Tables XXII-IL to obtain the actual position of 32 WO 03/087306 PCT/USO3/10462 the HLA peptides in their parental molecule. For example if a particular Search Peptide begins at position 150 of its parental molecule, one must add 150 - 1, i.e., 149 to each HLA peptide amino acid position to calculate the position of that amino acid in the parent molecule. II.A.) Uses of 98P4B6 Polynucleotides II.A.I.) Monitoring of Genetic Abnormalities The polynucleotides of the preceding paragraphs have a number of different specific uses. The human 98P4B6 gene maps to the chromosomal location set forth in the Example entitled "Chromosomal Mapping of 98P4B6." For example, because the 98P4B6 gene maps to this chromosome, polynucleotides that encode different regions of the 98P4B6 proteins are used to characterize cytogenetic abnormalities of this chromosomal locale, such as abnormalities that are identified as being associated with various cancers. In certain genes, a variety of chromosomal abnormalities including rearrangements have been identified as frequent cytogenetic abnormalities in a number of different cancers (see e.g. Krajinovic et al., Mutat. Res. 382(3-4): 81-83 (1998); Johansson et al., Blood 86(10): 3905-3914 (1995) and Finger et al., P.N.A.S. 85(23): 9158 9162 (1988)). Thus, polynucleotides encoding specific regions of the 98P4B6 proteins provide new tools that can be used to delineate, with greater precision than previously possible, cytogenetic abnormalities in the chromosomal region that encodes 98P4B6 that may contribute to the malignant phenotype. In this context, these polynucleotides satisfy a need in the art for expanding the sensitivity of chromosomal screening in order to identify more subtle and less common chromosomal abnormalities (see e.g. Evans et al., Am. J. Obstet. Gynecol 171(4): 1055-1057 (1994)). Furthermore, as 98P4B6 was shown to be highly expressed in prostate and other cancers, 98P4B6 polynucleotides are used in methods assessing the status of 98P4B6 gene products in normal versus cancerous tissues. Typically, polynucleotides that encode specific regions of the 98P4B6 proteins are used to assess the presence of perturbations (such as deletions, insertions, point mutations, or alterations resulting in a loss of an antigen etc.) in specific regions of the 98P4B6 gene, such as regions containing one or more motifs. Exemplary assays include both RT-PCR assays as well as single-strand conformation polymorphism (SSCP) analysis (see, e.g., Marrogi et al, J. Cutan. Pathol. 26(8): 369-378 (1999), both of which utilize polynucleotides encoding specific regions of a protein to examine these regions within the protein. II.A.2.) Antisense Embodiments Other specifically contemplated nucleic acid related embodiments of the invention disclosed herein are' genomic DNA, cDNAs, ribozymes, and antisense molecules, as well as nucleic acid molecules based on an altemative backbone, or including alternative bases, whether derived from natural sources or synthesized, and include molecules capable of inhibiting the RNA or protein expression of 98P4B6. For example, antisense molecules can be RNAs or other molecules, including peptide nucleic acids (PNAs) or non-nucleic acid molecules such as phosphorothioate derivatives that specifically bind DNA or RNA in a base pair-dependent manner. A skilled artisan can readily obtain these classes of nucleic acid molecules using the 98P4B6 polynucleotides and polynucleotide sequences disclosed herein. Antisense technology entails the administration of exogenous oligonucleotides that bind to a target polynucleotide located within the cells. The term "antisense" refers to the fact that such oligonucleotides are complementary to their intracellular targets, e.g., 98P4B6. See for example, Jack Cohen, Oligodeoxynucleotides, Antisense Inhibitors of Gene Expression, CRC Press, 1989; and Synthesis 1:1-5 (1988). The 98P4B6 antisense oligonucleotides of the present invention include derivatives such as S-oligonucleotides (phosphorothioate derivatives or S-oligos, see, Jack Cohen, supra), which exhibit enhanced cancer cell growth inhibitory action. S-oligos (nucleoside phosphorothioates) are isoelectronic analogs of an oligonucleotide (O-oligo) in which a nonbridging oxygen atom of the phosphate group is replaced by a sulfur atom. The S-oligos of the present invention can be prepared by treatment of the corresponding O-oligos with 3H-1,2-benzodithiol-3-one 1,1-dioxide, which is a sulfur transfer reagent. See, e.g., lyer, R. P. et at., J. Org. Chem. 55:4693-4698 (1990); and lyer, R. 33 WO 03/087306 PCT/US03/10462 P. etal., J. Am. Chem. Soc. 112:1253-1254 (1990). Additional 98P4B6 antisense oligonucleotides of the present invention include morpholino antisense oligonucleotides known in the art (see, e.g., Partridge etal., 1996, Antisense & Nucleic Acid Drug Development 6:169-175). The 98P4B6 antisense oligonucleotides of the present invention typically can be RNA or DNA that is complementary to and stably hybridizes with the first 100 5' codons or last 1003' codons of a 98P4B6 genomic sequence or the corresponding mRNA. Absolute complementarity is not required, although high degrees of complementarity are preferred. Use of an oligonucleotide complementary to this region allows for the selective hybridization to 98P4B6 mRNA and not to mRNA specifying other regulatory subunits of protein kinase. In one embodiment, 98P4B6 antisense oligonucleotides of the present invention are 15 to 30-mer fragments of the antisense DNA molecule that have a sequence that hybridizes to 98P4B6 mRNA. Optionally, 98P4B6 antisense oligonucleotide is a 30-mer oligonucleotide that is complementary to a region in the first 10 5' codons or last 10 3' codons of 98P4B6. Alternatively, the antisense molecules are modified to employ ribozymes in the inhibition of 98P4B6 expression, see, e.g., L. A. Couture & D. T. Stinchcomb; Trends Genet 12: 510-515 (1996). II.A.3.) Primers and Primer Pairs Further specific embodiments of these nucleotides of the invention include primers and primer pairs, which allow the specific amplification of polynucleotides of the invention or of any specific parts thereof, and probes that selectively or specifically hybridize to nucleic acid molecules of the invention or to any part thereof. Probes can be labeled with a detectable marker, such as, for example, a radioisotope, fluorescent compound, bioluminescent compound, a chemiluminescent compound, metal chelator or enzyme. Such probes and primers are used to detect the presence of a 98P4B6 polynucleotide in a sample and as a means for detecting a cell expressing a 98P4B6 protein. Examples of such probes include polypeptides comprising all or part of the human 98P4B6 cDNA sequence shown in Figure 2. Examples of primer pairs capable of specifically amplifying 98P4B6 mRNAs are also described in the Examples. As will be understood by the skilled artisan, a great many different primers and probes can be prepared based on the sequences provided herein and used effectively to amplify and/or detect a 98P4B6 mRNA. The 98P4B6 polynucleotides of the invention are useful for a variety of purposes, including but not limited to their use as probes and primers for the amplification and/or detection of the 98P4B6 gene(s), mRNA(s), or fragments thereof; as reagents for the diagnosis and/or prognosis of prostate cancer and other cancers; as coding sequences capable of directing the expression of 98P4B6 polypeptides; as tools for modulating or inhibiting the expression of the 98P4B6 gene(s) and/or translation of the 98P4B6 transcript(s); and as therapeutic agents. The present invention includes the use of any probe as described herein to identify and isolate a 98P4B6 or 98P4B6 related nucleic acid sequence from a naturally occurring source, such as humans or other mammals, as well as the isolated nucleic acid sequence per se, which would comprise all or most of the sequences found in the probe used. II.A.4.) Isolation of 98P4B6-Encoding Nucleic Acid Molecules The 98P4B6 cDNA sequences described herein enable the isolation of other polynucleotides encoding 98P4B6 gene product(s), as well as the isolation of polynucleotides encoding 98P4B6 gene product homologs, altematively spliced isoforms, allelic variants, and mutant forms of a 98P4B6 gene product as well as polynucleotides that encode analogs of 98P4B6-related proteins. Various molecular cloning methods that can be employed to isolate full length cDNAs encoding a 98P4B6 gene are well known (see, for example, Sambrook, J. et al., Molecular Cloning: A Laboratory Manual, 2d edition, Cold Spring Harbor Press, New York, 1989; Current Protocols in Molecular Biology. Ausubel et al., Eds., Wiley and Sons, 1995). For example, lambda phage cloning methodologies can be conveniently employed, using commercially available cloning systems (e.g., Lambda ZAP Express, Stratagene). Phage clones containing 98P4B6 gene cDNAs can be identified by probing with a labeled 98P4B6 cDNA or a fragment thereof. For example, in one embodiment, a 98P4B6 cDNA (e.g., Figure 2) or a portion thereof can be synthesized 34 WO 03/087306 PCT/USO3/10462 and used as a probe to retrieve overlapping and full-length cDNAs corresponding to a 98P4B6 gene. A 98P4B6 gene itself can be isolated by screening genomic DNA libraries, bacterial artificial chromosome libraries (BACs), yeast artificial chromosome libraries (YACs), and the like, with 98P4B6 DNA probes or primers. II.A.5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems The invention also provides recombinant DNA or RNA molecules containing a 98P4B6 polynucleotide, a fragment, analog or homologue thereof, including but not limited to phages, plasmids, phagemids, cosmids, YACs, BACs, as well as various viral and non-viral vectors well known in the art, and cells transformed or transfected with such recombinant DNA or RNA molecules. Methods for generating such molecules are well known (see, for example, Sambrook et aL, 1989, supra). The invention further provides a host-vector system comprising a recombinant DNA molecule containing a 98P4B6 polynucleotide, fragment, analog or homologue thereof within a suitable prokaryotic or eukaryotic host cell. Examples of suitable eukaryotic host cells include a yeast cell, a plant cell, or an animal cell, such as a mammalian cell or an insect cell (e.g., a baculovirus-infectible cell such as an Sf9 or HighFive cell). Examples of suitable mammalian cells include various prostate cancer cell lines such as DU145 and TsuPrl, other transfectable or transducible prostate cancer cell lines, primary cells (PrEC), as well as a number of mammalian cells routinely used for the expression of recombinant proteins (e.g., COS, CHO, 293, 293T cells). More particularly, a polynucleotide comprising the coding sequence of 98P4B6 or a fragment, analog or homolog thereof can be used to generate 98P4B6 proteins or fragments thereof using any number of host-vector systems routinely used and widely known in the art. A wide range of host-vector systems suitable for the expression of 98P4B6 proteins or fragments thereof are available, see for example, Sambrook et al, 1989, supra; Current Protocols in Molecular Biology, 1995, supra). Preferred vectors for mammalian expression include but are not limited to pcDNA 3.1 myc-His-tag (Invitrogen) and the retroviral vector pSR(xtkneo (Muller et al, 1991, MCB 11:1785). Using these expression vectors, 98P4B6 can be expressed in several prostate cancer and non-prostate cell lines, including for example 293, 293T, rat-1, NIH 3T3 and TsuPrl. The host-vector systems of the invention are useful for the production of a 98P4B6 protein or fragment thereof. Such host-vector systems can be employed to study the functional properties of 98P4B6 and 98P4B6 mutations or analogs. Recombinant human 98P4B6 protein or an analog or homolog or fragment thereof can be produced by mammalian cells transfected with a construct encoding a 98P4B6-related nucleotide. For example, 293T cells can be transfected with anr expression plasmid encoding 98P4B6 or fragment, analog or homolog thereof, a 98P4B6-related protein is expressed in the 293T cells, and the recombinant 98P4B6 protein is isolated using standard purification methods (e.g., affinity purification using anti-98P4B6 antibodies). In another embodiment, a 98P4B6 coding sequence is subcloned into the retroviral vector pSRaMSVtkneo and used to infect various mammalian cell lines, such as NIH 3T3, TsuPrl, 293 and rat-1 in order to establish 98P4B6 expressing cell lines. Various other expression systems well known in the art can also be employed. Expression constructs encoding a leader peptide joined in frame to a 98P4B6 coding sequence can be used for the generation of a secreted form of recombinant 98P4B6 protein. As discussed herein, redundancy in the genetic code permits variation in 98P4B6 gene sequences. In particular, it is known in the art that specific host species often have specific codon preferences, and thus one can adapt the disclosed sequence as preferred for a desired host. For example, preferred analog codon sequences typically have rare codons (i.e., codons having a usage frequency of less than about 20% in known sequences of the desired host) replaced with higher frequency codons. Codon preferences for a specific species are calculated, for example, by utilizing codon usage tables available on the INTERNET such as at URL dna.affrc.go.jp/-nakamura/codon.html. Additional sequence modifications are known to enhance protein expression in a cellular host. These include elimination of sequences encoding spurious polyadenylation signals, exon/intron splice site signals, transposon-like repeats, andlor other such well-characterized sequences that are deleterious to gene expression. The GC content of the sequence is 35 WO 03/087306 PCT/USO3/10462 adjusted to levels average for a given cellular host, as calculated by reference to known genes expressed in the host cell. Where possible, the sequence is modified to avoid predicted hairpin secondary mRNA structures. Other useful modifications include the addition of a translational initiation consensus sequence at the start of the open reading frame, as described in Kozak, Mol. Cell Biol, 9:5073-5080 (1989). Skilled artisans understand that the general rule that eukaryotic ribosomes initiate translation exclusively at the 5' proximal AUG codon is abrogated only under rare conditions (see, e.g., Kozak PNAS 92(7): 2662-2666, (1995) and Kozak NAR 15(20): 8125-8148 (1987)). IlL.) 98P4B6-related Proteins Another aspect of the present invention provides 98P4B6-related proteins. Specific embodiments of 98P4B6 proteins comprise a polypeptide having all or part of the amino acid sequence of human 98P4B6 as shown in Figure 2 or Figure 3. Alternatively, embodiments of 98P4B6 proteins comprise variant, homolog or analog polypeptides that have alterations in the amino acid sequence of 98P4B6 shown in Figure 2 or Figure 3. Embodiments of a 98P4B6 polypeptide include: a 98P4B6 polypeptide having a sequence shown in Figure 2, a peptide sequence of a 98P4B6 as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polypeptide having the sequence as shown in Figure 2; or, at least 10 contiguous peptides of a polypeptide having the sequence as shown in Figure 2 where T is U. For example, embodiments of 98P4B6 peptides comprise, without limitation: (I) a protein comprising, consisting essentially of, or consisting of an amino acid sequence as shown in Figure 2A-AL or Figure 3A-J; (11) a 98P4B6-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% homologous to an entire amino acid sequence shown in Figure 2A-AL; (111) a 98P4B6-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% identical to an entire amino acid sequence shown in Figure 2A-AL or 3A-J; (IV) a protein that comprises at least one peptide set forth in Tables VIll to XLIX, optionally with a proviso that it is not an entire protein of Figure 2; (V) a protein that comprises at least one peptide set forth in Tables VIII-XXI, collectively, which peptide is also set forth in Tables XXII to XLIX, collectively, optionally with a proviso that it is not an entire protein of Figure 2; (VI) a protein that comprises at least two peptides selected from the peptides set forth in Tables VIII-XLIX, optionally with a proviso that it is not an entire protein of Figure 2; (VII) a protein that comprises at least two peptides selected from the peptides set forth in Tables VIIIl to XLIX collectively, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; (VIII) a protein that comprises at least one peptide selected from the peptides set forth in Tables VIII-XXI, and at least one peptide selected from the peptides set forth in Tables XXII to XLIX, with a proviso that the protein is not a contiguous sequence from an amino acid sequence of Figure 2; (IX) a polypeptide comprising at least 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that 36 WO 03/087306 PCT/USO3/10462 includes at least 1, 2,3,4,5,6,7,8,9,10,11,12,13,14,15,16,17,18,19,20,21,22,23, 24,25,26,27,28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Hydrophilicity profile of Figure 5; (X) a polypeptide comprising at least 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9,10,11, 12,13,14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; (XI) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having-a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; (XII) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acids of a protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17,18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XIII) a polypeptide comprising at least 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, amino acids of a protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, 3G, 3H, 31 or 3J in any whole number increment up to 454, 45, 419, 490, 576, 490, 454, 454, 576, or 490 respectively that includes at least at least 1, 2, 3, 4, 5, 6, 7, 8, 9,10,11, 12,13, 14,15,16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino acid position(s) having a value greater than 0.5 in the Beta-turn profile of Figure 9; (XIV) a peptide that occurs at least twice in Tables VIII-XXI and XXII to XLIX, collectively; (XV) a peptide that occurs at least three times in Tables VIll-XXI and XXII to XLIX, collectively; (XVI) a peptide that occurs at least four times in Tables VIII-XXI and XXII to XLIX, collectively; (XVII) a peptide that occurs at least five times in Tables VIII-XXI and XXII to XLIX, collectively; (XVIII) a peptide that occurs at least once in Tables VIII-XXI, and at least once in tables XXII to XLIX; (XIX) a peptide that occurs at least once in Tables VIII-XXI, and at least twice in tables XXII to XLIX; (XX) a peptide that occurs at least twice in Tables VIII-XXI, and at least once in tables XXII to XLIX; (XXI) a peptide that occurs at least twice in Tables VIII-XXI, and at least twice in tables XXII to XLIX; (XXII) a peptide which comprises one two, three, four, or five of the following characteristics, or an oligonucleotide encoding such peptide: 37 WO 03/087306 PCT/USO3/10462 i) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Hydrophilicity profile of Figure 5; ii) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or less than 0.5, 0.4, 0.3, 0.2, 0.1, or having a value equal to 0.0, in the Hydropathicity profile of Figure 6; iii) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Percent Accessible Residues profile of Figure 7; iv) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Average Flexibility profile of Figure 8; or, v) a region of at least 5 amino acids of a particular peptide of Figure 3, in any whole number increment up to the full length of that protein in Figure 3, that includes an amino acid position having a value equal to or greater than 0.5, 0.6, 0.7, 0.8, 0.9, or having a value equal to 1.0, in the Beta-turn profile of Figure 9; (XXIII) a composition comprising a peptide of (I)-(XXII) or an antibody or binding region thereof together with a pharmaceutical excipient and/or in a human unit dose form. (XXIV) a method of using a peptide of (I)-(XXII), or an antibody or binding region thereof or a composition of (XXIII) in a method to modulate a cell expressing 98P4B6, (XXV) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition of (XXIII) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6 (XXVI) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition (XXIII) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cell expressing 98P4B6, said cell from a cancer of a tissue listed in Table I; (XXVII) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition of (XXIII) in a method to diagnose, prophylax, prognose, or treat a a cancer; (XXVIII) a method of using a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition of (XXIII) in a method to diagnose, prophylax, prognose, or treat a a cancer of a tissue listed in Table I; and, (XXIX) a method of using a a peptide of (I)-(XXII) or an antibody or binding region thereof or a composition (XXIII) in a method to identify or characterize a modulator of a cell expressing 98P4B6. As used herein, a range is understood to specifically disclose all whole unit positions thereof. Typical embodiments of the invention disclosed herein include 98P4B6 polynucleotides that encode specific portions of 98P4B6 mRNA sequences (and those which are complementary to such sequences) such as those that encode the proteins and/or fragments thereof, for example: (a) 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 38 WO 03/087306 PCT/USO3/10462 225, 250, 275, 300, 325, 350, 375, 400, 410, 420, 430, 440, 450, or 454 more contiguous amino acids of 98P4B6 variant 1; the maximal lengths relevant for other variants are: variant 52, 45 amino acids; variant 5, 419 amino acids, variant 6, 490, variant 7, 576 amino acids, variant 8, 490 amino acids, variant 13, 454, variant 14, 454 amino acids, variant 21, 576 amino acids, and variant 25, 490 amino acids.. In general, naturally occurring allelic variants of human 98P4B6 share a high degree of structural identity and homology (e.g., 90% or more homology). Typically, allelic variants of a 98P4B6 protein contain conservative amino acid substitutions within the 98P4B6 sequences described herein or contain a substitution of an amino acid from a corresponding position in a homologue of 98P4B6. One class of 98P4B6 allelic variants are proteins that share a high degree of homology with at least a small region of a particular 98P4B6 amino acid sequence, but further contain a radical departure from the sequence, such as a non-conservative substitution, truncation, insertion or frame shift. In comparisons of protein sequences, the terms, similarity, identity, and homology each have a distinct meaning as appreciated in the field of genetics. Moreover, orthology and paralogy can be important concepts describing the relationship of members of a given protein family in one organism to the members of the same family in other organisms. Amino acid abbreviations are provided in Table II. Conservative amino acid substitutions can frequently be made in a protein without altering either the conformation or the function of the protein. Proteins of the invention can comprise 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 conservative substitutions. Such changes include substituting any of isoleucine (I), valine (V), and leucine (L) for any other of these hydrophobic amino acids; aspartic acid (D) for glutamic acid (E) and vice versa; glutamine (Q) for asparagine (N) and vice versa; and seine (S) for threonine (T) and vice versa. Other substitutions can also be considered conservative, depending on the environment of the particular amino acid and its role in the three dimensional structure of the protein. For example, glycine (G) and alanine (A) can frequently be interchangeable, as can alanine (A) and valine (V). Methionine (M), which is relatively hydrophobic, can frequently be interchanged with leucine and isoleucine, and sometimes with valine. Lysine (K) and arginine (R) are frequently interchangeable in locations in which the significant feature of the amino acid residue is its charge and the differing pK's of these two amino acid residues are not significant. Still other changes can be considered "conservative" in particular environments (see, e.g. Table Ill herein; pages 13-15 "Biochemistry" 2nd ED. Lubert Stryer ed (Stanford University); Henikoff et al., PNAS 1992 Vol 89 10915-10919; Lei et al., J Biol Chem 1995 May 19; 270(20):11882-6). Embodiments of the invention disclosed herein include a wide variety of art-accepted variants or analogs of 98P4B6 proteins such as polypeptides having amino acid insertions, deletions and substitutions. 98P4B6 variants can be made using methods known in the art such as site-directed mutagenesis, alanine scanning, and PCR mutagenesis. Site directed mutagenesis (Carter et al., Nucl. Acids Res., 13:4331 (1986); Zoller et aL, Nucl. Acids Res., 10:6487 (1987)), cassette mutagenesis (Wells et al., Gene, 34:315 (1985)), restriction selection mutagenesis (Wells et al., Philos. Trans. R. Soc. London SerA, 317:415 (1986)) or other known techniques can be performed on the cloned DNA to produce the 98P4B6 variant DNA. Scanning amino acid analysis can also be employed to identify one or more amino acids along a contiguous sequence that is involved in a specific biological activity such as a protein-protein interaction. Among the preferred scanning amino acids are relatively small, neutral amino acids. Such amino acids include alanine, glycine, serine, and cysteine. Alanine is typically a preferred scanning amino acid among this group because it eliminates the side-chain beyond the beta carbon and is less likely to alter the main-chain conformation of the variant. Alanine is also typically preferred because it is the most common amino acid. Further, it is frequently found in both buried and exposed positions (Creighton, The Proteins, (W.H. Freeman & Co., N.Y.); Chothia, J. Mol. Biol., 150:1 (1976)). If alanine substitution does not yield adequate amounts of variant, an isosteric amino acid can be used. 39 WO 03/087306 PCT/USO3/10462 As defined herein, 98P4B6 variants, analogs or homologs, have the distinguishing attribute of having at least one epitope that is "cross reactive" with a 98P4B6 protein having an amino acid sequence of Figure 3. As used in this sentence, "cross reactive" means that an antibody or T cell that specifically binds to a 98P4B6 variant also specifically binds to a 98P4B6 protein having an amino acid sequence set forth in Figure 3. A polypeptide ceases to be a variant of a protein shown in Figure 3, when it no longer contains any epitope capable of being recognized by an antibody or T cell that specifically binds to the starting 98P4B6 protein. Those skilled in the art understand that antibodies that recognize proteins bind to epitopes of varying size, and a grouping of the order of about four or five amino acids, contiguous or not, is regarded as a typical number of amino acids in a minimal epitope. See, e.g., Nair et al., J. Immunol 2000 165(12): 6949-6955; Hebbes et al., Mol Immunol (1989) 26(9):865-73; Schwartz et aL, J Immunol (1985) 135(4):2598-608. Other classes of 98P4B6-related protein variants share 70%, 75%, 80%, 85% or 90% or more similarity with an amino acid sequence of Figure 3, or a fragment thereof. Another specific class of 98P4B6 protein variants or analogs comprises one or more of the 98P4B6 biological motifs described herein or presently known in the art. Thus, encompassed by the present invention are analogs of 98P4B6 fragments (nucleic or amino acid) that have altered functional (e.g. immunogenic) properties relative to the starting fragment. It is to be appreciated that motifs now or which become part of the art are to be applied to the nucleic or amino acid sequences of Figure 2 or Figure 3. As discussed herein, embodiments of the claimed invention include polypeptides containing less than the full amino acid sequence of a 98P4B6 protein shown in Figure 2 or Figure 3. For example, representative embodiments of the invention comprise peptides/proteins having any 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15 or more contiguous amino acids of a 98P4B6 protein shown in Figure 2 or Figure 3. Moreover, representative embodiments of the invention disclosed herein include polypeptides consisting of about amino acid 1 to about amino acid 10 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 10 to about amino acid 20 ofa 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 20 to about amino acid 30 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 30 to about amino acid 40 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 40 to about amino acid 50 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 50 to about amino acid 60 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 60 to about amino acid 70 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 70 to about amino acid 80 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 80 to about amino acid 90 of a 98P4B6 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 90 to about amino acid 100 of a 98P4B6 protein shown in Figure 2 or Figure 3, etc. throughout the entirety of a 98P4B6 amino acid sequence. Moreover, polypeptides consisting of about amino acid 1 (or 20 or 30 or 40 etc.) to about amino acid 20, (or 130, or 140 or 150 etc.) of a 98P4B6 protein shown in Figure 2 or Figure 3 are embodiments of the invention. It is to be appreciated that the starting and stopping positions in this paragraph refer to the specified position as well as that position plus or minus 5 residues. 98P4B6-related proteins are generated using standard peptide synthesis technology or using chemical cleavage methods well known in the art. Alternatively, recombinant methods can be used to generate nucleic acid molecules that encode a 98P4B6-related protein. In one embodiment, nucleic acid molecules provide a means to generate defined fragments of a 98P4B6 protein (or variants, homologs or analogs thereof). III.A.) Motif-bearing Protein Embodiments Additional illustrative embodiments of the invention disclosed herein include 98P4B6 polypeptides comprising the amino acid residues of one or more of the biological motifs contained within a 98P4B6 polypeptide sequence set forth in Figure 2 or Figure 3. Various motifs are known in the art, and a protein can be evaluated for the presence of such motifs by 40 WO 03/087306 PCT/US03/10462 a number of publicly available Internet sites (see, e.g., URL addresses: pfam.wustl.edu/; searchlauncher.bcm.tmc.edu/seq search/struc-predict.html; psort.ims.u-tokyo.ac.jpf; cbs.dtu.dk/; ebi.ac.uk/interpro/scan.html; expasy.ch/tools/scnpsitl.html; Epimatrix m and Epimer T m , Brown University, brown.edulResearchfTB-HIVLablepimatixlepimatrix.html; and BIMAS, bimas.dcrt.nih.gov/.). Motif bearing subsequences of all 98P4B6 variant proteins are set forth and identified in Tables VIII-XXI and XXII XLIX. Table V sets forth several frequently occurring motifs based on pfamsearches (see URL address pfam.wustl.edul). The columns of Table V list (1) motif name abbreviation, (2) percent identity found amongst the different member of the motif family, (3) motif name or description and (4) most common function; location information is included if the motif is relevant for location. Polypeptides comprising one or more of the 98P4B6 motifs discussed above are useful in elucidating the specific characteristics of a malignant phenotype in view of the observation that the 98P4B6 motifs discussed above are associated with growth dysregulation and because 98P486 is overexpressed in certain cancers (See, e.g., Table I). Casein kinase 11, cAMP and camp-dependent protein kinase, and Protein Kinase C, for example, are enzymes known to be associated with the development of the malignant phenotype (see e.g. Chen eta!., Lab Invest., 78(2): 165-174 (1998); Gaiddon et al., Endocrinology 136(10): 4331-4338 (1995); Hall et al, Nucleic Acids Research 24(6): 1119-1126 (1996); Peterziel eta., Oncogene 18(46): 6322-6329 (1999) and O'Brian, Oncol. Rep. 5(2): 305-309 (1998)). Moreover, both glycosylation and myristoylation are protein modifications also associated with cancer and cancer progression (see e.g. Dennis et al., Biochem. Biophys. Acta 1473(1):21-34 (1999); Raju et al., Exp. Cell Res. 235(1): 145-154 (1997)). Amidation is another protein modification also associated with cancer and cancer progression (see e.g. Treston et al., J. Natl. Cancer Inst. Monogr. (13): 169-175 (1992)). In another embodiment, proteins of the invention comprise one or more of the immunoreactive epitopes identified in accordance with art-accepted methods, such as the peptides set forth in Tables VIII-XXI and XXII-XLIX. CTL epitopes can be determined using specific algorithms to identify peptides within a 98P4B6 protein that are capable of optimally binding to specified HLA alleles (e.g., Table IV; Epimatrix m and Epimer m , Brown University, URL brown.edu/ResearchfTB HIVLab/epimatrix/epimatrix.html; and BIMAS, URL bimas.dcrt.nih.gov/.) Moreover, processes for identifying peptides that have sufficient binding affinity for HLA molecules and which are correlated with being immunogenic epitopes, are well known in the art, and are carried out without undue experimentation. In addition, processes for identifying peptides that are immunogenic epitopes, are well known in the art, and are carried out without undue experimentation either in vitro or in vivo. Also known in the art are principles for creating analogs of such epitopes in order to modulate immunogenicity. For example, one begins with an epitope that bears a CTL or HTL motif (see, e.g., the HLA Class I and HLA Class II motifs/supermotifs of Table IV). The epitope is analoged by substituting out an amino acid at one of the specified positions, and replacing it with another amino acid specified for that position. For example, on the basis of residues defined in Table IV, one can substitute out a deleterious residue in favor of any other residue, such as a preferred residue; substitute a less preferred residue with a preferred residue; or substitute an originally-occurring preferred residue with another preferred residue. Substitutions can occur at primary anchor positions or at other positions in a peptide; see, e.g., Table IV. A variety of references reflect the art regarding the identification and generation of epitopes in a protein of interest as well as analogs thereof. See, for example, WO 97/33602 to Chesnut et al.; Sette, Immunogenetics 1999 50(3-4): 201 212; Sette et al, J. Immunol. 2001 166(2): 1389-1397; Sidney et al., Hum. Immunol. 1997 58(1): 12-20; Kondo et al., Immunogenetics 1997 45(4): 249-258; Sidney et al., J. Immunol. 1996 157(8): 3480-90; and Falk et al., Nature 351: 290-6 (1991); Hunt et al., Science 255:1261-3 (1992); Parker et al., J. Immunol. 149:3580-7 (1992); Parker etal., J. Immunol. 152:163-75 (1994)); Kast at al., 1994 152(8): 3904-12; Borras-Cuesta et al., Hum. Immunol. 2000 61(3): 266-278; Alexander 41 WO 03/087306 PCT/US03/10462 et al., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander et al., PMID: 7895164, UI: 95202582; O'Sullivan et at., J. Immunol. 1991 147(8): 2663-2669; Alexander et al., Immunity 1994 1(9): 751-761 and Alexander et al., Immunol. Res. 1998 18(2): 79-92. Related embodiments of the invention include polypeptides comprising combinations of the different motifs set forth in Table VI, and/or, one or more of the predicted CTL epitopes of Tables VIII-XXI and XXII-XLIX, and/or, one or more of the predicted HTL epitopes of Tables XLVI-XLIX, and/or, one or more of the T cell binding motifs known in the art. Preferred embodiments contain no insertions, deletions or substitutions either within the motifs or within the intervening sequences of the polypeptides. In addition, embodiments which include a number of either N-terminal andlor C-terminal amino acid residues on either side of these motifs may be desirable (to, for example, include a greater portion of the polypeptide architecture in which the motif is located). Typically, the number of N-terminal and/or C-terminal amino acid residues on either side of a motif is between about 1 to about 100 amino acid residues, preferably 5 to about 50 amino acid residues. 98P4B6-related proteins are embodied in many forms, preferably in isolated form. A purified 98P4B6 protein molecule will be substantially free of other proteins or molecules that impair the binding of 98P4B6 to antibody, T cell or other ligand. The nature and degree of isolation and purification will depend on the intended use. Embodiments of a 98P4B6-related proteins include purified 98P4136-related proteins and functional, soluble 98P4B6-related proteins. In one embodiment, a functional, soluble 98P4B6 protein or fragment thereof retains the ability to be bound by antibody, T cell or other ligand. The invention also provides 98P4B6 proteins comprising biologically active fragments of a 98P4B6 amino acid sequence shown in Figure 2 or Figure 3. Such proteins exhibit properties of the starting 98P4B6 protein, such as the ability to elicit the generation of antibodies that specifically bind an epitope associated with the starting 98P4B6 protein; to be bound by such antibodies; to elicit the activation of HTL or CTL; and/or, to be recognized by HTL or CTL that also specifically bind to the starting protein. 98P4B6-related polypeptides that contain particularly interesting structures can be predicted and/or identified using various analytical techniques well known in the art, including, for example, the methods of Chou-Fasman, Gamier-Robson, Kyte Doolittle, Eisenberg, Karplus-Schultz or Jameson-Wolf analysis, or based on immunogenicity. Fragments that contain such structures are particularly useful in generating subunit-specific anti-98P4B6 antibodies or T cells or in identifying cellular factors that bind to 98P4B6. For example, hydrophilicity profiles can be generated, and immunogenic peptide fragments identified, using the method of Hopp, T.P. and Woods, K.R., 1981, Proc. Natl. Acad. Sci. U.S.A. 78:3824-3828. Hydropathicity profiles can be generated, and immunogenic peptide fragments identified, using the method of Kyte, J. and Doolittle, R.F., 1982, J. Mol. Biol. 157:105-132. Percent (%) Accessible Residues profiles can be generated, and immunogenic peptide fragments identified, using the method of Janin J., 1979, Nature 277:491-492. Average Flexibility profiles can be generated, and immunogenic peptide fragments identified, using the method of Bhaskaran R., Ponnuswamy P.K., 1988, Int. J. Pept. Protein Res. 32:242-255. Beta-turn profiles can be generated, and immunogenic peptide fragments identified, using the method of Deleage, G., Roux B., 1987, Protein Engineering 1:289-294. CTL epitopes can be determined using specific algorithms to identify peptides within a 98P4B6 protein that are capable of optimally binding to specified HLA alleles (e.g., by using the SYFPEITHI site at World Wide Web URL syfpeithi.bmi heidelberg.com/; the listings in Table IV(A)-(E); Epimatrix T M and Epimer T M , Brown University, URL (brown.edulResearch/TB HIV.Lab/epimatrixepimatrix.htm); and BIMAS, URL bimas.dcrt.nih.gov). Illustrating this, peptide epitopes from 98P4B6 that are presented in the context of human MHC Class I molecules, e.g., HLA-A1, A2, A3, All, A24, B7 and 835 were predicted (see, e.g., Tables VIll-XXI, XXII-XLIX). Specifically, the complete amino acid sequence of the 98P4B6 protein and relevant portions of other variants, i.e., for HLA Class I predictions 9 flanking residues on either side of a point mutation or exon juction, and for HLA Class II predictions 14 flanking residues on either side of a point mutation or exon junction corresponding to that variant, were entered into the HLA Peptide Motif Search algorithm found in the Bioinformatics and 42 WO 03/087306 PCT/USO3/10462 Molecular Analysis Section (BIMAS) web site listed above; in addition to the site SYFPEITHI, at URL syfpeithi.bmi heidelberg.com/. The HLA peptide motif search algorithm was developed by Dr. Ken Parker based on binding of specific peptide sequences in the groove of HLA Class I molecules, in particular HLA-A2 (see, e.g., Falk et al., Nature 351:290-6 (1991); Hunt et al., Science 255:1261-3 (1992); Parker et al., J. Immunol. 149:3580-7 (1992); Parker et al., J. Immunol. 152:163-75 (1994)). This algorithm allows location and ranking of 8-mer, 9-mer, and 10-mer peptides from a complete protein sequence for predicted binding to HLA-A2 as well as numerous other HLA Class I molecules. Many HLA class I binding peptides are 8 ,9-, 10 or 11-mers. For example, for Class I HLA-A2, the epitopes preferably contain a leucine (L) or methionine (M) at position 2 and a valine (V) or leucine (L) at the C-terminus (see, e.g., Parker etal., J. Immunol. 149:3580-7 (1992)). Selected results of 98P486 predicted binding peptides are shown in Tables VIII-XXI and XXII-XLIX herein. In Tables VIII-XXI and XXII-XLVII, selected candidates, 9-mers and 10-mers, for each family member are shown along with their location, the amino acid sequence of each specific peptide, and an estimated binding score. In Tables XLVI-XLIX, selected candidates, 15 mers, for each family member are shown along with their location, the amino acid sequence of each specific peptide, and an estimated binding score. The binding score corresponds to the estimated half time of dissociation of complexes containing the peptide at 37oC at pH 6.5. Peptides with the highest binding score are predicted to be the most tightly bound to HLA Class I on the cell surface for the greatest period of time and thus represent the best immunogenic targets for T-cell recognition. Actual binding of peptides to an HLA allele can be evaluated by stabilization of HLA expression on the antigen processing defective cell line T2 (see, e.g., Xue et aL., Prostate 30:73-8 (1997) and Peshwa et al, Prostate 36:129-38 (1998)). Immunogenicity of specific peptides can be evaluated in vitro by stimulation of CD8+ cytotoxic T lymphocytes (CTL) in the presence of antigen presenting cells such as dendritic cells. It is to be appreciated that every epitope predicted by the BIMAS site, Epimer T M and Epimatrix T M sites, or specified by the HLA class I or class II motifs available in the art or which become part of the art such as set forth in Table IV (or determined using World Wide Web site URL syfpeithi.bmi-heidelberg.com/, or BIMAS, bimas.dcrt.nih.gov) are to be "applied" to a 98P4B6 protein in accordance with the invention. As used in this context "applied" means that a 98P4B6 protein is evaluated, e.g., visually or by computer-based patterns finding methods, as appreciated by those of skill in the relevant art. Every subsequence of a 98P4B6 protein of 8, 9, 10, or 11 amino acid residues that bears an HLA Class I motif, or a subsequence of 9 or more amino acid residues that bear an HLA Class 11 motif are within the scope of the invention. III.B.) Expression of 98P4B6-related Proteins In an embodiment described in the examples that follow, 98P4B6 can be conveniently expressed in cells (such as 293T cells) transfected with a commercially available expression vector such as a CMV-driven expression vector encoding 98P486 with a C-terminal 6XHis and MYC tag (pcDNA3.1/mycHIS, Invitrogen or Tag5, GenHunter Corporation, Nashville TN). The Tag5 vector provides an IgGK secretion signal that can be used to facilitate the production of a secreted 98P4B6 protein in transfected cells. The secreted HIS-tagged 98P4B6 in the culture media can be purified, e.g., using a nickel column using standard techniques. Ill.C.) Modifications of 98P4B6-related Proteins Modifications of 98P4B6-related proteins such as covalent modifications are included within the scope of this invention. One type of covalent modification includes reacting targeted amino acid residues of a 98P4B6 polypeptide with an organic derivatizing agent that is capable of reacting with selected side chains or the N- or C- terminal residues of a 98P4B6 protein. Another type of covalent modification of a 98P4B6 polypeptide included within the scope of this invention comprises 43 WO 03/087306 PCT/USO3/10462 altering the native glycosylation pattern of a protein of the invention. Another type of covalent modification of 98P4B6 comprises linking a 98P4B6 polypeptide to one of a variety of nonproteinaceous polymers, e.g., polyethylene glycol (PEG), polypropylene glycol, or polyoxyalkylenes, in the manner set forth in U.S. Patent Nos. 4,640,835; 4,496,689; 4,301,144; 4,670,417; 4,791,192 or 4,179,337. The 98P4B6-related proteins of the present invention can also be modified to form a chimeric molecule comprising 98P4B6 fused to another, heterologous polypeptide or amino acid sequence. Such a chimeric molecule can be synthesized chemically or recombinantly. A chimeric molecule can have a protein of the invention fused to another tumor-associated antigen or fragment thereof. Alternatively, a protein in accordance with the invention can comprise a fusion of fragments of a 98P4B6 sequence (amino or nucleic acid) such that a molecule is created that is not, through its length, directly homologous to the amino or nucleic acid sequences shown in Figure 2 or Figure 3. Such a chimeric molecule can comprise multiples of the same subsequence of 98P4B6. A chimeric molecule can comprise a fusion of a 98P486-related protein with a polyhistidine epitope tag, which provides an epitope to which immobilized nickel can selectively bind, with cytokines or with growth factors. The epitope tag is generally placed at the amino- or carboxyl- terminus of a 98P4B6 protein. In an alternative embodiment, the chimeric molecule can comprise a fusion of a 98P4B6-related protein with an immunoglobulin or a particular region of an immunoglobulin. For a bivalent form of the chimeric molecule (also referred to as an "immunoadhesin"), such a fusion could be to the Fc region of an IgG molecule. The Ig fusions preferably include the substitution of a soluble (transmembrane domain deleted or inactivated) form of a 98P4B6 polypeptide in place of at least one variable region within an Ig molecule. In a preferred embodiment, the immunoglobulin fusion includes the hinge, CH2 and CH3, or the hinge, CHI, CH2 and CH3 regions of an IgGI molecule. For the production of immunoglobulin fusions see, e.g., U.S. Patent No. 5,428,130 issued June 27, 1995. III.D.) Uses of 98P4B6-related Proteins The proteins of the invention have a number of different specific uses. As 98P4B6 is highly expressed in prostate and other cancers, 98P4B6-related proteins are used in methods that assess the status of 98P4B6 gene products in normal versus cancerous tissues, thereby elucidating the malignant phenotype. Typically, polypeptides from specific regions of a 98P4B6 protein are used to assess the presence of perturbations (such as deletions, insertions, point mutations etc.) in those regions (such as regions containing one or more motifs). Exemplary assays utilize antibodies or T cells targeting 98P4B6-related proteins comprising the amino acid residues of one or more of the biological motifs contained within a 98P4B6 polypeptide sequence in order to evaluate the characteristics of this region in normal versus cancerous tissues or to elicit an immune response to the epitope. Alternatively, 98P4B6-related proteins that contain the amino acid residues of one or more of the biological motifs in a 98P4B6 protein are used to screen for factors that interact with that region of 98P4B6. 98P4B6 protein fragments/subsequences are particularly useful in generating and characterizing domain-specific antibodies (e.g., antibodies recognizing an extracellular or intracellular epitope of a 98P4B6 protein), for identifying agents or cellular factors that bind to 98P4B6 or a particular structural domain thereof, and in various therapeutic and diagnostic contexts, including but not limited to diagnostic assays, cancer vaccines and methods of preparing such vaccines. Proteins encoded by the 98P4B6 genes, or by analogs, homologs or fragments thereof, have a variety of uses, including but not limited to generating antibodies and in methods for identifying ligands and other agents and cellular constituents that bind to a 98P4B6 gene product Antibodies raised against a 98P4B6 protein or fragment thereof are useful in diagnostic and prognostic assays, and imaging methodologies in the management of human cancers characterized by expression of 98P486 protein, such as those listed in Table I. Such antibodies can be expressed intracellularly and used in methods of treating patients with such cancers. 98P4B6-related nucleic acids or proteins are also used in generating HTL or CTL responses. 44 WO 03/087306 PCT/US03/10462 Various immunological assays useful for the detection of 98P4B6 proteins are used, including but not limited to various types of radioimmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme-linked immunofluorescent assays (ELIFA), immunocytochemical methods, and the like. Antibodies can be labeled and used as immunological imaging reagents capable of detecting 98P4B6-expressing cells (e.g., in radioscintigraphic imaging methods). 98P4B6 proteins are also particularly useful in generating cancer vaccines, as further described herein. IV.) 98P4B6 Antibodies Another aspect of the invention provides antibodies that bind to 98P4B6-related proteins. Preferred antibodies specifically bind to a 98P4B6-related protein and do not bind (or bind weakly) to peptides or proteins that are not 98P4B6-related proteins under physiological conditions. In this context, examples of physiological conditions include: 1) phosphate buffered saline; 2) Tris-buffered saline containing 25mM Tris and 150 mM NaCI; or normal saline (0.9% NaCI); 4) animal serum such as human serum; or, 5) a combination of any of 1) through 4); these reactions preferably taking place at pH 7.5, alternatively in a range of pH 7.0 to 8.0, or alternatively in a range of pH 6.5 to 8.5; also, these reactions taking place at a temperature between 40C to 37 0 C. For example, antibodies that bind 98P4B6 can bind 98P4B6-related proteins such as the homologs or analogs thereof 98P4B6 antibodies of the invention are particularly useful in cancer (see, e.g., Table I) diagnostic and prognostic assays, and imaging methodologies. Similarly, such antibodies are useful in the treatment, diagnosis, and/or prognosis of other cancers, to the extent 98P4B6 is also expressed or overexpressed in these other cancers. Moreover, intracellularly expressed antibodies (e.g., single chain antibodies) are therapeutically useful in treating cancers in which the expression of 98P4B6 is involved, such as advanced or metastatic prostate cancers. The invention also provides various immunological assays useful for the detection and quantification of 98P4B6 and mutant 98P4B6-related proteins. Such assays can comprise one or more 98P4B6 antibodies capable of recognizing and binding a 98P4B6-related protein, as appropriate. These assays are performed within various immunological assay formats well known in the art, including but not limited to various types of radioimmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme linked immunofluorescent assays (ELIFA), and the like. Immunological non-antibody assays of the invention also comprise T cell immunogenicity assays (inhibitory or stimulatory) as well as major histocompatibility complex (MHC) binding assays. In addition, immunological imaging methods capable of detecting prostate cancer and other cancers expressing 98P4B6 are also provided by the invention, including but not limited to radioscintigraphic imaging methods using labeled 98P4B6 antibodies. Such assays are clinically useful in the detection, monitoring, and prognosis of 98P4B6 expressing cancers such as prostate cancer. 98P4B6 antibodies are also used in methods for purifying a 98P4B6-related protein and for isolating 98P4B6 homologues and related molecules. For example, a method of purifying a 98P4B6-related protein comprises incubating a 98P4B6 antibody, which has been coupled to a solid matrix, with a lysate or other solution containing a 98P4B6-related protein under conditions that permit the 98P4B6 antibody to bind to the 98P4B6-related protein; washing the solid matrix to eliminate impurities; and eluting the 98P4B6-related protein from the coupled antibody. Other uses of 98P4B6 antibodies in accordance with the invention include generating anti-idiotypic antibodies that mimic a 98P4B6 protein. Various methods for the preparation of antibodies are well known in the art. For example, antibodies can be prepared by immunizing a suitable mammalian host using a 98P4B6-related protein, peptide, or fragment, in isolated or immunoconjugated form (Antibodies: A Laboratory Manual, CSH Press, Eds., Harlow, and Lane (1988); Harlow, Antibodies, Cold Spring Harbor Press, NY (1989)). In addition, fusion proteins of 98P4B6 can also be used, such as a 98P4B6 GST-fusion protein. In a particular embodiment a GST fusion protein comprising all or most of the amino acid sequence of Figure 2 or Figure 3 is produced, then 45 WO 03/087306 PCT/US03/10462 used as an immunogen to generate appropriate antibodies. In another embodiment, a 98P4B6-related protein is synthesized and used as an immunogen. In addition, naked DNA immunization techniques known in the art are used (with or without purified 98P4B6-related protein or 98P4B6 expressing cells) to generate an immune response to the encoded immunogen (for review, see Donnelly et aL., 1997, Ann. Rev. Immunol. 15: 617-648). The amino acid sequence of a 98P4B6 protein as shown in Figure 2 or Figure 3 can be analyzed to select specific regions of the 98P4B6 protein for generating antibodies. For example, hydrophobicity and hydrophilicity analyses of a 98P4B6 amino acid sequence are used to identify hydrophilic regions in the 98P4B6 structure. Regions of a 98P4B6 protein that show immunogenic structure, as well as other regions and domains, can readily be identified using various other methods known in the art, such as Chou-Fasman, Gamier-Robson, Kyte-Doolittle, Eisenberg, Karplus-Schultz or Jameson-Wolfanalysis. Hydrophilicity profiles can be generated using the method of Hopp, T.P. and Woods, K.R., 1981, Proc. Natl. Acad. Sci. U.S.A. 78:3824 3828. Hydropathicity profiles can be generated using the method of Kyte, J. and Doolittle, R.F., 1982, J. Mol. Biol. 157:105 132. Percent (%) Accessible Residues profiles can be generated using the method of Janin J., 1979, Nature 277:491-492. Average Flexibility profiles can be generated using the method of Bhaskaran R., Ponnuswamy P.K., 1988, Int. J. Pept. Protein Res. 32:242-255. Beta-turn profiles can be generated using the method of Deleage, G., Roux B., 1987, Protein Engineering 1:289-294. Thus, each region identified by any of these programs or methods is within the scope of the present invention. Methods for the generation of 98P4B6 antibodies are further illustrated by way of the examples provided herein. Methods for preparing a protein or polypeptide for use as an immunogen are well known in the art. Also well known in the art are methods for preparing immunogenic conjugates of a protein with a carrier, such as BSA, KLH or other carrier protein. In some circumstances, direct conjugation using, for example, carbodiimide reagents are used; in other instances linking reagents such as those supplied by Pierce Chemical Co., Rockford, IL, are effective. Administration of a 98P4B6 immunogen is often conducted by injection over a suitable time period and with use of a suitable adjuvant, as is understood in the art. During the immunization schedule, titers of antibodies can be taken to determine adequacy of antibody formation. 98P4B6 monoclonal antibodies can be produced by various means well known in the art. For example, immortalized cell lines that secrete a desired monoclonal antibody are prepared using the standard hybridoma technology of Kohler and Milstein or modifications that immortalize antibody-producing B cells, as is generally known. Immortalized cell lines that secrete the desired antibodies are screened by immunoassay in which the antigen is a 98P4B6-related protein. When the appropriate immortalized cell culture is identified, the cells can be expanded and antibodies produced either from in vitro cultures or from ascites fluid. The antibodies or fragments of the invention can also be produced, by recombinant means. Regions that bind specifically to the desired regions of a 98P4B6 protein can also be produced in the context of chimeric or complementarity determining region (CDR) grafted antibodies of multiple species origin. Humanized or human 98P4B6 antibodies can also be produced, and are preferred for use in therapeutic contexts. Methods for humanizing murine and other non-human antibodies, by substituting one or more of the non-human antibody CDRs for corresponding human antibody sequences, are well known (see for example, Jones et aL., 1986, Nature 321: 522-525; Riechmann et al., 1988, Nature 332: 323-327; Verhoeyen et al, 1988, Science 239: 1534-1536). See also, Carter et al, 1993, Proc. Natl. Acad. Sci. USA 89:4285 and Sims etal., 1993, J. Immunol. 151: 2296. Methods for producing fully human monoclonal antibodies include phage display and transgenic methods (for review, see Vaughan et al., 1998, Nature Biolechnology 16: 535-539). Fully human 98P4B6 monoclonal antibodies can be generated using cloning technologies employing large human Ig gene combinatorial libraries (i.e., phage display) (Griffiths and Hoogenboom, Building an in vitro immune system: human antibodies from phage display libraries. In: Protein Engineering of Antibody Molecules for Prophylactic and Therapeutic Applications in Man, Clark, M. (Ed.), Nottingham Academic, pp 45-64 (1993); Burton and Barbas, Human Antibodies from combinatorial libraries. Id., pp 65-82). Fully human 98P4B6 monoclonal antibodies can also be produced 46 WO 03/087306 PCT/USO3/10462 using transgenic mice engineered to contain human immunoglobulin gene loci as described in PCT Patent Application WO98/24893, Kucherlapati and Jakobovits et al., published December 3,1997 (see also, Jakobovits, 1998, Exp. Opin. Invest. Drugs 7(4): 607-614; U.S. patents 6,162,963 issued 19 December 2000; 6,150,584 issued 12 November 2000; and, 6,114598 issued 5 September 2000). This method avoids the in vitro manipulation required with phage display technology and efficiently produces high affinity authentic human antibodies. Reactivity of 98P4B6 antibodies with a 98P4B6-related protein can be established by a number of well known means, including Western blot, immunoprecipitation, ELISA, and FACS analyses using, as appropriate, 98P4B6-related proteins, 98P4B6-expressing cells or extracts thereof. A 98P4B6 antibody or fragment thereof can be labeled with a detectable marker or conjugated to a second molecule. Suitable detectable markers include, but are not limited to, a radioisotope, a fluorescent compound, a bioluminescent compound, chemiluminescent compound, a metal chelator or an enzyme. Further, bi-specific antibodies specific for two or more 98P4B6 epitopes are generated using methods generally known in the art. Homodimeric antibodies can also be generated by cross-linking techniques known in the art (e.g., Wolff et al., Cancer Res. 53: 2560-2565). V.) 98P4B6 Cellular Immune Responses The mechanism by which T cells recognize antigens has been delineated. Efficacious peptide epitope vaccine compositions of the invention induce a therapeutic or prophylactic immune responses in very broad segments of the world wide population. For an understanding of the value and efficacy of compositions of the invention that induce cellular immune responses, a brief review of immunology-related technology is provided. A complex of an HLA molecule and a peptidic antigen acts as the ligand recognized by HLA-restricted T cells (Buus, S. et al., Cell 47:1071, 1986; Babbitt, B. P. eta., Nature 317:359, 1985; Townsend, A. and Bodmer, H., Annu. Rev. Immunol. 7:601, 1989; Germain, R. N., Annu. Rev. Immunol. 11:403,1993). Through the study of single amino acid substituted antigen analogs and the sequencing of endogenously bound, naturally processed peptides, critical residues that correspond to motifs required for specific binding to HLA antigen molecules have been identified and are set forth in Table IV (see also, e.g., Southwood, et at., J. Immunol. 160:3363, 1998; Rammensee, et al., Immunogerietics 41:178, 1995; Rammensee et al., SYFPEITHI, access via World Wide Web at URL (134.2.96.221/scripts.hlaserver.dllhome.htm); Sette, A. and Sidney, J. Curr. Opin. Immunol. 10:478, 1998; Engelhard, V. H., Curr. Opin. Immunol. 6:13, 1994; Sette, A. and Grey, H. M., Cur. Opin. Immunol. 4:79, 1992; Sinigaglia, F. and Hammer, J. Curr. Biol. 6:52, 1994; Ruppert et a., Cell 74:929-937, 1993; Kondo et a., J. Immuno. 155:4307-4312, 1995; Sidney et a., J. Immunol. 157:3480-3490, 1996; Sidney et a., Human Immunol. 45:79-93, 1996; Sette, A. and Sidney, J. Immunogenetics 1999 Nov; 50(3-4):201-12, Review). Furthermore, x-ray crystallographic analyses of HLA-peptide complexes have revealed pockets within the peptide binding cleft/groove of HLA molecules which accommodate, in an allele-specific mode, residues bome by peptide ligands; these residues in turn determine the HLA binding capacity of the peptides in which they are present. (See, e.g., Madden, D.R. Annu. Rev. Immunol. 13:587, 1995; Smith, et al., Immunity 4:203, 1996; Fremont et a., Immunity 8:305, 1998; Stern et a., Structure 2:245, 1994; Jones, E.Y. Curr. Opin. Immunol. 9:75,1997; Brown, J. H. et a., Nature 364:33, 1993; Guo, H. C. et a., Proc. Natl. Acad. Sci. USA 90:8053,1993; Guo, H. C. et a., Nature 360:364, 1992; Silver, M. L. et al., Nature 360:367, 1992; Matsumura, M. et at., Science 257:927, 1992; Madden et al., Cell 70:1035, 1992; Fremont, D. H. et al., Science 257:919, 1992; Saper, M. A., Bjorkman, P. J. and Wiley, D. C., J. Mol. Biol. 219:277, 1991.) Accordingly, the definition of class I and class 11 allele-specific HLA binding motifs, or class I or class II supermotifs allows identification of regions within a protein that are correlated with binding to particular HLA antigen(s). Thus, by a process of HLA motif identification, candidates for epitope-based vaccines have been identified; such candidates can be further evaluated by HLA-peptide binding assays to determine binding affinity and/or the time period of 47 WO 03/087306 PCT/US03/10462 association of the epitope and its corresponding HLA molecule. Additional confirmatory work can be performed to select, amongst these vaccine candidates, epitopes with preferred characteristics in terms of population coverage, and/or immunogenicity. Various strategies can be utilized to evaluate cellular immunogenicity, including: 1) Evaluation of primary T cell cultures from normal individuals (see, e.g., Wentworth, P. A. et al., Mol. Immunol. 32:603, 1995; Celis, E. et al., Proc. Natl. Acad. Sci. USA 91:2105, 1994; Tsai, V. et al, J. Immunol. 158:1796, 1997; Kawashima, I. et al., Human Immunol. 59:1, 1998). This procedure involves the stimulation of peripheral blood lymphocytes (PBL) from normal subjects with a test peptide in the presence of antigen presenting cells in vitro over a period of several weeks. T cells specific for the peptide become activated during this time and are detected using, e.g., a lymphokine- or 5 1 Cr-release assay involving peptide sensitized target cells. 2) Immunization of HLA transgenic mice (see, e.g., Wentworth, P. A. et al., J. Immunol. 26:97, 1996; Wentworth, P. A. et al., Int. Immunol. 8:651, 1996; Alexander, J. et al., J. Immunol. 159:4753, 1997). For example, in such methods peptides in incomplete Freund's adjuvant are administered subcutaneously to HLA transgenic mice. Several weeks following immunization, splenocytes are removed and cultured in vitro in the presence of test peptide for approximately one week. Peptide-specific T cells are detected using, e.g., a 51Cr-release assay involving peptide sensitized target cells and target cells expressing endogenously generated antigen. 3) Demonstration of recall T cell responses from immune individuals who have been either effectively vaccinated and/or from chronically ill patients (see, e.g., Rehermann, B. et aL, J Exp. Med. 181:1047, 1995; Doolan, D. L. et al, Immunity 7:97, 1997; Bertoni, R. et al., J. Clin. Invest. 100:503, 1997; Threlkeld, S. C. et al, J. Immunol. 159:1648, 1997; Diepolder, H. M. et al., J. Virol. 71:6011, 1997). Accordingly, recall responses are detected by culturing PBL from subjects that have been exposed to the antigen due to disease and thus have generated an immune response "naturally", or from patients who were vaccinated against the antigen. PBL from subjects are cultured in vitro for 1-2 weeks in the presence of test peptide plus antigen presenting cells (APC) to allow activation of "memory'" T cells, as compared to "naive" T cells. At the end of the culture period, T cell activity is detected using assays including 5 1 Cr release involving peptide-sensitized targets, T cell proliferation, or lymphokine release. VI.) 98P4B6 Transqenic Animals Nucleic acids that encode a 98P4B6-related protein can also be used to generate either transgenic animals or "knock out" animals that, in turn, are useful in the development and screening of therapeutically useful reagents. In accordance with established techniques, cDNA encoding 98P4B6 can be used to done genomic DNA that encodes 98P4B6. The cloned genomic sequences can then be used to generate transgenic animals containing cells that express DNA that encode 98P4B6. Methods for generating transgenic animals, particularly animals such as mice or rats, have become conventional in the art and are described, for example, in U.S. Patent Nos. 4,736,866 issued 12 April 1988, and 4,870,009 issued 26 September 1989. Typically, particular cells would be targeted for 98P4B6 transgene incorporation with tissue specific enhancers. Transgenic animals that include a copy of a transgene encoding 98P4B6 can be used to examine the effect of increased expression of DNA that encodes 98P4B6. Such animals can be used as tester animals for reagents thought to confer protection from, for example, pathological conditions associated with its overexpression. In accordance with this aspect of the invention, an animal is treated with a reagent and a reduced incidence of a pathological condition, compared to untreated animals that bear the transgene, would indicate a potential therapeutic intervention for the pathological condition. Alternatively, non-human homologues of 98P4B6 can be used to construct a 98P4B6 "knock out" animal that has a defective or altered gene encoding 98P4B6 as a result of homologous recombination between the endogenous gene 48 WO 03/087306 PCT/US03/10462 encoding 98P486 and altered genomic DNA encoding 98P4B6 introduced into an embryonic cell of the animal. For example, cDNA that encodes 98P4B6 can be used to clone genomic DNA encoding 98P4B6 in accordance with established techniques. A portion of the genomic DNA encoding 98P4B6 can be deleted or replaced with another gene, such as a gene encoding a selectable marker that can be used to monitor integration. Typically, several kilobases of unaltered flanking DNA (both at the 5' and 3' ends) are included in the vector (see, e.g., Thomas and Capecchi, Cell, 51:503 (1987) for a description of homologous recombination vectors). The vector is introduced into an embryonic stem cell line (e.g., by electroporation) and cells in which the introduced DNA has homologously recombined with the endogenous DNA are selected (see, e.g., Li et al., Cell, 69:915 (1992)). The selected cells are then injected into a blastocyst of an animal (e.g., a mouse or rat) to form aggregation chimeras (see, e.g., Bradley, in Teratocarcinomas and Embryonic Stem Cells: A Practical Approach, E. J. Robertson, ed. (IRL, Oxford, 1987), pp. 113-152). A chimeric embryo can then be implanted into a suitable pseudopregnant female foster animal, and the embryo brought to term to create a "knock out" animal. Progeny harboring the homologously recombined DNA in their germ cells can be identified by standard techniques and used to breed animals in which all cells of the animal contain the homologously recombined DNA. Knock out animals can be characterized, for example, for their ability to defend against certain pathological conditions or for their development of pathological conditions due to absence of a 98P4B6 polypeptide. VII.) Methods for the Detection of 98P4B6 Another aspect of the present invention relates to methods for detecting 98P4B6 polynucleotides and 98P4B6-related proteins, as well as methods for identifying a cell that expresses 98P4B6. The expression profile of 98P4B6 makes it a diagnostic marker for metastasized disease. Accordingly, the status of 98P4B6 gene products provides information useful for predicting a variety of factors including susceptibility to advanced stage disease, rate of progression, andlor tumor aggressiveness. As discussed in detail herein, the status of 98P4B6 gene products in patient samples can be analyzed by a variety protocols that are well known in the art including immunohistochemical analysis, the variety of Northemrn blotting techniques including in situ hybridization, RT-PCR analysis (for example on laser capture micro-dissected samples), Westemrn blot analysis and tissue array analysis. More particularly, the invention provides assays for the detection of 98P4B6 polynucleotides in a biological sample, such as serum, bone, prostate, and other tissues, urine, semen, cell preparations, and the like. Detectable 98P4B6 polynucleotides include, for example, a 98P4B6 gene or fragment thereof, 98P4B6 mRNA, alternative splice variant 98P4B6 mRNAs, and recombinant DNA or RNA molecules that contain a 98P4B6 polynucleotide. A number of methods for amplifying and/or detecting the presence of 98P4B6 polynucleotides are well known in the art and can be employed in the practice of this aspect of the invention. In one embodiment, a method for detecting a 98P4B6 mRNA in a biological sample comprises producing cDNA from the sample by reverse transcription using at least one primer; amplifying the cDNA so produced using a 98P486 polynucleotides as sense and antisense primers to amplify 98P4B6 cDNAs therein; and detecting the presence of the amplified 98P4B6 cDNA. Optionally, the sequence of the amplified 98P4B6 cDNA can be determined. In another embodiment, a method of detecting a 98P4B6 gene in a biological sample comprises first isolating genomic DNA from the sample; amplifying the isolated genomic DNA using 98P4B6 polynucleotides as sense and antisense primers; and detecting the presence of the amplified 98P4B6 gene. Any number of appropriate sense and antisense probe combinations can be designed from a 98P4B6 nucleotide sequence (see, e.g., Figure 2) and used for this purpose. The invention also provides assays for detecting the presence of a 98P4B6 protein in a tissue or other biological sample such as serum, semen, bone, prostate, urine, cell preparations, and the like. Methods for detecting a 98P4B6-related protein are also well known and include, for example, immunoprecipitation, immunohistochemical analysis, Westemrn blot analysis, molecular 49 WO 03/087306 PCT/USO3/10462 binding assays, ELISA, ELIFA and the like. For example, a method of detecting the presence of a 98P4B6-related protein in a biological sample comprises first contacting the sample with a 98P4B6 antibody, a 98P4B6-reactive fragment thereof, or a recombinant protein containing an antigen-binding region of a 98P4B6 antibody; and then detecting the binding of 98P4B6 related protein in the sample. Methods for identifying a cell that expresses 98P4B6 are also within the scope of the invention. In one embodiment, an assay for identifying a cell that expresses a 98P4B6 gene comprises detecting the presence of 98P4B6 mRNA in the cell. Methods for the detection of particular mRNAs in cells are well known and include, for example, hybridization assays using complementary DNA probes (such as in situ hybridization using labeled 98P4B6 riboprobes, Northern blot and related techniques) and various nucleic acid amplification assays (such as RT-PCR using complementary primers specific for 98P4B6, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the like). Alternatively, an assay for identifying a cell that expresses a 98P4B6 gene comprises detecting the presence of 98P4B6-related protein in the cell or secreted by the cell. Various methods for the detection of proteins are well known in the art and are employed for the detection of 98P4B6-related proteins and cells that express 98P4B6-related proteins. 98P4B6 expression analysis is also useful as a tool for identifying and evaluating agents that modulate 98P4B6 gene expression. For example, 98P4B6 expression is significantly upregulated in prostate cancer, and is expressed in cancers of the tissues listed in Table I. Identification of a molecule or biological agent that inhibits 98P4B6 expression or over expression in cancer cells is of therapeutic value. For example, such an agent can be identified by using a screen that quantifies 98P4B6 expression by RT-PCR, nucleic acid hybridization or antibody binding. VIII.) Methods for Monitoring the Status of 98P486-.related Genes and Their Products Oncogenesis is known to be a multistep process where cellular growth becomes progressively dysregulated and cells progress from a normal physiological state to precancerous and then cancerous states (see, e.g., Alers et al., Lab Invest. 77(5): 437-438 (1997) and Isaacs et al., Cancer Surv. 23:19-32 (1995)). In this context, examining a biological sample for evidence of dysregulated cell growth (such as aberrant 98P4B6 expression in cancers) allows for early detection of such aberrant physiology, before a pathologic state such as cancer has progressed to a stage that therapeutic options are more limited and or the prognosis is worse, In such examinations, the status of 98P4B6 in a biological sample of interest can be compared, for example, to the status of 98P4B6 in a corresponding normal sample (e.g. a sample from that individual or alternatively another individual that is not affected by a pathology). An alteration in the status of 98P4B6 in the biological sample (as compared to the normal sample) provides evidence of dysregulated cellular growth. In addition to using a biological sample that is not affected by a pathology as a normal sample, one can also use a predetermined normative value such as a predetermined normal level of mRNA expression (see, e.g., Grever et al, J. Comp. Neurol. 1996 Dec 9; 376(2): 306-14 and U.S. Patent No. 5,837,501) to compare 98P4B6 status in a sample. The term 'status" in this context is used according to its art accepted meaning and refers to the condition or state of a gene and its products. Typically, skilled artisans use a number of parameters to evaluate the condition or state of a gene and its products. These include, but are not limited to the location of expressed gene products (including the location of 98P4B6 expressing cells) as well as the level, and biological activity of expressed gene products (such as 98P4B6 mRNA, polynucleotides and polypeptides). Typically, an alteration in the status of 98P4B6 comprises a change in the location of 98P4B6 and/or 98P4B6 expressing cells and/or an increase in 98P4B6 mRNA andlor protein expression. 98P4B6 status in a sample can be analyzed by a number of means well known in the art, including without limitation, immunohistochemical analysis, in situ hybridization, RT-PCR analysis on laser capture micro-dissected samples, Westemrn blot analysis, and tissue array analysis. Typical protocols for evaluating the status of a 98P4B6 gene and gene products are found, for example in Ausubel et al. eds., 1995, Current Protocols In Molecular Biology, Units 2 (Northern Blotting), 4 (Southern 50 WO 03/087306 PCT/USO3/10462 Blotting), 15 (Immunoblotting) and 18 (PCR Analysis). Thus, the status of 98P4B6 in a biological sample is evaluated by various methods utilized by skilled artisans including, but not limited to genomic Southern analysis (to examine, for example perturbations in a 98P4B6 gene), Northern analysis and/or PCR analysis of 98P4B6 mRNA (to examine, for example alterations in the polynucleotide sequences or expression levels of 98P4B6 mRNAs), and, Western and/or immunohistochemical analysis (to examine, for example alterations in polypeptide sequences, alterations in polypeptide localization within a sample, alterations in expression levels of 98P4B6 proteins and/or associations of 98P4B6 proteins with polypeptide binding partners). Detectable 98P4B6 polynucleotides include, for example, a 98P4B6 gene or fragment thereof, 98P4B6 mRNA, alternative splice variants, 98P4B6 mRNAs, and recombinant DNA or RNA molecules containing a 98P486 polynucleotide. The expression profile of 98P4B6 makes it a diagnostic marker for local and/or metastasized disease, and provides information on the growth or oncogenic potential of a biological sample. In particular, the status of 98P4B6 provides information useful for predicting susceptibility to particular disease stages, progression, and/or tumor aggressiveness. The invention provides methods and assays for determining 98P4B6 status and diagnosing cancers that express 98P486, such as cancers of the tissues listed in Table I. For example, because 98P4B6 mRNA is so highly expressed in prostate and other cancers relative to normal prostate tissue, assays that evaluate the levels of 98P4B6 mRNA transcripts or proteins in a biological sample can be used to diagnose a disease associated with 98P4B6 dysregulation, and can provide prognostic information useful in defining appropriate therapeutic options. The expression status of 98P4B6 provides information including the presence, stage and location of dysplastic, precancerous and cancerous cells, predicting susceptibility to various stages of disease, and/or for gauging tumor aggressiveness. Moreover, the expression profile makes it useful as an imaging reagent for metastasized disease. Consequently, an aspect of the invention is directed to the various molecular prognostic and diagnostic methods for examining the status of 98P4B6 in biological samples such as those from individuals suffering from, or suspected of suffering from a pathology characterized by dysregulated cellular growth, such as cancer. As described above, the status of 98P4B6 in a biological sample can be examined by a number of well-known procedures in the art. For example, the status of 98P4B6 in a biological sample taken from a specific location in the body can be examined by evaluating the sample for the presence or absence of 98P4B6 expressing cells (e.g. those that express 98P4B6 mRNAs or proteins). This examination can provide evidence of dysregulated cellular growth, for example, when 98P4B6-expressing cells are found in a biological sample that does not normally contain such cells (such as a lymph node), because such alterations in the status of 98P4B6 in a biological sample are often associated with dysregulated cellular growth. Specifically, one indicator of dysregulated cellular growth is the metastases of cancer cells from an organ of origin (such as the prostate) to a different area of the body (such as a lymph node). In this context, evidence of dysregulated cellular growth is important for example because occult lymph node metastases can be detected in a substantial proportion of patients with prostate cancer, and such metastases are associated with known predictors of disease progression (see, e.g., Murphy et at., Prostate 42(4): 315-317 (2000);Su et al., Semin. Surg. Oncol. 18(1): 17-28 (2000) and Freeman et al., J Urol 1995 Aug 154(2 Pt 1):474-8). In one aspect, the invention provides methods for monitoring 98P4B6 gene products by determining the status of 98P4B6 gene products expressed by cells from an individual suspected of having a disease associated with dysregulated cell growth (such as hyperplasia or cancer) and then comparing the status so determined to the status of 98P4B6 gene products in a corresponding normal sample. The presence of aberrant 98P4B6 gene products in the test sample relative to the normal sample provides an indication of the presence of dysregulated cell growth within the cells of the individual. In another aspect, the invention provides assays useful in determining the presence of cancer in an individual, comprising detecting a significant increase in 98P4B6 mRNA or protein expression in a test cell or tissue sample relative to 51 WO 03/087306 PCT/USO3/10462 expression levels in the corresponding normal cell or tissue. The presence of 98P4B6 mRNA can, for example, be evaluated in tissues including but not limited to those listed in Table I. The presence of significant 98P4B6 expression in any of these tissues is useful to indicate the emergence, presence and/or severity of a cancer, since the corresponding normal tissues do not express 98P4B6 mRNA or express it at lower levels. In a related embodiment, 98P4B6 status is determined at the protein level rather than at the nucleic acid level. For example, such a method comprises determining the level of 98P4B6 protein expressed by cells in a test tissue sample and comparing the level so determined to the level of 98P4B6 expressed in a corresponding normal sample. In one embodiment, the presence of 98P4B6 protein is evaluated, for example, using immunohistochemical methods. 98P4B6 antibodies or binding partners capable of detecting 98P4B6 protein expression are used in a variety of assay formats well known in the art for this purpose. In a further embodiment, one can evaluate the status of 98P4B6 nucleotide and amino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules. These perturbations can include insertions, deletions, substitutions and the like. Such evaluations are useful because perturbations in the nucleotide and amino acid sequences are observed in a large number of proteins associated with a growth dysregulated phenotype (see, e.g., Marrogi et al., 1999, J. Cutan. Pathol. 26(8):369-378). For example, a mutation in the sequence of 98P4B6 may be indicative of the presence or promotion of a tumor. Such assays therefore have diagnostic and predictive value where a mutation in 98P4B6 indicates a potential loss of function or increase in tumor growth. A wide variety of assays for observing perturbations in nucleotide and amino acid sequences are well known in the art. For example, the size and structure of nucleic acid or amino acid sequences of 98P4B6 gene products are observed by the Northem, Southem, Westemrn, PCR and DNA sequencing protocols discussed herein. In addition, other methods for observing perturbations in nucleotide and amino acid sequences such as single strand conformation polymorphism analysis are well known in the art (see, e.g., U.S. Patent Nos. 5,382,510 issued 7 September 1999, and 5,952,170 issued 17 January 1995). Additionally, one can examine the methylation status of a 98P4B6 gene in a biological sample. Aberrant demethylation and/or hypermethylation of CpG islands in gene 5' regulatory regions frequently occurs in immortalized and transformed cells, and can result in altered expression of various genes. For example, promoter hypermethylation of the pi-class glutathione S transferase (a protein expressed in normal prostate but not expressed in >90% of prostate carcinomas) appears to permanently silence transcription of this gene and is the most frequently detected genomic alteration in prostate carcinomas (De Marzo et al, Am. J. Pathol. 155(6): 1985-1992 (1999)). In addition, this alteration is present in at least 70% of cases of high-grade prostatic intraepithelial neoplasia (PIN) (Brooks et al., Cancer Epidemiol. Biomarkers Prey., 1998, 7:531-536). In another example, expression of the LAGE-1 tumor specific gene (which is not expressed in normal prostate but is expressed in 25-50% of prostate cancers) is induced by deoxy-azacytidine in lymphoblastoid cells, suggesting that tumoral expression is due to demethylation (Lethe et al., Int. J. Cancer 76(6): 903-908 (1998)). A variety of assays for examining methylation status of a gene are well known in the art. For example, one can utilize, in Southemrn hybridization approaches, methylation sensitive restriction enzymes that cannot cleave sequences that contain methylated CpG sites to assess the methylation status of CpG islands. In addition, MSP (methylation specific PCR) can rapidly profile the methylation status of all the CpG sites present in a CpG island of a given gene. This procedure involves initial modification of DNA by sodium bisulfite (which will convert all unmethylated cytosines to uracil) followed by amplification using primers specific for methylated versus unmethylated DNA. Protocols involving methylation interference can also be found for example in Current Protocols In Molecular Biology, Unit 12, Frederick M. Ausubel et al. eds., 1995. Gene amplification is an additional method for assessing the status of 98P4B6. Gene amplification is measured in a sample directly, for example, by conventional Southern blotting or Northern blotting to quantitate the transcription of mRNA (Thomas, 1980, Proc. Natl. Acad. Sci. USA, 77:5201-5205), dot blotting (DNA analysis), or in situ hybridization, using an 52 WO 03/087306 PCT/USO3/10462 appropriately labeled probe, based on the sequences provided herein. Alternatively, antibodies are employed that recognize specific duplexes, including DNA duplexes, RNA duplexes, and DNA-RNA hybrid duplexes or DNA-protein duplexes. The antibodies in turn are labeled and the assay carried out where the duplex is bound to a surface, so that upon the formation of duplex on the surface, the presence of antibody bound to the duplex can be detected. Biopsied tissue or peripheral blood can be conveniently assayed for the presence of cancer cells using for example, Northern, dot blot or RT-PCR analysis to detect 98P4B6 expression. The presence of RT-PCR amplifiable 98P4B6 mRNA provides an indication of the presence of cancer. RT-PCR assays are well known in the art. RT-PCR detection assays for tumor cells in peripheral blood are currently being evaluated for use in the diagnosis and management of a number of human solid tumors. In the prostate cancer field, these include RT-PCR assays for the detection of cells expressing PSA and PSM (Verkaik et al., 1997, Urol. Res. 25:373-384; Ghossein etal., 1995, J. Clin. Oncol. 13:1195-2000; Heston etal., 1995, Clin. Chem. 41:1687 1688). A further aspect of the invention is an assessment of the susceptibility that an individual has for developing cancer. In one embodiment, a method for predicting susceptibility to cancer comprises detecting 98P4B6 mRNA or 98P4B6 protein in a tissue sample, its presence indicating susceptibility to cancer, wherein the degree of 98P4B6 mRNA expression correlates to the degree of susceptibility. In a specific embodiment the presence of 98P4B6 in prostate or other tissue is examined, with the presence of 98P4B6 in the sample providing an indication of prostate cancer susceptibility (or the emergence or existence of a prostate tumor). Similarly, one can evaluate the integrity 98P4B6 nucleotide and amino acid sequences in a biological sample, in order to identify perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like. The presence of one or more perturbations in 98P4B6 gene products in the sample is an indication of cancer susceptibility (or the emergence or existence of a tumor). The invention also comprises methods for gauging tumor aggressiveness. In one embodiment, a method for gauging aggressiveness of a tumor comprises determining the level of 98P4B6 mRNA or 98P4B6 protein expressed by tumor cells, comparing the level so determined to the level of 98P486 mRNA or 98P4B6 protein expressed in a corresponding normal tissue taken from the same individual or a normal tissue reference sample, wherein the degree of 98P4B6 mRNA or 98P4B6 protein expression in the tumor sample relative to the normal sample indicates the degree of aggressiveness. In a specific embodiment, aggressiveness of a tumor is evaluated by determining the extent to which 98P4B6 is expressed in the tumor cells, with higher expression levels indicating more aggressive tumors. Another embodiment is the evaluation of the integrity of 98P4B6 nucleotide and amino acid sequences in a biological sample, in order to identify perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like. The presence of one or more perturbations indicates more aggressive tumors. Another embodiment of the invention is directed to methods for observing the progression of a malignancy in an individual over time. In one embodiment, methods for observing the progression of a malignancy in an individual over time comprise determining the level of 98P4B6 mRNA or 98P4B6 protein expressed by cells in a sample of the tumor, comparing the level so determined to the level of 98P4B6 mRNA or 98P486 protein expressed in an equivalent tissue sample taken from the same individual at a different time, wherein the degree of 98P4B6 mRNA or 98P4B6 protein expression in the tumor sample over time provides information on the progression of the cancer. In a specific embodiment the progression of a cancer is evaluated by determining 98P4B6 expression in the tumor cells over time, where increased expression over time indicates a progression of the cancer. Also, one can evaluate the integrity 98P4B6 nucleotide and amino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules such as insertions, deletions, substitutions and the like, where the presence of one or more perturbations indicates a progression of the cancer. The above diagnostic approaches can be combined with any one of a wide variety of prognostic and diagnostic protocols known in the art For example, another embodiment of the invention is directed to methods for observing a coincidence between the expression of 98P4B6 gene and 98P4B6 gene products (or perturbations in 98P4B6 gene and 98P4B6 gene 53 WO 03/087306 PCT/USO3/10462 products) and a factor that is associated with malignancy, as a means for diagnosing and prognosticating the status of a tissue sample. A wide variety of factors associated with malignancy can be utilized, such as the expression of genes associated with malignancy (e.g. PSA, PSCA and PSM expression for prostate cancer etc.) as well as gross cytological observations (see, e.g., Bocking et al., 1984, Anal. Quant. Cytol. 6(2):74-88; Epstein, 1995, Hum. Pathol. 26(2):223-9; Thorson et al., 1998, Mod. Pathol. 11(6):543-51; Baisden et al., 1999, Am. J. Surg. Pathol. 23(8):918-24). Methods for observing a coincidence between the expression of 98P4B6 gene and 98P4B6 gene products (or perturbations in 98P4B6 gene and 98P4B6 gene products) and another factor that is associated with malignancy are useful, for example, because the presence of a set of specific factors that coincide with disease provides information crucial for diagnosing and prognosticating the status of a tissue sample. In one embodiment, methods for observing a coincidence between the expression of 98P4B6 gene and 98P4B6 gene products (or perturbations in 98P4136 gene and 98P4B6 gene products) and another factor associated with malignancy entails detecting the overexpression of 98P4B6 mRNA or protein in a tissue sample, detecting the overexpression of PSA mRNA or protein in a tissue sample (or PSCA or PSM expression), and observing a coincidence of 98P4B6 mRNA or protein and PSA mRNA or protein overexpression (or PSCA or PSM expression). In a specific embodiment, the expression of 98P4B6 and PSA mRNA in prostate tissue is examined, where the coincidence of 98P4B6 and PSA mRNA overexpression in the sample indicates the existence of prostate cancer, prostate cancer susceptibility or the emergence or status of a prostate tumor. Methods for detecting and quantifying the expression of 98P4B6 mRNA or protein are described herein, and standard nucleic acid and protein detection and quantification technologies are well known in the art. Standard methods for the detection and quantification of 98P4B6 mRNA include in situ hybridization using labeled 98P4B6 riboprobes, Northemrn blot and related techniques using 98P4B6 polynucleotide probes, RT-PCR analysis using primers specific for 98P4B6, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the like. In a specific embodiment, semi-quantitative RT-PCR is used to detect and quantify 98P4B6 mRNA expression. Any number of primers capable of amplifying 98P4B6 can be used for this purpose, including but not limited to the various primer sets specifically described herein. In a specific embodiment, polyclonal or monoclonal antibodies specifically reactive with the wild-type 98P4B6 protein can be used in an immunohistochemical assay of biopsied tissue. IX.) Identification of Molecules That Interact With 98P4B6 The 98P4B6 protein and nucleic acid sequences disclosed herein allow a skilled artisan to identify proteins, small molecules and other agents that interact with 98P4B6, as well as pathways activated by 98P4B6 via any one of a variety of art accepted protocols. For example, one can utilize one of the so-called interaction trap systems (also referred to as the "two-hybrid assay"). In such systems, molecules interact and reconstitute a transcription factor which directs expression of a reporter gene, whereupon the expression of the reporter gene is assayed. Other systems identify protein-protein interactions in vivo through reconstitution of a eukaryotic transcriptional activator, see, e.g., U.S. Patent Nos. 5,955,280 issued 21 September 1999, 5,925,523 issued 20 July 1999, 5,848,722 issued 8 December 1998 and 6,004,746 issued 21 December 1999. Algorithms are also available in the art for genome-based predictions of protein function (see, e.g., Marcotte, et atl, Nature 402: 4 November 1999, 83-86). Alternatively one can screen peptide libraries to identify molecules that interact with 98P4B6 protein sequences. In such methods, peptides that bind to 98P4B6 are identified by screening libraries that encode a random or controlled collection of amino acids. Peptides encoded by the libraries are expressed as fusion proteins of bacteriophage coat proteins, the bacteriophage particles are then screened against the 98P4B6 protein(s). Accordingly, peptides having a wide variety of uses, such as therapeutic, prognostic or diagnostic reagents, are thus identified without any prior information on the structure of the expected ligand or receptor molecule. Typical peptide 54 WO 03/087306 PCT/USO3/10462 libraries and screening methods that can be used to identify molecules that interact with 98P4B6 protein sequences are disclosed for example in U.S. Patent Nos. 5,723,286 issued 3 March 1998 and 5,733,731 issued 31 March 1998. Alternatively, cell lines that express 98P4B6 are used to identify protein-protein interactions mediated by 98P4B6. Such interactions can be examined using immunoprecipitation techniques (see, e.g., Hamilton B.J., et al. Biochem. Biophys. Res. Commun. 1999, 261:646-51). 98P4B6 protein can be immunoprecipitated from 98P4B6-expressing cell lines using anti-98P4B6 antibodies. Alternatively, antibodies against His-tag can be used in a cell line engineered to express fusions of 98P4B6 and a His-tag (vectors mentioned above). The immunoprecipitated complex can be examined for protein association by procedures such as Western blotting, 35 S-methionine labeling of proteins, protein microsequencing, silver staining and two-dimensional gel electrophoresis. Small molecules and ligands that interact with 98P4B6 can be identified through related embodiments of such screening assays. For example, small molecules can be identified that interfere with protein function, including molecules that interfere with 98P4B6's ability to mediate phosphorylation and de-phosphorylation, interaction with DNA or RNA molecules as an indication of regulation of cell cycles, second messenger signaling or tumorigenesis. Similarly, small molecules that modulate 98P4B6-related ion channel, protein pump, or cell communication functions are identified and used to treat patients that have a cancer that expresses 98P4B6 (see, e.g., Hille, B., Ionic Channels of Excitable Membranes 2nd Ed., Sinauer Assoc., Sunderland, MA, 1992). Moreover, ligands that regulate 98P4B6 function can be identified based on their ability to bind 98P4B6 and activate a reporter construct. Typical methods are discussed for example in U.S. Patent No. 5,928,868 issued 27 July 1999, and include methods for forming hybrid ligands in which at least one ligand is a small molecule. In an illustrative embodiment, cells engineered to express a fusion protein of 98P4B6 and a DNA-binding protein are used to co-express a fusion protein of a hybrid ligandismall molecule and a cDNA library transcriptional activator protein. The cells further contain a reporter gene, the expression of which is conditioned on the proximity of the first and second fusion proteins to each other, an event that occurs only if the hybrid ligand binds to target sites on both hybrid proteins. Those cells that express the reporter gene are selected and the unknown small molecule or the unknown ligand is identified. This method provides a means of identifying modulators, which activate or inhibit 98P4B6. An embodiment of this invention comprises a method of screening for a molecule that interacts with a 98P4B6 amino acid sequence shown in Figure 2 or Figure 3, comprising the steps of contacting a population of molecules with a 98P4B6 amino acid sequence, allowing the population of molecules and the 98P4B6 amino acid sequence to interact under conditions that facilitate an interaction, determining the presence of a molecule that interacts with the 98P4B6 amino acid sequence, and then separating molecules that do not interact with the 98P4B6 amino acid sequence from molecules that do. In a specific embodiment, the method further comprises purifying, characterizing and identifying a molecule that interacts with the 98P4B6 amino acid sequence. The identified molecule can be used to modulate a function performed by 98P4B6. In a preferred embodiment, the 98P4B6 amino acid sequence is contacted with a library of peptides. X.) Therapeutic Methods and Compositions The identification of 98P4B6 as a protein that is normally expressed in a restricted set of tissues, but which is also expressed in prostate and other cancers, opens a number of therapeutic approaches to the treatment of such cancers. As contemplated herein, 98P4B6 functions as a transcription factor involved in activating tumor-promoting genes or repressing genes that block tumorigenesis. Accordingly, therapeutic approaches that inhibit the activity of a 98P4B6 protein are useful for patents suffering from a cancer that expresses 98P4B6. These therapeutic approaches generally fall into two classes. One class comprises various methods for inhibiting the binding or association of a 98P4B6 protein with its binding partner or with other proteins. 55 WO 03/087306 PCT/US03/10462 Another class comprises a variety of methods for inhibiting the transcription of a 98P4B6 gene or translation of 98P4B6 mRNA. X.A.) Anti-Cancer Vaccines The invention provides cancer vaccines comprising a 98P4B6-related protein or 98P4B6-related nucleic acid. In view of the expression of 98P4B6, cancer vaccines prevent and/or treat 98P4B6-expressing cancers with minimal or no effects on non target tissues. The use of a tumor antigen in a vaccine that generates humoral and/or cell-mediated immune responses as anti cancer therapy is well known in the art and has been employed in prostate cancer using human PSMA and rodent PAP immunogens (Hodge et al., 1995, Int. J. Cancer 63:231-237; Fong et a., 1997, J. Immunol. 159:3113-3117). Such methods can be readily practiced by employing a 98P4B6-related protein, or a 98P4B6-encoding nucleic acid molecule and recombinant vectors capable of expressing and presenting the 98P4B6 immunogen (which typically comprises a number of antibody or T cell epitopes). Skilled artisans understand that a wide variety of vaccine systems for delivery of immunoreactive epitopes are known in the art (see, e.g., Heryln et al., Ann Med 1999 Feb 31(1):66-78; Maruyama et al., Cancer Immunol Immunother 2000 Jun 49(3):123-32) Briefly, such methods of generating an immune response (e.g. humoral and/or cell-mediated) in a mammal, comprise the steps of: exposing the mammal's immune system to an immunoreactive epitope (e.g. an epitope present in a 98P4B6 protein shown in Figure 3 or analog or homolog thereof) so that the mammal generates an immune response that is specific for that epitope (e.g. generates antibodies that specifically recognize that epitope). In a preferred method, a 98P4B6 immunogen contains a biological motif, see e.g., Tables VIll-XXI and XXII-XLIX, or a peptide of a size range from 98P4B6 indicated in Figure 5, Figure 6, Figure 7, Figure 8, and Figure 9. The entire 98P4B6 protein, immunogenic regions or epitopes thereof can be combined and delivered by various means. Such vaccine compositions can include, for example, lipopeptides (e.g.,Vitiello, A. et al., J. Clin. Invest. 95:341, 1995), peptide compositions encapsulated in pcly(DL-lactide-co-glycolide) ("PLG") microspheres (see, e.g., Eldridge, et al., Molec. Immunol. 28:287-294, 1991: Alonso et al., Vaccine 12:299-306, 1994; Jones et al., Vaccine 13:675-681, 1995), peptide compositions contained in immune stimulating complexes (ISCOMS) (see, e.g., Takahashi et al., Nature 344:873 875, 1990; Hu etal, Clin Exp Immunol. 113:235-243, 1998), multiple antigen peptide systems (MAPs) (see e.g., Tam, J. P., Proc. Natl. Acad. Sci. U.S.A. 85:5409-5413, 1988; Tam, J.P., J. Immunol. Methods 196:17-32, 1996), peptides formulated as multivalent peptides; peptides for use in ballistic delivery systems, typically crystallized peptides, viral delivery vectors (Perkus, M. E. et al., In: Concepts in vaccine development, Kaufmann, S. H. E., ed., p. 379, 1996; Chakrabarti, S. et al., Nature 320:535, 1986; Hu, S. L. et al., Nature 320:537, 1986; Kieny, M.-P. et al., AIDS Bio/Technology4:790, 1986; Top, F. H. eta!., J. Infect. Dis. 124:148, 1971; Chanda, P. K. et al., Virology 175:535, 1990), particles of viral or synthetic origin (e.g., Kofler, N. et al, J. Immunol. Methods. 192:25, 1996; Eldridge, J. H. et al., Sem. Hematol. 30:16, 1993; Falo, L. D., Jr. et al, Nature Med. 7:649, 1995), adjuvants (Warren, H. S., Vogel, F. R., and Chedid, L. A. Annu. Rev. Immunol. 4:369, 1986; Gupta, R. K. et al., Vaccine 11:293, 1993), liposomes (Reddy, R. et al., J. Immunol. 148:1585, 1992; Rock, K. L., Immunol. Today 17:131, 1996), or, naked or particle absorbed cDNA (Ulmer, J. B. et al, Science 259:1745, 1993; Robinson, H. L., Hunt, L. A., and Webster, R. G., Vaccine 11:957, 1993; Shiver, J. W. et al., In: Concepts in vaccine development, Kaufmann, S. H. E., ed., p. 423, 1996; Cease, K. B., and Berzofsky, J. A., Annu. Rev. Immunol. 12:923, 1994 and Eldridge, J. H. et al., Sem. Hematol. 30:16, 1993). Toxin-targeted delivery technologies, also known as receptor mediated targeting, such as those of Avant Immunotherapeutics, Inc. (Needham, Massachusetts) may also be used. In patients with 98P4B6-associated cancer, the vaccine compositions of the invention can also be used in conjunction with other treatments used for cancer, e.g., surgery, chemotherapy, drug therapies, radiation therapies, etc. including use in combination with immune adjuvants such as IL-2, IL-12, GM-CSF, and the like. Cellular Vaccines: 56 WO 03/087306 PCT/US03/10462 CTL epitopes can be determined using specific algorithms to identify peptides within 98P4B6 protein that bind corresponding HLA alleles (see e.g., Table IV; Epimer T m and Epimatrix T M , Brown University (URL brown.edulResearch/TB HIVLab/epimatrixlepimatrix.html); and, BIMAS, (URL bimas.dcrt.nih.gov/; SYFPEITHI at URL syfpeithi.bmi-heidelberg.com/). In a preferred embodiment, a 98P4B6 immunogen contains one or more amino acid sequences identified using techniques well known in the art, such as the sequences shown in Tables VIII-XXI and XXII-XLIX or a peptide of 8, 9, 10 or 11 amino acids specified by an HLA Class I motif/supermotif (e.g., Table IV (A), Table IV (D), or Table IV (E)) and/or a peptide of at least 9 amino acids that comprises an HLA Class II motif/supermotif (e.g., Table IV (B) or Table IV (C)). As is appreciated in the art, the HLA Class I binding groove is essentially closed ended so that peptides of only a particular size range can fit into the groove and be bound, generally HLA Class I epitopes are 8, 9, 10, or 11 amino acids long. In contrast, the HLA Class II binding groove is essentially open ended; therefore a peptide of about 9 or more amino acids can be bound by an HLA Class II molecule. Due to the binding groove differences between HLA Class I and II, HLA Class I motifs are length specific, i.e., position two of a Class I motif is the second amino acid in an amino to carboxyl direction of the peptide. The amino acid positions in a Class 11 motif are relative only to each other, not the overall peptide, i.e., additional amino acids can be attached to the amino and/or carboxyl termini of a motif-bearing sequence. HLA Class 11 epitopes are often 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, or 25 amino acids long, or longer than 25 amino acids. Antibody-based Vaccines A wide variety of methods for generating an immune response in a mammal are known in the art (for example as the first step in the generation of hybridomas). Methods of generating an immune response in a mammal comprise exposing the mammal's immune system to an immunogenic epitope on a protein (e.g. a 98P4B6 protein) so that an immune response is generated. A typical embodiment consists of a method for generating an immune response to 98P4B6 in a host, by contacting the host with a sufficient amount of at least one 98P4B6 B cell or cytotoxic T-cell epitope or analog thereof; and at least one periodic interval thereafter re-contacting the host with the 98P4B6 B cell or cytotoxic T-cell epitope or analog thereof. A specific embodiment consists of a method of generating an immune response against a 98P4B6-related protein or a man-made multiepitopic peptide comprising: administering 98P4B6 immunogen (e.g. a 98P4B6 protein or a peptide fragment thereof, a 98P4B6 fusion protein or analog etc.) in a vaccine preparation to a human or another mammal. Typically, such vaccine preparations further contain a suitable adjuvant (see, e.g., U.S. Patent No. 6,146,635) or a universal helper epitope such as a PADRETM peptide (Epimmune Inc., San Diego, CA; see, e.g., Alexander et al., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander et al., Immunity 1994 1(9): 751-761 and Alexander et al., Immunol. Res. 1998 18(2): 79-92). An alternative method comprises generating an immune response in an individual against a 98P4B6 immunogen by: administering in vivo to muscle or skin of the individual's body a DNA molecule that comprises a DNA sequence that encodes a 98P4B6 immunogen, the DNA sequence operatively linked to regulatory sequences which control the expression of the DNA sequence; wherein the DNA molecule is taken up by cells, the DNA sequence is expressed in the cells and an immune response is generated against the immunogen (see, e.g., U.S. Patent No. 5,962,428). Optionally a genetic vaccine facilitator such as anionic lipids; saponins; lectins; estrogenic compounds; hydroxylated lower alkyls; dimethyl sulfoxide; and urea is also administered. In addition, an antiidiotypic antibody can be administered that mimics 98P4B6, in order to generate a response to the target antigen. Nucleic Acid Vaccines: Vaccine compositions of the invention include nucleic acid-mediated modalities. DNA or RNA that encode protein(s) of the invention can be administered to a patient. Genetic immunization methods can be employed to generate prophylactic or therapeutic humoral and cellular immune responses directed against cancer cells expressing 98P4B6. Constructs comprising DNA encoding a 98P4B6-related protein/immunogen and appropriate regulatory sequences can be injected directly into muscle or skin of an individual, such that the cells of the muscle or skin take-up the construct and 57 WO 03/087306 PCT/USO3/10462 express the encoded 98P4B6 proteinlimmunogen. Alternatively, a vaccine comprises a 98P4B6-related protein. Expression of the 98P4B6-related protein immunogen results in the generation of prophylactic or therapeutic humoral and cellular immunity against cells that bear a 98P4B6 protein. Various prophylactic and therapeutic genetic immunization techniques known in the art can be used (for review, see information and references published at Internet address genweb.com). Nucleic acid-based delivery is described, for instance, in Wolff et. al., Science 247:1465 (1990) as well as U.S. Patent Nos, 5,580,859; 5,589,466; 5,804,566; 5,739,118; 5,736,524; 5,679,647; WO 98/04720. Examples of DNA-based delivery technologies include "naked DNA", facilitated (bupivicaine, polymers, peptide-mediated) delivery, cationic lipid complexes, and particle-mediated ("gene gun") or pressure-mediated delivery (see, e.g., U.S. Patent No. 5,922,687). For therapeutic or prophylactic immunization purposes, proteins of the invention can be expressed via viral or bacterial vectors. Various viral gene delivery systems that can be used in the practice of the invention include, but are not limited to, vaccinia, fowlpox, canarypox, adenovirus, influenza, poliovirus, adeno-associated virus, lentivirus, and sindbis virus (see, e.g., Restifo, 1996, Curr. Opin. Immunol. 8:658-663; Tsang et al. J. Natl. Cancer Inst. 87:982-990 (1995)). Non-viral delivery systems can also be employed by introducing naked DNA encoding a 98P4B6-related protein into the patient (e.g., intramuscularly or intradermally) to induce an anti-tumor response. Vaccinia virus is used, for example, as a vector to express nucleotide sequences that encode the peptides of the invention. Upon introduction into a host, the recombinant vaccinia virus expresses the protein immunogenic peptide, and thereby elicits a host immune response. Vaccinia vectors and methods useful in immunization protocols are described in, e.g., U.S. Patent No. 4,722,848. Another vector is BCG (Bacille Calmette Guerin). BCG vectors are described in Stover et al, Nature 351:456-460 (1991). A wide variety of other vectors useful for therapeutic administration or immunization of the peptides of the invention, e.g. adeno and adeno-associated virus vectors, retroviral vectors, Salmonella typhivectors, detoxified anthrax toxin vectors, and the like, will be apparent to those skilled in the art from the description herein. Thus, gene delivery systems are used to deliver a 98P4B-related nucleic acid molecule. In one embodiment, the full length human 98P4B6 cDNA is employed. In another embodiment, 98P4B6 nucleic acid molecules encoding specific cytotoxic T lymphocyte (CTL) and/or antibody epitopes are employed. Ex Vivo Vaccines Various ex vivo strategies can also be employed to generate an immune response. One approach involves the use of antigen presenting cells (APCs) such as dendritic cells (DC) to present 98P4B6 antigen to a patients immune system. Dendritic cells express MHC class I and II molecules, B7 co-stimulator, and IL-12, and are thus highly specialized antigen presenting cells. In prostate cancer, autologous dendritic cells pulsed with peptides of the prostate-specific membrane antigen (PSMA) are being used in a Phase I clinical trial to stimulate prostate cancer patients' immune systems (Tjoa et al., 1996, Prostate 28:65 69; Murphy et atl, 1996, Prostate 29:371-380). Thus, dendritic cells can be used to present 98P4B6 peptides to T cells in the context of MHC class I or II molecules. In one embodiment, autologous dendritic cells are pulsed with 98P4B6 peptides capable of binding to MHC class I and/or class 11 molecules. In another embodiment, dendritic cells are pulsed with the complete 98P4B6 protein. Yet another embodiment involves engineering the overexpression of a 98P486 gene in dendritic cells using various implementing vectors known in the art, such as adenovirus (Arthur et al., 1997, Cancer Gene Ther. 4:17 25), retrovirus (Henderson et al., 1996, Cancer Res. 56:3763-3770), lentivirus, adeno-associated virus, DNA transfection (Ribas et al, 1997, Cancer Res. 57:2865-2869), or tumor-derived RNA transfection (Ashley et al., 1997, J. Exp. Med. 186:1177-1182). Cells that express 98P486 can also be engineered to express immune modulators, such as GM-CSF, and used as immunizing agents. X.B.) 98P4B6 as a Target for Antibody-based Therapy 58 WO 03/087306 PCT/USO3/10462 98P4B6 is an attractive target for antibody-based therapeutic strategies. A number of antibody strategies are known in the art for targeting both extracellular and intracellular molecules (see, e.g., complement and ADCC mediated killing as well as the use of intrabodies). Because 98P4B6 is expressed by cancer cells of various lineages relative to corresponding normal cells, systemic administration of 98P4B6-immunoreactive compositions are prepared that exhibit excellent sensitivity without toxic, non-specific and/or non-target effects caused by binding of the immunoreactive composition to non-target organs and tissues. Antibodies specifically reactive with domains of 98P4B6 are useful to treat 98P4B6-expressing cancers systemically, either as conjugates with a toxin or therapeutic agent, or as naked antibodies capable of inhibiting cell proliferation or function. 98P4B6 antibodies can be introduced into a patient such that the antibody binds to 98P4B6 and modulates a function, such as an interaction with a binding partner, and consequently mediates destruction of the tumor cells and/or inhibits the growth of the tumor cells. Mechanisms by which such antibodies exert a therapeutic effect can include complement-mediated cytolysis, antibody-dependent cellular cytotoxicity, modulation of the physiological function of 98P4B6, inhibition of ligand binding or signal transduction pathways, modulation of tumor cell differentiation, alteration of tumor angiogenesis factor profiles, and/or apoptosis. Those skilled in the art understand that antibodies can be used to specifically target and bind immunogenic molecules such as an immunogenic region of a 98P4B6 sequence shown in Figure 2 or Figure 3. In addition, skilled artisans understand that it is routine to conjugate antibodies to cytotoxic agents (see, e.g., Slevers et al Blood 93:11 3678-3684 (June 1, 1999)). When cytotoxic and/or therapeutic agents are delivered directly to cells, such as by conjugating them to antibodies specific for a molecule expressed by that cell (e.g. 98P4B6), the cytotoxic agent will exert its known biological effect (i.e. cytotoxicity) on those cells. A wide variety of compositions and methods for using antibody-cytotoxic agent conjugates to kill cells are known in the art. In the context of cancers, typical methods entail administering to an animal having a tumor a biologically effective amount of a conjugate comprising a selected cytotoxic and/or therapeutic agent linked to a targeting agent (e.g. an anti 98P4B6 antibody) that binds to a marker (e.g. 98P4B6) expressed, accessible to binding or localized on the cell surfaces. A typical embodiment is a method of delivering a cytotoxic and/or therapeutic agent to a cell expressing 98P4B6, comprising conjugating the cytotoxic agent to an antibody that immunospecifically binds to a 98P4B6 epitope, and, exposing the cell to the antibody-agent conjugate. Another illustrative embodiment is a method of treating an individual suspected of suffering from metastasized cancer, comprising a step of administering parenterally to said individual a pharmaceutical composition comprising a therapeutically effective amount of an antibody conjugated to a cytotoxic and/or therapeutic agent. Cancer immunotherapy using anti-98P4B6 antibodies can be done in accordance with various approaches that have been successfully employed in the treatment of other types of cancer, including but not limited to colon cancer (Arlen et al, 1998, Crit. Rev. Immunol. 18:133-138), multiple myeloma (Ozaki et al, 1997, Blood 90:3179-3186, Tsunenari et al., 1997, Blood 90:2437-2444), gastric cancer (Kasprzyk et al, 1992, Cancer Res. 52:2771-2776), B-cell lymphoma (Funakoshi etal., 1996, J. Immunother. Emphasis Tumor Immunol. 19:93-101), leukemia (Zhong etal., 1996, Leuk. Res. 20:581-589), colorectal cancer (Moun et al., 1994, Cancer Res. 54:6160-6166; Velders et al., 1995, Cancer Res. 55:4398-4403), and breast cancer (Shepard et al., 1991,-J. Clin. Immunol. 11:117-127). Some therapeutic approaches involve conjugation of naked antibody to a toxin or radioisotope, such as the conjugation of Y9 or I13 to anti-CD20 antibodies (e.g., ZevalinTM, IDEC Pharmaceuticals Corp. or Bexxar

T

, Coulter Pharmaceuticals), while others involve co-administration of antibodies and other therapeutic agents, such as Herceptin

T

M (trastuzumab) with paclitaxel (Genentech, Inc.). The antibodies can be conjugated to a therapeutic agent. To treat prostate cancer, for example, 98P4B6 antibodies can be administered in conjunction with radiation, chemotherapy or hormone ablation. Also, antibodies can be conjugated to a toxin such as calicheamicin (e.g., Mylotarg

T

, Wyeth-Ayerst, Madison, NJ, a recombinant humanized IgG4 kappa antibody conjugated to antitumor antibiotic 59 WO 03/087306 PCT/US03/10462 calicheamicin) or a maytansinoid (e.g., taxane-based Tumor-Activated Prodrug, TAP, platform, ImmunoGen, Cambridge, MA, also see e.g., US Patent 5,416,064). Although 98P4B6 antibody therapy is useful for all stages of cancer, antibody therapy can be particularly appropriate in advanced or metastatic cancers. Treatment with the antibody therapy of the invention is indicated for patients who have received one or more rounds of chemotherapy. Alternatively, antibody therapy of the invention is combined with a chemotherapeutic or radiation regimen for patients who have not received chemotherapeutic treatment. Additionally, antibody therapy can enable the use of reduced dosages of concomitant chemotherapy, particularly for patients who do not tolerate the toxicity of the chemotherapeutic agent very well. Fan et al. (Cancer Res. 53:4637-4642, 1993), Prewett et al. (International J. of Onco. 9:217-224, 1996), and Hancock et al. (Cancer Res. 51:4575-4580, 1991) describe the use of various antibodies together with chemotherapeutic agents. Although 98P4B6 antibody therapy is useful for all stages of cancer, antibody therapy can be particularly appropriate in advanced or metastatic cancers. Treatment with the antibody therapy of the invention is indicated for patients who have received one or more rounds of chemotherapy. Alternatively, antibody therapy of the invention is combined with a chemotherapeutic or radiation regimen for patients who have not received chemotherapeutic treatment. Additionally, antibody therapy can enable the use of reduced dosages of concomitant chemotherapy, particularly for patients who do not tolerate the toxicity of the chemotherapeutic agent very well. Cancer patients can be evaluated for the presence and level of 98P4B6 expression, preferably using immunohistochemical assessments of tumor tissue, quantitative 98P4B6 imaging, or other techniques that reliably indicate the presence and degree of 98P4B6 expression. Immunohistochemical analysis of tumor biopsies or surgical specimens is preferred for this purpose. Methods for immunohistochemical analysis of tumor tissues are well known in the art. Anti-98P4B6 monoclonal antibodies that treat prostate and other cancers include those that initiate a potent immune response against the tumor or those that are directly cytotoxic. In this regard, anti-98P4B6 monoclonal antibodies (mAbs) can elicit tumor cell lysis by either complement-mediated or antibody-dependent cell cytotoxicity (ADCC) mechanisms, both of which require an intact Fc portion of the immunoglobulin molecule for interaction with effector cell Fc receptor sites on complement proteins. In addition, anti-98P4B6 mAbs that exert a direct biological effect on tumor growth are useful to treat cancers that express 98P4B6. Mechanisms by which directly cytotoxic mAbs act include: inhibition of cell growth, modulation of cellular differentiation, modulation of tumor angiogenesis factor profiles, and the induction of apoptosis. The mechanism(s) by which a particular anti-98P4B6 mAb exerts an anti-tumor effect is evaluated using any number of in vitro assays that evaluate cell death such as ADCC, ADMMC, complement-mediated cell lysis, and so forth, as is generally known in the art. In some patients, the use of murine or other non-human monoclonal antibodies, or human/mouse chimeric mAbs can induce moderate to strong immune responses against the non-human antibody. This can result in clearance of the antibody from circulation and reduced efficacy. In the most severe cases, such an immune response can lead to the extensive formation of immune complexes which, potentially, can cause renal failure. Accordingly, preferred monoclonal antibodies used in the therapeutic methods of the invention are those that are either fully human or humanized and that bind specifically to the target 98P4B6 antigen with high affinity but exhibit low or no antigenicity in the patient. Therapeutic methods of the invention contemplate the administration of single anti-98P4B6 mAbs as well as combinations, or cocktails, of different mAbs. Such mAb cocktails can have certain advantages inasmuch as they contain mAbs that target different epitopes, exploit different effector mechanisms or combine directly cytotoxic mAbs with mAbs that rely on immune effector functionality. Such mAbs in combination can exhibit synergistic therapeutic effects. In addition, anti 98P4B6 mAbs can be administered concomitantly with other therapeutic modalities, including but not limited to various chemotherapeutic agents, androgen-blockers, immune modulators (e.g., IL-2, GM-CSF), surgery or radiation. The anti 60 WO 03/087306 PCT/US03/10462 98P4B6 mAbs are administered in their "naked" or unconjugated form, or can have a therapeutic agent(s) conjugated to them. Anti-98P4B6 antibody formulations are administered via any route capable of delivering the antibodies to a tumor cell. Routes of administration include, but are not limited to, intravenous, intraperitoneal, intramuscular, intratumor, intradermal, and the like. Treatment generally involves repeated administration of the anti-98P486 antibody preparation, via an acceptable route of administration such as intravenous injection (IV), typically at a dose in the range of about 0.1, .2, .3, .4, .5,.6,.7,.8,.9., 1, 2, 3, 4, 5, 6, 7, 8, 9,10,15, 20, or 25 mg/kg body weight. In general, doses in the range of 10-1000 mg mAb per week are effective and well tolerated. Based on clinical experience with the HerceptinTM mAb in the treatment of metastatic breast cancer, an initial loading dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mg/kg IV of the anti 98P4B6 mAb preparation represents an acceptable dosing regimen. Preferably, the initial loading dose is administered as a 90-minute or longer infusion. The periodic maintenance dose is administered as a 30 minute or longer infusion, provided the initial dose was well tolerated. As appreciated by those of skill in the art, various factors can influence the ideal dose regimen in a particular case. Such factors include, for example, the binding affinity and half life of the Ab or mAbs used, the degree of 98P4B6 expression in the patient, the extent of circulating shed 98P4B6 antigen, the desired steady-state antibody concentration level, frequency of treatment, and the influence of chemotherapeutic or other agents used in combination with the treatment method of the invention, as well as the health status of a particular patient. Optionally, patients should be evaluated for the levels of 98P4B6 in a given sample (e.g. the levels of circulating 98P4B6 antigen and/or 98P4B6 expressing cells) in order to assist in the determination of the most effective dosing regimen, etc. Such evaluations are also used for monitoring purposes throughout therapy, and are useful to gauge therapeutic success in combination with the evaluation of other parameters (for example, urine cytology and/or ImmunoCyt levels in bladder cancer therapy, or by analogy, serum PSA levels in prostate cancer therapy). Anti-idiotypic anti-98P4B6 antibodies can also be used in anti-cancer therapy as a vaccine for inducing an immune response to cells expressing a 98P4B6-related protein. In particular, the generation of anti-idiotypic antibodies is well known in the art; this methodology can readily be adapted to generate anti-idiotypic anti-98P4B6 antibodies that mimic an epitope on a 98P4B6-related protein (see, for example, Wagner et al., 1997, Hybridoma 16: 33-40; Foon et al., 1995, J. Clin. Invest. 96:334-342; Herlyn et al., 1996, Cancer Immunol. Immunother. 43:65-76). Such an anti-idiotypic antibody can be used in cancer vaccine strategies. X.C.) 98P4B6 as a Target for Cellular Immune Responses Vaccines and methods of preparing vaccines that contain an immunogenically effective amount of one or more HLA-binding peptides as described herein are further embodiments of the invention. Furthermore, vaccines in accordance with the invention encompass compositions of one or more of the claimed peptides. A peptide can be present in a vaccine individually. Alternatively, the peptide can exist as a homopolymer comprising multiple copies of the same peptide, or as a heteropolymer of various peptides. Polymers have the advantage of increased immunological reaction and, where different peptide epitopes are used to make up the polymer, the additional ability to induce antibodies and/or CTLs that react with different antigenic determinants of the pathogenic organism or tumor-related peptide targeted for an immune response. The composition can be a naturally occurring region of an antigen or can be prepared, e.g., recombinantly or by chemical synthesis. Carriers that can be used with vaccines of the invention are well known in the art, and include, e.g., thyroglobulin, albumins such as human serum albumin, tetanus toxoid, polyamino acids such as poly L-lysine, poly L-glutamic acid, influenza, hepatitis B virus core protein, and the like. The vaccines can contain a physiologically tolerable (i.e., acceptable) 61 WO 03/087306 PCT/US03/10462 diluent such as water, or saline, preferably phosphate buffered saline. The vaccines also typically include an adjuvant. Adjuvants such as incomplete Freund's adjuvant, aluminum phosphate, aluminum hydroxide, or alum are examples of materials well known in the art. Additionally, as disclosed herein, CTL responses can be primed by conjugating peptides of the invention to lipids, such as tripalmitoyl-S-glycerylcysteinlyseryl- serine (PaCSS). Moreover, an adjuvant such as a synthetic cytosine-phosphorothiolated-guanine-containing (CpG) oligonucleotides has been found to increase CTL responses 10- to 100-fold. (see, e.g. Davila and Celis, J. Immunol. 165:539-547 (2000)) Upon immunization with a peptide composition in accordance with the invention, via injection, aerosol, oral, transdermal, transmucosal, intrapleural, intrathecal, or other suitable routes, the immune system of the host responds to the vaccine by producing large amounts of CTLs and/or HTLs specific for the desired antigen. Consequently, the host becomes at least partially immune to later development of cells that express or overexpress 98P486 antigen, or derives at least some therapeutic benefit when the antigen was tumor-associated. In some embodiments, it may be desirable to combine the class I peptide components with components that induce or facilitate neutralizing antibody and or helper T cell responses directed to the target antigen. A preferred embodiment of such a composition comprises class I and class II epitopes in accordance with the invention. An alternative embodiment of such a composition comprises a class I and/or class II epitope in accordance with the invention, along with a cross reactive HTL epitope such as PADRE T M (Epimmune, San Diego, CA) molecule (described e.g., in U.S. Patent Number 5,736,142). A vaccine of the invention can also include antigen-presenting cells (APC), such as dendritic cells (DC), as a vehicle to present peptides of the invention. Vaccine compositions can be created in vitro, following dendritic cell mobilization and harvesting, whereby loading of dendritic cells occurs in vitro. For example, dendritic cells are transfected, e.g., with a minigene in accordance with the invention, or are pulsed with peptides. The dendritic cell can then be administered to a patient to elicit immune responses in vivo. Vaccine compositions, either DNA- or peptide-based, can also be administered in vivo in combination with dendritic cell mobilization whereby loading of dendritic cells occurs in vivo. Preferably, the following principles are utilized when selecting an array of epitopes for inclusion in a polyepitopic composition for use in a vaccine, or for selecting discrete epitopes to be included in a vaccine and/or to be encoded by nucleic acids such as a minigene. It is preferred that each of the following principles be balanced in order to make the selection. The multiple epitopes to be incorporated in a given vaccine composition may be, but need not be, contiguous in sequence in the native antigen from which the epitopes are derived. 1.) Epitopes are selected which, upon administration, mimic immune responses that have been observed to be correlated with tumor clearance. For HLA Class I this includes 3-4 epitopes that come from at least one tumor associated antigen (TAA). For HLA Class II a similar rationale is employed; again 3-4 epitopes are selected from at least one TAA (see, e.g., Rosenberg et al., Science 278:1447-1450). Epitopes from one TAA may be used in combination with epitopes from one or more additional TAAs to produce a vaccine that targets tumors with varying expression patterns of frequently-expressed TAAs. 2.) Epitopes are selected that have the requisite binding affinity established to be correlated with immunogenicity: for HLA Class I an ICso of 500 nM or less, often 200 nM or less; and for Class II an ICso of 1000 nM or less. 3.) Sufficient supermotif bearing-peptides, or a sufficient array of allele-specific motif-bearing peptides, are selected to give broad population coverage. For example, it is preferable to have at least 80% population coverage. A Monte Carlo analysis, a statistical evaluation known in the art, can be employed to assess the breadth, or redundancy of, population coverage. 4.) When selecting epitopes from cancer-related antigens it is often useful to select analogs because the patient may have developed tolerance to the native epitope. 62 WO 03/087306 PCT/USO3/10462 5.) Of particular relevance are epitopes referred to as "nested epitopes." Nested epitopes occur where at least two epitopes overlap in a given peptide sequence. A nested peptide sequence can comprise B cell, HLA class I and/or HLA class II epitopes. When providing nested epitopes, a general objective is to provide the greatest number of epitopes per sequence. Thus, an aspect is to avoid providing a peptide that is any longer than the amino terminus of the amino terminal epitope and the carboxyl terminus of the carboxyl terminal epitope in the peptide. When providing a multi-epitopic sequence, such as a sequence comprising nested epitopes, it is generally important to screen the sequence in order to insure that it does not have pathological or other deleterious biological properties. 6.) If a polyepitopic protein is created, or when creating a minigene, an objective is to generate the smallest peptide that encompasses the epitopes of interest. This principle is similar, if not the same as that employed when selecting a peptide comprising nested epitopes. However, with an artificial polyepitopic peptide, the size minimization objective is balanced against the need to integrate any spacer sequences between epitopes in the polyepitopic protein. Spacer amino acid residues can, for example, be introduced to avoid junctional epitopes (an epitope recognized by the immune system, not present in the target antigen, and only created by the man-made juxtaposition of epitopes), or to facilitate cleavage between epitopes and thereby enhance epitope presentation. Junctional epitopes are generally to be avoided because the recipient may generate an immune response to that non-native epitope. Of particular concern is a junctional epitope that is a "dominant epitope." A dominant epitope may lead to such a zealous response that immune responses to other epitopes are diminished or suppressed. 7.) Where the sequences of multiple variants of the same target protein are present, potential peptide epitopes can also be selected on the basis of their conservancy. For example, a criterion for conservancy may define that the entire sequence of an HLA class I binding peptide or the entire 9-mer core of a class 11 binding peptide be conserved in a designated percentage of the sequences evaluated for a specific protein antigen. X.C.1. Minigene Vaccines A number of different approaches are available which allow simultaneous delivery of multiple epitopes. Nucleic acids encoding the peptides of the invention are a particularly useful embodiment of the invention. Epitopes for inclusion in a minigene are preferably selected according to the guidelines set forth in the previous section. A preferred means of administering nucleic acids encoding the peptides of the invention uses minigene constructs encoding a peptide comprising one or multiple epitopes of the invention. The use of multi-epitope minigenes is described below and in, Ishioka et al., J. Immunol. 162:3915-3925, 1999; An, L. and Whitton, J. L., J. Virol 71:2292, 1997; Thomson, S. A. et aL, J. Immunol. 157:822, 1996; Whitton, J. L. et al., J. Virol. 67:348, 1993; Hanke, R. et al., Vaccine 16:426, 1998. For example, a multi-epitope DNA plasmid encoding supermotif and/or motif-bearing epitopes derived 98P4B6, the PADRE® universal helper T cell epitope or multiple HTL epitopes from 98P4B6 (see e.g., Tables VIII-XXI and XXII to XLIX), and an endoplasmic reticulum-translocating signal sequence can be engineered. A vaccine may also comprise epitopes that are derived from other TAAs. The immunogenicity of a multi-epitopic minigene can be confirmed in transgenic mice to evaluate the magnitude of CTL induction responses against the epitopes tested. Further, the immunogenicity of DNA-encoded epitopes in vivo can be correlated with the in vitro responses of specific CTL lines against target cells transfected with the DNA plasmid. Thus, these experiments can show that the minigene serves to both: 1.) generate a CTL response and 2.) that the induced CTLs recognized cells expressing the encoded epitopes. For example, to create a DNA sequence encoding the selected epitopes (minigene) for expression in human cells, the amino acid sequences of the epitopes may be reverse translated. A human codon usage table can be used to guide the codon choice for each amino acid. These epitope-encoding DNA sequences may be directly adjoined, so that when translated, a continuous polypeptide sequence is created. To optimize expression and/or immunogenicity, additional 63 WO 03/087306 PCT/US03/10462 elements can be incorporated into the minigene design. Examples of amino acid sequences that can be reverse translated and included in the minigene sequence include: HLA class I epitopes, HLA class II epitopes, antibody epitopes, a ubiquitination signal sequence, and/or an endoplasmic reticulum targeting signal. In addition, HLA presentation of CTL and HTL epitopes may be improved by including synthetic (e.g. poly-alanine) or naturally-occurring flanking sequences adjacent to the CTL or HTL epitopes; these larger peptides comprising the epitope(s) are within the scope of the invention. The minigene sequence may be converted to DNA by assembling oligonucleotides that encode the plus and minus strands of the minigene. Overlapping oligonucleotides (30-100 bases long) may be synthesized, phosphorylated, purified and annealed under appropriate conditions using well known techniques. The ends of the oligonucleotides can be joined, for example, using T4 DNA ligase. This synthetic minigene, encoding the epitope polypeptide, can then be cloned into a desired expression vector. Standard regulatory sequences well known to those of skill in the art are preferably included in the vector to ensure expression in the target cells. Several vector elements are desirable: a promoter with a down-stream cloning site for minigene insertion; a polyadenylation signal for efficient transcription termination; an E. coil origin of replication; and an E. coil selectable marker (e.g. ampicillin or kanamycin resistance). Numerous promoters can be used for this purpose, e.g., the human cytomegalovirus (hCMV) promoter. See, e.g., U.S. Patent Nos. 5,580,859 and 5,589,466 for other suitable promoter sequences. Additional vector modifications may be desired to optimize minigene expression and immunogenicity. In some cases, introns are required for efficient gene expression, and one or more synthetic or naturally-occurring introns could be incorporated into the transcribed region of the minigene. The inclusion of mRNA stabilization sequences and sequences for replication in mammalian cells may also be considered for increasing minigene expression. Once an expression vector is selected, the minigene is cloned into the polylinker region downstream of the promoter. This plasmid is transformed into an appropriate E cofi strain, and DNA is prepared using standard techniques. The orientation and DNA sequence of the minigene, as well as all other elements included in the vector, are confirmed using restriction mapping and DNA sequence analysis. Bacterial cells harboring the correct plasmid can be stored as a master cell bank and a working cell bank. In addition, immunostimulatory sequences (ISSs or CpGs) appear to play a role in the immunogenicity of DNA vaccines. These sequences may be included in the vector, outside the minigene coding sequence, if desired to enhance immunogenicity. In some embodiments, a bi-cistronic expression vector which allows production of both the minigene-encoded epitopes and a second protein (included to enhance or decrease immunogenicity) can be used. Examples of proteins or polypeptides that could beneficially enhance the immune response if co-expressed include cytokines (e.g., IL-2, IL-12, GM CSF), cytokine-inducing molecules (e.g., LelF), costimulatory molecules, or for HTL responses, pan-DR binding proteins

(PADRE

T M , Epimmune, San Diego, CA). Helper (HTL) epitopes can be joined to intracellular targeting signals and expressed separately from expressed CTL epitopes; this allows direction of the HTL epitopes to a cell compartment different than that of the CTL epitopes. If required, this could facilitate more efficient entry of HTL epitopes into the HLA class II pathway, thereby improving HTL induction. In contrast to HTL or CTL induction, specifically decreasing the immune response by co-expression of immunosuppressive molecules (e.g. TGF-3) may be beneficial in certain diseases. Therapeutic quantities of plasmid DNA can be produced for example, by fermentation in E. coli, followed by purification. Aliquots from the working cell bank are used to inoculate growth medium, and grown to saturation in shaker flasks or a bioreactor according to well-known techniques. Plasmid DNA can be purified using standard bioseparation technologies such as solid phase anion-exchange resins supplied by QIAGEN, Inc. (Valencia, California). If required, supercoiled DNA can be isolated from the open circular and linear forms using gel electrophoresis or other methods. 64 WO 03/087306 PCT/US03/10462 Purified plasmid DNA can be prepared for injection using a variety of formulations. The simplest of these is reconstitution of lyophilized DNA in sterile phosphate-buffer saline (PBS). This approach, known as "naked DNA," is currently being used for intramuscular (IM) administration in clinical trials. To maximize the immunotherapeutic effects of minigene DNA vaccines, an alternative method for formulating purified plasmid DNA may be desirable. A variety of methods have been described, and new techniques may become available. Cationic lipids, glycolipids, and fusogenic liposomes can also be used in the formulation (see, e.g., as described by WO 93124640; Mannino & Gould-Fogerite, BioTechniques 6(7): 682 (1988); U.S. Pat No. 5,279,833; WO 91/06309; and FeIgner, et aL., Proc. Nat'l Acad. Sci. USA 84;7413 (1987). In addition, peptides and compounds referred to collectively as protective, interactive, non-condensing compounds (PINC) could also be complexed to purified plasmid DNA to influence variables such as stability, intramuscular dispersion, or trafficking to specific organs or cell types. Target cell sensitization can be used as a functional assay for expression and HLA class I presentation of minigene-encoded CTL epitopes. For example, the plasmid DNA is introduced into a mammalian cell line that is suitable as a target for standard CTL chromium release assays. The transfection method used will be dependent on the final formulation. Electroporation can be used for "naked" DNA, whereas cationic lipids allow direct in vitro transfection. A plasmid expressing green fluorescent protein (GFP) can be co-transfected to allow enrichment of transfected cells using fluorescence activated cell sorting (FACS). These cells are then chromium-51 ( 5 'Cr) labeled and used as target cells for epitope-specific CTL lines; cytolysis, detected by 51 Cr release, indicates both production of, and HLA presentation of, minigene-encoded CTL epitopes. Expression of HTL epitopes may be evaluated in an analogous manner using assays to assess HTL activity. In vivo immunogenicity is a second approach for functional testing of minigene DNA formulations. Transgenic mice expressing appropriate human HLA proteins are immunized with the DNA product. The dose and route of administration are formulation dependent (e.g., IM for DNA in PBS, intraperitoneal (i.p.) for lipid-complexed DNA). Twenty-one days after immunization, splenocytes are harvested and restimulated for one week in the presence of peptides encoding each epitope being tested. Thereafter, for CTL effector cells, assays are conducted for cytolysis of peptide-loaded, 5 1 Cr-labeled target cells using standard techniques. Lysis of target cells that were sensitized by HLA loaded with peptide epitopes, corresponding to minigene-encoded epitopes, demonstrates DNA vaccine function for in vivo induction of CTLs. Immunogenicity of HTL epitopes is confirmed in transgenic mice in an analogous manner. Alternatively, the nucleic acids can be administered using ballistic delivery as described, for instance, in U.S. Patent No. 5,204,253. Using this technique, particles comprised solely of DNA are administered. In a further alternative embodiment, DNA can be adhered to particles, such as gold particles. Minigenes can also be delivered using other bacterial or viral delivery systems well known in the art, e.g., an expression construct encoding epitopes of the invention can be incorporated into a viral vector such as vaccinia. X.C.2. Combinations of CTL Peptides with Helper Peptides Vaccine compositions comprising CTL peptides of the invention can be modified, e.g., analoged, to provide desired attributes, such as improved serum half life, broadened population coverage or enhanced immunogenicity. For instance, the ability of a peptide to induce CTL activity can be enhanced by linking the peptide to a sequence which contains at least one epitope that is capable of inducing a T helper cell response. Although a CTL peptide can be directly linked to a T helper peptide, often CTL epitope/HTL epitope conjugates are linked by a spacer molecule. The spacer is typically comprised of relatively small, neutral molecules, such as amino acids or amino acid mimetics, which are substantially uncharged under physiological conditions. The spacers are typically selected from, e.g., Ala, Gly, or other neutral spacers of nonpolar amino acids or neutral polar amino acids. It will be understood that the optionally present spacer need not be comprised of the same residues and thus may be a hetero- or homo-oligomer. When present, the spacer will 65 WO 03/087306 PCT/US03/10462 usually be at least one or two residues, more usually three to six residues and sometimes 10 or more residues. The CTL peptide epitope can be linked to the T helper peptide epitope either directly or via a spacer either at the amino or carboxy terminus of the CTL peptide. The amino terminus of either the immunogenic peptide or the T helper peptide may be acylated. In certain embodiments, the T helper peptide is one that is recognized by T helper cells present in a majority of a genetically diverse population. This can be accomplished by selecting peptides that bind to many, most, or all of the HLA class II molecules. Examples of such amino acid bind many HLA Class II molecules include sequences from antigens such as tetanus toxoid at positions 830-843 (QYIKANSKFIGITE; SEQ ID NO: 97), Plasmodium falciparum circumsporozoite (CS) protein at positions 378-398 (DIEKKIAKMEKASSVFNWNS; SEQ ID NO: 98), and Streptococcus l8kD protein at positions 116-131 (GAVDSILGGVATYGAA; SEQ ID NO: 99). Other examples include peptides bearing a DR 1-4-7 supermotif, or either of the DR3 motifs. Alternatively, it is possible to prepare synthetic peptides capable of stimulating T helper lymphocytes, in a loosely HLA-restricted fashion, using amino acid sequences not found in nature (see, e.g., PCT publication WO 95/07707). These synthetic compounds called Pan-DR-binding epitopes (e.g., PADRE T M , Epimmune, Inc., San Diego, CA) are designed, most preferably, to bind most HLA-DR (human HLA class II) molecules. For instance, a pan-DR-binding epitope peptide having the formula: XKXVAAWTLKAAX (SEQ ID NO: 100), where "X" is either cyclohexylalanine, phenylalanine, or tyrosine, and a is either D-alanine or L-alanine, has been found to bind to most HLA-DR alleles, and to stimulate the response of T helper lymphocytes from most individuals, regardless of their HLA type. An alternative of a pan-DR binding epitope comprises all "L" natural amino acids and can be provided in the form of nucleic acids that encode the epitope. HTL peptide epitopes can also be modified to alter their biological properties. For example, they can be modified to include D-amino acids to increase their resistance to proteases and thus extend their serum half life, or they can be conjugated to other molecules such as lipids, proteins, carbohydrates, and the like to increase their biological activity. For example, a T helper peptide can be conjugated to one or more palmitic acid chains at either the amino or carboxyl termini. X.C.3. Combinations of CTL Peptides with T Cell Priming Agents In some embodiments it may be desirable to include in the pharmaceutical compositions of the invention at least one component which primes B lymphocytes or T lymphocytes. Lipids have been identified as agents capable of priming CTL in vivo. For example, palmitic acid residues can be attached to the e-and c- amino groups of a lysine residue and then linked, e.g., via one or more linking residues such as Gly, Gly-Gly-, Ser, Ser-Ser, or the like, to an immunogenic peptide. The lipidated peptide can then be administered either directly in a micelle or particle, incorporated into a liposome, or emulsified in an adjuvant, e.g., incomplete Freund's adjuvant. In a preferred embodiment, a particularly effective immunogenic composition comprises palmitic acid attached to e- and a- amino groups of Lys, which is attached via linkage, e.g., Ser-Ser, to the amino terminus of the immunogenic peptide. As another example of lipid priming of CTL responses, E. colilipoproteins, such as tripalmitoyl-S glycerylcysteinlyseryl- serine (P3CSS) can be used to prime virus specific CTL when covalently attached to an appropriate peptide (see, e.g., Deres, et al., Nature 342:561, 1989). Peptides of the invention can be coupled to PaCSS, for example, and the lipopeptide administered to an individual to prime specifically an immune response to the target antigen. Moreover, because the induction of neutralizing antibodies can also be primed with P3CSS-conjugated epitopes, two such compositions can be combined to more effectively elicit both humoral and cell-mediated responses. X.C.4. Vaccine Compositions Comprising DC Pulsed with CTL andlor HTL Peptides An embodiment of a vaccine composition in accordance with the invention comprises ex vivo administration of a cocktail of epitope-bearing peptides to PBMC, or isolated DC therefrom, from the patient's blood. A pharmaceutical to facilitate harvesting of DC can be used, such as Progenipoietin T M (Pharmacia-Monsanto, St. Louis, MO) or GM-CSF/IL-4. 66 WO 03/087306 PCT/US03/10462 After pulsing the DC with peptides and prior to reinfusion into patients, the DC are washed to remove unbound peptides. In this embodiment, a vaccine comprises peptide-pulsed DCs which present the pulsed peptide epitopes complexed with HLA molecules on their surfaces. The DC can be pulsed ex vivo with a cocktail of peptides, some of which stimulate CTL responses to 98P4B6. Optionally, a helper T cell (HTL) peptide, such as a natural or artificial loosely restricted HLA Class II peptide, can be included to facilitate the CTL response. Thus, a vaccine in accordance with the invention is used to treat a cancer which expresses or overexpresses 98P4B6. X.D. Adoptive Immunotherapy Antigenic 98P4B6-related peptides are used to elicit a CTL and/or HTL response ex vivo, as well. The resulting CTL or HTL cells, can be used to treat tumors in patients that do not respond to other conventional forms of therapy, or will not respond to a therapeutic vaccine peptide or nucleic acid in accordance with the invention. Ex vivo CTL or HTL responses to a particular antigen are induced by incubating in tissue culture the patient's, or genetically compatible, CTL or HTL precursor cells together with a source of antigen-presenting cells (APC), such as dendritic cells, and the appropriate immunogenic peptide. After an appropriate incubation time (typically about 7-28 days), in which the precursor cells are activated and expanded into effector cells, the cells are infused back into the patient, where they will destroy (CTL) or facilitate destruction (HTL) of their specific target cell (e.g., a tumor cell). Transfected dendritic cells may also be used as antigen presenting cells. X.E. Administration of Vaccines for Therapeutic or Prophylactic Purposes Pharmaceutical and vaccine compositions of the invention are typically used to treat and/or prevent a cancer that expresses or overexpresses 98P4B6. In therapeutic applications, peptide and/or nucleic acid compositions are administered to a patient in an amount sufficient to elicit an effective B cell, CTL and/or HTL response to the antigen and to cure or at least partially arrest or slow symptoms and/or complications. An amount adequate to accomplish this is defined as "therapeutically effective dose." Amounts effective for this use will depend on, e.g., the particular composition administered, the manner of administration, the stage and severity of the disease being treated, the weight and general state of health of the patient, and the judgment of the prescribing physician. For pharmaceutical compositions, the immunogenic peptides of the invention, or DNA encoding them, are generally administered to an individual already bearing a tumor that expresses 98P4B6. The peptides or DNA encoding them can be administered individually or as fusions of one or more peptide sequences. Patients can be treated with the immunogenic peptides separately or in conjunction with other treatments, such as surgery, as appropriate. For therapeutic use, administration should generally begin at the first diagnosis of 98P4B6-associated cancer. This is followed by boosting doses until at least symptoms are substantially abated and for a period thereafter. The embodiment of the vaccine composition (i.e., including, but not limited to embodiments such as peptide cocktails, polyepitopic polypeptides, minigenes, or TAA-specific CTLs or pulsed dendritic cells) delivered to the patient may vary according to the stage of the disease or the patient's health status. For example, in a patient with a tumor that expresses 98P4B6, a vaccine comprising 98P4B6-specific CTL may be more efficacious in killing tumor cells in patient with advanced disease than alternative embodiments. It is generally important to provide an amount of the peptide epitope delivered by a mode of administration sufficient to stimulate effectively a cytotoxic T cell response; compositions which stimulate helper T cell responses can also be given in accordance with this embodiment of the invention. 67 WO 03/087306 PCT/US03/10462 The dosage for an initial therapeutic immunization generally occurs in a unit dosage range where the lower value is about 1, 5, 50, 500, or 1,000 pg and the higher value is about 10,000; 20,000; 30,000; or 50,000 pg. Dosage values for a human typically range from about 500 pg to about 50,000 pg per 70 kilogram patient. Boosting dosages of between about 1.0 pg to about 50,000 pg of peptide pursuant to a boosting regimen over weeks to months may be administered depending upon the patient's response and condition as determined by measuring the specific activity of CTL and HTL obtained from the patient's blood. Administration should continue until at least clinical symptoms or laboratory tests indicate that the neoplasia, has been eliminated or reduced and for a period thereafter. The dosages, routes of administration, and dose schedules are adjusted in accordance with methodologies known in the art. In certain embodiments, the peptides and compositions of the present invention are employed in serious disease states, that is, life-threatening or potentially life threatening situations. In such cases, as a result of the minimal amounts of extraneous substances and the relative nontoxic nature of the peptides in preferred compositions of the invention, it is possible and may be felt desirable by the treating physician to administer substantial excesses of these peptide compositions relative to these stated dosage amounts. The vaccine compositions of the invention can also be used purely as prophylactic agents. Generally the dosage for an initial prophylactic immunization generally occurs in a unit dosage range where the lower value is about 1, 5, 50, 500, or 1000 pg and the higher value is about 10,000; 20,000; 30,000; or 50,000 pg. Dosage values for a human typically range from about 500 pg to about 50,000 pg per 70 kilogram patient. This is followed by boosting dosages of between about 1.0 pg to about 50,000 pg of peptide administered at defined intervals from about four weeks to six months after the initial administration of vaccine. The immunogenicity of the vaccine can be assessed by measuring the specific activity of CTL and HTL obtained from a sample of the patients blood. The pharmaceutical compositions for therapeutic treatment are intended for parenteral, topical, oral, nasal, intrathecal, or local (e.g. as a cream or topical ointment) administration. Preferably, the pharmaceutical compositions are administered parentally, e.g., intravenously, subcutaneously, intradermally, or intramuscularly. Thus, the invention provides compositions for parenteral administration which comprise a solution of the immunogenic peptides dissolved or suspended in an acceptable carrier, preferably an aqueous carrier. A variety of aqueous carriers may be used, e.g., water, buffered water, 0.8% saline, 0.3% glycine, hyaluronic acid and the like. These compositions may be sterilized by conventional, well-known sterilization techniques, or may be sterile filtered. The resulting aqueous solutions may be packaged for use as is, or lyophilized, the lyophilized preparation being combined with a sterile solution prior to administration. The compositions may contain pharmaceutically acceptable auxiliary substances as required to approximate physiological conditions, such as pH-adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservatives, and the like, for example, sodium acetate, sodium lactate, sodium chloride, potassium chloride, calcium chloride, sorbitan monolaurate, triethanolamine oleate, etc. The concentration of peptides of the invention in the pharmaceutical formulations can vary widely, i.e., from less than about 0.1%, usually at or at least about 2% to as much as 20% to 50% or more by weight, and will be selected primarily by fluid volumes, viscosities, etc., in accordance with the particular mode of administration selected. A human unit dose form of a composition is typically included in a pharmaceutical composition that comprises a human unit dose of an acceptable carrier, in one embodiment an aqueous carrier, and is administered in a volume/quantity that is known by those of skill in the art to be used for administration of such compositions to humans (see, e.g., Remington's Pharmaceutical Sciences, 17 t h Edition, A. Gennaro, Editor, Mack Publishing Co., Easton, Pennsylvania, 1985). For example a peptide dose for initial immunization can be from about 1 to about 50,000 pg, generally 100-5,000 pg, for a 70 kg patient. For example, for nucleic acids an initial immunization may be performed using an expression vector in the form of naked 68 WO 03/087306 PCT/USO3/10462 nucleic acid administered IM (or SC or ID) in the amounts of 0.5-5 mg at multiple sites. The nucleic acid (0.1 to 1000 hg) can also be administered using a gene gun. Following an incubation period of 3-4 weeks, a booster dose is then administered. The booster can be recombinant fowlpox virus administered at a dose of 5-107 to 5x1i09 pfu. For antibodies, a treatment generally involves repeated administration of the anti-98P4B6 antibody preparation, via an acceptable route of administration such as intravenous injection (IV), typically at a dose in the range of about 0.1 to about 10 mg/kg body weight. In general, doses in the range of 10-500 mg mAb per week are effective and well tolerated. Moreover, an initial loading dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mg/kg IV of the anti- 98P4B6 mAb preparation represents an acceptable dosing regimen. As appreciated by those of skill in the art, various factors can influence the ideal dose in a particular case. Such factors include, for example, half life of a composition, the binding affinity of an Ab, the immunogenicity of a substance, the degree of 98P4B6 expression in the patient, the extent of circulating shed 98P4B6 antigen, the desired steady-state concentration level, frequency of treatment, and the influence of chemotherapeutic or other agents used in combination with the treatment method of the invention, as well as the health status of a particular patient. Non-limiting preferred human unit doses are, for example, 500pg - 1mg, img - 50mg, 50mg - 100mg, 100mg - 200mg, 200mg - 300mg, 400mg - 500mg, 500mg - 600mg, 600mg -700mg, 700mg 800mg, 800mg-900mg, 900mg - ig, or 1mg- 700mg. In certain embodiments, the dose is in a range of 2-5 mg/kg body weight, e.g., with follow on weekly doses of 1-3 mg/kg; 0.5mg, 1, 2, 3, 4, 5, 6, 7, 8, 9, 10mg/kg body weight followed, e.g., in two, three or four weeks by weekly doses; 0.5 - 10mg/kg body weight, e.g., followed in two, three or four weeks by weekly doses; 225, 250, 275, 300, 325, 350, 375, 400mg m 2 of body area weekly; 1-600mg m 2 of body area weekly; 225-400mg m 2 of body area weekly; these does can be followed by weekly doses for 2, 3, 4, 5, 6, 7, 8, 9, 19, 11, 12 or more weeks. In one embodiment, human unit dose forms of polynucleotides comprise a suitable dosage range or effective amount that provides any therapeutic effect. As appreciated by one of ordinary skill in the art a therapeutic effect depends on a number of factors, including the sequence of the polynucleotide, molecular weight of the polynucleotide and route of administration. Dosages are generally selected by the physician or other health care professional in accordance with a variety of parameters known in the art, such as severity of symptoms, history of the patient and the like. Generally, for a polynucleotide of about 20 bases, a dosage range may be selected from, for example, an independently selected lower limit such as about 0.1, 0.25, 0.5, 1,2, 5, 10, 20, 30, 40, 50, 60, 70, 80, 90, 100, 200, 300, 400 or 500 mg/kg up to an independently selected upper limit, greater than the lower limit, of about 60, 80, 100, 200, 300, 400, 500, 750, 1000, 1500, 2000, 3000, 4000, 5000, 6000, 7000, 8000, 9000 or 10,000 mg/kg. For example, a dose may be about any of the following: 0.1 to 100 mg/kg, 0.1 to 50 mg/kg, 0.1 to 25 mg/kg, 0.1 to 10 mg/kg, 1 to 500 mg/kg, 100 to 400 mg/kg, 200 to 300 mg/kg, 1 to 100 mg/kg, 100 to 200 mg/kg, 300 to 400 mg/kg, 400 to 500 mg/kg, 500 to 1000 mg/kg, 500 to 5000 mg/kg, or 500 to 10,000 mg/kg. Generally, parenteral routes of administration may require higher doses of polynucleotide compared to more direct application to the nucleotide to diseased tissue, as do polynucleotides of increasing length. In one embodiment, human unit dose forms of T-cells comprise a suitable dosage range or effective amount that provides any therapeutic effect. As appreciated by one of ordinary skill in the art, a therapeutic effect depends on a number of factors. Dosages are generally selected by the physician or other health care professional in accordance with a variety of parameters known in the art, such as severity of symptoms, history of the patient and the like. A dose may be about 104 cells to about 106 cells, about 106 cells to about 108 cells, about 108 to about 101l cells, or about 108 to about 5 x 1010 cells. A dose may also about 106 cells/m 2 to about 10 o 0 cells/m 2 , or about 106 cells/m 2 to about 108 cells/m2. Proteins(s) of the invention, and/or nucleic acids encoding the protein(s), can also be administered via liposomes, which may also serve to: 1) target the proteins(s) to a particular tissue, such as lymphoid tissue; 2) to target selectively to diseases cells; or, 3) to increase the half-life of the peptide composition. Liposomes include emulsions, foams, micelles, insoluble monolayers, liquid crystals, phospholipid dispersions, lamellar layers and the like. In these preparations, the 69 WO 03/087306 PCT/US03/10462 peptide to be delivered is incorporated as part of a liposome, alone or in conjunction with a molecule which binds to a receptor prevalent among lymphoid cells, such as monoclonal antibodies which bind to the CD45 antigen, or with other therapeutic or immunogenic compositions. Thus, liposomes either filled or decorated with a desired peptide of the invention can be directed to the site of lymphoid cells, where the liposomes then deliver the peptide compositions. Liposomes for use in accordance with the invention are formed from standard vesicle-forming lipids, which generally include neutral and negatively charged phospholipids and a sterol, such as cholesterol. The selection of lipids is generally guided by consideration of, e.g., liposome size, acid lability and stability of the liposomes in the blood stream. A variety of methods are available for preparing liposomes, as described in, e.g., Szoka, et aL, Ann. Rev. Biophys. Bioeng. 9:467 (1980), and U.S. Patent Nos. 4,235,871, 4,501,728, 4,837,028, and 5,019,369. For targeting cells of the immune system, a ligand to be incorporated into the liposome can include, e.g., antibodies or fragments thereof specific for cell surface determinants of the desired immune system cells. A liposome suspension containing a peptide may be administered intravenously, locally, topically, etc. in a dose which varies according to, inter alia, the manner of administration, the peptide being delivered, and the stage of the disease being treated. For solid compositions, conventional nontoxic solid carriers may be used which include, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharin, talcum, cellulose, glucose, sucrose, magnesium carbonate, and the like. For oral administration, a pharmaceutically acceptable nontoxic composition is formed by incorporating any of the normally employed excipients, such as those carriers previously listed, and generally 10 95% of active ingredient, that is, one or more peptides of the invention, and more preferably at a concentration of 25%-75%. For aerosol administration, immunogenic peptides are preferably supplied in finely divided form along with a surfactant and propellant. Typical percentages of peptides are about 0.01%-20% by weight, preferably about 1%-10%. The surfactant must, of course, be nontoxic, and preferably soluble in the propellant. Representative of such agents are the esters or partial esters of fatty acids containing from about 6 to 22 carbon atoms, such as caproic, octanoic, lauric, palmitic, stearic, linoleic, linolenic, olesteric and oleic acids with an aliphatic polyhydric alcohol or its cyclic anhydride. Mixed esters, such as mixed or natural glycerides may be employed. The surfactant may constitute about 0.1%-20% by weight of the composition, preferably about 0.25-5%. The balance of the composition is ordinarily propellant. A carrier can also be included, as desired, as with, e.g., lecithin for intranasal delivery. Xl.) Diagnostic and Prognostic Embodiments of 98P4B6. As disclosed herein, 98P4B6 polynucleotides, polypeptides, reactive cytotoxic T cells (CTL), reactive helper T cells (HTL) and anti-polypeptide antibodies are used in well known diagnostic, prognostic and therapeutic assays that examine conditions associated with dysregulated cell growth such as cancer, in particular the cancers listed in Table I (see, e.g., both its specific pattern of tissue expression as well as its overexpression in certain cancers as described for example in the Example entitled "Expression analysis of 98P486 in normal tissues, and patient specimens"). 98P4B6 can be analogized to a prostate associated antigen PSA, the archetypal marker that has been used by medical practitioners for years to identify and monitor the presence of prostate cancer (see, e.g., Merrill et al., J. Urol. 163(2): 503-5120 (2000); Polascik etal., J. Urol. Aug; 162(2):293-306 (1999) and Fortier et a., J. Nat. Cancer Inst. 91(19): 1635 1640(1999)). A variety of other diagnostic markers are also used in similar contexts including p53 and K-ras (see, e.g., Tulchinsky et al., Int J Mol Med 1999 Jul 4(1):99-102 and Minimoto et al., Cancer Detect Prey 2000;24(1):1-12). Therefore, this disclosure of 98P4B6 polynucleotides and polypeptides (as well as 98P4B6 polynucleotide probes and anti-98P4B6 antibodies used to identify the presence of these molecules) and their properties allows skilled artisans to utilize these molecules in methods that are analogous to those used, for example, in a variety of diagnostic assays directed to examining conditions associated with cancer. 70 WO 03/087306 PCT/USO3/10462 Typical embodiments of diagnostic methods which utilize the 98P4B6 polynucleotides, polypeptides, reactive T cells and antibodies are analogous to those methods from well-established diagnostic assays, which employ, e.g., PSA polynucleotides, polypeptides, reactive T cells and antibodies. For example, just as PSA polynucleotides are used as probes (for example in Northemrn analysis, see, e.g., Sharief et al., Biochem. Mol. Biol. Int. 33(3):567-74(1994)) and primers (for example in PCR analysis, see, e.g., Okegawa et al, J. Urol. 163(4): 1189-1190 (2000)) to observe the presence and/or the level of PSA mRNAs in methods of monitoring PSA overexpression or the metastasis of prostate cancers, the 98P4B6 polynucleotides described herein can be utilized in the same way to detect 98P4B6 overexpression or the metastasis of prostate and other cancers expressing this gene. Alternatively, just as PSA polypeptides are used to generate antibodies specific for PSA which can then be used to observe the presence andlor the level of PSA proteins in methods to monitor PSA protein overexpression (see, e.g., Stephan et al., Urology 55(4):560-3 (2000)) or the metastasis of prostate cells (see, e.g., Alanen et al., Pathol. Res. Pract. 192(3):233-7 (1996)), the 98P4B6 polypeptides described herein can be utilized to generate antibodies for use in detecting 98P4B6 overexpression or the metastasis of prostate cells and cells of other cancers expressing this gene. Specifically, because metastases involves the movement of cancer cells from an organ of origin (such as the lung or prostate gland etc.) to a different area of the body (such as a lymiph node), assays which examine a biological sample for the presence of cells expressing 98P4B6 polynucleotides and/or polypeptides can be used to provide evidence of metastasis. For example, when a biological sample from tissue that does not normally contain 98P4B6-expressing cells (lymph node) is found to contain 98P4B6-expressing cells such as the 98P4B6 expression seen in LAPC4 and LAPC9, xenografts isolated from lymph node and bone metastasis, respectively, this finding is indicative of metastasis. Alternatively 98P4B6 polynucleotides and/or polypeptides can be used to provide evidence of cancer, for example, when cells in a biological sample that do not normally express 98P4B6 or express 98P4B6 at a different level are found to express 98P4B6 or have an increased expression of 98P4B6 (see, e.g., the 98P4B6 expression in the cancers listed in Table I and in patient samples etc. shown in the accompanying Figures). In such assays, artisans may further wish to generate supplementary evidence of metastasis by testing the biological sample for the presence of a second tissue restricted marker (in addition to 98P4B6) such as PSA, PSCA etc. (see, e.g., Alanen et at., Pathol. Res. Pract. 192(3): 233 237 (1996)). Just as PSA polynucleotide fragments and polynucleotide variants are employed by skilled artisans for use in methods of monitoring PSA, 98P4B6 polynucleotide fragments and polynucleotide variants are used in an analogous manner. In particular, typical PSA polynucleotides used in methods of monitoring PSA are probes or primers which consist of fragments of the PSA cDNA sequence. Illustrating this, primers used to PCR amplify a PSA polynucleotide must include less than the whole PSA sequence to function in the polymerase chain reaction. In the context of such PCR reactions, skilled artisans generally create a variety of different polynucleotide fragments that can be used as primers in order to amplify different portions of a polynucleotide of interest or to optimize amplification reactions (see, e.g., Caetano-Anolles, G. Biotechniques 25(3): 472-476, 478-480 (1998); Robertson etal., Methods Mol. Biol. 98:121-154 (1998)). An additional illustration of the use of such fragments is provided in the Example entitled "Expression analysis of 98P4B6 in normal tissues, and patient specimens," where a 98P4B6 polynucleotide fragment is used as a probe to show the expression of 98P4B6 RNAs in cancer cells. In addition, variant polynucleotide sequences are typically used as primers and probes for the corresponding mRNAs in PCR and Northern analyses (see, e.g., Sawai et al., Fetal Diagn. Ther. 1996 Nov-Dec 11(6):407-13 and Current Protocols In Molecular Biology, Volume 2, Unit 2, Frederick M. Ausubel et at. eds., 1995)). Polynuclebtide fragments and variants are useful in this context where they are capable of binding to a target polynucleotide sequence (e.g., a 98P4B6 polynucleotide shown in Figure 2 or variant thereof) under conditions of high stringency. 71 WO 03/087306 PCT/USO3/10462 Furthermore, PSA polypeptides which contain an epitope that can be recognized by an antibody or T cell that specifically binds to that epitope are used in methods of monitoring PSA. 98P4B6 polypeptide fragments and polypeptide analogs or variants can also be used in an analogous manner. This practice of using polypeptide fragments or polypeptide variants to generate antibodies (such as anti-PSA antibodies or T cells) is typical in the art with a wide variety of systems such as fusion proteins being used by practitioners (see, e.g., Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubel et al. eds., 1995). In this context, each epitope(s) functions to provide the architecture with which an antibody or T cell is reactive. Typically, skilled artisans create a variety of different polypeptide fragments that can be used in order to generate immune responses specific for different portions of a polypeptide of interest (see, e.g., U.S. Patent No. 5,840,501 and U.S. Patent No. 5,939,533). For example it may be preferable to utilize a polypeptide comprising one of the 98P4B6 biological motifs discussed herein or a motif-bearing subsequence which is readily identified by one of skill in the art based on motifs available in the art. Polypeptide fragments, variants or analogs are typically useful in this context as long as they comprise an epitope capable of generating an antibody or T cell specific for a target polypeptide sequence (e.g. a 98P4B6 polypeptide shown in Figure 3). As shown herein, the 98P4B6 polynucleotides and polypeptides (as well as the 98P4B6 polynucleotide probes and anti-98P486 antibodies or T cells used to identify the presence of these molecules) exhibit specific properties that make them useful in diagnosing cancers such as those listed in Table I. Diagnostic assays that measure the presence of 98P4B6 gene products, in order to evaluate the presence or onset of a disease condition described herein, such as prostate cancer, are used to identify patients for preventive measures or further monitoring, as has been done so successfully with PSA. Moreover, these materials satisfy a need in the art for molecules having similar or complementary characteristics to PSA in situations where, for example, a definite diagnosis of metastasis of prostatic origin cannot be made on the basis of a test for PSA alone (see, e.g., Alanen et al., Pathol. Res. Pract. 192(3): 233-237 (1996)), and consequently, materials such as 98P4B6 polynucleotides and polypeptides (as well as the 98P4B6 polynucleotide probes and anti-98P4B6 antibodies used to identify the presence of these molecules) need to be employed to confirm a metastases of prostatic origin. Finally, in addition to their use in diagnostic assays, the 98P4B6 polynucleotides disclosed herein have a number of other utilities such as their use in the identification of oncogenetic associated chromosomal abnormalities in the chromosomal region to which the 98P4B6 gene maps (see the Example entitled "Chromosomal Mapping of 98P4B6" below). Moreover, in addition to their use in diagnostic assays, the 98P4B6-related proteins and polynucleotides disclosed herein have other utilities such as their use in the forensic analysis of tissues of unknown origin (see, e.g., Takahama K Forensic Sci Int 1996 Jun 28;80(1-2): 63-9). Additionally, 98P4B6-related proteins or polynucleotides of the invention can be used to treat a pathologic condition characterized by the over-expression of 98P4B6. For example, the amino acid or nucleic acid sequence of Figure 2 or Figure 3, or fragments of either, can be used to generate an immune response to a 98P4B6 antigen. Antibodies or other molecules that react with 98P4B6 can be used to modulate the function of this molecule, and thereby provide a therapeutic benefit. XlI.) Inhibition of 98P4B6 Protein Function The invention includes various methods and compositions for inhibiting the binding of 98P4B6 to its binding partner or its association with other protein(s) as well as methods for inhibiting 98P4B6 function. XII.A.) Inhibition of 98P4B6 With Intracellular Antibodies In one approach, a recombinant vector that encodes single chain antibodies that specifically bind to 98P4B6 are introduced into 98P4B6 expressing cells via gene transfer technologies. Accordingly, the encoded single chain anti-98P4B6 72 WO 03/087306 PCT/US03/10462 antibody is expressed intracellularly, binds to 98P4B6 protein, and thereby inhibits its function. Methods for engineering such intracellular single chain antibodies are well known. Such intracellular antibodies, also known as "intrabodies", are specifically targeted to a particular compartment within the cell, providing control over where the inhibitory activity of the treatment is focused. This technology has been successfully applied in the art (for review, see Richardson and Marasco, 1995, TIBTECH vol. 13). Intrabodies have been shown to virtually eliminate the expression of otherwise abundant cell surface receptors (see, e.g., Richardson et al., 1995, Proc. Natl. Acad. Sci. USA 92: 3137-3141; Beerli et al., 1994, J. Biol. Chem. 289: 23931-23936; Deshane et al., 1994, Gene Ther. 1: 332-337). Single chain antibodies comprise the variable domains of the heavy and light chain joined by a flexible linker polypeptide, and are expressed as a single polypeptide. Optionally, single chain antibodies are expressed as a single chain variable region fragment joined to the light chain constant region. Well-known intracellular trafficking signals are engineered into recombinant polynucleotide vectors encoding such single chain antibodies in order to target precisely the intrabody to the desired intracellular compartment. For example, intrabodies targeted to the endoplasmic reticulumrn (ER) are engineered to incorporate a leader peptide and, optionally, a C-terminal ER retention signal, such as the KDEL amino acid motif. Intrabodies intended to exert activity in the nucleus are engineered to include a nuclear localization signal. Lipid moieties are joined to intrabodies in order to tether the intrabody to the cytosolic side of the plasma membrane. Intrabodies can also be targeted to exert function in the cytosol. For example, cytosolic intrabodies are used to sequester factors within the cytosol, thereby preventing them from being transported to their natural cellular destination. In one embodiment, intrabodies are used to capture 98P4B6 in the nucleus, thereby preventing its activity within the nucleus. Nuclear targeting signals are engineered into such 98P4B6 intrabodies in order to achieve the desired targeting. Such 98P4B6 intrabodies are designed to bind specifically to a particular 98P4B6 domain. In another embodiment, cytosolic intrabodies that specifically bind to a 98P4B6 protein are used to prevent 98P4B6 from gaining access to the nucleus, thereby preventing it from exerting any biological activity within the nucleus (e.g., preventing 98P4B6 from forming transcription complexes with other factors). In order to specifically direct the expression of such intrabodies to particular cells, the transcription of the intrabody is placed under the regulatory control of an appropriate tumor-specific promoter and/or enhancer. In order to target intrabody expression specifically to prostate, for example, the PSA promoter and/or promoter/enhancer can be utilized (See, for example, U.S. Patent No. 5,919,652 issued 6 July 1999). XII.B.) Inhibition of 98P4B6 with Recombinant Proteins In another approach, recombinant molecules bind to 98P4B6 and thereby inhibit 98P4B6 function. For example, these recombinant molecules prevent or inhibit 98P4B6 from accessing/binding to its binding partner(s) or associating with other protein(s). Such recombinant molecules can, for example, contain the reactive part(s) of a 98P4B6 specific antibody molecule. In a particular embodiment, the 98P4B6 binding domain of a 98P486 binding partner is engineered into a dimeric fusion protein, whereby the fusion protein comprises two 98P4B6 ligand binding domains linked to the Fc portion of a human IgG, such as human IgGI. Such IgG portion can contain, for example, the CH2 and CH 3 domains and the hinge region, but not the CH1 domain. Such dimeric fusion proteins are administered in soluble form to patients suffering from a cancer associated with the expression of 98P4B6, whereby the dimeric fusion protein specifically binds to 98P4B6 and blocks 98P4B6 interaction with a binding partner. Such dimeric fusion proteins are further combined into multimeric proteins using known antibody linking technologies. 73 WO 03/087306 PCT/US03/10462 XII.C.) Inhibition of 98P4B6 Transcription or Translation The present invention also comprises various methods and compositions for inhibiting the transcription of the 98P4B6 gene. Similarly, the invention also provides methods and compositions for inhibiting the translation of 98P4B6 mRNA into protein. In one approach, a method of inhibiting the transcription of the 98P4B6 gene comprises contacting the 98P4B6 gene with a 98P4B6 antisense polynucleotide. In another approach, a method of inhibiting 98P4B6 mRNA translation comprises contacting a 98P4B6 mRNA with an antisense polynucleotide. In another approach, a 98P4B6 specific ribozyme is used to cleave a 98P4B6 message, thereby inhibiting translation. Such antisense and ribozyme based methods can also be directed to the regulatory regions of the 98P4B6 gene, such as 98P4B6 promoter and/or enhancer elements. Similarly, proteins capable of inhibiting a 98P4B6 gene transcription factor are used to inhibit 98P4B6 mRNA transcription. The various polynucleotides and compositions useful in the aforementioned methods have been described above. The use of antisense and ribozyme molecules to inhibit transcription and translation is well known in the art. Other factors that inhibit the transcription of 98P4B6 by interfering with 98P4B6 transcriptional activation are also useful to treat cancers expressing 98P4B6. Similarly, factors that interfere with 98P4B6 processing are useful to treat cancers that express 98P4B6. Cancer treatment methods utilizing such factors are also within the scope of the invention. XII.D.) General Considerations for Therapeutic Strategies Gene transfer and gene therapy technologies can be used to deliver therapeutic polynucleotide molecules to tumor cells synthesizing 98P4B6 (i.e., antisense, ribozyme, polynucleotides encoding intrabodies and other 98P4B6 inhibitory molecules). A number of gene therapy approaches are known in the art Recombinant vectors encoding 98P4B6 antisense polynucleotides, ribozymes, factors capable of interfering with 98P4B6 transcription, and so forth, can be delivered to target tumor cells using such gene therapy approaches. The above therapeutic approaches can be combined with any one of a wide variety of surgical, chemotherapy or radiation therapy regimens. The therapeutic approaches of the invention can enable the use of reduced dosages of chemotherapy (or other therapies) and/or less frequent administration, an advantage for all patients and particularly for those that do not tolerate the toxicity of the chemotherapeutic agent well. The anti-tumor activity of a particular composition (e.g., antisense, ribozyme, intrabody), or a combination of such compositions, can be evaluated using various in vitro and in vivo assay systems. In vitro assays that evaluate therapeutic activity include cell growth assays, soft agar assays and other assays indicative of tumor promoting activity, binding assays capable of determining the extent to which a therapeutic composition will inhibit the binding of 98P4B6 to a binding partner, etc. In vivo, the effect of a 98P4B6 therapeutic composition can be evaluated in a suitable animal model. For example, xenogenic prostate cancer models can be used, wherein human prostate cancer explants or passaged xenograft tissues are introduced into immune compromised animals, such as nude or SCID mice (Klein et al., 1997, Nature Medicine 3: 402-408). For example, PCT Patent Application WO98/16628 and U.S. Patent 6,107,540 describe various xenograft models of human prostate cancer capable of recapitulating the development of primary tumors, micrometastasis, and the formation of osteoblastic metastases characteristic of late stage disease. Efficacy can be predicted using assays that measure inhibition of tumor formation, tumor regression or metastasis, and the like. In vivo assays that evaluate the promotion of apoptosis are useful in evaluating therapeutic compositions. In one embodiment, xenografts from tumor bearing mice treated with the therapeutic composition can be examined for the presence of apoptotic foci and compared to untreated control xenograft-bearing mice. The extent to which apoptotic foci are found in the tumors of the treated mice provides an indication of the therapeutic efficacy of the composition. 74 WO 03/087306 PCT/USO3/10462 The therapeutic compositions used in the practice of the foregoing methods can be formulated into pharmaceutical compositions comprising a carrier suitable for the desired delivery method. Suitable carriers include any material that when combined with the therapeutic composition retains the anti-tumor function of the therapeutic composition and is generally non-reactive with the patient's immune system. Examples include, but are not limited to, any of a number of standard pharmaceutical carriers such as sterile phosphate buffered saline solutions, bacteriostatic water, and the like (see, generally, Remington's Pharmaceutical Sciences 16 th Edition, A. Osal., Ed., 1980). Therapeutic formulations can be solubilized and administered via any route capable of delivering the therapeutic composition to the tumor site. Potentially effective routes of administration include, but are not limited to, intravenous, parenteral, intraperitoneal, intramuscular, intratumor, intradermal, intraorgan, orthotopic, and the like. A preferred formulation for intravenous injection comprises the therapeutic composition in a solution of preserved bacteriostatic water, sterile unpreserved water, and/or diluted in polyvinylchloride or polyethylene bags containing 0.9% sterile Sodium Chloride for Injection, USP. Therapeutic protein preparations can be lyophilized and stored as sterile powders, preferably under vacuum, and then reconstituted in bacteriostatic water (containing for example, benzyl alcohol preservative) or in sterile water prior to injection. Dosages and administration protocols for the treatment of cancers using the foregoing methods will vary with the method and the target cancer, and will generally depend on a number of other factors appreciated in the art. XIII.) Identification, Characterization and Use of Modulators of 98P4B6 Methods to Identify and Use Modulators In one embodiment, screening is performed to identify modulators that induce or suppress a particular expression profile, suppress or induce specific pathways, preferably generating the associated phenotype thereby. In another embodiment, having identified differentially expressed genes important in a particular state; screens are performed to identify modulators that alter expression of individual genes, either increase or decrease. In another embodiment, screening is performed to identify modulators that alter a biological function of the expression product of a differentially expressed gene. Again, having identified the importance of a gene in a particular state, screens are performed to identify agents that bind andlor modulate the biological activity of the gene product. In addition, screens are done for genes that are induced in response to a candidate agent. After identifying a modulator (one that suppresses a cancer expression pattern leading to a normal expression pattern, or a modulator of a cancer gene that leads to expression of the gene as in normal tissue) a screen is performed to identify genes that are specifically modulated in response to the agent. Comparing expression profiles between normal tissue and agent-treated cancer tissue reveals genes that are not expressed in normal tissue or cancer tissue, but are expressed in agent treated tissue, and vice versa. These agent-specific sequences are identified and used by methods described herein for cancer genes or proteins. In particular these sequences and the proteins they encode are used in marking or identifying agent treated cells. In addition, antibodies are raised against the agent-induced proteins and used to target novel therapeutics to the treated cancer tissue sample. Modulator-related Identification and Screening Assays: Gene Expression-related Assays Proteins, nucleic acids, and antibodies of the invention are used in screening assays. The cancer-associated proteins, antibodies, nucleic acids, modified proteins and cells containing these sequences are used in screening assays, such as evaluating the effect of drug candidates on a "gene expression profile," expression profile of polypeptides or alteration of biological function. In one embodiment, the expression profiles are used, preferably in conjunction with high 75 WO 03/087306 PCT/US03/10462 throughput screening techniques to allow monitoring for expression profile genes after treatment with a candidate agent (e.g., Davis, GF, et al, J Biol Screen 7:69 (2002); Zlokarnik, et al., Science 279:84-8 (1998); Heid, Genome Res 6:986 94,1996). The cancer proteins, antibodies, nucleic acids, modified proteins and cells containing the native or modified cancer proteins or genes are used in screening assays. That is, the present invention comprises methods for screening for compositions which modulate the cancer phenotype or a physiological function of a cancer protein of the invention. This is done on a gene itself or by evaluating the effect of drug candidates on a "gene expression profile" or biological function. In one embodiment, expression profiles are used, preferably in conjunction with high throughput screening techniques to allow monitoring after treatment with a candidate agent, see Zlokamik, supra. A variety of assays are executed directed to the genes and proteins of the invention. Assays are run on an individual nucleic acid or protein level. That is, having identified a particular gene as up regulated in cancer, test compounds are screened for the ability to modulate gene expression or for binding to the cancer protein of the invention. "Modulation" in this context includes an increase or a decrease in gene expression. The preferred amount of modulation will depend on the original change of the gene expression in normal versus tissue undergoing cancer, with changes of at least 10%, preferably 50%, more preferably 100-300%, and in some embodiments 300-1000% or greater. Thus, if a gene exhibits a 4-fold increase in cancer tissue compared to normal tissue, a decrease of about four-fold is often desired; similarly, a 10-fold decrease in cancer tissue compared to normal tissue a target value of a 10-fold increase in expression by the test compound is often desired. Modulators that exacerbate the type of gene expression seen in cancer are also useful, e.g., as an upregulated target in further analyses. The amount of gene expression is monitored using nucleic acid probes and the quantification of gene expression levels, or, alternatively, a gene product itself is monitored, e.g., through the use of antibodies to the cancer protein and standard immunoassays. Proteomics and separation techniques also allow for quantification of expression. Expression Monitoring to Identify Compounds that Modify Gene Expression In one embodiment, gene expression monitoring, i.e., an expression profile, is monitored simultaneously for a number of entities. Such profiles will typically involve one or more of the genes of Figure 2. In this embodiment, e.g., cancer nucleic acid probes are attached to biochips to detect and quantify cancer sequences in a particular cell. Alternatively, PCR can be used. Thus, a series, e.g., wells of a microtiter plate, can be used with dispensed primers in desired wells. A PCR reaction can then be performed and analyzed for each well. Expression monitoring is performed to identify compounds that modify the expression of one or more cancer associated sequences, e.g., a polynucleotide sequence set out in Figure 2. Generally, a test modulator is added to the cells prior to analysis. Moreover, screens are also provided to identify agents that modulate cancer, modulate cancer proteins of the invention, bind to a cancer protein of the invention, or interfere with the binding of a cancer protein of the invention and an antibody or other binding partner. In one embodiment, high throughput screening methods involve providing a library containing a large number of potential therapeutic compounds (candidate compounds). Such "combinatorial chemical libraries" are then screened in one or more assays to identify those library members (particular chemical species or subclasses) that display a desired characteristic activity. The compounds thus identified can serve as conventional "lead compounds," as compounds for screening, or as therapeutics. In certain embodiments, combinatorial libraries of potential modulators are screened for an ability to bind to a cancer polypeptide or to modulate activity. Conventionally, new chemical entities with useful properties are generated by identifying a chemical compound (called a "lead compound") with some desirable property or activity, e.g., inhibiting activity, 76 WO 03/087306 PCT/US03/10462 creating variants of the lead compound, and evaluating the property and activity of those variant compounds. Often, high throughput screening (HTS) methods are employed for such an analysis. As noted above, gene expression monitoring is conveniently used to test candidate modulators (e.g., protein, nucleic acid or small molecule). After the candidate agent has been added and the cells allowed to incubate for a period, the sample containing a target sequence to be analyzed is, e.g., added to a biochip. If required, the target sequence is prepared using known techniques. For example, a sample is treated to lyse the cells, using known lysis buffers, electroporation, etc., with purification and/or amplification such as PCR performed as appropriate. For example, an in vitro transcription with labels covalently attached to the nucleotides is performed. Generally, the nucleic acids are labeled with biotin-FITC or PE, or with cy3 or cy5. The target sequence can be labeled with, e.g., a fluorescent, a chemiluminescent, a chemical, or a radioactive signal, to provide a means of detecting the target sequence's specific binding to a probe. The label also can be an enzyme, such as alkaline phosphatase or horseradish peroxidase, which when provided with an appropriate substrate produces a product that is detected. Alternatively, the label is a labeled compound or small molecule, such as an enzyme inhibitor, that binds but is not catalyzed or altered by the enzyme. The label also can be a moiety or compound, such as, an epitope tag or biotin which specifically binds to streptavidin. For the example of biotin, the streptavidin is labeled as described above, thereby, providing a detectable signal for the bound target sequence. Unbound labeled streptavidin is typically removed prior to analysis. As will be appreciated by those in the art, these assays can be direct hybridization assays or can comprise "sandwich assays", which include the use of multiple probes, as is generally outlined in U.S. Patent Nos. 5, 681,702; 5,597,909; 5,545,730; 5,594,117; 5,591,584; 5,571,670; 5,580,731; 5,571,670; 5,591,584; 5,624,802; 5,635,352; 5,594,118; 5,359,100; 5,124, 246; and 5,681,697. In this embodiment, in general, the target nucleic acid is prepared as outlined above, and then added to the biochip comprising a plurality of nucleic acid probes, under conditions that allow the formation of a hybridization complex. A variety of hybridization conditions are used in the present invention, including high, moderate and low stringency conditions as outlined above. The assays are generally run under stringency conditions which allow formation of the label probe hybridization complex only in the presence of target. Stringency can be controlled by altering a step parameter that is a thermodynamic variable, including, but not limited to, temperature, formamide concentration, salt concentration, chaotropic salt concentration pH, organic solvent concentration, etc. These parameters may also be used to control non-specific binding, as is generally outlined in U.S. Patent No. 5,681,697. Thus, it can be desirable to perform certain steps at higher stringency conditions to reduce non-specific binding. The reactions outlined herein can be accomplished in a variety of ways. Components of the reaction can be added simultaneously, or sequentially, in different orders, with preferred embodiments outlined below. In addition, the reaction may include a variety of other reagents. These include salts, buffers, neutral proteins, e.g. albumin, detergents, etc. which can be used to facilitate optimal hybridization and detection, and/or reduce nonspecific or background interactions. Reagents that otherwise improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, anti-microbial agents, etc., may also be used as appropriate, depending on the sample preparation methods and purity of the target. The assay data are analyzed to determine the expression levels of individual genes, and changes in expression levels as between states, forming a gene expression profile. Biological Activity-related Assays The invention provides methods identify or screen for a compound that modulates the activity of a cancer-related gene or protein of the invention. The methods comprise adding a test compound, as defined above, to a cell comprising a 77 WO 03/087306 PCT/US03/10462 cancer protein of the invention. The cells contain a recombinant nucleic acid that encodes a cancer protein of the invention. In another embodiment, a library of candidate agents is tested on a plurality of cells. In one aspect, the assays are evaluated in the presence or absence or previous or subsequent exposure of physiological signals, e.g. hormones, antibodies, peptides, antigens, cytokines, growth factors, action potentials, pharmacological agents including chemotherapeutics, radiation, carcinogenics, or other cells (i.e., cell-cell contacts). In another example, the determinations are made at different stages of the cell cycle process. In this way, compounds that modulate genes or proteins of the invention are identified. Compounds with pharmacological activity are able to enhance or interfere with the activity of the cancer protein of the invention. Once identified, similar structures are evaluated to identify critical structural features of the compound. In one embodiment, a method of modulating (e.g., inhibiting) cancer cell division is provided; the method comprises administration of a cancer modulator. In another embodiment, a method of modulating ( e.g., inhibiting) cancer is provided; the method comprises administration of a cancer modulator. In a further embodiment, methods of treating cells or individuals with cancer are provided; the method comprises administration of a cancer modulator. In one embodiment, a method for modulating the status of a cell that expresses a gene of the invention is provided. As used herein status comprises such art-accepted parameters such as growth, proliferation, survival, function, apoptosis, senescence, location, enzymatic activity, signal transduction, etc. of a cell. In one embodiment, a cancer inhibitor is an antibody as discussed above. In another embodiment, the cancer inhibitor is an antisense molecule. A variety of cell growth, proliferation, and metastasis assays are known to those of skill in the art, as described herein. High Throughput Screening to Identify Modulators The assays to identify suitable modulators are amenable to high throughput screening. Preferred assays thus detect enhancement or inhibition of cancer gene transcription, inhibition or enhancement of polypeptide expression, and inhibition or enhancement of polypeptide activity. In one embodiment, modulators evaluated in high throughput screening methods are proteins, often naturally occurring proteins or fragments of naturally occurring proteins. Thus, e.g., cellular extracts containing proteins, or random or directed digests of proteinaceous cellular extracts, are used. In this way, libraries of proteins are made for screening in the methods of the invention. Particularly preferred in this embodiment are libraries of bacterial, fungal, viral, and mammalian proteins, with the latter being preferred, and human proteins being especially preferred. Particularly useful test compound will be directed to the class of proteins to which the target belongs, e.g., substrates for enzymes, or ligands and receptors. Use of Soft Agar Growth and Colony Formation to Identify and Characterize Modulators Normal cells require a solid substrate to attach and grow. When cells are transformed, they lose this phenotype and grow detached from the substrate. For example, transformed cells can grow in stirred suspension culture or suspended in semi-solid media, such as semi-solid or soft agar. The transformed cells, when transfected with tumor suppressor genes, can regenerate normal phenotype and once again require a solid substrate to attach to and grow. Soft agar growth or colony formation in assays are used to identify modulators of cancer sequences, which when expressed in host cells, inhibit abnormal cellular proliferation and transformation. A modulator reduces or eliminates the host cells' ability to grow suspended in solid or semisolid media, such as agar. Techniques for soft agar growth or colony formation in suspension assays are described in Freshney, Culture of Animal Cells a Manual of Basic Technique (3rd ed., 1994). See also, the methods section of Garkavtsev et al. (1996), supra. Evaluation of Contact Inhibition and Growth Density Limitation to Identify and Characterize Modulators Normal cells typically grow in a flat and organized pattern in cell culture until they touch other cells. When the cells touch one another, they are contact inhibited and stop growing. Transformed cells, however, are not contact inhibited and 78 WO 03/087306 PCT/US03/10462 continue to grow to high densities in disorganized foci. Thus, transformed cells grow to a higher saturation density than corresponding normal cells. This is detected morphologically by the formation of a disoriented monolayer of cells or cells in foci. Alternatively, labeling index with ( 3 H)-thymidine at saturation density is used to measure density limitation of growth, similarly an MTT or Alamar blue assay will reveal proliferation capacity of cells and the the ability of modulators to affect same. See Freshney (1994), supra. Transformed cells, when transfected with tumor suppressor genes, can regenerate a normal phenotype and become contact inhibited and would grow to a lower density. In this assay, labeling index with 3 H)-thymidine at saturation density is a preferred method of measuring density limitation of growth. Transformed host cells are transfected with a cancer-associated sequence and are grown for 24 hours at saturation density in non-limiting medium conditions. The percentage of cells labeling with ( 3 H)-thymidine is determined by incorporated cpm. Contact independent growth is used to identify modulators of cancer sequences, which had led to abnormal cellular proliferation and transformation. A modulator reduces or eliminates contact independent growth, and returns the cells to a normal phenotype. Evaluation of Growth Factor or Serum Dependence to Identify and Characterize Modulators Transformed cells have lower serum dependence than their normal counterparts (see, e.g., Temin, J. Natl. Cancer Inst. 37:167-175 (1966); Eagle et al., J. Exp. Med 131:836-879 (1970)); Freshney, supra. This is in part due to release of various growth factors by the transformed cells. The degree of growth factor or serum dependence of transformed host cells can be compared with that of control. For example, growth factor or serum dependence of a cell is monitored in methods to identify and characterize compounds that modulate cancer-associated sequences of the invention. Use of Tumor-specific Marker Levels to Identify and Characterize Modulators Tumor cells release an increased amount of certain factors (hereinafter "tumor specific markers") than their normal counterparts. For example, plasminogen activator (PA) is released from human glioma at a higher level than from normal brain cells (see, e.g., Gullino, Angiogenesis, Tumor Vascularization, and Potential Interference with Tumor Growth, in Biological Responses in Cancer, pp. 178-184 (Mihich (ed.) 1985)). Similarly, Tumor Angiogenesis Factor (TAF) is released at a higher level in tumor cells than their normal counterparts. See, e.g., Folkman, Angiogenesis and Cancer, Sem Cancer Biol. (1992)), while bFGF is released from endothelial tumors (Ensoli, B et al). Various techniques which measure the release of these factors are described in Freshney (1994), supra. Also, see, Unkless et al., J. Biol. Chem. 249:4295-4305 (1974); Strickland & Beers, J. Biol. Chem. 251:5694-5702 (1976); Whur et al., Br. J. Cancer 42:305 312 (1980); Gullino, Angiogenesis, Tumor Vascularization, and Potential Interference with Tumor Growth, in Biological Responses in Cancer, pp. 178-184 (Mihich (ed.) 1985); Freshney, Anticancer Res. 5:111-130 (1985). For example, tumor specific marker levels are monitored in methods to identify and characterize compounds that modulate cancer-associated sequences of the invention. Invasiveness into Matrigel to Identify and Characterize Modulators The degree of invasiveness into Matrigel or an extracellular matrix constituent can be used as an assay to identify and characterize compounds that modulate cancer associated sequences. Tumor cells exhibit a positive correlation between malignancy and invasiveness of cells into Matrigel or some other extracellular matrix constituent. In this assay, tumorigenic cells are typically used as host cells. Expression of a tumor suppressor gene in these host cells would decrease invasiveness of the host cells. Techniques described in Cancer Res. 1999; 59:6010; Freshney (1994), supra, can be used. Briefly, the level of invasion of host cells is measured by using filters coated with Matrigel or some other extracellular matrix constituent. Penetration into the gel, or through to the distal side of the filter, is rated as invasiveness, and rated histologically by number of cells and distance moved, or by prelabeling the cells with 12s51 and counting the radioactivity on the distal side of the filter or bottom of the dish. See, e.g., Freshney (1984), supra. 79 WO 03/087306 PCT/USO3/10462 Evaluation of Tumor Growth In Vivo to Identify and Characterize Modulators Effects of cancer-associated sequences on cell growth are tested in transgenic or immune-suppressed organisms. Transgenic organisms are prepared in a variety of art-accepted ways. For example, knock-out transgenic organisms, e.g., mammals such as mice, are made, in which a cancer gene is disrupted or in which a cancer gene is inserted. Knock-out transgenic mice are made by insertion of a marker gene or other heterologous gene into the endogenous cancer gene site in the mouse genome via homologous recombination. Such mice can also be made by substituting the endogenous cancer gene with a mutated version of the cancer gene, or by mutating the endogenous cancer gene, e.g., by exposure to carcinogens. To prepare transgenic chimeric animals, e.g., mice, a DNA construct is introduced into the nuclei of embryonic stem cells. Cells containing the newly engineered genetic lesion are injected into a host mouse embryo, which is re implanted into a recipient female. Some of these embryos develop into chimeric mice that possess germ cells some of which are derived from the mutant cell line. Therefore, by breeding the chimeric mice it is possible to obtain a new line of mice containing the introduced genetic lesion (see, e.g., Capecchi et al., Science 244:1288 (1989)). Chimeric mice can be derived according to US Patent 6,365,797, issued 2 April 2002; US Patent 6,107,540 issued 22 August 2000; Hogan et al., Manipulating the Mouse Embryo: A laboratory Manual, Cold Spring Harbor Laboratory (1988) and Teratocarcinomas and Embryonic Stem Cells: A Practical Approach, Robertson, ed., IRL Press, Washington, D.C., (1987). Alternatively, various immune-suppressed or immune-deficient host animals can be used. For example, a genetically athymic "nude" mouse (see, e.g., Giovanella et al., J. Natl. Cancer Inst. 52:921 (1974)), a SCID mouse, a thymectornized mouse, or an irradiated mouse (see, e.g., Bradley et al., Br. J. Cancer 38:263 (1978); Selby et al., Br. J. Cancer 41:52 (1980)) can be used as a host. Transplantable tumor cells (typically about 106 cells) injected into isogenic hosts produce invasive tumors in a high proportion of cases, while normal cells of similar origin will not. In hosts which developed invasive tumors, cells expressing cancer-associated sequences are injected subcutaneously or orthotopically. Mice are then separated into groups, including control groups and treated experimental groups) e.g. treated with a modulator). After a suitable length of time, preferably 4-8 weeks, tumor growth is measured (e.g., by volume or by its two largest dimensions, or weight) and compared to the control. Tumors that have statistically significant reduction (using, e.g., Student's T test) are said to have inhibited growth. In Vitro Assays to Identify and Characterize Modulators Assays to identify compounds with modulating activity can be performed in vitro. For example, a cancer polypeptide is first contacted with a potential modulator and incubated for a suitable amount of time, e.g., from 0.5 to 48 hours. In one embodiment, the cancer polypeptide levels are determined in vitro by measuring the level of protein or mRNA. The level of protein is measured using immunoassays such as Western blotting, ELISA and the like with an antibody that selectively binds to the cancer polypeptide or a fragment thereof. For measurement of mRNA, amplification, e.g., using PCR, LCR, or hybridization assays, e. g., Northern hybridization, RNAse protection, dot blotting, are preferred. The level of protein or mRNA is detected using directly or indirectly labeled detection agents, e.g., fluorescently or radioactively labeled nucleic acids, radioactively or enzymatically labeled antibodies, and the like, as described herein. Alternatively, a reporter gene system can be devised using a cancer protein promoter operably linked to a reporter gene such as luciferase, green fluorescent protein, CAT, or P-gal. The reporter construct is typically transfected into a cell. After treatment with a potential modulator, the amount of reporter gene transcription, translation, or activity is measured according to standard techniques known to those of skill in the art (Davis GF, supra; Gonzalez, J. & Negulescu, P. Curr. Opin. Biotechnol. 1998: 9:624). 80 WO 03/087306 PCT/US03/10462 ) As outlined above, in vitro screens are done on individual genes and gene products. That is, having identified a particular differentially expressed gene as important in a particular state, screening of modulators of the expression of the gene or the gene product itself is performed. In one embodiment, screening for modulators of expression of specific gene(s) is performed. Typically, the expression of only one or a few genes is evaluated. In another embodiment, screens are designed to first find compounds that bind to differentially expressed proteins. These compounds are then evaluated for the ability to modulate differentially expressed activity. Moreover, once initial candidate compounds are identified, variants can be further screened to better evaluate structure activity relationships. Binding Assays to Identify and Characterize Modulators In binding assays in accordance with the invention, a purified or isolated gene product of the invention is generally used. For example, antibodies are generated to a protein of the invention, and immunoassays are run to determine the amount and/or location of protein. Alternatively, cells comprising the cancer proteins are used in the assays. Thus, the methods comprise combining a cancer protein of the invention and a candidate compound such as a ligand, and determining the binding of the compound to the cancer protein of the invention. Preferred embodiments utilize the human cancer protein; animal models of human disease of can also be developed and used. Also, other analogous mammalian proteins also can be used as appreciated by those of skill in the art. Moreover, in some embodiments variant or derivative cancer proteins are used. Generally, the cancer protein of the invention, or the ligand, is non-diffusibly bound to an insoluble support. The support can, e.g., be one having isolated sample receiving areas (a microtiter plate, an array, etc.). The insoluble supports can be made of any composition to which the compositions can be bound, is readily separated from soluble material, and is otherwise compatible with the overall method of screening. The surface of such supports can be solid or porous and of any convenient shape. Examples of suitable insoluble supports include microtiter plates, arrays, membranes and beads. These are typically made of glass, plastic (e.g., polystyrene), polysaccharide, nylon, nitrocellulose, or Teflon T

M

, etc. Microtiter plates and arrays are especially convenient because a large number of assays can be carried out simultaneously, using small amounts of reagents and samples. The particular manner of binding of the composition to the support is not crucial so long as it is compatible with the reagents and overall methods of the invention, maintains the activity of the composition and is nondiffusable. Preferred methods of binding include the use of antibodies which do not sterically block either the ligand binding site or activation sequence when attaching the protein to the support, direct binding to "sticky" or ionic supports, chemical crosslinking, the synthesis of the protein or agent on the surface, etc. Following binding of the protein or ligand/binding agent to the support, excess unbound material is removed by washing. The sample receiving areas may then be blocked through incubation with bovine serum albumin (BSA), casein or other innocuous protein or other moiety. Once a cancer protein of the invention is bound to the support, and a test compound is added to the assay. Alternatively, the candidate binding agent is bound to the support and the cancer protein of the invention is then added. Binding agents include specific antibodies, non-natural binding agents identified in screens of chemical libraries, peptide analogs, etc. Of particular interest are assays to identify agents that have a low toxicity for human cells. A wide variety of assays can be used for this purpose, including proliferation assays, cAMP assays, labeled in vitro protein-protein binding assays, electrophoretic mobility shift assays, immunoassays for protein binding, functional assays (phosphorylation assays, etc.) and the like. 81 WO 03/087306 PCT/USO3/10462 A determination of binding of the test compound (ligand, binding agent, modulator, etc.) to a cancer protein of the invention can be done in a number of ways. The test compound can be labeled, and binding determined directly, e.g., by attaching all or a portion of the cancer protein of the invention to a solid support, adding a labeled candidate compound (e.g., a fluorescent label), washing off excess reagent, and determining whether the label is present on the solid support. Various blocking and washing steps can be utilized as appropriate. In certain embodiments, only one of the components is labeled, e.g., a protein of the invention or ligands labeled. Alternatively, more than one component is labeled with different labels, e.g., 1125, for the proteins and a fluorophor for the compound. Proximity reagents, e.g., quenching or energy transfer reagents are also useful. Competitive Binding to Identify and Characterize Modulators In one embodiment, the binding of the "test compound" is determined by competitive binding assay with a "competitor." The competitor is a binding moiety that binds to the target molecule (e.g., a cancer protein of the invention). Competitors include compounds such as antibodies, peptides, binding partners, ligands, etc. Under certain circumstances, the competitive binding between the test compound and the competitor displaces the test compound. In one embodiment, the test compound is labeled. Either the test compound, the competitor, or both, is added to the protein for a time sufficient to allow binding. Incubations are performed at a temperature that facilitates optimal activity, typically between four and 40 0 C. Incubation periods are typically optimized, e.g., to facilitate rapid high throughput screening; typically between zero and one hour will be sufficient. Excess reagent is generally removed or washed away. The second component is then added, and the presence or absence of the labeled component is followed, to indicate binding. In one embodiment, the competitor is added first, followed by the test compound. Displacement of the competitor is an indication that the test compound is binding to the cancer protein and thus is capable of binding to, and potentially modulating, the activity of the cancer protein. In this embodiment, either component can be labeled. Thus, e.g., if the competitor is labeled, the presence of label in the post-test compound wash solution indicates displacement by the test compound. Alternatively, if the test compound is labeled, the presence of the label on the support indicates displacement. In an alternative embodiment, the test compound is added first, with incubation and washing, followed by the competitor. The absence of binding by the competitor indicates that the test compound binds to the cancer protein with higher affinity than the competitor. Thus, if the test compound is labeled, the presence of the label on the support, coupled with a lack of competitor binding, indicates that the test compound binds to and thus potentially modulates the cancer protein of the invention. Accordingly, the competitive binding methods comprise differential screening to identity agents that are capable of modulating the activity of the cancer proteins of the invention. In this embodiment, the methods comprise combining a cancer protein and a competitor in a first sample. A second sample comprises a test compound, the cancer protein, and a competitor. The binding of the competitor is determined for both samples, and a change, or difference in binding between the two samples indicates the presence of an agent capable of binding to the cancer protein and potentially modulating its activity. That is, if the binding of the competitor is different in the second sample relative to the first sample, the agent is capable of binding to the cancer protein. Alternatively, differential screening is used to identify drug candidates that bind to the native cancer protein, but cannot bind to modified cancer proteins. For example the structure of the cancer protein is modeled and used in rational drug design to synthesize agents that interact with that site, agents which generally do not bind to site-modified proteins. Moreover, such drug candidates that affect the activity of a native cancer protein are also identified by screening drugs for the ability to either enhance or reduce the activity of such proteins. 82 WO 03/087306 PCT/US03/10462 Positive controls and negative controls can be used in the assays. Preferably control and test samples are performed in at least triplicate to obtain statistically significant results. Incubation of all samples occurs for a time sufficient to allow for the binding of the agent to the protein. Following incubation, samples are washed free of non-specifically bound material and the amount of bound, generally labeled agent determined. For example, where a radiolabel is employed, the samples can be counted in a scintillation counter to determine the amount of bound compound. A variety of other reagents can be included in the screening assays. These include reagents like salts, neutral proteins, e.g. albumin, detergents, etc. which are used to facilitate optimal protein-protein binding and/or reduce non-specific or background interactions. Also reagents that otherwise improve the efficiency of the assay, such as protease inhibitors, nuclease inhibitors, anti-microbial agents, etc., can be used. The mixture of components is added in an order that provides for the requisite binding. Use of Polynucleotides to Down-regulate or Inhibit a Protein of the Invention. Polynucleotide modulators of cancer can be introduced into a cell containing the target nucleotide sequence by formation of a conjugate with a ligand-binding molecule, as described in WO 91/04753. Suitable ligand-binding molecules include, but are not limited to, cell surface receptors, growth factors, other cytokines, or other ligands that bind to cell surface receptors. Preferably, conjugation of the ligand binding molecule does not substantially interfere with the ability of the ligand binding molecule to bind to its corresponding molecule or receptor, or block entry of the sense or antisense oligonucleotide or its conjugated version into the cell. Alternatively, a polynucleotide modulator of cancer can be introduced into a cell containing the target nucleic acid sequence, e.g., by formation of a polynucleotide-lipid complex, as described in WO 90/10448. It is understood that the use of antisense molecules or knock out and knock in models may also be used in screening assays as discussed above, in addition to methods of treatment. Inhibitory and Antisense Nucleotides In certain embodiments, the activity of a cancer-associated protein is down-regulated, or entirely inhibited, by the use of antisense polynucleotide or inhibitory small nuclear RNA (snRNA), i.e., a nucleic acid complementary to, and which can preferably hybridize specifically to, a coding mRNA nucleic acid sequence, e.g., a cancer protein of the invention, mRNA, or a subsequence thereof. Binding of the antisense polynucleotide to the mRNA reduces the translation and/or stability of the mRNA. In the context of this invention, antisense polynucleotides can comprise naturally occurring nucleotides, or synthetic species formed from naturally occurring subunits or their close homologs. Antisense polynucleotides may also have altered sugar moieties or inter-sugar linkages. Exemplary among these are the phosphorothioate and other sulfur containing species which are known for use in the art. Analogs are comprised by this invention so long as they function effectively to hybridize with nucleotides of the invention. See, e.g., Isis Pharmaceuticals, Carlsbad, CA; Sequitor, Inc., Natick, MA. Such antisense polynucleotides can readily be synthesized using recombinant means, or can be synthesized in vitro. Equipment for such synthesis is sold by several vendors, including Applied Biosystems. The preparation of other oligonucleotides such as phosphorothioates and alkylated derivatives is also well known to those of skill in the art. Antisense molecules as used herein include antisense or sense oligonucleotides. Sense oligonucleotides can, e.g., be employed to block transcription by binding to the anti-sense strand. The antisense and sense oligonucleotide comprise a single stranded nucleic acid sequence (either RNA or DNA) capable of binding to target mRNA (sense) or DNA (antisense) sequences for cancer molecules. Antisense or sense oligonucleotides, according to the present invention, comprise a fragment generally at least about 12 nucleotides, preferably from about 12 to 30 nucleotides. The ability to derive 83 WO 03/087306 PCT/US03/10462 an antisense or a sense oligonucleotide, based upon a cDNA sequence encoding a given protein is described in, e.g., Stein &Cohen (Cancer Res. 48:2659 (1988 and van der Krol et al. (BioTechniques 6:958 (1988)). Ribozymes In addition to antisense polynucleotides, ribozymes can be used to target and inhibit transcription of cancer associated nucleotide sequences. A ribozyme is an RNA molecule that catalytically cleaves other RNA molecules. Different kinds of ribozymes have been described, including group I ribozymes, hammerhead ribozymes, hairpin ribozymes, RNase P, and axhead ribozymes (see, e.g., Castanotto et al., Adv. in Pharmacology 25: 289-317 (1994) for a general review of the properties of different ribozymes). The general features of hairpin ribozymes are described, e.g., in Hampel et al., Nucl. Acids Res. 18:299-304 (1990); European Patent Publication No. 0360257; U.S. Patent No. 5,254,678. Methods of preparing are well known to those of skill in the art (see, e.g., WO 94/26877; Ojwang et al., Proc. Natl. Acad. Sci. USA 90:6340-6344 (1993); Yamada et al., Human Gene Therapy 1:39-45 (1994); Leavitt et al., Proc. Natl. Acad Sci. USA 92:699- 703 (1995); Leavitt et al., Human Gene Therapy 5:1151-120 (1994); and Yamada et al., Virology 205:121-126 (1994)). Use of Modulators in Phenotypic Screening In one embodiment, a test compound is administered to a population of cancer cells, which have an associated cancer expression profile. By "administration" or "contacting" herein is meant that the modulator is added to the cells in such a manner as to allow the modulator to act upon the cell, whether by uptake and intracellular action, or by action at the cell surface. In some embodiments, a nucleic acid encoding a proteinaceous agent (i.e., a peptide) is put into a viral construct such as an adenoviral or retroviral construct, and added to the cell, such that expression of the peptide agent is accomplished, e.g., PCT US97/01019. Regulatable gene therapy systems can also be used. Once the modulator has been administered to the cells, the cells are washed if desired and are allowed to incubate under preferably physiological conditions for some period. The cells are then harvested and a new gene expression profile is generated. Thus, e.g., cancer tissue is screened for agents that modulate, e.g., induce or suppress, the cancer phenotype. A change in at least one gene, preferably many, of the expression profile indicates that the agent has an effect on cancer activity. Similarly, altering a biological function or a signaling pathway is indicative of modulator activity. By defining such a signature for the cancer phenotype, screens for new drugs that alter the phenotype are devised. With this approach, the drug target need not be known and need not be represented in the original gene/protein expression screening platform, nor does the level of transcript for the target protein need to change. The modulator inhibiting function will serve as a surrogate marker As outlined above, screens are done to assess genes or gene products. That is, having identified a particular differentially expressed gene as important in a particular state, screening of modulators of either the expression of the gene or the gene product itself is performed. Use of Modulators to Affect Peptides of the Invention Measurements of cancer polypeptide activity, or of the cancer phenotype are performed using a variety of assays. For example, the effects of modulators upon the function of a cancer polypeptide(s) are measured by examining parameters described above. A physiological change that affects activity is used to assess the influence of a test compound on the polypeptides of this invention. When the functional outcomes are determined using intact cells or animals, a variety of effects can be assesses such as, in the case of a cancer associated with solid tumors, tumor growth, tumor metastasis, neovascularization, hormone release, transcriptional changes to both known and uncharacterized genetic markers (e.g., by Northern blots), changes in cell metabolism such as cell growth or pH changes, and changes in intracellular second messengers such as cGNIP. 84 WO 03/087306 PCT/US03/10462 Methods of Identifying Characterizing Cancer-associated Sequences Expression of various gene sequences is correlated with cancer. Accordingly, disorders based on mutant or variant cancer genes are determined. In one embodiment, the invention provides methods for identifying cells containing variant cancer genes, e.g., determining the presence of, all or part, the sequence of at least one endogenous cancer gene in a cell. This is accomplished using any number of sequencing techniques. The invention comprises methods of identifying the cancer genotype of an individual, e.g., determining all or part of the sequence of at least one gene of the invention in the individual. This is generally done in at least one tissue of the individual, e.g., a tissue set forth in Table I, and may include the evaluation of a number of tissues or different samples of the same tissue. The method may include comparing the sequence of the sequenced gene to a known cancer gene, i.e., a wild-type gene to determine the presence of family members, homologies, mutations or variants. The sequence of all or part of the gene can then be compared to the sequence of a known cancer gene to determine if any differences exist. This is done using any number of known homology programs, such as BLAST, Bestlit, etc. The presence of a difference in the sequence between the cancer gene of the patient and the known cancer gene correlates with a disease state or a propensity for a disease state, as outlined herein. In a preferred embodiment, the cancer genes are used as probes to determine the number of copies of the cancer gene in the genome. The cancer genes are used as probes to determine the chromosomal localization of the cancer genes. Information such as chromosomal localization finds use in providing a diagnosis or prognosis in particular when chromosomal abnormalities such as translocations, and the like are identified in the cancer gene locus. XIV.) Kits/Articles of Manufacture For use in the diagnostic and therapeutic applications described herein, kits are also within the scope of the invention. Such kits can comprise a carrier, package or container that is compartmentalized to receive one or more containers such as vials, tubes, and the like, each of the container(s) comprising one of the separate elements to be used in the method. For example, the container(s) can comprise a probe that is or can be detectably labeled. Such probe can be an antibody or polynucleotide specific for a Figure 2-related protein or a Figure 2 gene or message, respectively. Where the method utilizes nucleic acid hybridization to detect the target nucleic acid, the kit can also have containers containing nucleotide(s) for amplification of the target nucleic acid sequence and/or a container comprising a reporter-means, such as a biotin-binding protein, such as avidin or streptavidin, bound to a reporter molecule, such as an enzymatic, florescent, or radioisotope label. The kit can include all or part of the amino acid sequences in Figure 2 or Figure 3 or analogs thereof, or a nucleic acid molecules that encodes such amino acid sequences. The kit of the invention will typically comprise the container described above and one or more other containers comprising materials desirable from a commercial and user standpoint, including buffers, diluents, filters, needles, syringes; carrier, package, container, vial and/or tube labels listing contents and/or instructions for use, and package inserts with instructions for use. A label can be present on the container to indicate that the composition is used for a specific therapy or non-therapeutic application, such as a diagnostic or laboratory application, and can also indicate directions for either in vivo or in vitro use, such as those described herein. Directions and or other information can also be included on an insert(s) or label(s) which is included with or on the kit. The terms "kit" and "article of manufacture" can be used as synonyms. In another embodiment of the invention, an article(s) of manufacture containing compositions, such as amino acid sequence(s), small molecule(s), nucleic acid sequence(s), and/or antibody(s), e.g., materials useful for the diagnosis, prognosis, prophylaxis and/or treatment of neoplasias of tissues such as those set forth in Table I is provided. The article of 85 WO 03/087306 PCT/US03/10462 manufacture typically comprises at least one container and at least one label. Suitable containers include, for example, bottles, vials, syringes, and test tubes. The containers can be formed from a variety of materials such as glass or plastic. The container can hold amino acid sequence(s), small molecule(s), nucleic acid sequence(s), and/or antibody(s), in one embodiment the container holds a polynucleotide for use in examining the mRNA expression profile of a cell,, together with reagents used for this purpose. The container can alternatively hold a composition which is effective for treating, diagnosis, prognosing or prophylaxing a condition and can have a sterile access port (for example the container can be an intravenous solution bag or a vial having a stopper pierceable by a hypodermic injection needle). The active agents in the composition can be an antibody capable of specifically binding 98P4B6 and modulating the function of 98P4B6. The label can be on or associated with the container. A label a can be on a container when letters, numbers or other characters forming the label are molded or etched into the container itself; a label can be associated with a container when it is present within a receptacle or carrier that also holds the container, e.g., as a package insert. The label can indicate that the composition is used for diagnosing, treating, prophylaxing or prognosing a condition, such as a neoplasia of a tissue set forth in Table I. The article of manufacture can further comprise a second container comprising a pharmaceutically-acceptable buffer, such as phosphate-buffered saline, Ringer's solution and/ordextrose solution. It can further include other materials desirable from a commercial and user standpoint, including other buffers, diluents, filters, stirrers, needles, syringes, and/or package inserts with indications and/or instructions for use. EXAMPLES: Various aspects of the invention are further described and illustrated by way of the several examples that follow, none of which are intended to limit the scope of the invention. Example 1: SSH-Generated Isolation of cDNA Fragqment of the 98P486 Gene To isolate genes that are over-expressed in prostate cancer we used the Suppression Subtractive Hybridization (SSH) procedure using cDNA derived from prostate tissues. The 98P4B6 SSH cDNA sequence was derived from normal prostate minus LAPC-4AD prostate xenograft cDNAs. The 98P4B6 cDNA was identified as highly expressed in prostate cancer. Materials and Methods Human Tissues: The patient cancer and normal tissues were purchased from different sources such as the NDRI (Philadelphia, PA). mRNA for some normal tissues were purchased from Clontech, Palo Alto, CA. RNA Isolation: Tissues were homogenized in Trizol reagent (Life Technologies, Gibco BRL) using 10 ml/ g tissue isolate total RNA. Poly A RNA was purified from total RNA using Qiagen's Oligotex mRNA Mini and Midi kits. Total and mRNA were quantified by spectrophotometric analysis (O.D. 260/280 nm) and analyzed by gel electrophoresis. Oligonucleotides: The following HPLC purified oligonucleotides were used. DPNCDN (cDNA synthesis primer): 5'TTTTGATCAAGCTT3o3' (SEQ ID NO: 101) Adaptor 1: 5'CTAATACGACTCACTATAGGGCTCGAGCGGCCGCCCGGGCAG3' (SEQ ID NO: 102) 86 WO 03/087306 PCT/US03/10462 3'GGCCCGTCCTAG5' (SEQ ID NO: 103) Adaptor 2: 5'GTAATACGACTCACTATAGGGCAGCGTGGTCGCGGCCGAG3' (SEQ ID NO: 104) 3'CGGCTCCTAG5' (SEQ ID NO: 105) PCR primer 1: 5'CTAATACGACTCACTATAGGGC3' (SEQ ID NO: 106) Nested primer (NP)1: 5'TCGAGCGGCCGCCCGGGCAGGA3' (SEQ ID NO: 107) Nested primer (NP)2: 5'AGCGTGGTCGCGGCCGAGGA3' (SEQ ID NO: 108) Suppression Subtractive Hybridization: Suppression Subtractive Hybridization (SSH) was used to identify cDNAs corresponding to genes that may be differentially expressed in prostate cancer. The SSH reaction utilized cDNA from prostate cancer xenograft and normal tissues. The gene 98P486 sequence was derived from normal prostate tissue minus prostate cancer xenograft LAPC-4AD cDNA subtraction. The SSH DNA sequence (Figure 1) was identified. The cDNA derived from LAPC-4AD was used as the source of the "driver" cDNA, while the cDNA from normal prostate was used as the source of the "tester" cDNA. Double stranded cDNAs corresponding to tester and driver cDNAs were synthesized from 2 pg of poly(A)* RNA isolated from the relevant tissue, as described above, using CLONTECH's PCR-Select cDNA Subtraction Kit and 1 ng of oligonucleotide DPNCDN as primer. First- and second-strand synthesis were carried out as described in the Kit's user manual protocol (CLONTECH Protocol No. PT1117-1, Catalog No. K1804-1). The resulting cDNA was digested with Dpn II for 3 hrs at 3700. Digested cDNA was extracted with phenol/chloroform (1:1) and ethanol precipitated. Driver cDNA was generated by combining in a 1:1 ratio Dpn II digested cDNA from the relevant tissue source (see above) with digested cDNAs derived from normal tissue. Tester cDNA was generated by diluting 1 p1 of Dpn II digested cDNA from the relevant tissue source (see above) (400 ng) in 5 pl of water. The diluted cDNA (2 pl, 160 ng) was then ligated to 2 pl of Adaptor 1 and Adaptor 2 (10 pM), in separate ligation reactions, in a total volume of 10 pl at 160C overnight, using 400 u ofT4 DNA ligase (CLONTECH). Ligation was terminated with 1 pl of 0.2 M EDTA and heating at 72oC for 5 min. The first hybridization was performed by adding 1.5 pI (600 ng) of driver cDNA to each of two tubes containing 1.5 1( 2 0 ng) Adaptor 1- and Adaptor 2- ligated tester cDNA. In a final volume of 4 p, the samples were overlaid with mineral oil, denatured in an MJ Research thermal cycler at 980C for 1.5 minutes, and then were allowed to hybridize for 8 hrs at 68oC. The two hybridizations were then mixed together with an additional 1 p of fresh denatured driver cDNA and were allowed to hybridize overnight at 68oC. The second hybridization was then diluted in 200 pl of 20 mM Hepes, pH 8.3, 50 mM NaCl, 0.2 mM EDTA, heated at 70oC for 7 min. and stored at -20oC. PCR Amplification, Cloning and Sequencing of Gene Fragments Generated from SSH: To amplify gene fragments resulting from SSH reactions, two PCR amplifications were performed. In the primary PCR reaction 1 pl of the diluted final hybridization mix was added to 1 pl of PCR primer 1 (10 pM), 0.5 pl dNTP mix (10 pM), 2.5 p 10 x reaction buffer (CLONTECH) and 0.5 p 50 x Advantage cDNA polymerase Mix (CLONTECH) in a final volume of 25 pl. PCR 1 was conducted using the following conditions: 75oC for 5 min., 94oC for 25 sec., then 27 cycles of 94oC for 10 sec, 660C for 30 sec, 72oC for 1.5 min. Five separate primary PCR reactions were performed for each experiment. The products were pooled and diluted 1:10 with water. For the secondary PCR reaction, 1 pl from the pooled and diluted primary PCR reaction was added to the 87 WO 03/087306 PCT/USO3/10462 same reaction mix as used for PCR 1, except that primers NP1 and NP2 (10 pM) were used instead of PCR primer 1. PCR 2 was performed using 10-12 cycles of 94oC for 10 sec, 680C for 30 sec, and 72oC for 1.5 minutes. The PCR products were analyzed using 2% agarose gel electrophoresis. The PCR products were inserted into pCR2.1 using the T/A vector cloning kit (Invitrogen). Transformed E. coli were subjected to blue/white and ampicillin selection. White colonies were picked and arrayed into 96 well plates and were grown in liquid culture overnight. To identify inserts, PCR amplification was performed on 1 ul of bacterial culture using the conditions of PCR1 and NP1 and NP2 as primers. PCR products were analyzed using 2% agarose gel electrophoresis. Bacterial clones were stored in 20% glycerol in a 96 well format. Plasmid DNA was prepared, sequenced, and subjected to nucleic acid homology searches of the GenBank, dBest, and NCI-CGAP databases. RT-PCR Expression Analysis: First strand cDNAs can be generated from 1 pig of mRNA with oligo (dT)12-18 priming using the Gibco-BRL Superscript Preamplification system. The manufacturer's protocol was used which included an incubation for 50 min at 420C with reverse transcriptase followed by RNAse H treatment at 37oC for 20 min. After completing the reaction, the volume can be increased to 200 p with water prior to normalization. First strand cDNAs from 16 different normal human tissues can be obtained from Clontech. Normalization of the first strand cDNAs from multiple tissues was performed by using the primers 5'atatcgccgcgctcgtcgtcgacaa3' (SEQ ID NO: 109) and 5'agccacacgcagctcattgtagaagg 3' (SEQ ID NO: 110) to amplify P3-actin. First strand cDNA (5 pl) were amplified in a total volume of 50 pl containing 0.4 pM primers, 0.2 pM each dNTPs, 1XPCR buffer (Clontech, 10 mM Tris-HCL, 1.5 mM MgCI2, 50 mM KCI, pH8.3) and 1X Klentaq DNA polymerase (Clontech). Five pl of the PCR reaction can be removed at 18, 20, and 22 cycles and used for agarose gel electrophoresis. PCR was performed using an MJ Research thermal cycler under the following conditions: Initial denaturation can be at 94oC for 15 sec, followed by a 18, 20, and 22 cycles of 94oC for 15, 6500 for 2 min, 72oC for 5 sec. A final extension at 72oC was carried out for 2 min. After agarose gel electrophoresis, the band intensities of the 283 bp p-actin bands from multiple tissues were compared by visual inspection. Dilution factors for the first strand cDNAs were calculated to result in equal P-actin band intensities in all tissues after 22 cycles of PCR. Three rounds of normalization can be required to achieve equal band intensities in all tissues after 22 cycles of PCR. To determine expression levels of the 98P4B6 gene, 5 pl of normalized first strand cDNA were analyzed by PCR using 26, and 30 cycles of amplification. Semi-quantitative expression analysis can be achieved by comparing the PCR products at cycle numbers that give light band intensities. The primers used for RT-PCR were designed using the 98P4B6 SSH sequence and are listed below: 98P4B6.1 5'- GACTGAGCTGGAACTGGAATTTGT - 3' (SEQ ID NO: 111) 98P4B6.2 5'- TTTGAGGAGACTTCATCTCACTGG - 3' (SEQ ID NO: 112) Example 2: Isolation of Full Length 98P4B6 Encoding cDNA The 98P4B6 SSH cDNA sequence was derived from a substraction consisting of normal prostate minus prostate cancer xenograft. The SSH cDNA sequence (Figure 1) was designated 98P4B6. The 98P4B6 SSH DNA sequence of 183 bp is shown in Figure 1. Full-length 98P486 v.1 (clone GTD3) of 2453 bp was cloned from prostate cDNA library, revealing an ORF of 454 amino acids (Figure 2 and Figure 3). 98P4B6 v.6 was also cloned from normal prostate library. Other variants of 98P4B6 were also identified and these are listed in Figures 2 and 3. 88 WO 03/087306 PCT/USO3/10462 98P4B6 v.2, v.3, v.4, v.5, v.6, v.7 and v.8 are splice variants of 98P4B6 v.1. 98P4B6 v.9 through v.19 are SNP variants and differ from v.1 by one amino acid. 98P4B6 v.20 through v.24 are SNP variants of v.7. 98P4B6 v.25 through v.38 are SNP variants of v.8. Though these SNP variants were shown separately, they could also occur in any combinations and in any transcript variants. Example 3: Chromosomal Mapping of 98P4B6 Chromosomal localization can implicate genes in disease pathogenesis. Several chromosome mapping approaches are available including fluorescent in situ hybridization (FISH), human/hamster radiation hybrid (RH) panels (Walter et al., 1994; Nature Genetics 7:22; Research Genetics, Huntsville AI), human-rodent somatic cell hybrid panels such as is available from the Cornell Institute (Camden, New Jersey), and genomic viewers utilizing BLAST homologies to sequenced and mapped genomic clones (NCBI, Bethesda, Maryland). 98P4B6 maps to chromosome 7q21using 98P4B6 sequence and the NCBI BLAST tool: located on the World Wide Web at .ncbi.nlm.nih.gov/genome/seq/page.cgi?F=HsBlast.html&&ORG=Hs). Example 4: Expression Analysis of 98P4B6 Expression analysis by RT-PCR demonstrated that 98P4B6 is strongly expressed in prostate cancer patient specimens (Figure 14). First strand cDNA was generated from normal stomach, normal brain, normal heart, normal liver, normal skeletal muscle, normal testis, normal prostate, normal bladder, normal kidney, normal colon, normal lung, normal pancreas, and a pool of cancer specimens from prostate cancer patients, bladder cancer patients, kidney cancer patients, colon cancer patients, lung cancer patients, pancreas cancer patients, and a pool of 2 patient prostate metastasis to lymph node. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers directed to 98P4B6 v.1, v.13, or/and v.14 (A), or directed specifically to the splice variants 98P4B6 v.6 and v.8 (8), was performed at 26 and 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Results show strong expression of 98P4B6 and its splice variants v.6 and v.8 in normal prostate and in prostate cancer. Expression was also detected in bladder cancer, kidney cancer, colon cancer, lung cancer, pancreas cancer, breast cancer, cancer metastasis as well as in the prostate cancer metastasis to lymph node specimens, compared to all normal tissues tested. As noted below, e.g., in Example 6, as 98P4B6 v.1 is in expressed in cancer tissues such as those listed in Table 1, the other protein-encoding 98P4B6 variants are expressed in these tissues as well; this principle is corroborated by data in (Figure 14) for the proteins herein designated 98P4B6 v.6 or v.8 is found, e.g., in prostate, lung, ovary, bladder, breast, colon, kidney and pancreas, cancers, as well as in the literature (Porkka et al., Lab Invest, 2002 and Korkmaz et al., JBC, 2002) where the protein 98P4B6 v.8 is identified in normal prostate and prostate cancer. When the genomic region to which a gene maps is modulated in a particular cancer, the alternative transcripts or splice variants of the gene are modulated as well. Disclosed herein is that 98P4B6 has a particular expression profile related to cancer. Alternative transcripts and splice variants of 98P4B6 are also involved in cancers in the same or additional tissues, thus serving as tumor-associated markers/antigens. Expression of 98P4B6 v.1, v.13, and/or v.14 was detected in prostate, lung, ovary, bladder, cervix, uterus and pancreas cancer patient specimens (Figure 15). First strand cDNA was prepared from a panel of patient cancer specimens. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers to 98P4B6, was performed at 26 and 30 cycles of amplification. Samples were run on an agarose gel, and PCR products were quantitated using the Alphalmager software. Expression was recorded as absent, low, medium or strong. Results show expression of 98P4B6 in the majority of all patient cancer specimens tested. 89 WO 03/087306 PCT/US03/10462 Figure 16 shows that 98P4B6 is expressed in stomach cancer patient specimens. (A) RNA was extracted from normal stomach (N) and from 10 different stomach cancer patient specimens (T). Northern blot with 10 ptg of total RNA/Ilane was probed with 98P4B6 sequence. Results show strong expression of 98P4B6 in the stomach tumor tissues and lower expression in normal stomach. The lower panel represents ethidium bromide staining of the blot showing quality of the RNA samples. (B) Expression of 98P4B6 was assayed in a panel of human stomach cancers (T) and their respective matched normal tissues (N) on RNA dot blots. 98P4B6 was detected in 7 out of 8 stomach tumors but not in the matched normal tissues. Example 5: Transcript Variants of 98P4B6 Transcript variants are variants of mature mRNA from the same gene which arise by alternative transcription or alternative splicing. Alternative transcripts are transcripts from the same gene but start transcription at different points. Splice variants are mRNA variants spliced differently from the same transcript. In eukaryotes, when a multi-exon gene is transcribed from genomic DNA, the initial RNA is spliced to produce functional mRNA, which has only exons and is used for translation into an amino acid sequence. Accordingly, a given gene can have zero to many alternative transcripts and each transcript can have zero to many splice variants. Each transcript variant has a unique exon makeup, and can have different coding and/or non-coding (5' or 3' end) portions, from the original transcript. Transcript variants can code for similar or different proteins with the same or a similar function or can encode proteins with different functions, and can be expressed in the same tissue at the same time or in different tissues at the same time or in the same tissue at different times or in different tissues at different times. Proteins encoded by transcript variants can have similar or different cellular or extracellular localizations, e.g., secreted versus intracellular. Transcript variants are identified by a variety of art-accepted methods. For example, alternative transcripts and splice variants are identified by full-length cloning experiment, or by use of full-length transcript and EST sequences. First, all human ESTs were grouped into clusters which show direct or indirect identity with each other. Second, ESTs in the same duster were further grouped into sub-clusters and assembled into a consensus sequence. The original gene sequence is compared to the consensus sequence(s) or other full-length sequences. Each consensus sequence is a potential splice variant for that gene. Even when a variant is identified that is not a full-length clone, that portion of the variant is very useful for antigen generation and for further cloning of the full-length splice variant, using techniques known in the art. Moreover, computer programs are available in the art that identify transcript variants based on genomic sequences. Genomic-based transcript variant identification programs include FgenesH (A. Salamov and V. Solovyev, "Ab initio gene finding in Drosophila genomic DNA," Genome Research. 2000 April;10(4):516-22); Grail (URL compbio.ornl.gov/Grail-bin/EmptyGrailForm) and GenScan (URL genes.mit.edu/GENSCAN.html). For a general discussion of splice variant identification protocols see., e.g., Southan, C., A genomic perspective on human proteases, FEBS Lett. 2001 Jun 8; 498(2-3):214-8; de Souza, S.J., etal., Identification of human chromosome 22 transcribed sequences with ORF expressed sequence tags, Proc. NatI Acad Sci U S A. 2000 Nov 7; 97(23):12690-3. To further confirm the parameters of a transcript variant, a variety of techniques are available in the art, such as full-length cloning, proteomic validation, PCR-based validation, and 5' RACE validation, etc. (see e.g., Proteomic Validation: Brennan, S.O., et aL., Albumin banks peninsula: a new termination variant characterized by electrospray mass spectrometry, Biochem Biophys Acta. 1999 Aug 17;1433(1-2):321-6; Ferranti P, et at, Differential splicing of pre-messenger RNA produces multiple forms of mature caprinealpha(sl)-casein, Eur J Biochem. 1997 Oct 1;249(1):1-7. For PCR-based Validation: Wellmann S, et aL., Specific reverse transcription-PCR quantification of vascular endothelial growth factor (VEGF) splice variants by LightCycler technology, Clin Chem. 2001 Apr;47(4):654-60; Jia, H.P., et al., Discovery of new human beta defensins using a genomics-based approach, Gene. 2001 Jan 24; 263(1-2):211-8. For PCR-based and 5' RACE Validation: 90 WO 03/087306 PCT/USO3/10462 Brigle, K.E., et al., Organization of the murine reduced folate carrier gene and identification of variant splice forms, Biochem Biophys Acta. 1997 Aug 7; 1353(2): 191-8). It is known in the art that genomic regions are modulated in cancers. Recently, Porkka et al. (2002) reported that transcript variants of STEAP2 were expressed and were found in both normal and malignant prostate tissue (Porkka, K.P., et al. Cloning and characterization of a novel six-transmembrane protein STEAP2, expressed in normal and malignant prostate. Laboratory Investigation 2002 Nov; 82(11):1573-1582). Another group of scientists also reported that transcript variants of STEAP2 (98P4B6 v.6 herein) also were expressed significantly higher in prostate cancer than normal prostate (Korkmaz, K.S., et al. Molecular cloning and characterization of STAMP1, a highly prostate-specific six transmembrane protein that is overexpressed in prostate cancer. The Journal of Biological Chemistry. 2002 Sept. 277(39):36689-36696.). When the genomic region to which a gene maps is modulated in a particular cancer, the alternative transcripts or splice variants of the gene are modulated as well. Disclosed herein is that 98P4B6 has a particular expression profile related to cancer. Alternative transcripts and splice variants of 98P4B6 are also involved in cancers in the same or additional tissues, thus serving as tumor-associated markers/antigens. Using the full-length gene and EST sequences, seven transcript variants were identified, designated as 98P4B6 v.2, v.3, v.4, v.5, v.6, v.7 and v.8, as shown in Figure 12. The boundaries of exons in the original transcript, 98P4B6 v.1 were shown in Table LI. The first 22 bases of v.1 were not in the nearby 5' region of v.1 on the current assembly of the human genome. Compared with 98P4B6 v.1, variant v.2 was a single exon transcript whose 3' portion was the same as the last exon of v.1. The first two exons of v.3 were in intron 1 of v. 1. Variants v.4, v.5, and v.6 spliced out 224-334 in the first exon of v.1. In addition, v.5 spliced out exon 5 while v.6 spliced out exon 6 but extended exon 5 of v.1. Variant v.7 used alternative transcription start and different 3' exons. Variant v.8 extended 5' end and kept the whole intron 5 of v.1. Theoretically, each different combination of exons in spatial order, e.g. exons 2 and 3, is a potential splice variant. Tables LII through LV are set forth on a variant-by-variant basis. Tables LII(a) - (g) show the nucleotide sequence of the transcript variant. Tables LIII (a) - (g) show the alignment of the transcript variant with the nucleic acid sequence of 98P4B6 v.1. Tables LIV(a) - (g) lay out the amino acid translation of the transcript variant for the identified reading frame orientation. Tables LV(a) - (g) display alignments of the amino acid sequence encoded by the splice variant with that of 98P4B6 v.1. Additionally, single nucleotide polymorphisms (SNP) are noted in the alignment. Example 6: Single Nucleotide Polymorphisms of 98P4B6 A Single Nucleotide Polymorphism (SNP) is a single base pair variation in a nucleotide sequence at a specific location. At any given point of the genome, there are four possible nucleotide base pairs: A/T, C/G, G/C and T/A. Genotype refers to the specific base pair sequence of one or more locations in the genome of an individual. Haplotype refers to the base pair sequence of more than one location on the same DNA molecule (or the same chromosome in higher organisms), often in the context of one gene or in the context of several tightly linked genes. SNP that occurs on a cDNA is called cSNP. This cSNP may change amino acids of the protein encoded by the gene and thus change the functions of the protein. Some SNP cause inherited diseases; others contribute to quantitative variations in phenotype and reactions to environmental factors including diet and drugs among individuals. Therefore, SNP and/or combinations of alleles (called haplotypes) have many applications, including diagnosis of inherited diseases, determination of drug reactions and dosage, identification of genes responsible for diseases, and analysis of the genetic relationship between individuals (P. Nowotny, J. M. Kwon and A. M. Goate," SNP analysis to dissect human traits," Curr. Opin. Neurobiol. 2001 Oct; 11(5):637-641; M. Pirmohamed and B. K. Park, "Genetic susceptibility to adverse drug reactions," Trends Pharmacol. Sci. 2001 Jun; 22(6):298-305; J. H. Riley, C. J. Allan, E. Lai and A. Roses, " The use of single nucleotide polymorphisms in the isolation of common disease genes," 91 WO 03/087306 PCT/USO3/10462 Pharmacogenomics. 2000 Feb; 1(1):39-47; R. Judson, J. C. Stephens and A. Windemuth, "The predictive power of haplotypes in clinical response," Pharmacogenomics. 2000 feb; 1(1):15-26). SNP are identified by a variety of art-accepted methods (P. Bean, "The promising voyage of SNP target discovery," Am. Clin. Lab. 2001 Oct-Nov; 20(9):18-20; K. M. Weiss, "In search of human variation," Genome Res. 1998 Jul; 8(7):691 697; M. M. She, "Enabling large-scale pharmacogenetic studies by high-throughput mutation detection and genotyping technologies," Clin. Chem. 2001 Feb; 47(2):164-172). For example, SNP can be identified by sequencing DNA fragments that show polymorphism by gel-based methods such as restriction fragment length polymorphism (RFLP) and denaturing gradient gel electrophoresis (DGGE). They can also be discovered by direct sequencing of DNA samples pooled from different individuals or by comparing sequences from different DNA samples. With the rapid accumulation of sequence data in public and private databases, one can discover SNP by comparing sequences using computer programs (Z. Gu, L. Hillier and P. Y. Kwok, "Single nucleotide polymorphism hunting in cyberspace," Hum. Mutat. 1998; 12(4):221-225). SNP can be verified and genotype or haplotype of an individual can be determined by a variety of methods including direct sequencing and high throughput microarrays (P. Y. Kwok, "Methods for genotyping single nucleotide polymorphisms," Annu. Rev. Genomics Hum. Genet. 2001; 2:235-258; M. Kokoris, K. Dix, K. Moynihan, J. Mathis, B. Erwin, P. Grass, B. Hines and A. Duesterhoeft, "High-throughput SNP genotyping with the Masscode system," Mol. Diagn. 2000 Dec; 5(4):329-340). Using the methods described above, eleven SNP were identified in the original transcript, 98P4B6 v.1, at positions 46 (NG), 179 (C/T), 180 (A/G), 269 (NG), 404 (G/T), 985 (C/T), 1170 (T/C), 1497 (NG), 1746 (T/G), 2046 (T/G) and 2103 (T/C). The transcripts or proteins with alternative allele were designated as variant 98P4B6 v.9 through v.19, as shown in Figure 10 a. Figure 11 shows the schematic alignment of protein variants, corresponding to nucleotide variants. Nucleotide variants that code for the same amino acid sequence as v.1 are not shown in Figure 11. These alleles of the SNP, though shown separately here, can occur in different combinations (haplotypes) and in any one of the transcript variants (such as 98P4B6 v.5) that contains the site of the SNP. In addition, there were SNP in other transcript variants in regions not shared with v.1. For example, there were fourteen SNP in the fifth intron of v.1, which was part of transcript variants v.2, v.6 and v.8. These SNP are shown in Figure 10c and listed as following (numbers relative v.8): 1760 (G/A), 1818 (Gr), 1870 (C/T), 2612 (T/C), 2926 (T/A), 4241 (T/A), 4337 (NAG), 4338 (NAC), 4501 (A/G), 4506 (CIT), 5434 (CIA), 5434 (C/G), 5434 (C/Tf) and 5589 (C/A). Figure 10b shows the SNP in the unique regions of transcript variant v.7: 1956 (A/C), 1987 (TIA), 2010 (G/C), 2010 (GIT) and 2059 (G/A) (numbers correspond to nucleotide sequence of v.7). Example 7: Production of Recombinant 98P4B6 in Prokarvotic Systems To express recombinant 98P4B6 and 98P4B6 variants in prokaryotic cells, the full or partial length 98P4B6 and 98P4B6 variant cDNA sequences are cloned into any one of a variety of expression vectors known in the art. One or more of the following regions of 98P4B6 variants are expressed: the full length sequence presented in Figures 2 and 3, or any 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 98P4B6, variants, or analogs thereof. A. In vitro transcription and translation constructs: gRIL To generate 98P4B6 sense and anti-sense RNA probes for RNA in situ investigations, pCRII constructs (Invitrogen, Carlsbad CA) are generated encoding either all or fragments of the 98P4B6 cDNA. The pCRII vector has Sp6 and T7 promoters flanking the insert to drive the transcription of 98P4B6 RNA for use as probes in RNA in situ hybridization experiments. These probes are used to analyze the cell and tissue expression of 98P4B6 at the RNA level. Transcribed 98P4B6 RNA representing the cDNA amino acid coding region of the 98P4B6 gene is used in in vitro translation systems such as the Tn

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M Coupled Reticulolysate System (Promega, Corp., Madison, WI) to synthesize 98P4B6 protein. 92 WO 03/087306 PCT/US03/10462 B. Bacterial Constructs: pGEX Constructs: To generate recombinant 98P4B6 proteins in bacteria that are fused to the Glutathione S transferase (GST) protein, all or parts of the 98P4B6 cDNA protein coding sequence are cloned into the pGEX family of GST-fusion vectors (Amersham Pharmacia Biotech, Piscataway, NJ). These constructs allow controlled expression of recombinant 98P486 protein sequences with GST fused at the amino-terminus and a six histidine epitope (6X His) at the carboxyl-terminus. The GST and 6X His tags permit purification of the recombinant fusion protein from induced bacteria with the appropriate affinity matrix and allow recognition of the fusion protein with anti-GST and anti-His antibodies. The 6X His tag is generated by adding 6 histidine codons to the cloning primer at the 3' end, e.g., of the open reading frame (ORF). A proteolytic cleavage site, such as the PreScissionTM recognition site in pGEX-6P-1, may be employed such that it permits cleavage of the GST tag from 98P486-related protein. The ampicillin resistance gene and pBR322 origin permits selection and maintenance of the pGEX plasmids in E col. A glutathione-S-transferase (GST) fusion protein encompassing amino acids 2-204 of the STEAP-2 protein sequence was generated in the pGEX vector. The recombinant GST-STEAP-2 fusion protein was purified from induced bacteria by glutathione-sepaharose affinity chromatography and used as immunogen for generation of a polyclonal antibody. pMAL Constructs: To generate, in bacteria, recombinant 98P4B6 proteins that are fused to maltose-binding protein (MBP), all or parts of the 98P4B6 cDNA protein coding sequence are fused to the MBP gene by cloning into the pMAL-c2X and pMAL-p2X vectors (New England Biolabs, Beverly, MA). These constructs allow controlled expression of recombinant 98P4B6 protein sequences with MBP fused at the amino-terminus and a 6X His epitope tag at the carboxyl terminus. The MBP and 6X His tags permit purification of the recombinant protein from induced bacteria with the appropriate affinity matrix and allow recognition of the fusion protein with anti-MBP and anti-His antibodies. The 6X His epitope tag is generated by adding 6 histidine codons to the 3' cloning primer. A Factor Xa recognition site permits cleavage of the pMAL tag from 98P4B6. The pMAL-c2X and pMAL-p2X vectors are optimized to express the recombinant protein in the cytoplasm or periplasm respectively. Periplasm expression enhances folding of proteins with disulfide bonds. pET Constructs: To express 98P4B6 in bacterial cells, all or parts of the 98P4B6 cDNA protein coding sequence are cloned into the pET family of vectors (Novagen, Madison, WI). These vectors allow tightly controlled expression of recombinant 98P4B6 protein in bacteria with and without fusion to proteins that enhance solubility, such as NusA and thioredoxin (Trx), and epitope tags, such as 6X His and S-Tag

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M that aid purification and detection of the recombinant protein. For example, constructs are made utilizing pET NusA fusion system 43.1 such that regions of the 98P4B6 protein are expressed as amino-terminal fusions to NusA. C. Yeast Constructs: pESC Constructs: To express 98P4B6 in the yeast species Saccharomyces cerevisiae for generation of recombinant protein and functional studies, all or parts of the 98P4B6 cDNA protein coding sequence are cloned into the pESC family of vectors each of which contain 1 of 4 selectable markers, HIS3, TRP1, LEU2, and URA3 (Stratagene, La Jolla, CA). These vectors allow controlled expression from the same plasmid of up to 2 different genes or cloned sequences containing either FlagTM or Myc epitope tags in the same yeast cell. This system is useful to confirm protein-protein interactions of 98P4B6. In addition, expression in yeast yields similar post-translational modifications, such as glycosylations and phosphorylations, that are found when expressed in eukaryotic cells. pESP Constructs: To express 98P4B6 in the yeast species Saccharomyces pombe, all or parts of the 98P4B6 cDNA protein coding sequence are cloned into the pESP family of vectors. These vectors allow controlled high level of expression of a 98P4B6 protein sequence that is fused at either the amino terminus or at the carboxyl terminus to GST which aids purification of the recombinant protein. A FlagTM epitope tag allows detection of the recombinant protein with anti- Flag T M antibody. 93 WO 03/087306 PCT/US03/10462 Example 8: Production of Recombinant 98P4B6 in Hiqher Eukaryotic Systems A. Mammalian Constructs: To express recombinant 98P4B6 in eukaryotic cells, the full or partial length 98P4B6 cDNA sequences can be cloned into any one of a variety of expression vectors known in the art. One or more of the following regions of 98P4B6 are expressed in these constructs, amino acids 1 to 255, or any 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 98P4B6 v.1 through v.11; amino acids 1 to 1266, or any 8, 9, 10, 11, 12, 13, 14, 15, 16,17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30 or more contiguous amino acids from 98P4B6 v.12 and v.13, variants, or analogs thereof. The constructs can be transfected into any one of a wide variety of mammalian cells such as 293T cells. Transfected 293T cell lysates can be probed with the anti-98P4B6 polyclonal serum, described herein. pcDNA41HisMax Constructs: To express 98P4B6 in mammalian cells, a 98P4B6 ORF, or portions thereof, of 98P4B6 are cloned into pcDNA4/HisMax Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter and the SP16 translational enhancer. The recombinant protein has Xpress

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M and six histidine (6X His) epitopes fused to the amino-terminus. The pcDNA4/HisMax vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Zeocin resistance gene allows for selection of mammalian cells expressing the protein and the ampicillin resistance gene and ColE1 origin permits selection and maintenance of the plasmid in E. coi. pcDNA3.11MycHis Constructs: To express 98P4B6 in mammalian cells, a 98P4B6 ORF, or portions thereof, of 98P4B6 with a consensus Kozak translation initiation site was cloned into pcDNA3.1/MycHis Version A (Invitrogen, Carlsbad, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter. The recombinant proteins have the myc epitope and 6X His epitope fused to the carboxyl-terminus. The pcDNA3.1/MycHis vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability, along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Neomycin resistance gene can be used, as it allows for selection of mammalian cells expressing the protein and the ampicillin resistance gene and ColE1 origin permits selection and maintenance of the plasmid in E. co/i. pcDNA3.1/GFP Construct: To express 98P4B6 in mammalian cells and to allow detection of the recombinant proteins using fluorescence, the 98P4B6 ORF sequence was codon optimized according to Mirzabekov et al. (1999), and was cloned into pcDNA3.1/GFP vector to generate 98P4B6.GFP.pcDNA3.1 construct. Protein expression was driven from the cytomegalovirus (CMV) promoter. The recombinant protein had the Green Fluorescent Protein (GFP) fused to the carboxyl-terminus facilitating non-invasive, in vivo detection and cell biology studies. The pcDNA3.1/GFP vector also contains the bovine growth hormone (BGH) polyadenylation signal and transcription termination sequence to enhance mRNA stability along with the SV40 origin for episomal replication and simple vector rescue in cell lines expressing the large T antigen. The Neomycin resistance gene allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and ColE1 origin permits selection and maintenance of the plasmid in E. coli. Transfection of 98P4B6.GFP.pcDNA3.1 into 293T cells was performed as shown in Figure 17 and 18. Results show strong expression of the fusion protein by western blot analysis (Figure 17), flow cytometry (Figure 18A) and fluorescent microscopy (Figure 188). Additional constructs with an amino-terminal GFP fusion are made in pcDNA3.1/NT-GFP-TOPO spanning the entire length of a 98P4B6 protein. PAPtag: A 98P4B6 ORF, or portions thereof, is cloned into pAPtag-5 (GenHunter Corp. Nashville, TN). This construct generates an alkaline phosphatase fusion at the carboxyl-terminus of a 98P4B6 protein while fusing the IgGK 94 WO 03/087306 PCT/US03/10462 signal sequence to the amino-terminus. Constructs are also generated in which alkaline phosphatase with an amino-terminal IgGK signal sequence is fused to the amino-terminus of a 98P4B6 protein. The resulting recombinant 98P4B6 proteins are optimized for secretion into the media of transfected mammalian cells and can be used to identify proteins such as ligands or receptors that interact with 98P4B6 proteins. Protein expression is driven from the CMV promoter and the recombinant proteins also contain myc and 6X His epitopes fused at the carboxyl-terminus that facilitates detection and purification. The Zeocin resistance gene present in the vector allows for selection of mammalian cells expressing the recombinant protein and the ampicillin resistance gene permits selection of the plasmid in E. coli. pag5: A 98P4B6 ORF, or portions thereof, is cloned into pTag-5. This vector is similar to pAPtag but without the alkaline phosphatase fusion. This construct generates 98P4B6 protein with an amino-terminal IgGK signal sequence and myc and 6X His epitope tags at the carboxyl-terminus that facilitate detection and affinity purification. The resulting recombinant 98P4B6 protein is optimized for secretion into the media of transfected mammalian cells, and is used as immunogen or ligand to identify proteins such as ligands or receptors that interact with the 98P4B6 proteins. Protein expression is driven from the CMV promoter. The Zeocin resistance gene present in the vector allows for selection of mammalian cells expressing the protein, and the ampicillin resistance gene permits selection of the plasmid in E coil. PsecFc: A 98P4B6 ORF, or portions thereof, is also cloned into psecFc. The psecFc vector was assembled by cloning the human immunoglobulin G1 (lgG) Fc (hinge, CH2, CH3 regions) into pSecTag2 (Invitrogen, California). This construct generates an IgG1 Fc fusion at the carboxyl-terminus of the 98P4B6 proteins, while fusing the IgGK signal sequence to N-terminus. 98P4B6 fusions utilizing the murine IgG1 Fc region are also used. The resulting recombinant 98P4B6 proteins are optimized for secretion into the media of transfected mammalian cells, and can be used as immunogens or to identify proteins such as ligands or receptors that interact with 98P4B6 protein. Protein expression is driven from the CMV promoter. The hygromycin resistance gene present in the vector allows for selection of mammalian cells that express the recombinant protein, and the ampicillin resistance gene permits selection of the plasmid in E. coli. pSRa Constructs: To generate mammalian cell lines that express 98P4B6 constitutively, 98P4B6 ORF, or portions thereof, of 98P4B6 were cloned into pSRL constructs. Amphotropic and ecotropic retroviruses were generated by transfection of pSRoa constructs into the 293T-10A1 packaging line or co-transfection of pSRa and a helper plasmid (containing deleted packaging sequences) into the 293 cells, respectively. The retrovirus is used to infect a variety of mammalian cell lines, resulting in the integration of the cloned gene, 98P4B6, into the host cell-lines. Protein expression is driven from a long terminal repeat (LTR). The Neomycin resistance gene present in the vector allows for selection of mammalian cells that express the protein, and the ampicillin resistance gene and ColE1 origin permit selection and maintenance of the plasmid in E. coil. The retroviral vectors can thereafter be used for infection and generation of various cell lines using, for example, PC3, NIH 3T3, TsuPri, 293 or rat-1 cells. Additional pSRa constructs are made that fuse an epitope tag such as the FLAGTM tag to the carboxyl-terminus of 98P4B6 sequences to allow detection using anti-Flag antibodies. For example, the FLAGTM sequence 5' gat tac aag gat gac gac gat aag 3' (SEQ ID NO: 113) is added to cloning primer at the 3' end of the ORF. Additional pSRa constructs are made to produce both amino-terminal and carboxyl-terminal GFP and myc/6X His fusion proteins of the full-length 98P4B6 proteins. Additional Viral Vectors: Additional constructs are made for viral-mediated delivery and expression of 98P4B6. High virus titer leading to high level expression of 98P4B6 is achieved in viral delivery systems such as adenoviral vectors and herpes amplicon vectors. A 98P4B6 coding sequences or fragments thereof are amplified by PCR and subcloned into the AdEasy shuttle vector (Stratagene). Recombination and virus packaging are performed according to the manufacturers instructions to generate adenoviral vectors. Altematively, 98P4B6 coding sequences or fragments thereof are cloned into 95 WO 03/087306 PCT/US03/10462 the HSV-1 vector (Imgenex) to generate herpes viral vectors. The viral vectors are thereafter used for infection of various cell lines such as PC3, NIH 3T3, 293 or rat-1 cells. Regulated Expression Systems: To control expression of 98P4B6 in mammalian cells, coding sequences of 98P4B6, or portions thereof, are cloned into regulated mammalian expression systems such as the T-Rex System (Invitrogen), the GeneSwitch System (Invitrogen) and the tightly-regulated Ecdysone System (Sratagene). These systems allow the study of the temporal and concentration dependent effects of recombinant 98P4B6. These vectors are thereafter used to control expression of 98P4B6 in various cell lines such as PC3, NIH 3T3, 293 or rat-1 cells. B. Baculovirus Expression Systems To generate recombinant 98P4B6 proteins in a baculovirus expression system, 98P4B6 ORF, or portions thereof, are cloned into the baculovirus transfer vector pBlueBac 4.5 (Invitrogen), which provides a His-tag at the N-terminus. Specifically, pBlueBac-98P4B6 is co-transfected with helper plasmid pBac-N-Blue (Invitrogen) into SF9 (Spodoptera frugiperda) insect cells to generate recombinant baculovirus (see Invitrogen instruction manual for details). Baculovirus is then collected from cell supernatant and purified by plaque assay. Recombinant 98P4B6 protein is then generated by infection of HighFive insect cells (Invitrogen) with purified baculovirus. Recombinant 98P4B6 protein can be detected using anti-98P4B6 or anti-His-tag antibody. 98P4B6 protein can be purified and used in various cell-based assays or as immunogen to generate polyclonal and monoclonal antibodies specific for 98P4B6. Example 9: Antiqenicity Profiles and Secondary Structure Figure 5(A-E), Figure 6(A-E), Figure 7(A-E), Figure 8(A-E), and Figure 9(A-E) depict graphically five amino acid profiles of 98P4B6 variants 1, 2, 5-7, each assessment available by accessing the ProtScale website located on the World Wide Web at .expasy.chlcgi-bin/protscale.pl) on the ExPasy molecular biology server. These profiles: Figure 5, Hydrophilicity, (Hopp T.P., Woods K.R., 1981. Proc. Natl. Acad. Sci. U.S.A. 78:3824 3828); Figure 6, Hydropathicity, (Kyte J., Doolittle R.F., 1982. J. Mol. Biol. 157:105-132); Figure 7, Percentage Accessible Residues (Janin J., 1979 Nature 277:491-492); Figure 8, Average Flexibility, (Bhaskaran R., and Ponnuswamy P.K., 1988. Int. J. Pept. Protein Res. 32:242-255); Figure 9, Beta-turn (Deleage, G., Roux B. 1987 Protein Engineering 1:289-294); and optionally others available in the art, such as on the ProtScale website, were used to identify antigenic regions of each of the 98P4B6 variant proteins. Each of the above amino acid profiles of 98P4B6 variants were generated using the following ProtScale parameters for analysis: 1) A window size of 9; 2) 100% weight of the window edges compared to the window center; and, 3) amino acid profile values normalized to lie between 0 and 1. Hydrophilicity (Figure 5), Hydropathicity (Figure 6) and Percentage Accessible Residues (Figure 7) profiles were used to determine stretches of hydrophilic amino acids (i.e., values greater than 0.5 on the Hydrophilicity and Percentage Accessible Residues profile, and values less than 0.5 on the Hydropathicity profile). Such regions are likely to be exposed to the aqueous environment, be present on the surface of the protein, and thus available for immune recognition, such as by antibodies. Average Flexibility (Figure 8) and Beta-turn (Figure 9) profiles determine stretches of amino acids (i.e., values greater than 0.5 on the Beta-turn profile and the Average Flexibility profile) that are not constrained in secondary structures such as beta sheets and alpha helices. Such regions are also more likely to be exposed on the protein and thus accessible to immune recognition, such as by antibodies. Antigenic sequences of the 98P4B6 variant proteins indicated, e.g., by the profiles set forth in Figure 5(A-E), Figure 6(A-E), Figure 7(A-E), Figure 8(A-E), and/or Figure 9(A-E) are used to prepare immunogens, either peptides or nucleic acids that encode them, to generate therapeutic and diagnostic anti-98P4B6 antibodies. The immunogen can be any 5, 6, 7, 8, 9, 96 WO 03/087306 PCT/US03/10462 10, 11, 12, 13, 14,15,16, 17, 18,19, 20, 21, 22, 23, 24, 25, 30, 35, 40, 45, 50 or more than 50 contiguous amino acids, or the corresponding nucleic acids that encode them, from the 98P4B6 protein variants 1, 2, 5-7 listed in Figures 2 and 3. In particular, peptide immunogens of the invention can comprise, a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Hydrophilicity profiles of Figure 5; a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figures 6 ; a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profiles of Figure 7; a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Average Flexibility profiles on Figure 8; and, a peptide region of at least 5 amino acids of Figures 2 and 3 in any whole number increment that includes an amino acid position having a value greater than 0.5 in the Beta-turn profile of Figures 9. Peptide immunogens of the invention can also comprise nucleic acids that encode any of the forgoing. All immunogens of the invention, peptide or nucleic acid, can be embodied in human unit dose form, or comprised by a composition that includes a pharmaceutical excipient compatible with human physiology. The secondary structure of 98P4B6 protein variants 1, 2, 5-7, namely the predicted presence and location of alpha helices, extended strands, and random coils, is predicted from the primary amino acid sequence using the HNN Hierarchical Neural Network method (Guermeur, 1997, http://pbil.ibcp.fr/cgi-bin/npsaautomat.pl?page=npsann.htm), accessed from the ExPasy molecular biology server (located on the World Wide Web at.expasy.ch/tools/). The analysis indicates that 98P486 variant 1 is composed of 54.41% alpha helix, 12.33% extended strand, and 33.26% random coil (Figure 13A). Variant 2 is composed of 17.78% alpha helix, 6.67% extended strand, and 75.56% random coil (Figure 13B). Variant 5 is composed of 51.55% alpha helix, 13.13% extended strand, and 35.32% random coil (Figure 13C). Variant 6 is composed of 54.49% alpha helix, 11.84% extended strand, and 33.67% random coil (Figure 13D). Variant 7 is composed of 48.26% alpha helix, 15.28% extended strand, and 36.46% random coil (Figure 13E). Analysis for the potential presence of transmembrane domains in the 98P4B6 variant proteins was carried out using a variety of transmembrane prediction algorithms accessed from the ExPasy molecular biology server (located on the World Wide Web at.expasy.ch/tools/). Shown graphically in figure 13F and 13G are the results of analysis of variant 1 depicting the presence and location of 6 transmembrane domains using the TMpred program (Figure 13F) and 5 transmembrane domains using the TMHMM program (Figure 130). Shown graphically in figure 13H and 131 are the results of analysis of variant 2 depicting the presence and location of 1 transmembrane domains using the TMpred program (Figure 13H) and no transmembrane domains using the TMHMM program (Figure 131). Shown graphically in figure 13J and 13K are the results of analysis of variant 5 depicting the presence and location of 6 transmembrane domains using the TMpred program (Figure 13J) and 4 transmembrane domains using the TMHMM program (Figure 13K). Shown graphically in figure 13L and 13M are the results of analysis of variant 6 depicting the presence and location of 6 transmembrane domains using the TMpred program (Figure 13L) and 6 transmembrane domains using the TMHMM program (Figure 13M). Shown graphically in figure 13N and 130 are the results of analysis of variant 7 depicting the presence and location of 6 transmembrane domains using the TMpred program (Figure 13N) and 4 transmembrane domains using the TMHMM program (Figure 130). The results of each program, namely the amino acids encoding the transmembrane domains are summarized in Table VI. Example 10: Generation of 98P4B6 Polyclonal Antibodies Polyclonal antibodies can be raised in a mammal, for example, by one or more injections of an immunizing agent and, if desired, an adjuvant. Typically, the immunizing agent and/or adjuvant will be injected in the mammal by multiple 97 WO 03/087306 PCT/USO3/10462 subcutaneous or intraperitoneal injections. In addition to immunizing with a full length 98P4B6 protein variant, computer algorithms are employed in design of immunogens that, based on amino acid sequence analysis contain characteristics of being antigenic and available for recognition by the immune system of the immunized host (see Example 9 entitled "Antigenicity Profiles and Secondary Structure"). Such regions would be predicted to be hydrophilic, flexible, in beta-turn conformations, and be exposed on the surface of the protein (see, e.g., Figure 5(A-E), Figure 6(A & B), Figure 7(A-E), Figure 8(A -E), or Figure 9(A-E) for amino acid profiles that indicate such regions of 98P4B6 protein variants). For example, recombinant bacterial fusion proteins or peptides containing hydrophilic, flexible, beta-tum regions of 98P4B6 protein variants are used as antigens to generate polyclonal antibodies in New Zealand White rabbits or monoclonal antibodies as described in Example 11. For example, in 98P4B6 variant 1, such regions include, but are not limited to, amino acids 153-165, amino acids 240-260, and amino acids 345-358. In sequence specific for variant 2, such regions include, but are not limited to, amino acids 26-38. In sequence specific for variant 5, such regions include, but are not limited to, amino acids 400-410. In sequence specific for variant 6, such regions include, but are not limited to, amino acids 455 490. In sequence specific for variant 7, such regions include, but are not limited to, amino acids 451-465 and amino acids 472-498. It is useful to conjugate the immunizing agent to a protein known to be immunogenic in the mammal being immunized. Examples of such immunogenic proteins include, but are not limited to, keyhole limpet hemocyanin (KLH), serum albumin, bovine thyroglobulin, and soybean trypsin inhibitor. In one embodiment, a peptide encoding amino acids 153-165 of 98P4B6 variant 1 was conjugated to KLH and used to immunize a rabbit. Alternatively the immunizing agent may include all or portions of the 98P4B6 variant proteins, analogs or fusion proteins thereof. For example, the 98P4B6 variant 1 amino acid sequence can be fused using recombinant DNA techniques to any one of a variety of fusion protein partners that are well known in the art, such as glutathione-S-transferase (GST) and HIS tagged fusion proteins. In another embodiment, amino acids 2-204 of 98P4B6 variant 1 was fused to GST using recombinant techniques and the pGEX expression vector, expressed, purified and used to immunize a rabbit. Such fusion proteins are purified from induced bacteria using the appropriate affinity matrix. Other recombinant bacterial fusion proteins that may be employed include maltose binding protein, LacZ, thioredoxin, NusA, or an immunoglobulin constant region (see the section entitled "Production of 98P4B6 in Prokaryotic Systems" and Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubul et al. eds., 1995; Linsley, P.S., Brady, W., Urnes, M., Grosmaire, L., Damle, N., and Ledbetter, L.(1991) J.Exp. Med. 174, 561-566). In addition to bacterial derived fusion proteins, mammalian expressed protein antigens are also used. These antigens are expressed from mammalian expression vectors such as the Tag5 and Fc-fusion vectors (see the section entitled "Production of Recombinant 98P4B6 in Eukaryotic Systems"), and retain post-translational modifications such as glycosylations found in native protein. In one embodiment, amino acids 324-359 of variant 1, encoding an extracellular loop between transmembrane domains, is cloned into the Tag5 mammalian secretion vector. The recombinant protein is purified by metal chelate chromatography from tissue culture supernatant of 293T cells stably expressing the recombinant vector. The purified Tag5 98P4B6 protein is then used as immunogen. During the immunization protocol, it is useful to mix or emulsify the antigen in adjuvants that enhance the immune response of the host animal. Examples of adjuvants include, but are not limited to, complete Freund's adjuvant (CFA) and MPL-TDM adjuvant (monophosphoryl Lipid A, synthetic trehalose dicorynomycolate). In a typical protocol, rabbits are initially immunized subcutaneously with up to 200 pg, typically 100-200 p.g, of fusion protein or peptide conjugated to KLH mixed in complete Freund's adjuvant (CFA). Rabbits are then injected subcutaneously every two weeks with up to 200 gg, typically 100-200 jag, of the immunogen in incomplete Freund's adjuvant (IFA). Test bleeds are taken approximately 7-10 days following each immunization and used to monitor the titer of the antiserum by ELISA. 98 WO 03/087306 PCT/US03/10462 To test reactivity and specificity of immune serum, such as the rabbit serum derived from immunization with the Tag5 -98P4B6 variant 1 protein, the full-length 98P4B6 variant 1 cDNA is cloned into pCDNA 3.1 myc-his expression vector (Invitrogen, see the Example entitled "Production of Recombinant 98P4B6 in Eukaryotic Systems"). After transfection of the constructs into 293T cells, cell lysates are probed with the anti-98P4B6 serum and with anti-His antibody (Santa Cruz Biotechnologies, Santa Cruz, CA) to determine specific reactivity to denatured 98P4B6 protein using the Western blot technique. Detection of 98P4B6 variant 1 protein expressed in 293T with polyclonal antibodies raised to a GST-fusion protein and peptide is shown in Figure 17B and 17C, respectively. In addition, the immune serum is tested by fluorescence microscopy, flow cytometry and immunoprecipitation against 293T and other recombinant 98P4B6-expressing cells to determine specific recognition of native protein. Western blot, immunoprecipitation, fluorescent microscopy, and flow cytometric techniques using cells that endogenously express 98P4B6 are also carried out to test reactivity and specificity. Anti-serum from rabbits immunized with 98P4B6 variant fusion proteins, such as GST and MBP fusion proteins, are purified by depletion of antibodies reactive to the fusion partner sequence by passage over an affinity column containing the fusion partner either alone or in the context of an irrelevant fusion protein. For example, antiserum derived from a GST 98P4B6 variant 1 fusion protein was first purified by passage over a column of GST protein covalently coupled to AffiGel matrix (BioRad, Hercules, Calif.). The antiserum is then affinity purified by passage ever a column composed of a MBP 98P4B6 fusion protein covalently coupled to Affigel matrix. The serum is then further purified by protein G affinity chromatography to isolate the IgG fraction. Sera from other His-tagged antigens and peptide immunized rabbits as well as fusion partner depleted sera are affinity purified by passage over a column matrix composed of the original protein immunogen or free peptide, such as the anti-peptide polyclonal antibody used in Figure 17C. Example 11: Generation of 98P4B6 Monoclonal Antibodies (mAbs) In one embodiment, therapeutic mAbs to 98P4B6 variants comprise those that react with epitopes specific for each variant protein or specific to sequences in common between the variants that would disrupt or modulate the biological function of the 98P4B6 variants, for example those that would disrupt the interaction with ligands and binding partners. Immunogens for generation of such mAbs include those designed to encode or contain the entire 98P4B6 protein variant sequence, regions of the 98P4B6 protein variants predicted to be antigenic from computer analysis of the amino acid sequence (see, e.g., Figure 5(A-E), Figure 6(A-E), Figure 7(A-E), Figure 8(A-E), or Figure 9(A-E), and Example 9 entitled "Antigenicity Profiles and Secondary Structure"). Immunogens include peptides, recombinant bacterial proteins, and mammalian expressed Tag 5 proteins and human and murine IgG FC fusion proteins. In addition, cells engineered to express high levels of a respective 98P4B6 variant, such as 293T-98P4B6 variant 1 or 300.19-98P4B6 variant 1murine Pre B cells, are used to immunize mice. To generate mAbs to a 98P4B6 variant, mice are first immunized intraperitoneally (IP) with, typically, 10-50 pg of protein immunogen or 107 98P4B6-expressing cells mixed in complete Freund's adjuvant. Mice are then subsequently immunized IP every 2-4 weeks with, typically, 10-50 I.g of protein immunogen or 107 cells mixed in incomplete Freund's adjuvant. Altematively, MPL-TDM adjuvant is used in immunizations. In addition to the above protein and cell-based immunization strategies, a DNA-based immunization protocol is employed in which a mammalian expression vector encoding a 98P4B6 variant sequence is used to immunize mice by direct injection of the plasmid DNA. For example, amino acids 324 359 is cloned into the Tag5 mammalian secretion vector and the recombinant vector is used as immunogen. In another example the same amino acids are cloned into an Fc-fusion secretion vector in which the 98P4B6 variant 1 sequence is fused at the amino-terminus to an IgK leader sequence and at the carboxyl-terminus to the coding sequence of the human or murine IgG Fc region. This recombinant vector is then used as immunogen. The plasmid immunization protocols are used 99 WO 03/087306 PCT/US03/10462 in combination with purified proteins expressed from the same vector and with cells expressing the respective 98P4B6 variant. During the immunization protocol, test bleeds are taken 7-10 days following an injection to monitor titer and specificity of the immune response. Once appropriate reactivity and specificity is obtained as determined by ELISA, Western blotting, immunoprecipitation, fluorescence microscopy, and flow cytometric analyses, fusion and hybridoma generation is then carried out with established procedures well known in the art (see, e.g., Harlow and Lane, 1988). In one embodiment for generating 98P4B6 monoclonal antibodies, a Tag5-98P4B6 variant 1 antigen encoding amino acids 324-359, is expressed and purified from stably transfected 293T cells. Balb C mice are initially immunized intraperitoneally with 25 p.g of the Tag5-98P4B6 variant 1 protein mixed in complete Freund's adjuvant. Mice are subsequently immunized every two weeks with 25 pig of the antigen mixed in incomplete Freund's adjuvant for a total of three immunizations. ELISA using the Tag5 antigen determines the titer of serum from immunized mice. Reactivity and specificity of serum to full length 98P4B6 variant 1 protein is monitored by Western blotting, immunoprecipitation and flow cytometry using 293T cells transfected with an expression vector encoding the 98P4B6 variant 1 cDNA (see e.g., the Example entitled "Production of Recombinant 98P4B6 in Eukaryotic Systems" and Figure 20). Other recombinant 98P4B6 variant 1-expressing cells or cells endogenously expressing 98P4B6 variant 1 are also used. Mice showing the strongest reactivity are rested and given a final injection of Tag5 antigen in PBS and then sacrificed four days later. The spleens of the sacrificed mice are harvested and fused to SPO/2 myeloma cells using standard procedures (Harlow and Lane, 1988). Supemrnatants from HAT selected growth wells are screened by ELISA, Western blot, immunoprecipitation, fluorescent microscopy, and flow cytometry to identify 98P4B6 specific antibody-producing clones. To generate monoclonal antibodies that are specific for each 98P4B6 variant protein, immunogens are designed to encode sequences unique for each variant. In one embodiment, a Tag5 antigen encoding the full sequence of 98P4B6 variant 2 (AA 1-45) is produced, purified and used as immunogen to derive monoclonal antibodies specific to 98P4B6 variant 2. In another embodiment, an antigenic peptide composed of amino acids 400-410 of 98P486 variant 5 is coupled to KLH and used as immunogen. In another embodiment, a GST fusion protein encoding amino acids 455-490 of 98P4B6 of variant 6 is used as immunogen to derive variant 6 specific monoclonal antibodies. In another embodiment, a peptide composed of amino acids 472-498 of variant 7 is coupled to KLH and used as immunogen to generate variant 7 specific monoclonal antibodies. Hybridoma supernatants are then screened on the respective antigen and then further screened on cells expressing the specific variant and cross-screened on cells expressing the other variants to derive variant-specific monoclonal antibodies. The binding affinity of a 98P4B6 variant monoclonal antibody is determined using standard technologies. Affinity measurements quantify the strength of antibody to epitope binding and are used to help define which 98P4B6 variant monoclonal antibodies preferred for diagnostic or therapeutic use, as appreciated by one of skill in the art. The BIAcore system (Uppsala, Sweden) is a preferred method for determining binding affinity. The BIAcore system uses surface plasmon resonance (SPR, Welford K. 1991, Opt. Quant Elect. 23:1; Morton and Myszka, 1998, Methods in Enzymology 295: 268) to monitor biomolecular interactions in real time. BIAcore analysis conveniently generates association rate constants, dissociation rate constants, equilibrium dissociation constants, and affinity constants. Example 12: HLA Class I and Class II Binding Assays HLA class I and class II binding assays using purified HLA molecules are performed in accordance with disclosed protocols (e.g., PCT publications WO 94/20127 and WO 94/03205; Sidney et a., Current Protocols in Immunology 18.3.1 (1998); Sidney, et al., J. Immunol. 154:247 (1995); Sette, et a., Mol. Immunol. 31:813 (1994)). Briefly, purified MHC molecules (5 to 500 nM) are incubated with various unlabeled peptide inhibitors and 1-10 nM 12I-radiolabeled probe peptides 100 WO 03/087306 PCT/US03/10462 as described. Following incubation, MHC-peptide complexes are separated from free peptide by gel filtration and the fraction of peptide bound is determined. Typically, in preliminary experiments, each MHC preparation is titered in the presence of fixed amounts of radiolabeled peptides to determine the concentration of HLA molecules necessary to bind 10-20% of the total radioactivity. All subsequent inhibition and direct binding assays are performed using these HLA concentrations. Since under these conditions [label]<[HLA] and ICso>[HLA], the measured IC5o values are reasonable approximations of the true KD values. Peptide inhibitors are typically tested at concentrations ranging from 120 pg/ml to 1.2 ng/ml, and are tested in two to four completely independent experiments. To allow comparison of the data obtained in different experiments, a relative binding figure is calculated for each peptide by dividing the ICso of a positive control for inhibition by the ICso for each tested peptide (typically unlabeled versions of the radiolabeled probe peptide). For database purposes, and inter-experiment comparisons, relative binding values are compiled. These values can subsequently be converted back into ICso nM values by dividing the ICso nM of the positive controls for inhibition by the relative binding of the peptide of interest. This method of data compilation is accurate and consistent for comparing peptides that have been tested on different days, or with different lots of purified MHC. Binding assays as outlined above may be used to analyze HLA supermotif and/or HLA motif-bearing peptides (see Table IV). Example 13: Identification of HLA Supermotif- and Motif-Bearing CTL Candidate Epitopes HLA vaccine compositions of the invention can include multiple epitopes. The multiple epitopes can comprise multiple HLA supermotifs or motifs to achieve broad population coverage. This example illustrates the identification and confirmation of supermotif- and motif-bearing epitopes for the inclusion in such a vaccine composition. Calculation of population coverage is performed using the strategy described below. Computer searches and algorithms for identification of supermotif and/or motif-bearing epitopes The searches performed to identify the motif-bearing peptide sequences in the Example entitled "Antigenicity Profiles" and Tables Vill-XXI and XXII-XLIX employ the protein sequence data from the gene product of 98P4B6 set forth in Figures 2 and 3, the specific search peptides used to generate the tables are listed in Table VII. Computer searches for epitopes bearing HLA Class I or Class II supermotifs or motifs are performed as follows. All translated 98P4B6 protein sequences are analyzed using a text string search software program to identify potential peptide sequences containing appropriate HLA binding motifs; such programs are readily produced in accordance with information in the art in view of known motif/supermotif disclosures. Furthermore, such calculations can be made mentally. Identified A2-, A3-, and DR-supermotif sequences are scored using polynomial algorithms to predict their capacity to bind to specific HLA-Class I or Class II molecules. These polynomial algorithms account for the impact of different amino acids at different positions, and are essentially based on the premise that the overall affinity (or AG) of peptide-HLA molecule interactions can be approximated as a linear polynomial function of the type: "AG" = a x ai x ai ...... x ani where all is a coefficient which represents the effect of the presence of a given amino acid (j) at a given position (i) along the sequence of a peptide of n amino acids. The crucial assumption of this method is that the effects at each position are essentially independent of each other (i.e., independent binding of individual side-chains). When residue j occurs at position i in the peptide, it is assumed to contribute a constant amount ji to the free energy of binding of the peptide irrespective of the sequence of the rest of the peptide. The method of derivation of specific algorithm coefficients has been described in Gulukota et al., J. Mol. Biol. 267:1258-126, 1997; (see also Sidney et aL, Human Immunol. 45:79-93, 1996; and Southwood et al., J. Immunol. 160:3363 3373, 1998). Briefly, for all i positions, anchor and non-anchor alike, the geometric mean of the average relative binding 101 WO 03/087306 PCT/US03/10462 (ARB) of all peptides carrying j is calculated relative to the remainder of the group, and used as the estimate of ji. For Class II peptides, if multiple alignments are possible, only the highest scoring alignment is utilized, following an iterative procedure. To calculate an algorithm score of a given peptide in a test set, the ARB values corresponding to the sequence of the peptide are multiplied. If this product exceeds a chosen threshold, the peptide is predicted to bind. Appropriate thresholds are chosen as a function of the degree of stringency of prediction desired. Selection of HLA-A2 supertype cross-reactive peptides Protein sequences from 98P4B6 are scanned utilizing motif identification software, to identify 8-, 9- 10- and 11-mer sequences containing the HLA-A2-supermotif main anchor specificity. Typically, these sequences are then scored using the protocol described above and the peptides corresponding to the positive-scoring sequences are synthesized and tested for their capacity tobind purified HLA-A*0201 molecules in vitro (HLA-A*0201 is considered a prototype A2 supertype molecule). These peptides are then tested for the capacity to bind to additional A2-supertype molecules (A*0202, A*0203, A*0206, and A*6802). Peptides that bind to at least three of the five A2-supertype alleles tested are typically deemed A2 supertype cross-reactive binders. Preferred peptides bind at an affinity equal to or less than 500 nM to three or more HLA A2 supertype molecules. Selection of HLA-A3 supermotif-bearinq epitopes The 98P4B6 protein sequence(s) scanned above is also examined for the presence of peptides with the HLA-A3 supermotif primary anchors. Peptides corresponding to the HLA A3 supermotif-bearing sequences are then synthesized and tested for binding to HLA-A*0301 and HLA-A*1101 molecules, the molecules encoded by the two most prevalent A3 supertype alleles. The peptides that bind at least one of the two alleles with binding affinities of _500 nM, often < 200 nM, are then tested for binding cross-reactivity to the other common A3-supertype alleles (e.g., A*3101, A*3301, and A*6801) to identify those that can bind at least three of the five HLA-A3-supertype molecules tested. Selection of HLA-B7 supermotif bearing epitopes The 98P4B6 protein(s) scanned above is also analyzed for the presence of 8-, 9- 10-, or 11-mer peptides with the HLA-B7-supermotif. Corresponding peptides are synthesized and tested for binding to HLA-B*0702, the molecule encoded by the most common B7-supertype allele (i.e., the prototype B7 supertype allele). Peptides binding B*0702 with IC5o of 500 nM are identified using standard methods. These peptides are then tested for binding to other common B7-supertype molecules (e.g., B*3501, B*5101, B*5301, and B*5401). Peptides capable of binding to three or more of the five B7 supertype alleles tested are thereby identified. Selection of Al and A24 motif-bearing epitopes To further increase population coverage, HLA-A1 and -A24 epitopes can also be incorporated into vaccine compositions. An analysis of the 98P4B6 protein can also be performed to identify HLA-A1- and A24-motif-containing sequences. High affinity and/or cross-reactive binding epitopes that bear other motif and/or supermotifs are identified using analogous methodology. Example 14: Confirmation of Immunogenicity Cross-reactive candidate CTL A2-supermotif-bearing peptides that are identified as described herein are selected to confirm in vitro immunogenicity. Confirmation is performed using the following methodology: 102 WO 03/087306 PCT/US03/10462 Target Cell Lines for Cellular Screening: The .221A2.1 cell line, produced by transferring the HLA-A2.1 gene into the HLA-A, -B, -C null mutant human B lymphoblastoid cell line 721.221, is used as the peptide-loaded target to measure activity of HLA-A2.1-restricted CTL. This cell line is grown in RPMI-1640 medium supplemented with antibiotics, sodium pyruvate, nonessential amino acids and 10% (viv) heat inactivated FCS. Cells that express an antigen of interest, or transfectants comprising the gene encoding the antigen of interest, can be used as target cells to confirm the ability of peptide-specific CTLs to recognize endogenous antigen. Primary CTL Induction Cultures: Generation of Dendritic Cells (DC): PBMCs are thawed in RPMI with 30 pg/ml DNAse, washed twice and resuspended in complete medium (RPMI-1640 plus 5% AB human serum, non-essential amino acids, sodium pyruvate, L glutamine and penicillin/streptomycin). The monocytes are purified by plating 10 x 106 PBMC/well in a 6-well plate. After 2 hours at 37°C, the non-adherent cells are removed by gently shaking the plates and aspirating the supernatants. The wells are washed a total of three times with 3 ml RPMI to remove most of the non-adherent and loosely adherent cells. Three ml of complete medium containing 50 ng/ml of GM-CSF and 1,000 Ulml of IL-4 are then added to each well. TNFc is added to the DCs on day 6 at 75 ng/ml and the cells are used for CTL induction cultures on day 7. Induction of CTL with DC and Peptide: CD8+ T-cells are isolated by positive selection with Dynal immunomagnetic beads (Dynabeads@ M-450) and the detacha-bead® reagent. Typically about 200-250x10 6 PBMC are processed to obtain 24x10 6 CD8 + T-cells (enough for a 48-well plate culture). Briefly, the PBMCs are thawed in RPMI with 30pgIml DNAse, washed once with PBS containing 1% human AB serum and resuspended in PBS/1% AB serum at a concentration of 20xl0 6 cells/ml. The magnetic beads are washed 3 times with PBS/AB serum, added to the cells (140pl beads/20x10 6 cells) and incubated for 1 hour at 4 0 C with continuous mixing. The beads and cells are washed 4x with PBS/AB serum to remove the nonadherent cells and resuspended at 100x10 6 cells/ml (based on the original cell number) in PBS/AB serum containing 100pl/ml detacha-bead® reagent and 30 pg/ml DNAse. The mixture is incubated for 1 hour at room temperature with continuous mixing. The beads are washed again with PBS/AB/DNAse to collect the CD8+ T-cells. The DC are collected and centrifuged at 1300 rpm for 5-7 minutes, washed once with PBS with 1% BSA, counted and pulsed with 40pg/ml of peptide at a cell concentration of 1-2x10 )ml in the presence of 3pg/ml 92- microglobulin for 4 hours at 20 0 C. The DC are then irradiated (4,200 rads), washed 1 time with medium and counted again. Setting up induction cultures: 0.25 ml cytokine-generated DC (at 1x10 5 cells/ml) are co-cultured with 0.25ml of CD8+ T-cells (at 2x10 6 cell/mIl) in each well of a 48-well plate in the presence of 10 ng/ml of IL-7. Recombinant human IL-10 is added the next day at a final concentration of 10 ng/ml and rhuman IL-2 is added 48 hours later at 10 IU/ml. Restimulation of the induction cultures with peptide-pulsed adherent cells: Seven and fourteen days after the primary induction, the cells are restimulated with peptide-pulsed adherent cells. The PBMCs are thawed and washed twice with RPMI and DNAse. The cells are resuspended at 5x10 6 cells/ml and irradiated at -4200 rads. The PBMCs are plated at 2x10 6 in 0.5 ml complete medium per well and incubated for 2 hours at 37 0 C. The plates are washed twice with RPMI by tapping the plate gently to remove the nonadherent cells and the adherent cells pulsed with 10pg/mil of peptide in the presence of 3 pg/ml 1 2 microglobulin in 0.25ml RPMI/5%AB per well for 2 hours at 37 0 C. Peptide solution from each well is aspirated and the wells are washed once with RPMI. Most of the media is aspirated from the induction cultures (CD8+ cells) and brought to 0.5 ml with fresh media. The cells are then transferred to the wells containing the peptide-pulsed adherent cells. Twenty four hours later recombinant human IL-10 is added at a final concentration of 10 ng/ml and recombinant human IL2 is added the next day and again 2-3 days later at 501U/ml (Tsai et al., Critical Reviews in Immunology 18(1-2):65-75, 1998). Seven days later, the cultures are assayed for CTL activity in a 5 'Cr release assay. In some experiments the cultures are assayed for peptide-specific recognition in the in situ IFNy ELISA at the time of the second 103 WO 03/087306 PCT/US03/10462 restimulation followed by assay of endogenous recognition 7 days later. After expansion, activity is measured in both assays for a side-by-side comparison. Measurement of CTL lytic activity by 51 Cr release. Seven days after the second restimulation, cytotoxicity is determined in a standard (5 hr) 51 Cr release assay by assaying individual wells at a single E:T. Peptide-pulsed targets are prepared by incubating the cells with 10pg/ml peptide overnight at 37 0 C. Adherent target cells are removed from culture flasks with trypsin-EDTA. Target cells are labeled with 200pCi of 51 Cr sodium chromate (Dupont, Wilmington, DE) for 1 hour at 370C. Labeled target cells are resuspended at 106 per ml and diluted 1:10 with K562 cells at a concentration of 3.3x106/ml (an NK-sensitive erythroblastoma cell line used to reduce non specific lysis). Target cells (100 pl) and effectors (100pl) are plated in 96 well round-bottom plates and incubated for 5 hours at 37 0 C. At that time, 100 pl of supernatant are collected from each well and percent lysis is determined according to the formula: [(cpm of the test sample- cpm of the spontaneous 5 'Cr release sample)/(cpm of the maximal 61 Cr release sample cpm of the spontaneous 51 Cr release sample)] x 100. Maximum and spontaneous release are determined by incubating the labeled targets with 1% Triton X-100 and media alone, respectively. A positive culture is defined as one in which the specific lysis (sample- background) is 10% or higher in the case of individual wells and is 15% or more at the two highest E:T ratios when expanded cultures are assayed. In situ Measurement of Human IFNy Production as an Indicator of Peotide-specific and Endoqenous Recognition Immulon 2 plates are coated with mouse anti-human IFNy monoclonal antibody (4 pg/ml 0.1M NaHCO3, pH8.2) overnight at 4*C. The plates are washed with Ca 2 , Mg 2 +-free PBS/0.05% Tween 20 and blocked with PBS/10% FCS for two hours, after which the CTLs (100 p1lwell) and targets (100 pi/well) are added to each well, leaving empty wells for the standards and blanks (which received media only). The target cells, either peptide-pulsed or endogenous targets, are used at a concentration of lx1 06 cells/ml. The plates are incubated for 48 hours at 370C with 5% CO2. Recombinant human IFN-gamma is added to the standard wells starting at 400 pg or 1200pg/100 microliter/well and the plate incubated for two hours at 37*C. The plates are washed and 100 0l of biotinylated mouse anti-human IFN gamma monoclonal antibody (2 microgram/ml in PBS/3%FCS/0.05% Tween 20) are added and incubated for 2 hours at room temperature. After washing again, 100 microliter HRP-streptavidin (1:4000) are added and the plates incubated for one hour at room temperature. The plates are then washed 6x with wash buffer, 100 microliter/well developing solution (TMB 1:1) are added, and the plates allowed to develop for 5-15 minutes. The reaction is stopped with 50 microliter/well 1M H3P04 and read at OD450. A culture is considered positive if it measured at least 50 pg of IFN-gammalwell above background and is twice the background level of expression. CTL Expansion. Those cultures that demonstrate specific lytic activity against peptide-pulsed targets and/or tumor targets are expanded over a two week period with anti-CD3. Briefly, 5x10 4 CD8+ cells are added to a T25 flask containing the following: lx106 irradiated (4,200 rad) PBMC (autologous or allogeneic) per ml, 2x10 6 irradiated (8,000 rad) EBV- transformed cells per ml, and OKT3 (anti-CD3) at 30ng per ml in RPMI-1640 containing 10% (v/v) human AB serum, non-essential amino acids, sodium pyruvate, 25pM 2-mercaptoethanol, L-glutamine and penicillin/streptomycin. Recombinant human IL2 is added 24 hours later at a final concentration of 2001U/ml and every three days thereafter with fresh media at 501U/ml. The cells are split if the cell concentration exceeds lx1 0 6 /ml and the cultures are assayed between days 13 and 15 at E:T ratios of 30, 10, 3 and 1:1 in the 51 Cr release assay or at 1x10 6 /ml in the in situ IFNy assay using the same targets as before the expansion. Cultures are expanded in the absence of anti-CD3+ as follows. Those cultures that demonstrate specific lytic activity against peptide and endogenous targets are selected and 5x1 04 CD8, cells are added to a T25 flask containing the 104 WO 03/087306 PCT/US03/10462 following: 1x10 6 autologous PBMC per ml which have been peptide-pulsed with 10 pg/ml peptide for two hours at 37°C and irradiated (4,200 rad); 2x10 s irradiated (8,000 rad) EBV-transformed cells per ml RPMI-1640 containing 10%(viv) human AB serum, non-essential AA, sodium pyruvate, 25mM 2-ME, L-glutamine and gentamicin. Immunoqenicity of A2 supermotif-bearing peptides A2-supermotif cross-reactive binding peptides are tested in the cellular assay for the ability to induce peptide specific CTL in normal individuals. In this analysis, a peptide is typically considered to be an epitope if it induces peptide specific CTLs in at least individuals, and preferably, also recognizes the endogenously expressed peptide. Immunogenicity can also be confirmed using PBMCs isolated from patients bearing a tumor that expresses 98P4B6. Briefly, PBMCs are isolated from patients, re-stimulated with peptide-pulsed monocytes and assayed for the ability to recognize peptide-pulsed target cells as well as transfected cells endogenously expressing the antigen. Evaluation of A*03/A11 immunogenicity HLA-A3 supermotif-bearing cross-reactive binding peptides are also evaluated for immunogenicity using methodology analogous for that used to.evaluate the immunogenicity of the HLA-A2 supermotif peptides. Evaluation of B7 immunogenicity Immunogenicity screening of the B7-supertype cross-reactive binding peptides identified as set forth herein are confirmed in a manner analogous to the confirmation of A2-and A3-supermotif-bearing peptides. Peptides bearing other supermotifs/motifs, e.g., HLA-A1, HLA-A24 etc. are also confirmed using similar methodology Example 15: Implementation of the Extended Supermotif to Improve the Binding Capacity of Native Epitopes by Creating Analogs HLA motifs and supermotifs (comprising primary andlor secondary residues) are useful in the identification and preparation of highly cross-reaclive native peptides, as demonstrated herein. Moreover, the definition of HLA motifs and supermotifs also allows one to engineer highly cross-reactive epitopes by identifying residues within a native peptide sequence which can be analoged to confer upon the peptide certain characteristics, e.g. greater cross-reactivity within the group of HLA molecules that comprise a supertype, and/or greater binding affinity for some or all of those HLA molecules. Examples of analoging peptides to exhibit modulated binding affinity are set forth in this example. Analoging at Primary Anchor Residues Peptide engineering strategies are implemented to further increase the cross-reactivity of the epitopes. For example, the main anchors of A2-supermotif-bearing peptides are altered, for example, to introduce a preferred L, I, V, or M at position 2, and I or V at the C-terminus. To analyze the cross-reactivity of the analog peptides, each engineered analog is initially tested for binding to the prototype A2 supertype allele A*0201, then, if A*0201 binding capacity is maintained, for A2-supertype cross-reactivity. Alternatively, a peptide is confirmed as binding one or all supertype members and then analoged to modulate binding affinity to any one (or more) of the supertype members to add population coverage. The selection of analogs for immunogenicity in a cellular screening analysis is typically further restricted by the capacity of the parent wild type (WT) peptide to bind at least weakly, i.e., bind at an IC50 of 5000nM or less, to three of more A2 supertype alleles. The rationale for this requirement is that the WT peptides must be present endogenously in sufficient quantity to be biologically relevant. Analoged peptides have been shown to have increased immunogenicity and cross reactivity by T cells specific for the parent epitope (see, e.g., Parkhurst et al., J. Immunol. 157:2539, 1996; and Pogue et aL, Proc. Nati. Acad. Sci. USA 92:8166, 1995). 105 WO 03/087306 PCT/USO3/10462 In the cellular screening of these peptide analogs, it is important to confirm that analog-specific CTLs are also able to recognize the wild-type peptide and, when possible, target cells that endogenously express the epitope. Analoqinq of HLA-A3 and B7-supermotif-bearing peptides Analogs of HLA-A3 supermotif-bearing epitopes are generated using strategies similar to those employed in analoging HLA-A2 supermotif-bearing peptides. For example, peptides binding to 3/5 of the A3-supertype molecules are engineered at primary anchor residues to possess a preferred residue (V, S, M, or A) at position 2. The analog peptides are then tested for the ability to bind A*03 and A*11 (prototype A3 supertype alleles). Those peptides that demonstrate < 500 nM binding capacity are then confirmed as having A3-supertype cross-reactivity. Similarly to the A2- and A3- motif bearing peptides, peptides binding 3 or more B7-supertype alleles can be improved, where possible, to achieve increased cross-reactive binding or greater binding affinity or binding half life. B7 supermotif-bearing peptides are, for example, engineered to possess a preferred residue (V, I, L, or F) at the C-terminal primary anchor position, as demonstrated by Sidney et al. (J. Immunol. 157:3480-3490, 1996). Analoging at primary anchor residues of other motif and/or supermotif-bearing epitopes is performed in a like manner. The analog peptides are then be confirmed for immunogenicity, typically in a cellular screening assay. Again, it is generally important to demonstrate that analog-specific CTLs are also able to recognize the wild-type peptide and, when possible, targets that endogenously express the epitope. Analoging at Secondary Anchor Residues Moreover, HLA supermotifs are of value in engineering highly cross-reactive peptides and/or peptides that bind HLA molecules with increased affinity by identifying particular residues at secondary anchor positions that are associated with such properties. For example, the binding capacity of a B7 supermotif-bearing peptide with an F residue at position 1 is analyzed. The peptide is then analoged to, for example, substitute L for F at position 1. The analoged peptide is evaluated for increased binding affinity, binding half life and/or increased cross-reactivity. Such a procedure identifies analoged peptides with enhanced properties. Engineered analogs with sufficiently improved binding capacity or cross-reactivity can also be tested for immunogenicity in HLA-B7-transgenic mice, following for example, IFA immunization or lipopeptide immunization. Analoged peptides are additionally tested for the ability to stimulate a recall response using PBMC from patients with 98P4B6 expressing tumors. Other analoqing strategies Another form of peptide analoging, unrelated to anchor positions, involves the substitution of a cysteine with a amino butyric acid. Due to its chemical nature, cysteine has the propensity to form disulfide bridges and sufficiently alter the peptide structurally so as to reduce binding capacity. Substitution of a-amino butyric acid for cysteine not only alleviates this problem, but has been shown to improve binding and crossbinding capabilities in some instances (see, e.g., the review by Sette et al., In: Persistent Viral infections, Eds. R. Ahmed and I. Chen, John Wiley & Sons, England, 1999). Thus, by the use of single amino acid substitutions, the binding properties and/or cross-reactivity of peptide ligands for HLA supertype molecules can be modulated. Example 16: Identification and confirmation of 98P4B6-derived sequences with HLA.DR binding motifs Peptide epitopes bearing an HLA class II supermotif or motif are identified and confirmed as outlined below using methodology similar to that described for HLA Class I peptides. 106 WO 03/087306 PCT/US03/10462 Selection of HLA-DR-supermotif-bearing epitopes. To identify 98P4B6-derived, HLA class II HTL epitopes, a 98P4B6 antigen is analyzed for the presence of sequences bearing an HLA-DR-motif or supermotif. Specifically, 15-mer sequences are selected comprising a DR supermotif, comprising a 9-mer core, and three-residue N- and C-terminal flanking regions (15 amino acids total). Protocols for predicting peptide binding to DR molecules have been developed (Southwood et al., J. Immunot. 160:3363-3373, 1998). These protocols, specific for individual DR molecules, allow the scoring, and ranking, of 9-mer core regions. Each protocol not only scores peptide sequences for the presence of DR-supermotif primary anchors (i.e., at position 1 and position 6) within a 9-mer core, but additionally evaluates sequences for the presence of secondary anchors. Using allele-specific selection tables (see, e.g., Southwood et al., ibid.), it has been found that these protocols efficiently select peptide sequences with a high probability of binding a particular DR molecule. Additionally, it has been found that performing these protocols in tandem, specifically those for DR1, DR4w4, and DR7, can efficiently select DR cross-reactive peptides. The 98P4B8-derived peptides identified above are tested for their binding capacity for various common HLA-DR molecules. All peptides are initially tested for binding to the DR molecules in the primary panel: DR1, DR4w4, and DR7. Peptides binding at least two of these three DR molecules are then tested for binding to DR2w2 p1, DR2w2 p2, DR6w19, and DR9 molecules in secondary assays. Finally, peptides binding at least two of the four secondary panel DR molecules, and thus cumulatively at least four of seven different DR molecules, are screened for binding to DR4w15, DR5w1 1, and DR8w2 molecules in tertiary assays. Peptides binding at least seven of the ten DR molecules comprising the primary, secondary, and tertiary screening assays are considered cross-reactive DR binders. 98P4B6-derived peptides found to bind common HLA-DR alleles are of particular interest. Selection of DR3 motif peptides Because HLA-DR3 is an allele that is prevalent in Caucasian, Black, and Hispanic populations, DR3 binding capacity is a relevant criterion in the selection of HTL epitopes. Thus, peptides shown to be candidates may also be assayed for their DR3 binding capacity. However, in view of the binding specificity of the DR3 motif, peptides binding only to DR3 can also be considered as candidates for inclusion in a vaccine formulation. To efficiently identify peptides that bind DR3, target 98P4B6 antigens are analyzed for sequences carrying one of the two DR3-specific binding motifs reported by Geluk et al (J. Immunof. 152:5742-5748, 1994). The corresponding peptides are then synthesized and confirmed as having the ability to bind DR3 with an affinity of 1pM or better, i.e., less than 1 pM. Peptides are found that meet this binding criterion and qualify as HLA class 11 high affinity binders. DR3 binding epitopes identified in this manner are included in vaccine compositions with DR supermotif-bearing peptide epitopes. Similarly to the case of HLA class I motif-bearing peptides, the class 11 motif-bearing peptides are analoged to improve affinity or cross-reactivity. For example, aspartic acid at position 4 of the 9-mer core sequence is an optimal residue for DR3 binding, and substitution for that residue often improves DR 3 binding. Example 17: Immunogenicity of 98P4B6-derived HTL epitopes This example determines immunogenic DR supermotif- and DR3 motif-bearing epitopes among those identified using the methodology set forth herein. Immunogenicity of HTL epitopes are confirmed in a manner analogous to the determination of immunogenicity of CTL epitopes, by assessing the ability to stimulate HTL responses and/or by using appropriate transgenic mouse models. Immunogenicity is determined by screening for: 1.) in vitro primary induction using normal PBMC or 2.) recall responses from patients who have 98P4B6-expressing tumors. 107 WO 03/087306 PCT/US03/10462 Example 18: Calculation of phenotypic frequencies of HLA-supertypes in various ethnic backgrounds to determine breadth of population coverage This example illustrates the assessment of the breadth of population coverage of a vaccine composition comprised of multiple epitopes comprising multiple supermotifs and/or motifs. In order to analyze population coverage, gene frequencies of HLA alleles are determined. Gene frequencies for each HLA allele are calculated from antigen or allele frequencies utilizing the binomial distribution formulae gf=-1-(SQRT(1 at)) (see, e.g., Sidney et al., Human Immunol. 45:79-93, 1996). To obtain overall phenotypic frequencies, cumulative gene frequencies are calculated, and the cumulative antigen frequencies derived by the use of the inverse formula [af=1l-(1-Cgf) 2 ]. Where frequency data is not available at the level of DNA typing, correspondence to the serologically defined antigen frequencies is assumed. To obtain total potential supertype population coverage no linkage disequilibrium is assumed, and only alleles confirmed to belong to each of the supertypes are included (minimal estimates). Estimates of total potential coverage achieved by inter-loci combinations are made by adding to the A coverage the proportion of the non-A covered population that could be expected to be covered by the B alleles considered (e.g., total=A+B*(1-A)). Confirmed members of the A3-like supertype are A3, All, A31, A*3301, and A*6801. Although the A3-like supertype may also include A34, A66, and A*7401, these alleles were not included in overall frequency calculations. Likewise, confirmed members of the A2-like supertype family are A*0201, A*0202, A*0203, A*0204, A*0205, A*0206, A*0207, A*6802, and A*6901. Finally, the B7-like supertype-confirmed alleles are: 87, 8*3501-03, 851, 8*5301, B*5401, B*5501-2, B*5601, B*6701, and B*7801 (potentially also B*1401, B*3504-06, B*4201, and B*5602). Population coverage achieved by combining the A2-, A3- and B7-supertypes is approximately 86% in five major ethnic groups. Coverage may be extended by including peptides bearing the Al and A24 motifs. On average, Al is present in 12% and A24 in 29% of the population across five different major ethnic groups (Caucasian, North American Black, Chinese, Japanese, and Hispanic). Together, these alleles are represented with an average frequency of 39% in these same ethnic populations. The total coverage across the major ethnicities when Al and A24 are combined with the coverage of the A2-, A3- and B7-supertype alleles is >95%, see, e.g., Table IV (G). An analogous approach can be used to estimate population coverage achieved with combinations of class 11 motif-bearing epitopes. Immunogenicity studies in humans (e.g., Bertoni et al., J. Clin. Invest. 100:503, 1997; Doolan et al, Immunity 7:97, 1997; and Threlkeld et al., J. Immunol. 159:1648, 1997) have shown that highly cross-reactive binding peptides are almost always recognized as epitopes. The use of highly cross-reactive binding peptides is an important selection criterion in identifying candidate epitopes for inclusion in a vaccine that is immunogenic in a diverse population. With a sufficient number of epitopes (as disclosed herein and from the art), an average population coverage is predicted to be greater than 95% in each of five major ethnic populations. The game theory Monte Carlo simulation analysis, which is known in the art (see e.g., Osborne, M.J. and Rubinstein, A. "A course in game theory" MIT Press, 1994), can be used to estimate what percentage of the individuals in a population comprised of the Caucasian, North American Black, Japanese, Chinese, and Hispanic ethnic groups would recognize the vaccine epitopes described herein. A preferred percentage is 90%. A more preferred percentage is 95%. Example 19: CTL Recognition Of Endogenously Processed Antigens After Priming This example confirms that CTL induced by native or analoged peptide epitopes identified and selected as described herein recognize endogenously synthesized, i.e., native antigens. Effector cells isolated from transgenic mice that are immunized with peptide epitopes, for example HLA-A2 supermotif-bearing epitopes, are re-stimulated in vitro using peptide-coated stimulator cells. Six days later, effector cells are 108 WO 03/087306 PCT/US03/10462 assayed for cytotoxicity and the cell lines that contain peptide-specific cytotoxic activity are further re-stimulated. An additional six days later, these cell lines are tested for cytotoxic activity on s 51 Cr labeled Jurkat-A2.1/Kb target cells in the absence or presence of peptide, and also tested on 51 Cr labeled target cells bearing the endogenously synthesized antigen, i.e. cells that are stably transfected with 98P4B6 expression vectors. The results demonstrate that CTL lines obtained from animals primed with peptide epitope recognize endogenously synthesized 98P4B6 antigen. The choice of transgenic mouse model to be used for such an analysis depends upon the epitope(s) that are being evaluated. In addition to HLA-A*0201/Kb transgenic mice, several other transgenic mouse models including mice with human A11, which may also be used to evaluate A3 epitopes, and 87 alleles have been characterized and others (e.g., transgenic mice for HLA-A1 and A24) are being developed. HLA-DR1 and HLA DR3 mouse models have also been developed, which may be used to evaluate HTL epitopes. Example 20: Activity Of CTL-HTL Conjugated Epitopes In Transgenic Mice This example illustrates the induction of CTLs and HTLs in transgenic mice, by use of a 98P4B6-derived CTL and HTL peptide vaccine compositions. The vaccine composition used herein comprise peptides to be administered to a patient with a 98P4B6-expressing tumor. The peptide composition can comprise multiple CTL and/or HTL epitopes. The epitopes are identified using methodology as described herein. This example also illustrates that enhanced immunogenicity can be achieved by inclusion of one or more HTL epitopes in a CTL vaccine composition; such a peptide composition can comprise an HTL epitope conjugated to a CTL epitope. The CTL epitope can be one that binds to multiple HLA family members at an affinity of 500 nM or less, or analogs of that epitope. The peptides may be lipidated, if desired. Immunization procedures: Immunization of transgenic mice is performed as described (Alexander et al., J. Immunol. 159:4753-4761, 1997). For example, A2/Kb mice, which are transgenic for the human HLA A2.1 allele and are used to confirm the immunogenicity of HLA-A*0201 motif- or HLA-A2 supermotif-bearing epitopes, and are primed subcutaneously (base of the tail) with a 0.1 ml of peptide in Incomplete Freund's Adjuvant, or if the peptide composition is a lipidated CTL/HTL conjugate, in DMSO/saline, or if the peptide composition is a polypeptide, in PBS or Incomplete Freund's Adjuvant. Seven days after priming, splenocytes obtained from these animals are restimulated with syngenic irradiated LPS activated lymphoblasts coated with peptide. Cell lines: Target cells for peptide-specific cytotoxicity assays are Jurkat cells transfected with the HLA-A2.1/Kb chimeric gene (e.g., Vitiello et al., J Exp. Med. 173:1007, 1991) In vitro CTL activation: One week after priming, spleen cells (30x10 6 cells/flask) are co-cultured at 37°C with syngeneic, irradiated (3000 rads), peptide coated lymphoblasts (10x10 6 cells/flask) in 10 ml of culture medium/T25 flask. After six days, effector cells are harvested and assayed for cytotoxic activity. Assay for cytotoxic activity: Target cells (1.0 to 1.5x106) are incubated at 37°C in the presence of 200 pl of 51 Cr, After 60 minutes, cells are washed three times and resuspended in R10 medium. Peptide is added where required at a concentration of 1 pg/ml. For the assay, 104 6'Cr-labeled target cells are added to different concentrations of effector cells (final volume of 200 pl) in U-bottom 96-well plates. After a six hour incubation period at 37 0 C, a 0.1 ml aliquotof supernatant is removed from each well and radioactivity is determined in a Micromedic automatic gamma counter. The percent specific lysis is determined by the formula: percent specific release = 100 x (experimental release - spontaneous release)/(maximum release - spontaneous release). To facilitate comparison between separate CTL assays run under the same conditions, % 51 Cr release data is expressed as lytic units/106 cells. One lytic unit is arbitrarily defined as the number of effector cells required to achieve 30% lysis of 10,000 target cells in a six hour 51 Cr release assay. To obtain specific lytic units/106, the lytic units/i 06 obtained in the absence of peptide is subtracted from the lytic units/1 06 obtained in the presence of peptide. For example, if 30% 51 Cr release is obtained at the effector (E): target (T) ratio of 50:1 (i.e., 5x106 effector cells for 10,000 109 WO 03/087306 PCT/USO3/10462 targets) in the absence of peptide and 5:1 (i.e., 5x104 effector cells for 10,000 targets) in the presence of peptide, the specific lytic units would be: [(1/50,000)-(1/500,000)] x 106 = 18 LU. The results are analyzed to assess the magnitude of the CTL responses of animals injected with the immunogenic CTL/HTL conjugate vaccine preparation and are compared to the magnitude of the CTL response achieved using, for example, CTL epitopes as outlined above in the Example entitled "Confirmation of Immunogenicity." Analyses similar to this may be performed to confirm the immunogenicity of peptide conjugates containing multiple CTL epitopes and/or multiple HTL epitopes. In accordance with these procedures, it is found that a CTL response is induced, and concomitantly that an HTL response is induced upon administration of such compositions. Example 21: Selection of CTL and HTL epitopes for inclusion in a 98P4B6.specific vaccine. This example illustrates a procedure for selecting peptide epitopes for vaccine compositions of the invention. The peptides in the composition can be in the form of a nucleic acid sequence, either single or one or more sequences (i.e., minigene) that encodes peptide(s), or can be single and/or polyepitopic peptides. The following principles are utilized when selecting a plurality of epitopes for inclusion in a vaccine composition. Each of the following principles is balanced in order to make the selection. Epitopes are selected which, upon administration, mimic immune responses that are correlated with 98P4B6 clearance. The number of epitopes used depends on observations of patients who spontaneously clear 98P4B6. For example, if it has been observed that patients who spontaneously clear 98P486-expressing cells generate an immune response to at least three (3) epitopes from 98P4B6 antigen, then at least three epitopes should be included for HLA class I. A similar rationale is used to determine HLA class 11 epitopes. Epitopes are often selected that have a binding affinity of an IC5o of 500 nM or less for an HLA class I molecule, or for class II, an ICso of 1000 nM or less; or HLA Class I peptides with high binding scores from the BIMAS web site, at URL bimas.dcrt.nih.gov/. In order to achieve broad coverage of the vaccine through out a diverse population, sufficient supermotif bearing peptides, or a sufficient array of allele-specific motif bearing peptides, are selected to give broad population coverage. In one embodiment, epitopes are selected to provide at least 80% population coverage. A Monte Carlo analysis, a statistical evaluation known in the art, can be employed to assess breadth, or redundancy, of population coverage. When creating polyepitopic compositions, or a minigene that encodes same, it is typically desirable to generate the smallest peptide possible that encompasses the epitopes of interest. The principles employed are similar, if not the same, as those employed when selecting a peptide comprising nested epitopes. For example, a protein sequence for the vaccine composition is selected because it has maximal number of epitopes contained within the sequence, i.e., it has a high concentration of epitopes. Epitopes may be nested or overlapping (i.e., frame shifted relative to one another). For example, with overlapping epitopes, two 9-mer epitopes and one 10-mer epitope can be present in a 10 amino acid peptide. Each epitope can be exposed and bound by an HLA molecule upon administration of such a peptide. A multi-epitopic, peptide can be generated synthetically, recombinantly, or via cleavage from the native source. Alternatively, an analog can be made of this native sequence, whereby one or more of the epitopes comprise substitutions that alter the cross-reactivity and/or binding affinity properties of the polyepitopic peptide. Such a vaccine composition is administered for therapeutic or prophylactic purposes. This embodiment provides for the possibility that an as yet undiscovered aspect of immune system processing will apply to the native nested sequence and thereby facilitate the production of therapeutic or prophylactic immune response-inducing vaccine compositions. Additionally such an embodiment provides for the possibility of motif bearing epitopes for an HLA makeup that is presently unknown. Furthermore, this embodiment (absent the creating of any analogs) directs the immune response to multiple peptide sequences that are actually present in 98P4B6, thus avoiding the 110 WO 03/087306 PCT/US03/10462 need to evaluate any junctional epitopes. Lastly, the embodiment provides an economy of scale when producing nucleic acid vaccine compositions. Related to this embodiment, computer programs can be derived in accordance with principles in the art, which identify in a target sequence, the greatest number of epitopes per sequence length. A vaccine composition comprised of selected peptides, when administered, is safe, efficacious, and elicits an immune response similar in magnitude to an immune response that controls or clears cells that bear or overexpress 98P4B6. Example 22: Construction of "Minigene" Multi-Epitope DNA Plasmids This example discusses the construction of a minigene expression plasmid. Minigene plasmids may, of course, contain various configurations of B cell, CTL and/or HTL epitopes or epitope analogs as described herein. A minigene expression plasmid typically includes multiple CTL and HTL peptide epitopes. In the present example, HLA-A2, -A3, -B7 supermotif-bearing peptide epitopes and HLA-A1 and -A24 motif-bearing peptide epitopes are used in conjunction with DR supermotif-bearing epitopes and/or DR3 epitopes. HLA class I supermotif or motif-bearing peptide epitopes derived 98P4B6, are selected such that multiple supermotifs/motifs are represented to ensure broad population coverage. Similarly, HLA class II epitopes are selected from 98P4B6 to provide broad population coverage, i.e. both HLA DR-1-4-7 supermotif-bearing epitopes and HLA DR-3 motif-bearing epitopes are selected for inclusion in the minigene construct. The selected CTL and HTL epitopes are then incorporated into a minigene for expression in an expression vector. Such a construct may additionally include sequences that direct the HTL epitopes to the endoplasmic reticulum. For example, the Ii protein may be fused to one or more HTL epitopes as described in the art, wherein the CLIP sequence of the li protein is removed and replaced with an HLA class II epitope sequence so that HLA class II epitope is directed to the endoplasmic reticulum, where the epitope binds to an HLA class II molecules. This example illustrates the methods to be used for construction of a minigene-bearing expression plasmid. Other expression vectors that may be used for minigene compositions are available and known to those of skill in the art. The minigene DNA plasmid of this example contains a consensus Kozak sequence and a consensus murine kappa Ig-light chain signal sequence followed by CTL and/or.HTL epitopes selected in accordance with principles disclosed herein. The sequence encodes an open reading frame fused to the Myc and His antibody epitope tag coded for by the pcDNA 3.1 Myc-His vector. Overlapping oligonucleotides that can, for example, average about 70 nucleotides in length with 15 nucleotide overlaps, are synthesized and HPLC-purified. The oligonucleotides encode the selected peptide epitopes as well as appropriate linker nucleotides, Kozak sequence, and signal sequence. The final multiepitope minigene is assembled by extending the overlapping oligonucleotides in three sets of reactions using PCR. A Perkin/Elmer 9600 PCR machine is used and a total of 30 cycles are performed using the following conditions: 95*C for 15 sec, annealing temperature (5 ° below the lowest calculated Tm of each primer pair) for 30 sec, and 72°C for 1 min. For example, a minigene is prepared as follows. For a first PCR reaction, 5 ptg of each of two oligonucleotides are annealed and extended: In an example using eight oligonucleotides, i.e., four pairs of primers, oligonucleotides 1+2, 3+4, 5+6, and 7+8 are combined in 100 p reactions containing Pfu polymerase buffer (lx= 10 mM KCL, 10 mM (NH4)2SO4, 20 mM Tris-chloride, pH 8.75, 2 mM MgSO4, 0.1% Triton X-100, 100 pg/ml BSA), 0.25 mM each dNTP, and 2.5 U of Pfu polymerase. The full-length dimer products are gel-purified, and two reactions containing the product of 1+2 and 3+4, and the product of 5+6 and 7+8 are mixed, annealed, and extended for 10 cycles. Half of the two reactions are then mixed, and 5 cycles of annealing and extension carried out before flanking primers are added to amplify the full length product. The full length product is gel-purified and cloned into pCR-blunt (Invitrogen) and individual clones are screened by sequencing. Example 23: The Plasmid Construct and the Degree to Which It Induces Immunogenicity. 111 WO 03/087306 PCT/US03/10462 The degree to which a plasmid construct, for example a plasmid constructed in accordance with the previous Example, is able to induce immunogenicity is confirmed in vitro by determining epitope presentation by APC following transduction or transfection of the APC with an epitope-expressing nucleic acid construct. Such a study determines "antigenidcity" and allows the use of human APC. The assay determines the ability of the epitope to be presented by the APC in a context that is recognized by a T cell by quantifying the density of epitope-HLA class I complexes on the cell surface. Quantitation can be performed by directly measuring the amount of peptide eluted from the APC (see, e.g., Sijts et al., J. Immunol. 156:683-692, 1996; Demotz et aL, Nature 342:682-684, 1989); or the number of peptide-HLA class I complexes can be estimated by measuring the amount of lysis or lymphokine release induced by diseased or transfected target cells, and then determining the concentration of peptide necessary to obtain equivalent levels of lysis or lymphokine release (see, e.g., Kageyama et al., J. Immunol. 154:567-576, 1995). Alternatively, immunogenicity is confirmed through in vivo injections into mice and subsequent in vitro assessment of CTL and HTL activity, which are analyzed using cytotoxicity and proliferation assays, respectively, as detailed e.g., in Alexander etal., Immunity 1:751-761, 1994. For example, to confirm the capacity of a DNA minigene construct containing at least one HLA-A2 supermotif peptide to induce CTLs in vivo, HLA-A2.1/Kb transgenic mice, for example, are immunized intramuscularly with 100 pg of naked cDNA. As a means of comparing the level of CTLs induced by cDNA immunization, a control group of animals is also immunized with an actual peptide composition that comprises multiple epitopes synthesized as a single polypeptide as they would be encoded by the minigene. Splenocytes from immunized animals are stimulated twice with each of the respective compositions (peptide epitopes encoded in the minigene or the polyepitopic peptide), then assayed for peptide-specific cytotoxic activity in a s 51 Cr release assay. The results indicate the magnitude of the CTL response directed against the A2-restricted epitope, thus indicating the in vivo immunogenicity of the minigene vaccine and polyepitopic vaccine. It is, therefore, found that the minigene elicits immune responses directed toward the HLA-A2 supermotif peptide epitopes as does the polyepitopic peptide vaccine. A similar analysis is also performed using other HLA-A3 and HLA-B7 transgenic mouse models to assess CTL induction by HLA-A3 and HLA-B7 motif or supermotif epitopes, whereby it is also found that the minigene elicits appropriate immune responses directed toward the provided epitopes. To confirm the capacity of a class II epitope-encoding minigene to induce HTLs in vivo, DR transgenic mice, or for those epitopes that cross react with the appropriate mouse MHC molecule, I-Ab-restricted mice, for example, are immunized intramuscularly with 100 pg of plasmid DNA. As a means of comparing the level of HTLs induced by DNA immunization, a group of control animals is also immunized with an actual peptide composition emulsified in complete Freund's adjuvant. CD4+ T cells, i.e. HTLs, are purified from splenocytes of immunized animals and stimulated with each of the respective compositions (peptides encoded in the minigene). The HTL response is measured using a 3 H-thymidine incorporation proliferation assay, (see, e.g., Alexander et al. Immunity 1:751-761, 1994). The results indicate the magnitude of the HTL response, thus demonstrating the in vivo immunogenicity of the minigene. DNA minigenes, constructed as described in the previous Example, can also be confirmed as a vaccine in combination with a boosting agent using a prime boost protocol. The boosting agent can consist of recombinant protein (e.g., Barnett et al., Aids Res. and Human Retroviruses 14, Supplement 3:S299-S309, 1998) or recombinant vaccinia, for example, expressing a minigene or DNA encoding the complete protein of interest (see, e.g., Hanke et al., Vaccine 16:439 445, 1998; Sedegah et al, Proc. Natl. Acad. Sci USA 95:7648-53, 1998; Hanke and McMichael, Immunol Letters 66:177 181, 1999; and Robinson et aL., Nature Med. 5:526-34, 1999). For example, the efficacy of the DNA minigene used in a prime boost protocol is initially evaluated in transgenic mice. In this example, A2.1/K b transgenic mice are immunized IM with 100 pg of a DNA minigene encoding the 112 WO 03/087306 PCT/US03/10462 immunogenic peptides including at least one HLA-A2 supermotif-bearing peptide. After an incubation period (ranging from 3 9 weeks), the mice are boosted IP with 107 pfu/mouse of a recombinant vaccinia virus expressing the same sequence encoded by the DNA minigene. Control mice are immunized with 100 pg of DNA or recombinant vaccinia without the minigene sequence, or with DNA encoding the minigene, but without the vaccinia boost. After an additional incubation period of two weeks, splenocytes from the mice are immediately assayed for peptide-specific activity in an ELISPOT assay. Additionally, splenocytes are stimulated in vitro with the A2-restricted peptide epitopes encoded in the minigene and recombinant vaccinia, then assayed for peptide-specific activity in an alpha, beta and/or gamma IFN ELISA. It is found that the minigene utilized in a prime-boost protocol elicits greater immune responses toward the HLA-A2 supermotif peptides than with DNA alone. Such an analysis can also be performed using HLA-Al 1 or HLA-B7 transgenic mouse models to assess CTL induction by HLA-A3 or HLA-B7 motif or supermotif epitopes. The use of prime boost protocols in humans is described below in the Example entitled "Induction of CTL Responses Using a Prime Boost Protocol." Example 24: Peptide Compositions for Prophylactic Uses Vaccine compositions of the present invention can be used to prevent 98P4B6 expression in persons who are at risk for tumors that bear this antigen. For example, a polyepitopic peptide epitope composition (or a nucleic acid comprising the same) containing multiple CTL and HTL epitopes such as those selected in the above Examples, which are also selected to target greater than 80% of the population, is administered to individuals at risk for a 98P4B6-associated tumor. For example, a peptide-based composition is provided as a single polypeptide that encompasses multiple epitopes. The vaccine is typically administered in a physiological solution that comprises an adjuvant, such as Incomplete Freunds Adjuvant. The dose of peptide for the initial immunization is from about 1 to about 50,000 pg, generally 100-5,000 ig, for a 70 kg patient. The initial administration of vaccine is followed by booster dosages at 4 weeks followed by evaluation of the magnitude of the immune response in the patient, by techniques that determine the presence of epitope-specific CTL populations in a PBMC sample. Additional booster doses are administered as required. The composition is found to be both safe and efficacious as a prophylaxis against 98P4B6-associated disease. Alternatively, a composition typically comprising transfecting agents is used for the administration of a nucleic acid based vaccine in accordance with methodologies known in the art and disclosed herein. Example 25: Polyepitopic Vaccine Compositions Derived from Native 98P4B6 Sequences A native 98P4B6 polyprotein sequence is analyzed, preferably using computer algorithms defined for each class I and/or class II supermotif or motif, to identify "relatively short" regions of the polyprotein that comprise multiple epitopes. The "relatively short" regions are preferably less in length than an entire native antigen. This relatively short sequence that contains multiple distinct or overlapping, "nested" epitopes can be used to generate a minigene construct. The construct is engineered to express the peptide, which corresponds to the native protein sequence. The "relatively short" peptide is generally less than 250 amino acids in length, often less than 100 amino acids in length, preferably less than 75 amino acids in length, and more preferably less than 50 amino acids in length. The protein sequence of the vaccine composition is selected because it has maximal number of epitopes contained within the sequence, i.e., it has a high concentration of epitopes. As noted herein, epitope motifs may be nested or overlapping (i.e., frame shifted relative to one another). For example, with overlapping epitopes, two 9-mer epitopes and one 10-mer epitope can be present in a 10 amino acid peptide. Such a vaccine composition is administered for therapeutic or prophylactic purposes. The vaccine composition will include, for example, multiple CTL epitopes from 98P4B6 antigen and at least one HTL epitope. This polyepitopic native sequence is administered either as a peptide or as a nucleic acid sequence which 113 WO 03/087306 PCT/US03/10462 encodes the peptide. Alternatively, an analog can be made of this native sequence, whereby one or more of the epitopes comprise substitutions that alter the cross-reactivity and/or binding affinity properties of the polyepitopic peptide. The embodiment of this example provides for the possibility that an as yet undiscovered aspect of immune system processing will apply to the native nested sequence and thereby facilitate the production of therapeutic or prophylactic immune response-inducing vaccine compositions. Additionally, such an embodiment provides for the possibility of motif bearing epitopes for an HLA makeup(s) that is presently unknown. Furthermore, this embodiment (excluding an analoged embodiment) directs the immune response to multiple peptide sequences that are actually present in native 98P4B6, thus avoiding the need to evaluate any junctional epitopes. Lastly, the embodiment provides an economy of scale when producing peptide or nucleic acid vaccine compositions. Related to this embodiment, computer programs are available in the art which can be used to identify in a target sequence, the greatest number of epitopes per sequence length. Example 26: Polyepitopic Vaccine Compositions from Multiple Antigens The 98P4B6 peptide epitopes of the present invention are used in conjunction with epitopes from other target tumor-associated antigens, to create a vaccine composition that is useful for the prevention or treatment of cancer that expresses 98P4B6 and such other antigens. For example, a vaccine composition can be provided as a single polypeptide that incorporates multiple epitopes from 98P4B6 as well as tumor-associated antigens that are often expressed with a target cancer associated with 98P4B6 expression, or can be administered as a composition comprising a cocktail of one or more discrete epitopes. Alternatively, the vaccine can be administered as a minigene construct or as dendritic cells which have been loaded with the peptide epitopes in vitro. Example 27: Use of peptides to evaluate an immune response Peptides of the invention may be used to analyze an immune response for the presence of specific antibodies, CTL or HTL directed to 98P4B6. Such an analysis can be performed in a manner described by Ogg et al, Science 279:2103-2106, 1998. In this Example, peptides in accordance with the invention are used as a reagent for diagnostic or prognostic purposes, not as an immunogen. In this example highly sensitive human leukocyte antigen tetrameric complexes ("tetramers") are used for a cross sectional analysis of, for example, 98P4B6 HLA-A*0201-specific CTL frequencies from HLA A*0201-positive individuals at different stages of disease or following immunization comprising a 98P4B6 peptide containing an A*0201 motif. Tetrameric complexes are synthesized as described (Musey et al., N. Engl. J. Med. 337:1267, 1997). Briefly, purified HLA heavy chain (A*0201 in this example) and p2-microglobulin are synthesized by means of a prokaryotic expression system. The heavy chain is modified by deletion of the transmembrane-cytosolic tail and COOH-terminal addition of a sequence containing a BirA enzymatic biotinylation site. The heavy chain, 32-microglobulin, and peptide are refolded by dilution. The 45-kD refolded product is isolated by fast protein liquid chromatography and then biotinylated by BirA in the presence of biotin (Sigma, St. Louis, Missouri), adenosine 5' triphosphate and magnesium. Streptavidin-phycoerythrin conjugate is added in a 1:4 molar ratio, and the tetrameric product is concentrated to 1 mg/mI. The resulting product is referred to as tetramer phycoerythrin. For the analysis of patient blood samples, approximately one million PBMCs are centrifuged at 300g for 5 minutes and resuspended in 50 pl of cold phosphate-buffered saline. Tri-color analysis is performed with the tetramer-phycoerythrin, along with anti-CD8-Tricolor, and anti-CD38. The PBMCs are incubated with tetramer and antibodies on ice for 30 to 60 min and then washed twice before formaldehyde fixation. Gates are applied to contain >99.98% of control samples. Controls for the tetramers include both A*0201-negative individuals and A*0201-positive non-diseased donors. The percentage of cells 114 WO 03/087306 PCT/USO3/10462 stained with the tetramer is then determined by flow cytometry. The results indicate the number of cells in the PBMC sample that contain epitope-restricted CTLs, thereby readily indicating the extent of immune response to the 98P4B6 epitope, and thus the status of exposure to 98P4B6, or exposure to a vaccine that elicits a protective or therapeutic response. Example 28: Use of Peptide Epitopes to Evaluate Recall Responses The peptide epitopes of the invention are used as reagents to evaluate T cell responses, such as acute or recall responses, in patients. Such an analysis may be performed on patients who have recovered from 98P4B6-associated disease or who have been vaccinated with a 98P4B136 vaccine. For example, the class I restricted CTL response of persons who have been vaccinated may be analyzed. The vaccine may be any 98P4B6 vaccine. PBMC are collected from vaccinated individuals and HLA typed. Appropriate peptide epitopes of the invention that, optimally, bear supermotifs to provide cross-reactivity with multiple HLA supertype family members, are then used for analysis of samples derived from individuals who bear that HLA type. PBMC from vaccinated individuals are separated on Ficoll-Histopaque density gradients (Sigma Chemical Co., St. Louis, MO), washed three times in HBSS (GIBCO Laboratories), resuspended in RPMI-1640 (GIBCO Laboratories) supplemented with L-glutamine (2mM), penicillin (50U/ml), streptomycin (50 pg/ml), and Hepes (10mM) containing 10% heat-inactivated human AB serum (complete RPMI) and plated using microculture formats. A synthetic peptide comprising an epitope of the invention is added at 10 pg/mI to each well and HBV core 128-140 epitope is added at 1 pg/ml to each well as a source of T cell help during the first week of stimulation. In the microculture format, 4 x 105 PBMC are stimulated with peptide in 8 replicate cultures in 96-well round bottom plate in 100 pl/well of complete RPMI. On days 3 and 10, 100 pl of complete RPMI and 20 U/ml final concentration of rlL-2 are added to each well. On day 7 the cultures are transferred into a 96-well flat-bottom plate and restimulated with peptide, rlL-2 and 105 irradiated (3,000 rad) autologous feeder cells. The cultures are tested for cytotoxic activity on day 14. A positive CTL response requires two or more of the eight replicate cultures to display greater than 10% specific 51 Cr release, based on comparison with non-diseased control subjects as previously described (Rehermann, et aL., Nature Med. 2:1104,1108, 1996; Rehermann et al., J. Clin. Invest. 97:1655-1665, 1996; and Rehermann etal. J. Clin. Invest. 98:1432 1440,1996). Target cell lines are autologous and allogeneic EBV-transformed B-LCL that are either purchased from the American Society for Histocompatibility and Immunogenetics (ASHI, Boston, MA) or established from the pool of patients as described (Guilhot, et al. J. Virol. 66:2670-2678, 1992). Cytotoxicity assays are performed in the following manner. Target cells consist of either allogeneic HLA-matched or autologous EBV-transformed B lymphoblastoid cell line that are incubated overnight with the synthetic peptide epitope of the invention at 10 pM, and labeled with 100 pCi of 51 Cr (Amersham Corp., Arlington Heights, IL) for 1 hour after which they are washed four times with HBSS. Cytolytic activity is determined in a standard 4-h, split well 51 Cr release assay using U-bottomed 96 well plates containing 3,000 targets/well. Stimulated PBMC are tested at effector/target (ET) ratios of 20-50:1 on day 14. Percent cytotoxicity is determined from the formula: 100 x [(experimental release-spontaneous release)/maximum release spontaneous release)]. Maximum release is determined by lysis of targets by detergent (2% Triton X-100; Sigma Chemical Co., St. Louis, MO). Spontaneous release is <25% of maximum release for all experiments. The results of such an analysis indicate the extent to which HLA-restricted CTL populations have been stimulated by previous exposure to 98P4B6 or a 98P4B6 vaccine. 115 WO 03/087306 PCT/USO3/10462 Similarly, Class 11 restricted HTL responses may also be analyzed. Purified PBMC are cultured in a 96-well flat bottom plate at a density of 1.5x105 cells/well and are stimulated with 10 pg/ml synthetic peptide of the invention, whole 98P4B6 antigen, or PHA. Cells are routinely plated in replicates of 4-6 wells for each condition. After seven days of culture, the medium is removed and replaced with fresh medium containing 10U/ml IL-2. Two days later, 1 pCi 3 H-thymidine is added to each well and incubation is continued for an additional 18 hours. Cellular DNA is then harvested on glass fiber mats and analyzed for 3 H-thymidine incorporation. Antigen-specific T cell proliferation is calculated as the ratio of 3H thymidine incorporation in the presence of antigen divided by the 3 H-thymidine incorporation in the absence of antigen. Example 29: Induction Of Specific CTL Response In Humans A human clinical trial for an immunogenic composition comprising CTL and HTL epitopes of the invention is set up as an IND Phase I, dose escalation study and carried out as a randomized, double-blind, placebo-controlled trial. Such a trial is designed, for example, as follows: A total of about 27 individuals are enrolled and divided into 3 groups: Group I: 3 subjects are injected with placebo and 6 subjects are injected with 5 g of peptide composition; Group II: 3 subjects are injected with placebo and 6 subjects are injected with 50 pg peptide composition; Group Ill: 3 subjects are injected with placebo and 6 subjects are injected with 500 tg of peptide composition. After 4 weeks following the first injection, all subjects receive a booster inoculation at the same dosage. The endpoints measured in this study relate to the safety and tolerability of the peptide composition as well as its immunogenicity. Cellular immune responses to the peptide composition are an index of the intrinsic activity of this the peptide composition, and can therefore be viewed as a measure of biological efficacy. The following summarize the clinical and laboratory data that relate to safety and efficacy endpoints. Safety: The incidence of adverse events is monitored in the placebo and drug treatment group and assessed in terms of degree and reversibility. Evaluation of Vaccine Efficacy: For evaluation of vaccine efficacy, subjects are bled before and after injection. Peripheral blood mononuclear cells are isolated from fresh heparinized blood by Ficoll-Hypaque density gradient centrifugation, aliquoted in freezing media and stored frozen. Samples are assayed for CTL and HTL activity. The vaccine is found to be both safe and efficacious. Example 30: Phase II Trials In Patients Expressing 98P4B6 Phase II trials are performed to study the effect of administering the CTL-HTL peptide compositions to patients having cancer that expresses 98P4B6. The main objectives of the trial are to determine an effective dose and regimen for inducing CTLs in cancer patients that express 98P4B6, to establish the safety of inducing a CTL and HTL response in these patients, and to see to what extent activation of CTLs improves the clinical picture of these patients, as manifested, e.g., by the reduction and/or shrinking of lesions. Such a study is designed, for example, as follows: The studies are performed in multiple centers. The trial design is an open-label, uncontrolled, dose escalation protocol wherein the peptide composition is administered as a single dose followed six weeks later by a single booster shot of the same dose. The dosages are 50, 500 and 5,000 micrograms per injection. Drug-associated adverse effects (severity and reversibility) are recorded. There are three patient groupings. The first group is injected with 50 micrograms of the peptide composition and the second and third groups with 500 and 5,000 micrograms of peptide composition, respectively. The patients within each group range in age from 21-65 and represent diverse ethnic backgrounds. All of them have a tumor that expresses 98P4B6. 116 WO 03/087306 PCT/US03/10462 Clinical manifestations or antigen-specific T-cell resppnses are monitored to assess the effects of administering the peptide compositions. The vaccine composition is found to be both safe and efficacious in the treatment of 98P4B6 associated disease. Example 31: Induction of CTL Responses Usingq a Prime Boost Protocol A prime boost protocol similar in its underlying principle to that used to confirm the efficacy of a DNA vaccine in transgenic mice, such as described above in the Example entitled "The Plasmid Construct and the Degree to Which It Induces Immunogenicity," can also be used for the administration of the vaccine to humans. Such a vaccine regimen can include an initial administration of, for example, naked DNA followed by a boost using recombinant virus encoding the vaccine, or recombinant protein/polypeptide or a peptidemixture administered in an adjuvant. For example, the initial immunization may be performed using an expression vector, such as that constructed in the Example entitled "Construction of "Minigene" Multi-Epitope DNA Plasmids" in the form of naked nucleic acid administered IM (or SC or ID) in the amounts of 0.5-5 mg at multiple sites. The nucleic acid (0.1 to 1000 p.g) can also be administered using a gene gun. Following an incubation period of 3-4 weeks, a booster dose is then administered. The booster can be recombinant fowlpox virus administered at a dose of 5-107 to 5x109 pfu. An alternative recombinant virus, such as an MVA, canarypox, adenovirus, or adeno-associated virus, can also be used for the booster, or the polyepitopic protein or a mixture of the peptides can be administered. For evaluation of vaccine efficacy, patient blood samples are obtained before immunization as well as at intervals following administration of the initial vaccine and booster doses of the vaccine. Peripheral blood mononuclear cells are isolated from fresh heparinized blood by Ficoll-Hypaque density gradient centrifugation, aliquoted in freezing media-and stored frozen. Samples are assayed for CTL and HTL activity. Analysis of the results indicates that a magnitude of response sufficient to achieve a therapeutic or protective immunity against 98P4B6 is generated. Example 32: Administration of Vaccine Compositions Using Dendritic Cells (DC) Vaccines comprising peptide epitopes of the invention can be administered using APCs, or "professional" APCs such as DC. In this example, peptide-pulsed DC are administered to a patient to stimulate a CTL response in vivo. In this method, dendritic cells are isolated, expanded, and pulsed with a vaccine comprising peptide CTL and HTL epitopes of the invention. The dendritic cells are infused back into the patient to elicit CTL and HTL responses in vivo. The induced CTL and HTL then destroy or facilitate destruction, respectively, of the target cells that bear the 98P4B6 protein from which the epitopes in the vaccine are derived. For example, a cocktail of epitope-comprising peptides is administered ex vivo to PBMC, or isolated DC therefrom. A pharmaceutical to facilitate harvesting of DC can be used, such as ProgenipoietinTM (Monsanto, St. Louis, MO) or GM CSF/IL-4. After pulsing the DC with peptides, and prior to reinfusion into patients, the DC are washed to remove unbound peptides. As appreciated clinically, and readily determined by one of skill based on clinical outcomes, the number of DC reinfused into the patient can vary (see, e.g., Nature Med. 4:328, 1998; Nature Med. 2:52, 1996 and Prostate 32:272, 1997). Although 2-50 x 106 DC per patient are typically administered, larger number of DC, such as 107 or 108 can also be provided. Such cell populations typically contain between 50-90% DC. In some embodiments, peptide-loaded P8MC are.injected into patients without purification of the DC. For example, PBMC generated after treatment with an agent such as ProgenipoietinTM are injected into patients without 117 WO 03/087306 PCT/USO3/10462 purification of the DC. The total number of PBMC that are administered often ranges from 108 to 1010 . Generally, the cell doses injected into patients is based on the percentage of DC in the blood of each patient, as determined, for example, by immunofluorescence analysis with specific anti-DC antibodies. Thus, for example, if ProgenipoietinTM mobilizes 2% DC in the peripheral blood of a given patient, and that patient is to receive 5 x 106 DC, then the patient will be injected with a total of 2.5 x 108 peptide-loaded PBMC. The percent DC mobilized by an agent such as Progenipoietin T M is typically estimated to be between 2-10%, but can vary as appreciated by one of skill in the art. Ex vivo activation of CTL/HTL responses Alternatively, ex vivo CTL or HTL responses to 98P4B6 antigens can be induced by incubating, in tissue culture, the patient's, or genetically compatible, CTL or HTL precursor cells together with a source of APC, such as DC, and immunogenic peptides. After an appropriate incubation time (typically about 7-28 days), in which the precursor cells are activated and expanded into effector cells, the cells are infused into the patient, where they will destroy (CTL) or facilitate destruction (HTL) of their specific target cells, i.e., tumor cells. Example 33: An Alternative Method of Identifying and Confirming Motif-Bearing Peptides Another method of identifying and confirming motif-bearing peptides is to elute them from cells bearing defined MHC molecules. For example, EBV transformed B cell lines used for tissue typing have been extensively characterized to determine which HLA molecules they express. In certain cases these cells express only a single type of HLA molecule. These cells can be transfected with nucleic acids that express the antigen of interest, e.g. 98P4B6. Peptides produced by endogenous antigen processing of peptides produced as a result of transfection will then bind to HLA molecules within the cell and be transported and displayed on the cell's surface. Peptides are then eluted from the HLA molecules by exposure to mild acid conditions and their amino acid sequence determined, e.g., by mass spectral analysis (e.g., Kubo et al, J. Immunol. 152:3913, 1994). Because the majority of peptides that bind a particular HLA-molecule are motif-bearing, this is an alternative modality for obtaining the motif-bearing peptides correlated with the particular HLA molecule expressed on the cell. Alternatively, cell lines that do not express endogenous HLA molecules can be transfected with an expression construct encoding a single HLA allele. These cells can then be used as described, i.e., they can then be transfected with nucleic acids that encode 98P4B6 to isolate peptides corresponding to 98P4B6 that have been presented on the cell surface. Peptides obtained from such an analysis will bear motif(s) that correspond to binding to the single HLA allele that is expressed in the cell. As appreciated by one in the art, one can perform a similar analysis on a cell bearing more than one HLA allele and subsequently determine peptides specific for each HLA allele expressed. Moreover, one of skill would also recognize that means other than transfection, such as loading with a protein antigen, can be used to provide a source of antigen to the cell. Example 34: Complementary Polynucleotides Sequences complementary to the 98P486-encoding sequences, or any parts thereof, are used to detect, decrease, or inhibit expression of naturally occurring 98P4B6. Although use of oligonucleotides comprising from about 15 to 30 base pairs is described, essentially the same procedure is used with smaller or with larger sequence fragments. Appropriate oligonucleotides are designed using, e.g., OLIGO 4.06 software (National Biosciences) and the coding sequence of 98P4B6. To inhibit transcription, a complementary oligonucleotide is designed from the most unique 5' sequence and used to prevent promoter binding to the coding sequence. To inhibit translation, a complementary oligonucleotide is designed to prevent ribosomal binding to a 98P4B6-encoding transcript. 118 WO 03/087306 PCT/US03/10462 Example 35: Purification of Naturally-occurring or Recombinant 98P4B6 Using 98P4B6-Specific Antibodies Naturally occurring or recombinant 98P4B6 is substantially purified by immunoaffinity chromatography using antibodies specific for 98P4B6. An immunoaffinity column is constructed by covalently coupling anti-98P4B6 antibody to an activated chromatographic resin, such as CNBr-activated SEPHAROSE (Amersham Pharmacia Biotech). After the coupling, the resin is blocked and washed according to the manufacturer's instructions. Media containing 98P4B6 are passed over the immunoaffinity column, and the column is washed under conditions that allow the preferential absorbance of 98P4B6 (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/98P4B6 binding (e.g., a buffer of pH 2 to pH 3, or a high concentration of a chaotrope, such as urea or thiocyanate ion), and GCR.P is collected. Example 36: Identification of Molecules Which Interact with 98P4B6 ' 98P4B6, or biologically active fragments thereof, are labeled with 121 1 Bolton-Hunter reagent. (See, e.g., Bolton et al. (1973) Biochem. J. 133:529.) Candidate molecules previously arrayed in the wells of a multi-well plate are incubated with the labeled 98P4B6, washed, and any wells with labeled 98P4B6 complex are assayed. Data obtained using different concentrations of 98P4B6 are used to calculate values for the number, affinity, and association of 98P4B6 with the candidate molecules. Example 37: In Vivo Assay for 98P4B6 Tumor Growth Promotion The effect of the 98P4B6 protein on tumor cell growth is evaluated in vivo by gene overexpression in tumor-bearing mice. For example, prostate (PC3), lung (A427), stomach, ovarian (PAl) and uterus cell lines are engineered to express 98P4B6. SCID mice are injected subcutaneously on each flank with 1 x 106 of PC3, A427, PAl, or NIH-3T3 cells containing tkNeo empty vector or 98P486. At least two strategies may be used: (1) Constitutive 98P4B6 expression under regulation of a promoter such as a constitutive promoter obtained from the genomes of viruses such as polyoma virus, fowlpox virus (UK 2,211,504 published 5 July 1989), adenovirus (such as Adenovirus 2), bovine papilloma virus, avian sarcoma virus, cytomegalovirus, a retrovirus, hepatitis-B virus, and Simian Virus 40 (SV40), or from heterologous mammalian promoters, e.g., the actin promoter or an immunoglobulin promoter, provided such promoters are compatible with the host cell systems, and (2) Regulated expression under control of an inducible vector system, such as ecdysone, tet, etc., provided such promoters are compatible with the host cell systems. Tumor volume is then monitored at the appearance of palpable tumors and followed over time to determine if 98P4B6-expressing cells grow at a faster rate and whether tumors produced by 98P4B6-expressing cells demonstrate characteristics of altered aggressiveness (e.g. enhanced metastasis, vascularization, reduced responsiveness to chemotherapeutic drugs). Additionally, mice can be implanted with 1 x 101 of the same cells orthotopically to determine if 98P486 has an effect on local growth in the prostate or on the ability of the cells to metastasize, specifically to lungs, lymph nodes, and bone marrow. The assay is also useful to determine the 98P4B6 inhibitory effect of candidate therapeutic compositions, such as for example, 98P4B6 intrabodies, 98P4B6 antisense molecules and ribozymes. Example 38: 98P4B6 Monoclonal Antibody-mediated inhibition of Tumors In Vivo. The significant expression of 98P4B6 in prostate, lung, stomach, ovary, and uterus cancer tissues, its restrictive expression in normal tissues, together with its expected cell surface expression makes 98P4B6 an excellent target for antibody therapy. Similarly, 98P4B6 is a target for T-cell based immunotherapy. Thus, the therapeutic efficacy of anti 119 WO 03/087306 PCT/US03/10462 98P4B6 mAbs in human prostate cancer xenograft mouse models is evaluated by using androgen-independent LAPC-4 and LAPC-9 xenografts (Craft, N., et at., Cancer Res, 1999. 59(19): p. 5030-6) and the androgen independent recombinant cell line PC3-98P4B6 (see, e.g., Kaighn, M.E., et al., invest Urol, 1979. 17(1): p. 16-23). Similar approaches using patient derived xenografts or xenograft cell lines are used for cancers listed in Table I. Antibody efficacy on tumor growth and metastasis formation is studied, e.g., in a mouse orthotopic prostate cancer xenograft models and mouse lung, uterus, or stomach xenograft models. The antibodies can be unconjugated, as discussed in this Example, or can be conjugated to a therapeutic modality, as appreciated in the art. Anti-98P4B6 mAbs inhibit formation of both the androgen-dependent LAPC-9 and androgen-independent PC3-98P4B6 tumor xenografts. Anti-98P4B6 mAbs also retard the growth of established orthotopic tumors and prolonged survival of tumor-bearing mice. These results indicate the utility of anti-98P4B6 mAbs in the treatment of local and advanced stages of cancer. (See, e.g., (Saffran, D., et al., PNAS 10:1073-1078 or URL located on the World Wide Web at .pnas.org/cgildoi/10.1073/pnas.051624698). Administration of the anti-98P4B6 mAbs can lead to retardation of established orthotopic tumor growth and inhibition of metastasis to distant sites, resulting in a significant prolongation in the survival of tumor-bearing mice. These studies indicate that 98P4B6 is an attractive target for immunotherapy and demonstrate the therapeutic potential of anti 98P4B6 mAbs for the treatment of local and metastatic cancer. This example demonstrates that unconjugated 98P4B6 monoclonal antibodies are effective to inhibit the growth of human prostate tumor xenografts, as well as lung, uterus, or stomach xenograft grown in SCID mice; accordingly a combination of such efficacious monoclonal antibodies is also effective. Tumor inhibition using multiple unconjugated 98P4B6 mAbs Materials and Methods 98P4B6 Monoclonal Antibodies: Monoclonal antibodies are raised against 98P4B6 as described in Example 11 entitled "Generation of 98P4B6 Monoclonal Antibodies (mAbs)." The antibodies are characterized by ELISA, Western blot, FACS, and immunoprecipitation for their capacity to bind 98P4B6. Epitope mapping data for the anti-98P4B6 mAbs, as determined by ELISA and Western analysis, recognize epitopes on the 98P4B6 protein. Immunohistochemical analysis of cancer tissues and cells with these antibodies is performed. The monoclonal antibodies are purified from ascites or hybridoma tissue culture supernatants by Protein-G Sepharose chromatography, dialyzed against PBS, filter sterilized, and stored at -20 0 C. Protein determinations are performed by a Bradford assay (Bio-Rad, Hercules, CA). A therapeutic monoclonal antibody or a cocktail comprising a mixture of individual monoclonal antibodies is prepared and used for the treatment of mice receiving subcutaneous or orthotopic injections of LAPC-9 tumor xenografts. Cancer Xenografts and Cell Lines The LAPC-9 xenograft, which expresses a wild-type androgen receptor and produces prostate-specific antigen (PSA), is passaged in 6- to 8-week-old male ICR-severe combined immunodeficient (SCID) mice (Taconic Farms) by s.c. trocar implant (Craft, N., et al., supra). The prostate (PC3), lung (A427), ovarian (PAl) carcinoma cell lines (American Type Culture Collection) are maintained in RPMI or DMEM supplemented with L-glutamine and 10% FBS. PC3-98P4B6, A427-98P4B6, PA1-98P4B6 and 3T3-98P4B6 cell populations are generated by retroviral gene transfer as described in Hubert, R.S., et al., STEAP: a prostate-specific cell-surface antigen highly expressed in human prostate tumors. Proc NatI Acad Sci U S A, 1999. 96(25): p. 14523-8. Anti-98P4B6 staining is detected by using an FITC conjugated goat anti-mouse antibody (Southern Biotechnology Associates) followed by analysis on a Coulter Epics-XL f low cytometer. 120 WO 03/087306 PCT/US03/10462 Xenograft Mouse Models. Subcutaneous (s.c.) tumors are generated by injection of 1 x 10 6 LAPC-9, PC3, PC3-98P4B6, A427, A427 98P4B6, PAl, PAI-98P4B6, 3T3 or 3T3-98P4B6 cells mixed at a 1:1 dilution with Matrigel (Collaborative Research) in the right flank of male SCID mice. To test antibody efficacy on tumor formation, i.p. antibody injections are started on the same day as tumor-cell injections. As a control, mice are injected with either purified mouse IgG (ICN) or PBS; or a purified monoclonal antibody that recognizes an irrelevant antigen not expressed in human cells. In preliminary studies, no difference is found between mouse IgG or PBS on tumor growth. Tumor sizes are determined by vernier caliper measurements, and the tumor volume is calculated as length x width x height. Mice with s.c. tumors greater than 1.5 cm in diameter are sacrificed. PSA levels are determined by using a PSA ELISA kit (Anogen, Mississauga, Ontario). Circulating levels of anti-98P4B6 mAbs are determined by a capture ELISA kit (Bethyl Laboratories, Montgomery, TX). (See, e.g., (Saffran, D., et al., PNAS 10:1073-1078 or URL located on the World Wide Web at.pnas.org/cgi/ doi/10.1073/pnas.051624698) Orthotopic injections are performed under anesthesia by using ketamine/xylazine. For prostate orthotopic studies, an incision is made through the abdominal muscles to expose the bladder and seminal vesicles, which then are delivered through the incision to expose the dorsal prostate. LAPC-9 or PC3 cells (5 x 105 ) mixed with Matrigel are injected into each dorsal lobe in a 10-pl volume. To monitor tumor growth, mice are bled on a weekly basis for determination of PSA levels. The mice are segregated into groups for the appropriate treatments, with anti-98P4B6 or control mAbs being injected i.p. Anti-98P4B6 mAbs Inhibit Growth of 98P4B6-Expressing Xenograft-Cancer Tumors The effect of anti-98P4B6 mAbs on tumor formation is tested by using LAPC-9 and PC3-98P4B6 orthotopic models. As compared with the s.c. tumor model, the orthotopic model, which requires injection of tumor cells directly in the mouse prostate, lung, or ovary, respectively, results in a local tumor growth, development of metastasis in distal sites, deterioration of mouse health, and subsequent death (Saffran, D., et al., PNAS supra; Fu, X., et al., Int J Cancer, 1992. 52(6): p. 987-90; Kubota, T., J Cell Biochem, 1994. 56(1): p. 4-8). The features make the orthotopic model more representative of human disease progression and allowed us to follow the therapeutic effect of mAbs on clinically relevant end points. Accordingly, tumor cells are injected into the mouse prostate, lung, or ovary, and 2 days later, the mice are segregated into two groups and treated with either: a) 200-500pg, of anti-98P4B6 Ab, or b) PBS three times per week for two to five weeks. A major advantage of the orthotopic cancer model is the ability to study the development of metastases. Formation of metastasis in mice bearing established orthotopic tumors is studies by IHC analysis on lung sections using an antibody against a prostate-specific cell-surface protein STEAP expressed at high levels in LAPC-9 xenografts (Hubert, R.S., et al., Proc Natl Acad Sci US A, 1999. 96(25): p. 14523-8). Mice bearing established orthotopic LAPC-9 or PC3-98P486 tumors are administered 1000 pg injections of either anti-98P4B6 mAb or PBS over a 4-week period. Mice in both groups are allowed to establish a high tumor burden (PSA levels greater than 300 ng/ml for IAPC-9), to ensure a high frequency of metastasis formation in mouse lungs. Mice then are killed and their prostate and lungs are analyzed for the presence of tumor cells by IHC analysis. These studies demonstrate a broad anti-tumor efficacy of anti-98P4B6 antibodies on initiation and progression of prostate cancer in xenograft mouse models. Anti-98P4B6 antibodies inhibit tumor formation of both androgen-dependent and androgen-independent tumors as well as retarding the growth of already established tumors and prolong the survival of treated mice. Moreover, anti-98P4B6 mAbs demonstrate a dramatic inhibitory effect on the spread of local prostate tumor to distal sites, even in the presence of a large tumor burden. Thus, anti-98P4B6 mAbs are efficacious on major clinically relevant end points (tumor growth), prolongation of survival, and health. 121 WO 03/087306 PCT/USO3/10462 Example 39: Therapeutic and Diagnostic use of Anti-98P4B6 Antibodies in Humans. Anti-98P4B6 monoclonal antibodies are safely and effectively used for diagnostic, prophylactic, prognostic and/or therapeutic purposes in humans. Western blot and immunohistochemical analysis of cancer tissues and cancer xenografts with anti-98P4B6 mAb show strong extensive staining in carcinoma but significantly lower or undetectable levels in normal tissues. Detection of 98P4B6 in carcinoma and in metastatic disease demonstrates the usefulness of the mAb as a diagnostic and/or prognostic indicator. Anti-98P4B6 antibodies are therefore used in diagnostic applications such as immunohistochemistry of kidney biopsy specimens to detect cancer from suspect patients. As determined by flow cytometry, anti-98P4B6 mAb specifically binds to carcinoma cells. Thus, anti-98P4B6 antibodies are used in diagnostic whole body imaging applications, such as radioimmunoscintigraphy and radioimmunotherapy, (see, e.g., Potamianos S., et. al. Anticancer Res 20(2A):925-948 (2000)) for the detection of localized and metastatic cancers that exhibit expression of 98P4B6. Shedding or release of an extracellular domain of 98P4B6 into the extracellular milieu, such as that seen for alkaline phosphodiesterase B10 (Meerson, N. R., Hepatology 27:563-568 (1998)), allows diagnostic detection of 98P4B6 by anti-98P4B6 antibodies in serum and/or urine samples from suspect patients. Anti-98P4B6 antibodies that specifically bind 98P4B6 are used in therapeutic applications for the treatment of cancers that express 98P4B6. Anti-98P4B6 antibodies are used as an unconjugated modality and as conjugated form in which the antibodies are attached to one of various therapeutic or imaging modalities well known in the art, such as a prodrugs, enzymes or radioisotopes. In preclinical studies, unconjugated and conjugated anti-98P4B6 antibodies are tested for efficacy of tumor prevention and growth inhibition in the SCID mouse cancer xenograft models, e.g., kidney cancer models AGS-K3 and AGS-K6, (see, e.g., the Example entitled "98P4B6 Monoclonal Antibody-mediated Inhibition of Bladder and Lung Tumors In Vivo'). Either conjugated and unconjugated anti-98P4B6 antibodies are used as a therapeutic modality in human clinical trials either alone or in combination with other treatments as described in following Examples. Example 40: Human Clinical Trials for the Treatment and Diagnosis of Human Carcinomas through use of Human Anti-98P4B6 Antibodies In vivo Antibodies are used in accordance with the present invention which recognize an epitope on 98P4B6, and are used in the treatment of certain tumors such as those listed in Table I. Based upon a number of factors, including 98P4B6 expression levels, tumors such as those listed in Table I are presently preferred indications. In connection with each of these indications, three clinical approaches are successfully pursued. I.) Adjunctive therapy: In adjunctive therapy, patients are treated with anti-98P4B6 antibodies in combination with a chemotherapeutic or antineoplastic agent and/or radiation therapy. Primary cancer targets, such as those listed in Table I, are treated under standard protocols by the addition anti-98P486 antibodies to standard first and second line therapy. Protocol designs address effectiveness as assessed by reduction in tumor mass as well as the ability to reduce usual doses of standard chemotherapy. These dosage reductions allow additional and/or prolonged therapy by reducing dose-related toxicity of the chemotherapeutic agent. Anti-98P4B6 antibodies are utilized in several adjunctive clinical trials in combination with the chemotherapeutic or antineoplastic agents adriamycin (advanced prostrate carcinoma), cisplatin (advanced head and neck and lung carcinomas), taxol (breast cancer), and doxorubicin (preclinical). II.) Monotherapy: In connection with the use of the anti-98P4B6 antibodies in monotherapy of tumors, the antibodies are administered to patients without a chemotherapeutic or antineoplastic agent. In one embodiment, monotherapy is conducted clinically in end stage cancer patients with extensive metastatic disease. Patients show some disease stabilization. Trials demonstrate an effect in refractory patients with cancerous tumors. 122 WO 03/087306 PCT/US03/10462 Ill.) Imaging Agent: Through binding a radionuclide (e.g., iodine or yttrium (1131, YN) to anti-98P4B6 antibodies, the radiolabeled antibodies are utilized as a diagnostic and/or imaging agent. In such a role, the labeled antibodies localize to both solid tumors, as well as, metastatic lesions of cells expressing 98P4B6. In connection with the use of the anti-98P4B6 antibodies as imaging agents, the antibodies are used as an adjunct to surgical treatment of solid tumors, as both a pre-surgical screen as well as a post-operative follow-up to determine what tumor remains and/or returns. In one embodiment, a (111 In)-98P4B6 antibody is used as an imaging agent in a Phase I human clinical trial in patients having a carcinoma that expresses 98P4B6 (by analogy see, e.g., Divgi et al. J. Natl. Cancer Inst. 83:97-104 (1991)). Patients are followed with standard anterior and posterior gamma camera. The results indicate that primary lesions and metastatic lesions are identified Dose and Route of Administration As appreciated by those of ordinary skill in the art, dosing considerations can be determined through comparison with the analogous products that are in the clinic. Thus, anti-98P4B6 antibodies can be administered with doses in the range of 5 to 400 mg/m 2, with the lower doses used, e.g., in connection with safety studies. The affinity of anti-98P4B6 antibodies relative to the affinity of a known antibody for its target is one parameter used by those of skill in the art for determining analogous dose regimens. Further, anti-98P4B6 antibodies that are fully human antibodies, as compared to the chimeric antibody, have slower clearance; accordingly, dosing in patients with such fully human anti-98P4B6 antibodies can be lower, perhaps in the range of 50 to 300 mg/m 2 , and still remain efficacious. Dosing in mg/m 2 , as opposed to the conventional measurement of dose in mg/kg, is a measurement based on surface area and is a convenient dosing measurement that is designed to include patients of all sizes from infants to adults. Three distinct delivery approaches are useful for delivery of anti-98P4B6 antibodies. Conventional intravenous delivery is one standard delivery technique for many tumors. However, in connection with tumors in the peritoneal cavity, such as tumors of the ovaries, biliary duct, other ducts, and the like, intraperitoneal administration may prove favorable for obtaining high dose of antibody at the tumor and to also minimize antibody clearance. In a similar manner, certain solid tumors possess vasculature that is appropriate for regional perfusion. Regional perfusion allows for a high dose of antibody at the site of a tumor and minimizes short term clearance of the antibody. Clinical Development Plan (CDP) Overview: The CDP follows and develops treatments of anti-98P486 antibodies in connection with adjunctive therapy, monotherapy, and as an imaging agent. Trials initially demonstrate safety and thereafter confirm efficacy in repeat doses. Trails are open label comparing standard chemotherapy with standard therapy plus anti-98P4B6 antibodies. As will be appreciated, one criteria that can be utilized in connection with enrollment of patients is 98P4B6 expression levels in their tumors as determined by biopsy. As with any protein or antibody infusion-based therapeutic, safety concerns are related primarily to (i) cytokine release syndrome, i.e., hypotension, fever, shaking, chills; (ii) the development of an immunogenic response to the material (i.e., development of human antibodies by the patient to the antibody therapeutic, or HAHA response); and, (iii) toxicity to normal cells that express 98P4B6. Standard tests and follow-up are utilized to monitor each of these safety concerns. Anti 98P4B6 antibodies are found to be safe upon human administration. Example 41: Human Clinical Trial Adjunctive Therapy with Human Anti-98P4B6 Antibody and Chemotherapeutic Agent A phase I human clinical trial is initiated to assess the safety of six intravenous doses of a human anti-98P4B6 antibody in connection with the treatment of a solid tumor, e.g., a cancer of a tissue listed in Table I. In the study, the safety 123 WO 03/087306 PCT/USO3/10462 of single doses of anti-98P4B6 antibodies when utilized as an adjunctive therapy to an antineoplastic or chemotherapeutic agent as defined herein, such as, without limitation: cisplatin, topotecan, doxorubicin, adriamycin, taxol, or the like, is assessed. The trial design includes delivery of six single doses of an anti-98P486 antibody with dosage of antibody escalating from approximately about 25 mg/m 2to about 275 mg/m 2 over the course of the treatment in accordance with the following schedule: Day 0 Day 7 Day 14 Day 21 Day 28 Day 35 mAb Dose 25 75 125 175 225 275 mg/m 2 mg/m 2 mg/m 2 mg/m 2 mg/m 2 mg/m 2 Chemotherapy + + + + + + (standard dose) Patients are closely followed for one-week following each administration of antibody and chemotherapy. In particular, patients are assessed for the safety concerns mentioned above: (i) cytokine release syndrome, i.e., hypotension, fever, shaking, chills; (ii) the development of an immunogenic response to the material (i.e., development of human antibodies by the patient to the human antibody therapeutic, or HAHA response); and, (iii) toxicity to normal cells that express 98P4B6. Standard tests and follow-up are utilized to monitor each of these safety concerns. Patients are also assessed for clinical outcome, and particularly reduction in tumor mass as evidenced by MRI or other imaging. The anti-98P4B6 antibodies are demonstrated to be safe and efficacious, Phase II trials confirm the efficacy and refine optimum dosing. Example 42: Human Clinical Trial: Monotherapy with Human Anti-98P4B6 Antibody Anti-98P4B6 antibodies are safe in connection with the above-discussed adjunctive trial, a Phase II human clinical trial confirms the efficacy and optimum dosing for monotherapy. Such trial is accomplished, and entails the same safety and outcome analyses, to the above-described adjunctive trial with the exception being that patients do not receive chemotherapy concurrently with the receipt of doses of anti-98P4B6 antibodies. Example 43: Human Clinical Trial: Diagnostic Imaging with Anti-98P4B6 Antibody Once again, as the adjunctive therapy discussed above is safe within the safety criteria discussed above, a human clinical trial is conducted concerning the use of anti-98P4B6 antibodies as a diagnostic imaging agent. The protocol is designed in a substantially similar manner to those described in the art, such as in Divgi et al. J. Natl. Cancer inst. 83:97-104 (1991). The antibodies are found to be both safe and efficacious when used as a diagnostic modality. Example 44: Homology Comparison of 98P4B6 to Known Sequences The 98P4B6 gene is homologous to a cloned and sequenced gene, namely human STAMP1 (gi 15418732) (Korkmaz, K.S et al, J. Biol. Chem. 2002, 277: 36689), showing 99% identity and 99% homology to that gene (figure 4). The 98P4B6 protein also shows 99% identity and 99% homology to another human six transmembrane epithelial antigen of prostate 2 (gi 23308593) (Walker, M.G et al, Genome Res. 1999, 9:1198; Porkka, K.P., Helenius, M.A. and Visakorpi, T, Lab. Invest. 2002, 82: 1573). The closest mouse homolog to 98P4B6is six transmembrane epithelial antigen of prostate 2 (gi 28501136), with 97% identity and 99% homology. We have identified several variants of the 98P4B6 protein, including 4 splice variants and 3 SNPs (Figure 11fl). The 98P4B6 v.1 protein consists of 454 amino acids, with calculated molecular weight of 52kDa, and pl of 8.7. It is a 6 transmembrane protein that can localize to the cell surface or possibly to the 124 WO 03/087306 PCT/USO3/10462 endoplasmic reticulum (Table VI). Several 98P4B6 variants, including v.1, v.5-8, v.13, v.14, v.21, v.25 share similar features, such protein motifs with functional significance, as well as structural commonalities such as multiple transmembrane domains. The 98P4B6 v.2 is a short protein with no known motifs. Motif analysis revealed the presence of several known motifs, including oxido-reductase, homocysteine hydrolase and dudulin motifs. Variant v.7 and SNPs of this variant also carry an Ets motif, often associated with transcriptional activity. Several oxidoreductases have been identified in mammalian cells, including the NADH/quinone oxidoreductase. This protein associate with the cell membrane and function as a proton/Na+ pump, which regulates the protein degradation of the tumor suppressor p53, and protects mammalian cells from oxidative stress, cytotoxicity, and mutages (Asher G, et al, Proc Natl Acad Sci U S A. 2002, 99:13125; Jaiswal AK, Arch Biochem Biophys 2000, 375:62 Yano T, Mol Aspects Med 2002, 23:345). Homocysteine hydrolase is an enzyme known to catalyze the breakdown of S-adenosylhomocysteine to homocysteine and adenosine, ultimately regulating trans-methylation, therby regulating protein expression, cell cycle and .proliferation (Turner MAet al. Cell Biochem Biophys 2000;33:101;Zhang et al, J Biol Chem. 2001; 276:35867) This information indicates that 98P4B6 plays a role in the cell growth of mammalian cells, regulate gene transcription and transport of electrons and small molecules. Accordingly, when 98P4B6 functions as a regulator of cell growth, tumor formation, or as a modulator of transcription involved in activating genes associated with inflammation, tumorigenesis, or proliferation, 98P4B6 is used for therapeutic, diagnostic, prognostic and/or preventative purposes. In addition, when a molecule, such as a variant or polymorphism of 98P4B6 is expressed in cancerous tissues, it is used for therapeutic, diagnostic, prognostic and/or preventative purposes. Example 45: Phenotypic Effects of STEAP-2 Expression Experiments regarding the expression of STEAP-2 protein having the amino acid sequence shown in Figure 2 and encoded by a cDNA insert in a plasmid deposited with the American Type Culture Collection on 02-July-1999 and assigned as ATCC Accession No. PTA-311. As deduced from the coding sequence, the open reading frame encodes 454 amino acids with 6 transmembrane domains. A summary of the characteristics associated with STEAP-2 proteinis shown on Figure 19. The data set forth in the present patent application provide an expression profile of the STEAP-2 protein that is predominantly specific for the prostate among normal tissues, for certain types of prostate tumors as well as other tumors. This evidence is based on detecting messenger RNA using Northern blotting. In keeping with standard practice in this industry, Northern blots are routinely used to assess gene expression, as it does not require the time consuming process of synthesizing the relevant protein, raising antibodies, assuring the specificity of the antibodies, required for Western blotting of proteins and the histological examination of tissues. Northern blotting offers a credible and efficient method of assessing RNA expression and expression levels. This Example demonstrates that STEAP-2 protein is, indeed, produced. In summary, the experiments show that PC-3 cells and 3T3 cells which were modified to contain an expression system for STEAP-2 showed enhanced levels of tyrosine phosphorylation in general, and of phosphorylation of ERK protein in particular. The data also show that PC-3 cells that contain an expression system for STEAP-2 showed modified calcium flux, a modified response to paclitaxel, and a general inhibition of drug-induced apoptosis. These are effects exhibited at the protein level, thus these data alone are probative that the STEAP-2 protein exists. Furthermore, although such phenotypic effects are protein-mediated, further evidence indicates that the STEAP-2 protein itself is the mediator of the effects. This evidence is obtained by utilizing a modified STEAP-2 protein. An expression system is stably introduced into PC3 and 3T3 cells which allows the expression of a modified form of STEAP-2, designated STEAP-2CFI, where "Fl" stands for flag. STEAP-2CFI is a STEAP-2 protein having a peptide extension, i.e., a Flag epitope 125 WO 03/087306 PCT/US03/10462 that alters the physical conformation of this protein. The Flag epitope is a string 8 amino acids, often introduced at either the amino or carboxy termini of protein as a means of identifying and following a recombinant protein in engineered cells (Slootstra JW et al, Mol Divers 1997, 2:156). In most cases, the introduction of the Flag epitope at either termini of a protein has little effect on the natural function and location of that protein (Molloy SS et al, EMBO J 1994, 13:18). However, this is dependent on the characteristics of the protein being Flag tagged. Recent studies have shown that a Flag tag affects the function and conformation of select proteins such as the CLN3 protein (see, e.g., Haskell RE, etal. Mol Genet Metab 1999, 66:253). As with CLN3, introducing a Flag epitope tag to the C-terminus of STEAP-2 alters the physical conformation and properties of this protein. Altering the STEAP-2 protein with the C-Flag epitope resulted in a significant decrease in the effects otherwise observed, including phosphorylation of ERK and resistance to drug-induced cell death. The data indicate that it is the STEAP-2 protein that mediated these phenotypic effects. Finally, in vitmro translation studies using rabbit reticulocyte lysate, showed that the STEAP-2 protein is translated and exhibits the expected molecular weight. Figures 20 and 21 show the results obtained when PC-3 and 3T3 cells, respectively, were modified to contain the retroviral expression system pSRI encoding the indicated proteins, including STEAP-1, STEAP-2 and STEAP-2CFI, respectively. Gene-specific protein expression was driven from a long terminal repeat (LTR), and the Neomycin resistance gene was used for selection of mammalian cells that stably express the protein. PC-3 and 3T3 cells were transduced with the retrovirus, selected in the presence of G418 and cultured under conditions which permit expression of the STEAP-2 coding sequence. The cells were grown overnight in low concentrations of FBS (0.5-1% FBS) and were then stimulated with 10% FBS. The cells were lysed in RIPA buffer and quantitated for protein concentration. Whole cell lysates were separated by SDS-PAGE and analyzed by Western blotting using anti-phospho-ERK (Cell Signaling Inc.) or anti-phosphotyrosine (UBI) antibodies (Figures 20, 21, and 22). As shown on Figure 20, as compared to untransformed PC-3 cells, cells modified to contain STEAP-2 contain enhanced amounts of phosphorylated tyrosine. Similar results from an analogous experiment on 3T3 cells are shown on page 3. In this latter experiment, the STEAP-2CFI expression system was also transfected into 3T3 cells, which cells were used as a control. As shown on Figure 21, the enhanced phosphorylation found in the presence of native STEAP-2 was significantly reduced when the conformation of the protein was altered. These results thus show conclusively that the STEAP-2 protein was produced and mediated the above-described phenotypic effects. Figure 22 shows similar results, both in PC-3 and 3T3 cells where phosphorylation of ERK, specifically, is detected. The protocol is similar to that set forth in paragraph 5 above, except that rather than probing the gels with antibodies specific for phosphotyrosine the gels were probed both the anti-ERK and anti-phospho-ERK antibodies. As shown on Figure 22, in the presence of 10% FBS, both PC-3 cells and 3T3 cells modified to express STEAP-2 showed phosphorylation of ERK which was not detectable in cells transformed to contain STEAP-2CFI. In contrast to control PC-3 cells which exhibit no background ERK phosphorylation, control 3T3-neo cells show low levels of endogenous ERK phosphorylation. Treatment with 10% FBS enhanced phosphorylation of ERK protein in cells expressing STEAP-2 relative to 3T3-neo cells, while no increase in ERK phosphorylation was observed in 3T3 cells expressing modified STEAP-2, i.e. STEAP-2 CFI. Other effects on cellular metabolism in cells modified to contain a STEAP-2 expression system were also shown in our data. Figure 23 shows that when cells with and without expression systems for STEAP-2 were measured for calcium flux in the presence of LPA, calcium flux was enhanced in the STEAP-2 containing cells. Using FACS analysis and commercially available indicators (Molecular Probes), parental cells and cells expressing STEAP-2 were compared for their ability to transport calcium. PC3-neo and PC3-STEAP-2 cells were loaded with calcium responsive indicators Fluo4 and Fura red, incubated in the presence or absence of calcium and LPA, and analyzed by flow cytometry. PC3 cells expressing a known calcium transporter, PC3-83P3H3 pCaT were used as positive control (Biochem Biophys Res Commun. 2001, 282:729). The table on Figure 23 shows that STEAP-2 mediates calcium flux in response to LPA, and that the magnitude of calcium flux is comparable to that produced by a known calcium channel. 126 WO 03/087306 PCT/USO3/10462 In addition, STEAP-2 expressing PC3 cells demonstrated increased sensitivity to agatoxin, a calcium channel blocker as compared to PC3-neo cells. These results indicate that STEAP-2 expression renders PC3 cells sensitive to treatment with the Ca++ channel inhibitors. Information derived from the above experiments provides a mechanism by which cancer cells are regulated. This is particularly relevant in the case of calcium, as calcium channel inhibitors have been reported to induce the death of certain cancer cells, including prostate cancer cell lines (see, e.g., Batra S, Popper LD, Hartley-Asp B. Prostate. 1991, 19:299). Figure 24 shows that cells transfected with a STEAP-2 expression system have enhanced ability to survive exposure to paclitaxel. In order to determine the effect of STEAP-2 on survival, PC3 cells lacking or expressing STEAP-2 were treated with chemotherapeutic agents currently used in the clinic. Effect of treatment was evaluated by measuring cell proliferation using the Alamare blue assay (Figure 23). While only 5.2% of PC3-neo cells were able to metabolize Alalmare Blue and proliferate in the presence of 5 pM paclitaxel, 44.8% of PC3-STEAP-2 cells survived under the same conditions. These results indicate that expression of STEAP-2 imparts resistance to paclitaxel. These findings have significant in vivo implications, as they indicate that STEAP-2 provides a growth advantage for prostate tumor cells in patients treated with common therapeutic agents. A more detailed form of these results is shown on Figures 25 and 26. Results in these two pages demonstrate the mode of action by which STEAP-2 supports the survival of PC3 cells. In these studies, PC3 cells expressing or lacking STEAP-2 were treated with paclitaxel for 60 hours, and assayed for apoptosis using annexin V conjugated to FITC and propidium iodide staining. In apoptotic cells, the membrane phospholipid phosphatidylserine (PS) is translocated from the inner to the outer leaflet of the membrane, thereby exposing PS to the external cellular environment. PS is recognized by and binds to annexin V, providing scientists with a reliable means of identifying cells undergoing programmed cell death. Staining with propidium iodide identifies dead cells. Figure 25 show that expression of STEAP-2 inhibits paclitaxel-mediated apoptosis by 45% relative to paclitaxel-treated PC3-neo cells. The protective effect of STEAP-2 is inhibited when STEAP-2 is modified by the presence of Flag at its C-terminus Figure 26. The publicly available literature contains several examples of prostate and other cancers that exhibit similar phenotypic characteristics as those observed in PC3 cells that express STEAP-2. In particular, clinical studies have reported transient tumor regression and/or only partial responses in patients treated with paclitaxel. For instance, only around 50% of prostate cancer patients entered in a single agent clinical trial of paclitaxel showed reduced PSA levels when treated with doses of paclitaxel that induced grade 3 and grade 4 toxicity; a much higher level of response would have been expected based on this dose level, thus this data indicates the development of paclitaxel resistance in prostate cancer patients (Beer TM et al, Ann Oncol 2001, 12:1273). A similar phenomenon of reduced responsiveness and progressive tumor recurrence was observed in other studies (see, e.g., Obasaju C, and Hudes GR. Hematol Oncol Clin North Am 2001,15:525). In addition, inhibition of calcium flux in cells that endogenously express STEAP-2, such as LNCaP cells, induces their cell death (Skryma R et al, J Physiol. 2000, 527:71). Thus, STEAP-2 protein is produced not only in the cells tested, but also in unmodified tumor cells or unmodified prostate cells where the presence of mRNA has been shown. The Northern blot data in the specification clearly show that the messenger RNA encoding STEAP-2 is produced in certain prostate and tumor cells. The 3T3 and PC-3 cells, which are themselves tumor cell lines, are clearly able to translate the messenger RNA into protein. Because it has been shown that there is no barrier to translation of the message in cells similar to those tumor and prostate cells in which the mRNA has been shown to be produced, it can properly be concluded that the protein itself can be detected in the unmodified tumor or prostate cells, given the fact that it is shown that mRNA is produced. This conclusion is also supported by the pattems of phenotypic changes seen in cells specifically modified to express STEAP-2, these changes comport with changes seen in 127 WO 03/087306 PCT/USO3/10462 cancer cells. Based on the above data, it is scientifically concluded that cells and tissues which produce mRNA encoding STEAP-2 also produce the protein itself. Example 46: Identification and Confirmation of Potential Signal Transduction Pathways Many mammalian proteins have been reported to interact with signaling molecules and to participate in regulating signaling pathways (J Neurochem. 2001; 76:217-223. Using immunoprecipitation and Western blotting techniques, proteins are identified that associate with 98P4B6 and mediate signaling events. Several pathways known to play a role in cancer biology can be regulated by 98P4B6, including phospholipid pathways such as PI3K, AKT, etc, adhesion and migration pathways, including FAK, Rho, Rac-1, etc, as well as mitogenic/survival cascades such as ERK, p38, etc (Cell Growth Differ. 2000,11:279; J Biol Chem. 1999, 274:801; Oncogene. 2000,19:3003, J. Cell Biol. 1997,138:913.). To confirm that 98P4B6 directly or indirectly activates known signal transduction pathways in cells, luciferase (luc) based transcriptional reporter assays are carried out in cells expressing individual genes. These transcriptional reporters contain consensus-binding sites for known transcription factors that lie downstream of well-characterized signal transduction pathways. The reporters and examples of these associated transcription factors, signal transduction pathways, and activation stimuli are listed below. 1. NFkB-luc, NFkB/Rel; Ik-kinase/SAPK; growthlapoptosis/stress 2. SRE-luc, SRF/TCF/ELK1; MAPKISAPK; growth/differentiation 3. AP-1-luc, FOS/JUN; MAPKISAPKIPKC; growth/apoptosis/stress 4. ARE-luc, androgen receptor; steroids/MAPK; growth/differentiation/apoptosis 5. p53-luc, p53; SAPK; growth/differentiation/apoptosis 6. CRE-luc, CREB/ATF2; PKAlp38; growth/apoptosis/stress Gene-mediated effects can be assayed in cells showing mRNA expression. Luciferase reporter plasmids can be introduced by lipid-mediated transfection (TFX-50, Promega). Luciferase activity, an indicator of relative transcriptional activity, is measured by incubation of cell extracts with luciferin substrate and luminescence of the reaction is monitored in a luminometer. Signaling pathways activated by 98P4B6 are mapped and used for the identification and validation of therapeutic targets. When 98P4B6 is involved in cell signaling, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 47: 98P4B6 Functions as a Proton or small molecule transporter Sequence and homology analysis of 98P4B6 indicate that the 98P4B6 may function as a transporter. To confirm that STEAP-1 functions as an ion channel, FACS analysis and fluorescent microscopy techniques are used (Gergely L, et al., Clin Diagn Lab Immunol. 1997; 4:70; Skryma R, et al., J Physiol. 2000, 527: 71). Using FACS analysis and commercially available indicators (Molecular Probes), parental cells and cells expressing 98P4B6 are compared for their ability to transport electrons, sodium, calcium; as well as other small molecules in cancer and normal cell lines. For example, PC3 and PC3 98P4B6 cells were loaded with calcium responsive indicators Fluo4 and Fura red, incubated in the presence or absence of calcium and lipophosphatidic acid (LPA), and analyzed by flow cytometry. Ion flux represents an important mechanism by which cancer cells are regulated. This is particularly true in the case of calcium, as calcium channel inhibitors have been 128 WO 03/087306 PCT/US03/10462 reported to induce the death of certain cancer cells, including prostate cancer cell lines (Batra S, Popper LD, Hartley-Asp B. Prostate. 1991, 19: 299). Similar studies are conducted using sodium, potassium, pH, etc indicators. Due to its homology to an oxidoreductase, 98P486 can participate in imparting drug resistance by mobilizing and transporting small molecules. The effect of 98P4B6 on small molecule transport is investigated using a modified MDR assay. Control and 98P4B6 expressing cells are loaded with a fluorescent small molecule such as calcein AM. Extrusion of calcein from the cell is measured by examining the supernatants for fluorescent compound. MOR-like activity is confirmed using MDR inhibitors. When 98P4B6 functions as a transporter, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 48: Involvement in Tumor Progression The 98P4B6 gene can contribute to the growth of cancer cells. The role of 98P4B6 in tumor growth is confirmed in a variety of primary and transfected cell lines including prostate as well as NIH 3T3 cells engineered to stably express 98P4B6. Parental cells lacking 98P4B6 and cells expressing 98P4B6 are evaluated for cell growth using a well-documented proliferation assay (Fraser SP, Grimes JA, Djamgoz MB. Prostate. 2000;44:61, Johnson DE, Ochieng J, Evans SL. Anticancer Drugs. 1996, 7:288). To confirm the role of 98P4B6 in the transformation process, its effect in colony forming assays is investigated. Parental NIH-3T3 cells lacking 98P4B6 are compared to NIH-3T3 cells expressing 98P486, using a soft agar assay under stringent and more permissive conditions (Song Z. et al. Cancer Res. 2000;60:6730). To confirm the role of 98P4B6 in invasion and metastasis of cancer cells, a well-established assay is used, e.g., a Transwell Insert System assay (Becton Dickinson) (Cancer Res. 1999; 59:6010). Control cells, including prostate and fibroblast cell lines lacking 98P4B6 are compared to cells expressing 98P4B6. Cells are loaded with the fluorescent dye, calcein, and plated in the top well of the Transwell insert coated with a basement membrane analog. Invasion is determined by fluorescence of cells in the lower chamber relative to the fluorescence of the entire cell population. 98P4B6 can also play a role in cell cycle and apoptosis. Parental cells and cells expressing 98P4B6 are compared for differences in cell cycle regulation using a well-established BrdU assay (Abdel-Malek ZA. J Cell Physiol. 1988, 136:247). In short, cells are grown under both optimal (full serum) and limiting (low serum) conditions are labeled with BrdU and stained with anti-BrdU Ab and propidium iodide. Cells are analyzed for entry into the G1, S, and G2M phases of the cell cycle. Altematively, the effect of stress on apoptosis is evaluated in control parental cells and cells expressing 98P4B6, including normal and tumor prostate cells. Engineered and parental cells are treated with various chemotherapeutic agents, such as etoposide, flutamide, etc, and protein synthesis inhibitors, such as cycloheximide. Cells are stained with annexin V FITC and cell death is measured by FACS analysis. The modulation of cell death by 98P4B6 can play a critical role in regulating tumor progression and tumor load. When 98P4B6 plays a role in cell growth, transformation, invasion or apoptosis, it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 49: Involvement in Angiogqenesis Angiogenesis or new capillary blood vessel formation is necessary for tumor growth (Hanahan D, Folkman J. Cell. 1996, 86:353; Folkman J. Endocrinology. 1998 139:441). Based on the effect of phsophodieseterase inhibitors on endothelial cells, 98P4B6 plays a role in angiogenesis (DeFouw Let al, Microvasc Res 2001, 62:263). Several assays have been developed to measure angiogenesis in vitro and in vivo, such as the tissue culture assays endothelial cell tube 129 WO 03/087306 PCT/US03/10462 formation and endothelial cell proliferation. Using these assays as well as in vitro neo-vascularization, the role of 98P4B6 in angiogenesis, enhancement or inhibition, is confirmed. For example, endothelial cells engineered to express 98P4B6 are evaluated using tube formation and proliferation assays. The effect of 98P4B6 is also confirmed in animal models in vivo. For example, cells either expressing or lacking 98P4B6 are implanted subcutaneously in immunocompromised mice. Endothelial cell migration and angiogenesis are evaluated 5-15 days later using immunohistochemistry techniques. 98P4B6 affects angiogenesis, and it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 50: Regulation of Transcription The localization of 98P4B6 and its similarity to hydrolases as well as its Ets motif (v.7) indicate that 98P486 is effectively used as a modulator of the transcriptional regulation of eukaryotic genes. Regulation of gene expression is confirmed, e.g., by studying gene expression in cells expressing or lacking 98P4B6. For this purpose, two types of experiments are performed. In the first set of experiments, RNA from parental and 98P4B6-expressing cells are extracted and hybridized to commercially available gene arrays (Clontech) (Smid-Koopman E et al. Br J Cancer. 2000. 83:246). Resting cells as well as cells treated with FBS or androgen are compared. Differentially expressed genes are identified in accordance with procedures known in the art. The differentially expressed genes are then mapped to biological pathways (Chen K et al. Thyroid. 2001. 11:41.). In the second set of experiments, specific transcriptional pathway activation is evaluated using commercially available (Stratagene) luciferase reporter constructs including: NFkB-luc, SRE-luc, ELKi-luc, ARE-luc, p53-luc, and CRE-luc. These transcriptional reporters contain consensus binding sites for known transcription factors that lie downstream of well characterized signal transduction pathways, and represent a good tool to ascertain pathway activation and screen for positive and negative modulators of pathway activation. Thus, 98P4B6 plays a role in gene regulation. When 98P4B6 is involved in gene regulation it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 51: Protein - Protein Association Several 6TM proteins have been shown to interact with other proteins, thereby regulating signal transduction, gene transcription, transformation, and cell adhesion. Using immunoprecipitation techniques as well as two yeast hybrid systems, proteins are identified that associate with 98P4B6. Immunoprecipitates from cells expressing 98P486 and cells lacking 98P4B6 are compared for specific protein-protein associations. Studies are performed to confirm the extent of association of 98P4B6 with effector molecules, such as nuclear proteins, transcription factors, kinases, phsophates etc. Studies comparing 98P4B6 positive and 98P4B6 negative cells as well as studies comparing unstimulated/resting cells and cells treated with epithelial cell activators, such as cytokines, growth factors, androgen and anti-integrin Ab reveal unique interactions. In addition, protein-protein interactions are confirmed using two yeast hybrid methodology (Curr Opin Chem Biol. 1999, 3:64). A vector carrying a library of proteins fused to the activation domain of a transcription factor is introduced into yeast expressing a 98P4B6-DNA-binding domain fusion protein and a reporter construct. Protein-protein interaction is detected by colorimetric reporter activity. Specific association with effector molecules and transcription factors directs one of skill to the mode of action of 98P4B6, and thus identifies therapeutic, prognostic, preventative and/or diagnostic targets for cancer. This and similar assays are also used to identify and screen for small molecules that interact with 98P4B6. 130 WO 03/087306 PCT/US03/10462 Thus it is found that 98P486 associates with proteins and small molecules. Accordingly, 98P4B6and these proteins and small molecules are used for diagnostic, prognostic, preventative and/or therapeutic purposes. Throughout this application, various website data content, publications, patent applications and patents are referenced. (Websites are referenced by their Uniform Resource Locator, or URL, addresses on the World Wide Web.) The disclosures of each of these references are hereby incorporated by reference herein in their entireties. The present invention is not to be limited in scope by the embodiments disclosed herein, which are intended as single illustrations of individual aspects of the invention, and any that are functionally equivalent are within the scope of the invention. Various modifications to the models and methods of the invention, in addition to those described herein, will become apparent to those skilled in the art from the foregoing description and teachings, and are similarly intended to fall within the scope of the invention. Such modifications or other embodiments can be practiced without departing from the true scope and spirit of the invention. 131 WO 03/087306 PCT/USO3/10462 TABLES: TABLE I: Tissues that Express 98P4B6: a. Malignant Tissues a Bladder b. Breast c. Cervix d. Colon e. Kidney f. Lung g. Ovary h. Pancreas i. Prostate j. Stomach k. Uterus TABLE II: Amino Acid Abbreviations SINGLE LETTER THREE LETTER FULL NAME F Phe phenylalanine L Leu leucine S Ser serine Y Tyr tyrosine C Cys cysteine W Trp tryptophan P Pro proline H His histidine Q Gin glutamine R Arg arginine I le isoleucine M Met methionine T Thr threonine N Asn asparagine K Lys lysine V Val valine A Ala alanine D Asp aspartic acid E Glu glutamic acid G Gly glycine 132 WO 03/087306 PCT/US03/10462 TABLE III: Amino Acid Substitution Matrix Adapted from the GCG Software 9.0 BLOSUM62 amino acid substitution matrix (block substitution matrix). The higher the value, the more likely a substitution is found in related, natural proteins. (See world wide web URL ikp.unibe.ch/manual/blosum62.html) A C D E F G H I K L MN P Q R S T V W Y. 4 0-2-1-2 0-2-1-1-1-1-2-1-1-1 1 0 0 -3 -2A 9 -3 -4 -2 -3 -3 -1 -3 -1 -1 -3 -3 -3 -3 -1 -1 -1 -2 -2 C 6 2 -3 -1 -1 -3 -1 -4 -3 1 -1 0 -2 0 -1 -3 -4 -3 D 5 -3 -2 0 -3 1 -3 -2 0 -1 2 0 0 -1 -2 -3 -2 E 6 -3 -1 0 -3 0 0 -3 -4 -3 -3 -2 -2 -1 1 3 F 6-2 -4 -2 -4-3 0 -2 -2-2 0 -2 -3 -2 -3G 8 -3 -1 -3 -2 1 -2 0 0 -1 -2 -3 -2 2 H 4 -3 2 1 -3 -3 -3 -3 -2 -1 3 -3 -1 I 5 -2 -1 0 -1 1 2 0 -1 -2 -3 -2 K 4 2 -3 -3 -2 -2 -2 -1 1 -2 -1 L 5 -2 -2 0 -1 -1 -1 1 -1 -1 M 6-2 0 0 1 0-3 -4 -2N 7 -1 -2 -1 -1 -2 -4 -3 P 5 1 0 -1 -2 -2 -1 Q 5 -1 -1 -3 -3 -2 R 4 1 -2 -3 -2 S 5 0 -2 -2 T 4 -3 -1 V 11 2 W 7Y 133 WO 03/087306 PCT/USO3/10462 TABLE IV: HLA Class 1111 Motifs/Supermotifs TABLE IV (A): HLA Class I SupermotifslMotifs SUPERMOTIF POSITION POSITION POSITION 2 (Primary Anchor) 3 (Primary Anchor) C Terminus (Primary Anchor) Al TIL VMS FWY A2 LIVMATQ IVMATL A3 VSMATLI RK A24 YFWIVLMT FIYWLM B7 P VILFMWYA B27 RHK FYLWMIVA B44 ED FWYLIMVA B58 ATS FWYLIVMA 862 QLIVMP FWYMIVLA MOTIFS Al TSM Y Al DEAS Y A2.1 LMVQIAT VLIMAT A3 LMVISATFCGD KYRHFA All VTMLISAGNCDF KRYH A24 YFWM FLIW A*3101 MVTALIS RK A*3301 MVALFIST RK A*6801 AVTMSLI RK B*0702 P LMFWYAIV B*3501 P LMFWYIVA B51 P LIVFWYAM B*5301 P IMFWYALV B*5401 P ATIVLMFWY Bolded residues are preferred, italicized residues are less preferred: A peptide is considered motif-bearing if it has primary anchors at each primary anchor position for a motif or supermotif as specified in the above table. TABLE IV (B): HLA Class II Supermotif 1 6 9 W F, Y, V, .1, L A, V, 1, L, P, C, S, T A, V, I, L, C, S, T, M, Y 134 WO 03/087306 PCT/USO3/10462 TABLE IV (C): HLA Class II Motifs MOTIFS 10 anchor 1 2 3 4 5 1

°

anchor6 7 8 9 DR4 preferred FMYLIVW M T I VSTCPALIM MH MH deleterious W R WDE DR1 preferred MFLIVWY PAMQ VMATSPLIC M AVM deleterious C CH FD CWD GDE D DR7 preferred MFLIVWY M W A IVMSACTPL M IV deleterious C G GRD N G DR3 MOTIFS 1* anchor 1 2 3 1 anchor4 5 1* anchor 6 Motif a preferred LIVMFY D Motif b preferred LIVMFAY DNQEST KRH DR Supermotif MFLIVWY VMSTACPLI Italicized residues indicate less preferred or "tolerated" residues TABLE IV (D): HLA Class I Supermotifs POSITION: 1 2 3 4 5 6 7 8 C-terminus

SUPER

MOTIFS Al 1 Anchor 1 Anchor TILVMS FWY A2 1' Anchor 1 Anchor LIVMATQ LIVMAT A3 Preferred 1 Anchor YFW YFW YFW P 1 Anchor VSMATLI (4/5) (3/5) (4/5) (4/5) RK deleterious DE (3/5); DE P (5/5) (4/5) A24 l Anchor 1 Anchor YFWVLMT FIYWLM B7 Preferred FWY (5/5) 1 * Anchor FWY FWY 1 Anchor LIVM (3/5) P (4/5) (3/5) VILFMWYA deleterious DE (3/5); DE G QN DE P(5/5); (3/5) (4/5) (4/5) (4/5) G(4/5); A(3/5); QN(3/5) B27 1 * Anchor 1 "Anchor RHK FYLWMIVA B44 1 Anchor 1" Anchor ED FWYLIMVA B58 1" Anchor 1" Anchor ATS FWYLIVMA B62 1 Anchor 10 Anchor QUIVMP FWYMIVLA Italicized residues indicate less preferred or "tolerated" residues 135 WO 03/087306 PCT/USO3/10462 TABLE IV (E): HLA Class I Motifs POSITION 1 2 3 4 5 6 7 8 9 C terminus or C-terminus Al preferred GFYW 1"Anchor DEA YFW P DEQN YFW 1"Anchor 9-mer STM Y deleterious DE RHKLIVMP A G A Al preferred GRHK ASTCLIVM 1*Anchor GSTC ASTC LIVM DE 1*Anchor 9-mer DEAS Y deleterious A RHKDEPYFW DE PQN RHK PG GP Al preferred YFW IAnchor DEAQN A YFWQN PASTC GDE P I'Anchor 10- STM Y mer deleterious GP RHKGLIVM DE RHK QNA RHKYFW RHK A Al preferred YFW STCLIVM 1°Anchor A YFW PG G YFW 1'Anchor 10- DEAS Y mer deleterious RHK RHKDEPYFW P G PRHK QN A2.1 preferred YFW lAnchor YFW STC YFW A P 1*Anchor 9-mer LMIVQAT VLIMAT deleterious DEP DERKH RKH DERKH POSITION: 1 2 3 4 5 6 7 8 9 C Terminus A2.1 preferred AYFW 1'Anchor LVIM G G FYWL 1°Anchor 10- LMIVQAT VIM VLIMAT mer deleterious DEP DE RKHA P RKH DERK RKH H A3 preferred RHK 1*Anchor YFW PRHKYF A YFW P 1*Anchor LMVISATFCGD W KYRHFA deleterious DEP DE All preferred A 1Anchor YFW YFW A YFW YFW P 1"Anchor VTLMISAGNCD KRYH F deleterious DEP A G A24 preferred YFWRHK lAnchor STC YFW YFW 1°Anchor 9-mer YFWM FLIW deleterious DEG DE G QNP DERH G AQN K A24 Preferred 1 Anchor P YFWP P 1*Anchor 10- YFWM FLIW mer Deleterious GDE QN RHK DE A QN DEA A310 Preferred RHK 1 Anchor YFW P YFW YFW AP 1Anchor 1 MVTALIS RK Deleterious DEP DE ADE DE DE DE A330 Preferred 1 Anchor YFW AYFW 1*Anchor 1 MVALFIST RK Deleterious GP DE A680 Preferred YFWSTC 1*Anchor YFWLIV YFW P 1*Anchor 1 AVTMSLI M RK deleterious GP DEG RHK A B070 Preferred RHKFWY 1 Anchor RHK RHK RHK RHK PA 1 Anchor 2 P LMFWYAI V deleterious DEQNP DEP DE DE GDE QN DE 136 WO 03/087306 PCT/USO3/10462 POSITION 1 2 3 4 5 6 7 8 9 C terminus or C-terminus Al preferred GFYW 1 Anchor DEA YFW P DEQN YFW 1°Anchor 9-mer STM Y deleterious DE RHKLIVMP A G A Al preferred GRHK ASTCLIVM 1°Anchor GSTC ASTC LIVM DE 1°Anchor 9-mer DEAS y deleterious A RHKDEPYFW DE PQN RHK PG GP B350 Preferred FWYLIVM 1 Anchor FWY FWY 1"Anchor 1 P LMFWYIV A deleterious AGP G G B51 Preferred LIVMFWY 1 *Anchor FWY STC FWY G FWY 1*Anchor P LIVFWYA M deleterious AGPDER DE G DEQN GDE HKSTC B530 preferred LIVMFWY 1 *Anchor FWY STC FWY LIVMFW FWY 1°Anchor 1 P Y IMFWYAL V deleterious AGPQN G RHKQN DE B540 preferred FWY 1IAnchor FWYLIVM LIVM ALIVM FWYA 1°Anchor 1 P P ATIVLMF vvWY deleterious GPQNDE GDESTC RHKDE DE QNDGE DE 137 WO 03/087306 PCT/US03/10462 TABLE IV (F): Summary of HLA-supertypes Overall phenotypic frequencies of HLA-supertypes in different ethnic populations Specificity Phenotypic frequency Supertype osition 2 C-TerminusCaucasian N.A. Black Japanese Chinese Hispanic verag B7 P AILMVFWY43.2 55.1 57.1 43.0 49.3 49.5 A3 AILMVST RK 37.5 42,1 5.8 52.7 43.1 44.2 A2 AILMVT AILMVT 45.8 39.0 2.4 45.9 43.0 42.2 A24 YF (WIVLMT)F I (YWLM) 23.9 38.9 58.6 40.1 38:3 40.0 B44 E (D) FWYLIMVA43.0 21,2 42.9 39.1 39.0 37.0 A1 I (LVMS) FWY 47.1 16.1 21.8 14.7 26.3 25.2 27 RHK FYL (WMI) 28.4 26.1 13.3 13.9 35.3 23.4 B62 QL (IVMP) FWY (MIV) 12.6 4.8 36.5 25.4 11.1 18.1 B58 ATS FWY (LIV) 10.0 25.1 1.6 9.0 5.9 10.3 TABLE IV (G): Calculated population coverage afforded by different HLA-supertype combinations HLA-supertypes Phenotypic frequency Caucasian N.A Blacks Japanese Chinese Hispanic Average 83.0 86.1 87.5 8.4 6.3 86.2 , A3 and B7 99.5 98.1 100.0 99.5 9.4 99.3 A2, A3, B7, A24, 844 99.9 99.6 100.0 99.8 9.9 99.8 and Al A2, A3, B7, A24, 844, A1, B27, B62, and B 58 Motifs indicate the residues defining supertype specificites. The motifs incorporate residues determined on the basis of published data to be recognized by multiple alleles within the supertype. Residues within brackets are additional residues also predicted to be tolerated by multiple alleles within the supertype. Table V: Frequently Occurring Motifs Name avrg. % Namedentity Description Potential Function Nucleic acid-binding protein functions as transcription factor, nuclear location zf-C2H2 34% Zinc finger, C2H2 type probable Cytochrome b(N- membrane bound oxidase, generate cytochromebN 68% terminal)/b6/petB superoxide domains are one hundred amino acids long and include a conserved Ig 19% Immunoglobulin domain intradomain disulfide bond. tandem repeats of about 40 residues, each containing a Trp-Asp motif. Function in signal transduction and WD40 18% WD domain, G-beta repea protein interaction may function in targeting signaling PDZ 23% PDZ domain molecules to sub-membranous sites LRR 28% Leucine Rich Repeat short sequence motifs involved in protein-protein interactions conserved catalytic core common to both serinelthreonine and tyrosine rotein kinases containing an ATP Pkinase 23% Protein kinase domain binding site and a catalytic site 138 WO 03/087306 PCT/US03/10462 pleckstrin homology involved in intracellular signaling or as constituents PH 16% PH domain of the cytoskeleton 30-40 amino-acid long found in the extracellular domain of membrane EGF 34% EGF-like domain bound proteins or in secreted proteins Reverse transcriptase (RNA-dependent DNA Rvt 49% polymerase) Cytoplasmic protein, associates integral Ank 25% Ank repeat membrane proteins to the cytoskeleton NADH- membrane associated. Involved in Ubiquinone/plastoquinone proton translocation across the Oxidoredgql 32% (complex I), various chains membrane calcium-binding domain, consists of a12 residue loop flanked on both sides by a Efhand 24% EF hand 12 residue alpha-helical domain Retroviral aspartyl Asparty or acid proteases, centered on Rvp 79% protease a catalytic aspartyl residue extracellular structural proteins involved in formation of connective tissue. The Collagen triple helix repeat sequence consists of the G-X-Y and the Collagen 42% (20 copies) polypeptide chains forms a triple helix. Located in the extracellular ligand binding region of receptors and is about 200 amino acid residues long with two pairs of cysteines involved in disulfide Fn3 20% Fibronectin type III domain bonds seven hydrophobic transmembrane egions, with the N-terminus located 7 transmembrane receptor extracellularly while the C-terminus is 7tm 1 19% (rhodopsin family) ytoplasmic. Signal through G proteins Table VI: Motifs and Post-translational Modifications of 98P4B6 cAMP- and cGMP-dependent protein kinase phosphorylation site. 176- 179 RKET (SEQ ID NO: 114) Protein kinase C phosphorylation site. 235 - 237 SVK Casein kinase II phosphorylation site. 9 -12 SATD (SEQ ID NO: 115) 50- 53 TVME (SEQ ID NO: 116) 130- 133 SCTD (SEQ ID NO: 117) 172 -175 SPEE (SEQ ID NO: 118) N-myristoylation site. 14 - 19 GLSIST (SEQ ID NO: 119) G-protein coupled receptors family 1 signature. 52 - 68 MESSVLLAMAFDRFVAV (SEQ ID NO: 120) Table VII: Search Peptides v.1 aal-454 (SEQ ID NO: 121) 9-mers, 10-mers and 15-mers MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 139 WO 03/087306 PCT/USO3/10462 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE EEYYRFYTPP NFVLALVLPS IVILDLLQLC RYPD v.2 aal-45 (SEQ ID NO: 122) 9-mers, 10-mers, 15-mers SGSPGLQALSL SLSSGFTPFS CLSLPSSWDY RCPPPCPADF FLYF v.5, (one aa diff at 211 and different c-terminal) Part A 9-mers: aa203-219 NLPLRLFTFWRGPVVVA (SEQ ID NO: 123) 10-mers: aa202-220 ENLPLRLFTFWRGPVVVAI (SEQ ID NO: 124) 15-mers: aa197-225 SAREIENLPLRLFTFWRGPVVVAISLATF (SEQ ID NO: 125) Part B 9-mers: aa388-419 WREFSFIQIFCSFADTQTELELEFVFLLTLLL (SEQ ID NO: 126) 10-mers: aa387-419 NWREFSFIQIFCSFADTQTELELEFVFLLTLLL (SEQ ID NO: 127) 15-mers: aa382-419 VSNALNWREFSFIQIFCSFADTQTELELEFVFLLTLLL (SEQ IDNO: 128) v.6, (different from our original in 445-490) 9-mers; aa447-490 (SEQ ID NO: 129) VLPSIVILGKIILFLPCISRKLKRIKKGWEKSQFLEEGIGGTIPHVSPERVTVM 10-mers: aa446-490 (SEQ ID NO: 130) LVLPSIVILGKI ILFLPCISRKLKRIKKGWEKSQFLEEGIGGTIPHVSPERVTVM 15-mers: aa441-490 (SEQ ID NO: 131) NFVLALVLPSIVILGKIILFLPCISRKLKRIKKGWEKSQFLEEGIGGTIPHVSPERVTVM v.7, (deleting our original 340-394, 392-576 is different) Part A 9-mers: aa334-350 FLNMAYQQSTLGYVALL (SEQ ID NO: 132) 10-mers: aa333-351 LFLNMAYQQSTLGYVALLI (SEQ ID NO: 133) 15-mers: aa328-355 RSERYLFLNMAYQQSTLGYVALLISTFHV (SEQ ID NO: 134) Part B 9-mers: aa384-576 (SEQ ID NO: 135) PSIVILDLSVEVLASPAAAWKCLGANILRGGLSEIVLPIEWQQDRKIPPLSTPPPPA MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDSIDPPESPDRALKAANSWRNPV 140 WO 03/087306 PCT/USO3/10462 LPHTNGVGPLWEFLLRLLKSQAASGTLSLAFTSWSLGEFLGSGTWMKLETIILSKLTQEQKSKHCMF SLISGS 10-.mers: aa383-576 (SEQ ID NO: 136) LPSIVILDLSVEVLASPAAAWKCLGANILRGGLSEIVLPIEWQQDRKIPPLSTPPPPA MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDSIDPPESPDRALKAANSWRNPV LPHTNGVGPLWEFLLRLLKSQAASGTLSLAFTSWSLG EFLGSGTWMK LETIILSKLT QEQKSKHCMF SLISGS 15-mers: aa378-576 (SEQ ID NO: 137) VLALVLPSIVILDLSVEVLASPAAAWKCLGANILRGGLSEIVLPIEWQQDRKIPPLSTPPPPA MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDSIDPPESPDRALKAANSWRNPV LPHTNGVGPLWEFLLRLLKSQAASGTLSLAFTSWSLG EFLGSGTWMK LETIILSKLT QEQKSKHCMF SLISGS v.8, SNP variant of v.6, one aa different at 475 9-mers: aa466-482 KSQFLEEGMGGTIPHVS (SEQIDNO: 138) 10-mers: aa465-483 EKSQFLEEGMGGTIPHVSP (SEQ IDNO: 139) 15-mers: aa460-489 IKKGWEKSQFLEEGMGGTIPHVSPERVTV (SEQ IDNO: 140) V13 9-mers: aa9-25 SPKSLSETFLPNGINGI (SEQIDNO: 141) 10-mers: aa8-26 GSPKSLSETFLPNGINGIK (SEQIDNO: 142) 15-mers: aa3-31 SISMMGSPKSLSETFLPNGINGIKDARKV (SEQIDNO: 143) v.14 9-mers: aa203-219 NLPLRLFTFWRGPVVVA (SEQ ID NO: 144) 10-mers: aa202-220 ENLPLRLFTFWRGPVVVAI (SEQIDNO: 145) 15-mers: aal97-225 SAREIENLPLRLFTFWRGPVVVAISLATF (SEQ IDNO: 146) V. 21 9-mers 557-572 SKLTQEQKTKHCMFSLI (SEQ ID NO: 147) 10-mers 556-573 LSKLTQEQKTKHCMFSLIS (SEQID NO: 148) 15-mers 551-576 LETIILSKLTQEQKTKHCMFSLISGS (SEQIDNO: 149) V. 25 9-mers aa 447-463 ILFLPCISQKLKRIKKG (SEQIDNO: 150) 10-mers aa 446-464 IILFLPCISQKLKRIKKGW (SEQ IDNO: 151) 141 WO 03/087306 PCT/USO3/10462 15-mers aa440-468 VILGKIILFLPCISQKLKRIKKGWEKSQF (SEQ ID NO: 152) 142 WO 03/087306 PCT/USO3/10462 Tables VIII - XXI: TableVIII-VI-HLA-A1-9mers- TableVIlI-Vi-HLA.Al.9mers. TableVIIlI-VI-HLA.Al-9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position for amino acids, and the end position for each peptide is the start position plus each peptide is the start position plus each peptide is the start position plus eight. eit. . eight. [Start Subsequence Score start[ Subsequence Isequen Score l 447 IL DLLQLCR ] 25.000 420 EEEYYRFYT 0.225 432 FVLALVLPS 10.050 129 1[ NAEYLASLF 9.000 38B WREFSFIQS 0.225 [12 SLSETCLPN I0.050 294 WLETWLQCR 9.000 1981 AREIENLPL I0.225 106 HLLVGKILI I 0.0501 113 LIDVSNNMR 5.000 7 1 [ VIGSRNPKF [ 0.200 311 FFAMVHVAY 0.050 200] EIENLPLRL 4.500 J 56 WIGSRNPK 0.2007 269 LVYLAGLLA -0.050 244 QSDFYKIPI 3.750 1 217 WAISLATF 0.200 216I VWvAISLAT 0.050 405 ISTFHVLIY ~3750 I3 SISMMGSPK 2 0.200 124 QYPESNAEY 0.050 13I LSETCLPNG 2.700 [417 RAFEEEYYR 0.200 1166 YICSNNIQA 0.050 221 SLATFFFLY 2.500 4361 LVLPSIVIL I 0.200 258 J TLPIVAITL 10.050 r263 AITLLSLW 12.500] 377 TSIPSVSNA 0.5 18_1 LPNGINGIK 0.050 2761 LAAAYQLYY I2.500 158 PKDASROVY 0.125 j435 ALVLPSIVI 0.050 1 419 FEEEYYRFY 2.250 101 LWDLRHLLV 0.125 i 25 IKDARKVTV 0.050 1551 QLGPKDASR 112.000 1171 SNNMRINQY 0 ~273 WDVrHHED 00 r66 ] ASEFFPHW 1.350 J SFIQSTLGY 0125 222 LATFFFLYS 0. 2772 ]I LAGLLAY 1.000 202 1 ENLPLRLFT[ 0.12 5 I QLNFIPIDL 0.050 351! VIGSGDFAK 1.000 3 3301 RYLFLNMAY I 0.12 5 I367 SLGLLSLLA 0.050 I178I VIELARQLN 0.900 138 SGDFAKSLT 0.125 46! TIRLIRCGY 0.050 35 RIEMYISFG 98 .9o YTSLWDLRH 0.125 31 GLLSFFFAM 0.050 _4181 AFEEEYYRF I 0900 40 61 STFHVLIYG I0.125 I261 IVAITLLSL 0.050 319 YSLCLPMRR 10.750 181 VAISLATFF I 0.100 i 12031 NLPLRLFTL i 0.050 I431 KSLTIRLIR 0.750 I167I ICSNNIQAR 0.100 I327 I RSERYLFLN 1 0.675 400 YVALLISTF iI 0.100 TableVIIIl-V2-HLA*AI -9mers 14271 YTPPNFVLA 0.0 [235I VIHPYARNQ I0.100 98P4B6 S304 II QLGLLSFFF 10.500 13811 SVSNALNWR 0.100 Each peptide is a portion of SEQ ID F257 ~~NO: 5; ech startpoions 257 ] KTLPIVAIT 0.[0500 22 INGIKDARK . NO: 5; each start position is specified, the length of peptide is 9 135jI SLFPDSLIV I 0.500 [21[ GINGIKDAR 0.100 amino acids, and the end position 122311 ATFFFLYSF t0.500 281 QLYYGTKYR I0.100 for each peptide is the start position 27 LLAAAYQLY iI 322 CLPMRRSER II 0.100 plus eight. i385 1 ALNWREFSF 0.500 4 i11 I LIYGWKRAF I .10 Sr Subsuence I S2197 AISLATFFF 9 500 ii DLGSLSSAR II01 .00 23 I LSLPSSWDY 7.500 16 TCLPNGING 0.500 409[ HVLYGWKR 0.100 1 33 CPPPCPADF 1 .5 90 FVAIHREHY 0.500 3441 NIENSWNEE ] . 361 PCPADFFLY 10.250 l -87l NIIFVAIHR 0.5 PIEIVNKTL LSLSLSSGF 0.150I F2491 KIPIEIVNK I= o308 [ LSFFFAMVH 07 37 CPADFFLYF I 0.125 1 37 FPDSLIVKG I 0.250 195 LSSAREIEN 0.075 171 FTPFSCLSL]0 h 1891 PIDLGSLSS 0.250 NNMRINQ 0.075 24I SLPSSWDYR 01 I241 RNQQSDFYK 0 28L 0 I QLYYGTKY I07 12"1 SLSSGFTPF ]0.100 351 EEEVWRIEM I1 i 22.II ISLATFFFL ] 7 14 SSGFTPFSC 0.075 34911 WNEEEVWRI II 0.225 175j RQQVIELAR 0.075 I GLQALSLSL I YPESNAEYL I0.22] 1 27 ESNAEYLAS 5 7 I QALSLSLSS 05 I 143 WO 03/087306 PCT/USO3/10462 TableVIII-V2-HLA-Ai-9mers- "4 LRLFTFWRG 0.001 TableVll-V6-HLA-Ai-9mers 98P4B6 2 LPLRLFTFW 0.000 I 98P4B6 Each peptide is a portion of SEQ ID 91 FWRGPVVVA 0.000 Each peptide is a portion of SEQ ID NO: 5; each start position is _ITF GP _1oooI NO: 13; each start position is specified, the length of peptide is 9 TFWRGVVV 0.000 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position for each peptide is the start position TableVIll-V5B-HLA-AI-9mers- for each peptide is the start position plus eight. 98P4B6 L _ plus eight. iStart Subsequence Score I Each peptide is a portion of SEQ ID Start II Subsequence Score 13 LSSGFTPFS 0.030 I NO: 5; each start position is 2 I LPSIVILGK 0.250 ~2 [ GSPGLQLS [~ 0030 specified, the length of peptide is 9 42 TPHVSPER 020 S 0.030 amino acids, and the end position 0.200 Io FfLSLPSS am0.030 I or each peptide is the start position 45 SPERVTV 0200 i1 SGSPGLQAL 0.025 plus eight. 13_I LFLPCISRK I .1 0 I 732 I RCPPPCPAD 0.020 Start jSubsequence Score 16 PCSRKLKR ET0.050 35 IPPCPADFFLI 0.013 21 ELEFVFLLT 4.500 1 1 VLPSIVILG I 0.050 3F SPGLQALSLf 0.013 171 QTELELEFV 2.250 151 LPCISRKLK 0It0 0 121I SCLSLPSSW I0.0101 19 iI ELELEFVFL I1.800 I si IVILGKIIL I!0.0501 8 1 ALSLSLSSG 0.010 1 WREFSFIQI I 0.225 I 35 LEEGIGGTI I .045 10I SLSLSSGFT 0.010 6 TQTELELEF .075 I 41 GTIPHVSPE I 0.025 11J LSLSSGFT'rP 0.007 4_ FSFIQIFCS 0 .075 38 GIGGTIPHV 0.020 [251 LPSSWDYRC 0.005] 12411 FVFLLTLLL 0.050 Ii0 KlLFLPCI 1020 i I3 G AFSCLS 005 1 13 FA 0.050 1 31 I KSQFLEEGI 0.015 F28 I SWDYRCPPP 0.005 18 TELELEFVF 0.025 46 I VSPERVTVM II 0.015 I 31 .J YRCPPPCPA 0.005 8 QIFCSFADT I 6 0.020 37 EGIGGTIPH M0.013 15 SGFTPFSCL I0.0 l 1 FCSFADTQT I0010 4F SIVILGKII I 0.010I 347 PPPCPADFF 0003 6 FIQIFCSFA 10.0101 14 FLPCISRKL 0.010 6I LQALSLSLS 0.002 1211 REFSFIQIF 0.005 L 1 IILFLPCIS 10.010I [2211 CLSLPSSWD 0.001 51 SFIQIFCSF 10.005 19 SRKLKRIKK 11 0.005 F19 II PFSCLSLPS 0.000 1 DTQTELELE 0.00 "7 ILGKIILFL 00 [18 TPFSCLSLP 110.000 201 LELEFVFLL 0.003 26 KKGWEKSQF I 0.005 1 PGLQALSLS 0.000 22 1 LEFVFLLTL 0.003 F18 ISRKLKRIK 0.003 S27I SSWDYRCPP II .0 14 I ADTQTELEL 00 QFLEEGIGG ]0.003 t26 PSSWDYRCP 0.000 3 EFSFIQIFC I0.003 43 IPHVSPERV J 0.003 F 29 WDYRCPPPC 0 000 11 CSFADTQTE 0.002 9 GKIILFLPC 0.003 301 DYRCPPPCP 0.0 ~[ IF IQIFCSFAD I 0.001 39 IGGTIPHVS 0.003 _ 23 EFVFLLTLL1 0.001 28 TGWEKSQFLE 0. F12 SFADTQTEL 0.001 3 I PSIVILGKI I0.002 I IFCSFADTQ 0.001 [32 I SQFLEEGIG TableVlll-V5A-HLA-Ai-9mers- 23 II KRIKKGWEK I0.001 98P4B6 [171 CISRKLKRI 0.001 Each peptide is a portion of SEQ ID TableVllFV6-HLA-A-9mers- 401 GGTIPHVSP 0.001 NO: 11; each start position is 98P46 30 EKSQFLEEG 0I.001 specified, the length of peptide is 9 Each peptide is a portion of SEQ ID 27 KGWEKSQFL 0.000 amino acids, and the end position for NO: 13; each start position is M ach peptide is the start position plus specified, the length of peptide is 9 8 I LGKIILFLP IF 0. eight. amino acids, and the end position 24 RIKKGWEKS 0.000 IStrt I Sb I Score for each peptide is the start position 21 IF KLKRIKKGW .00 a e cplus eight I 3 II EEGIGGTI IF =1 NLPLRLFTF] 0.500 F36 EGGGI 0.000 1 NLPLRLF.F .[ 0.500 ] Start Subsequence Score ISl . 7 FTFWRGPVVW I 0.050 FLEEGI44 PHVSPERVT 0 .0 3 PF20I RKLKRIKKG 0.000ooo -51 PULRTFWR IF 0.005 1 I 2 ILFLPCISR I.00 1 1 KKGWEKSQ' ___0 5 RLFTFWRGP I2Go.ooi I 5 K S 0 VILGKIILF.000 I6 II TFWRGPV 0.001 WEKSQFLEE 0.000 144 WO 03/087306 PCT/US03/10462 TableVIII-V6-HLA-Ai.Smers. Each pepltide is a portion of SEQ ID TableVIll.-V7C.HLA-Al -9mers 98P4B6 NO: 15; each start position is 98P4B6 Each peptde is a portion of SEQ ID specified, the length of peptide is 9 Each peptide is a portion of SEQ ID NO: 13; each start position is amino acids, and the end position NO: 15; each start position is specified, the length of peptide is 9 for each peptide is the start position specified, the length of peptide is 9 amino acids, and the end position plus eight. amino acids, and the end position for each peptide is the start position Subsequence Score ] for each peptide is the start position plus eight. [If KLETIILSK 119.0 plus eight. Start Subsequence Score [59 I WTEEAGATA II 4.500 Start Subsequence II Score 22 1 LKRIKKGWE 000 [13 LASPAAAWK .000_ 79 SSSSQIPW 10.030 69 I! AQESGIRNK 2.700 125 NGVGPLWEF r 0.025 [ 38 If PIEWQQDRK II1.00 ] 65 [ ATAEAQESG I 0.025 3 TableVilll.VA-HILAA1-gmers- 7 1r180 F6 7 TEQS -,o2 TableVI98P4B6 66 i TAEAQESGI I0.90 37 I LPIEWQQDR 0.025 [9"I SVEVLASPA II0.900 I 92 ]1EDDEAQDSI 0F.025' Each peptide is a portion of SEQ ID F, I SVELASPA II 0.900 19 EDDEAQS 0.025 NO: 15; each start position is I ASGTLSLAF 1 0069[ ETIILSKLT 0.025 specified, the length of peptide is 9 [99 I SIPPESPD I 756 1 LTQEQKSKH I0.025 amino acids, and the end position 51 I STPPPPAMW j ] 91 TEDDEAQDS I 0._025 for each peptide is the start position 51. ILDLSVEVL 0.5 102 PPESPDRAL 0.022 plus eight 0.500 PESPDRAL 0.02 [Start Subsequenc 21f71 I KCLGANILR 1I oo 3 PESPDRALK 0I.0 t1 LSETFLPNG l71 I VTEDDEAQD II 0.450 EVLASPAAA ]r0020 I4 1 SLSETFLPN I0.050' [ 50[II LSTPPPPAM I 0.300. 83i QIPVVGVVT 1020 7_ 1 ETFLPNGIN 1.025 32I LSEIVLPIE I0.27 4 IL VILDLSVEV 1020 S8 ITFLPNGING I 07.0275151i FTSWSLGEF I 12 VLASPAAAW 10020 8 FLPNGINGI 0! o.o0 156 II LGEFLGSGT [I 0.225[42 QQDRKIPP[ 0]015 9 LPGNG .010 r16 3 KSLSETFLP 0.007 1 175 If KLTQEQKSK II 0.200 71 ESGIRNKSS 10.015 W SPKSLSETF K00031 [ "-- 1961 AQDSIDPPE 10.015 1SPKSLSETF 0.003~WK70.1 I[67 SETFLPNGI i 0. 0 1 [ 177 TQEQKSKHC 0.135 F14 ASPAAAWKC .015 I2I PKSLSETFL 0.00 F1 128 GPLWEFLLR I!0.125 82l SQIPWGVV II. 1 GTLSLAFTS f1 139 I KSQAASGTL I0.015 TableVIII.V7B-HLA-Al-9mers-

I

52 TPPPPAMWT 0 .1 25 i i147 LSLAFTSWS I0.015 98P4B6 126 GVGPLWEFL I0 i 29i RGGLSEIVL 0.013 Each peptide is a portion of SEQ ID 35 IVLPIEWQQ I 0.100 Ii05 SPDRALKAA 0.013 NO: 15; each start position is 100 IDPPESPDR I .100 162 SGTWMKLET 0.013 specified, the length of peptide is 9 1 ESPDRALKA I .075 160 LGSGTWMKL 0.013 amino acids, and the end position 10_I 4 sssP EI 075 0.01731VGLEFL'i or each peptide is the start position SSSSSQIPV 0.075 1 7. VGPLWEFLL 0.013] [mn plusedght 1e5 I WSLGEFLGS I I 0.075 I 146 TLSLAFTSW " 0.010 [Sta Subsequence 1 Score i31I WEFLLRLLK I0.050 I 88 I GVVTEDDEA 0.010 ___ AYQQSTLGY 1.125 22 CLGANILRG II0.050 142 AASGTLSLA 0.010 19 STLGYVALL 01.050 [68 EAQESGIRN I0.050 64 " GATAEAQES 0.010 I8 3/ QSTLGYVAL II0.030 [184 HCMFSLISG 0.050 1 9 PVLPHTNGV 0.010 1l FLNMAYQQS 0f010I 7 DLSVEVLAS 0.050 46 KIPPLSTPP .010 I4 MAYQQSTLG I 0.01i0 177[ TIILSKLTQ 0~. 0 EAGATAEAQ I0.00 13 NMAYQQSTL 0.005 2L SIVILDLSV 05 L1lI ALKAANSWR I0.010 I 7 3 QQSTLGYVA ! 0.003 17 I AAAWKCLGA 0.050 1148 I SLAFTSWSL I 0.01 21 LNMAYQQST 00031 141 I QAASGTLSL I0. 050 I2 AANSWRNPV 0I. I6 II YQQSTLGYV 0.002 12 HTNGVGPLW 0.050 LAFTSWSLG 0010 31I GLSEIVLPI 000 34 EIVLPIEWQ 0010 [130 I LWEFLLRLL I 0.045 116 I WRNPVLPHT 0.010 .. [173 ILSKLTQEQK 10.030 24 GANILRGGL 0.010i TableVII-V7C-HLA-A-9mers- 8 I SSSQPVVG 0030 89 I VVTEDDEAQ 0.010 98P4B6 81 S SQIPWGV 0 l 15I SLGEFLGSG 0.010 145 WO 03/087306 PCT/USO3/10462 TableVIII.V7C-HLA.Ai-9mers- TablelX-V1-HLA.Ai.10Omers. TablelX-V1-HLA-AI.-10mers. 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is specified, the length of peptide is amino acids, and the end position 10 amino acids, and the end 10 amino acids, and the end for each peptide is the start position position for each peptide is the start position for each peptide is the start plus eight. position plus nine. position plus nine. i-S-tart Subsequence I[Score! [Start[ Subsequence Sce Start Subsequence [Score 1120 VLPHTNGVG [ 0.010 257I KTLPIVAITL 1.250 86 TNIIFVAIHR 10.125 181 KSKHCMFSL 0.0 271 YLAGLLAAAY I1.000 J32 TVGVIGSGDF .100 J113 ANSWRNPVL 0.0J05 34 GVIGSGDFAK I1.000 ! 2351 VlHPYARNQQ 0,.100 67 AEAQESGIR 0.0~ 1321f LCLPMRRSER fi 1.000 410 f VLIYGWKRAF o.100 185 CMFSLISGS ]0.005 98f AREIENLPLR 0.900 11 ILIDVSNNMR ] 0.100 144 SGTLSLAFT 0 [.005 116 VSNNMRINQY f60.750 [I YICSNNIQAR 0.100 I93 DDEAQDSID ]0.005 [327 RSERYLFLNM I0f.675 r 16i TCLPNGINGI 1.100 1 [ TEEAGATA'E ]10.005] [l.1138 SGDFAKSLTI f 0625i [21f WAISLATFF Il 0 8 LSVEVLASP ]0.003 [384 NALNWREFSF 0-500 155[ QLGPKDASRQ J0o.10 1831 KHCMFSLIS 0.003 2L1If VAISLATFFF 0.500 13441 NIENSWNEEE 0.090 25 ANILRGGLS 0.003 2741 GLLAAAYQLY 0.500 [139 DSLIVKGFNV 0.075I 165[ WMKLETIIL 0.003 81[ DALTKTNIF 0.500 405I ISTFHVLIYG 0.075 I0 10 DPPESPDRA 0.003 322 I CLPMRRSERY 0.500 f366 MSLGLLSLLA 110.075 5I SPAAAWKCL 0.003 73I WDVTHHEDA 10.500 [ 11 KSLSETCLPN 1 0.075 1 232 I VRDVIHPYAR 10.500 1 134 f ASLFPDSLIV I 0.075 TablelX-V1-HLA-Al-10mers- 442 VILDLLQLCR 0.500] [43 KSLTIRLIRC 10.075 98P4B6 125 f YPESNAEYLA f0 .450 1 33 KQLGLLSFFF 1 0.075 Each peptide is a portion of SEQ ID [294 NAEYLASLFP 50 36 1 ISFGIMSLGL 1 0.075 NO: 3; each start position is GIGIKDARK 0.400 1304 I specified, the length of peptide is .. 10 amino acids, and the end 2. ESISMMGSPK If 0.300 1 07 1 LLVGKILIDV 0.050 position for each peptide is the start 66 ASEFFPHWD .270 i 1160 SRNPKFASEF I0 50 position plus nine. 1__ 49I FEEEYYRFYT [0.225 2[ LVYLAGL 0 [tl i ue, p sco, f 350I NEEEVWRIEM 0.225 434f LALVLPSIVI 1782 VIELARQLNF 5 .f22 LATFFFLYSF 0.200 [397 TLGWYVALLIS 0.050I 1443 I ILDLLQLCRY 56 o f WIGSRNPKF 0.200 364 GIMSLGLLSL 00500 294 f WLETWLQCRK I 18.000 F281 I QLYYGTKYRR I0.200 401 VALLISTFHV 0.050 1351 SLFPDSLIVK 10.000 F5f HWIGSRNPK 0.2 ] [17 NWSAWALQL 0.0501 F20f0 EIENLPLRLF ff 278 AAYQLYYGTK 0.200 89I PIDLGSLSSA 0.0 1 1 R5EMYSFGI 0 "417f RAFEEEYYRF f 264 ITLLSLVYLA 0.050 F220I ISLATFFFLY I 3.750 1216t WVAISLATF 0.200 307 LLSFFFAMVH 0.050 39 FSFQSTLGY 3f 311 f0 YKIPIEIVNK f3 1 FFFAMVHVAY 11 050 I767I VTHHEDALTK. 317 VAYSLCLPMR fI 0200 7 ,209 FTLWRGPVW I0050 404 . LISTFHVLIY 7 2.500 17 11 CLPNGINGIK 0210 1894 SLSSAREIEN II 0.050 F2 VAITLLSLVY F45457 r _II QSDFYKIPIE f 0.10 [240U ARNQQSDFYK 0.050 27 1 LLAAAYQLYY 1 2.500 TIPSVSNAL f 298 WLQCRKQLGL I0.05 113 LIDVSNNMRI f2 500 382 VSNALNWREF I 0.150 40I SIVILDLLQL 0.050 I01 EEEVWRIEMY I2.2 f 202 I ENLPLRLFTL .15 221 SLATFFFLYS 0.050T] T112 AFEEEYYRFY If 12.25f Fi01 1 LWDLRHLLVG 0.125 436 LVLPSIVILD I0.050 ] 123] NQYPESNAEY If [.5f 329 J ERYLFLNMAY If0. 125 [406 STFHVLYGW 0.0-90 113 LSETCLPNGI 1350 F, 1 ETCLPNGING 1 I137 FPDSLIVKGF_ 5_ 39 STLGYVALLI f1.25 TabelX.V2-HLA-Al-l Omers-. YTPPNFVLAL 1.250 4 LTIRLIRCGY 0,125 98P4B6 146 WO 03/087306 PCT/USO3/10462 Each peptide is a portion of SEQ ID Start I Subsequence Score specified, the length of peptide is 10 NO: 5; each start position is 1 ENLPLRLFTF I amino acids, and the end position for specified, the length of peptide is F. T R 1100 each peptide is the start position plus 10 amino acids, and the end 8 FTF w RGPVVV 0.050 nine. position for each peptide is the start I 3 i LPLRLFTFWR I .013 [Siart[ Subsequence lScore position plus nine. 2 2 F NLPLRLFTFW ] 0.010 I 42 ][ GTIPHVSPER ] 5.000 IStartl Subsequence iScore 6 1 RLFTFWRGPV 0.010 F 2[ 1 VLPSIVILGK IjY0 32 I RCPPPCPADF 7 I LFTFWRGPW I 35 FLEEGGGTI 0.900 23I LSLPSSWDYR 1[ 1.500 4[ PLRLFTFWRG II 0.000 [ I L G 0500 ... _E(R L1 ILVLPSIVILG 0.500 35'1 PPCPADFFLY 1I0 6250 1 FWRGPVVVAI 0.000 12 J IILFLPCISR I0.500 L221 CLSLPSSWDY 0 500 5[ LRLFTFWRGP 0 .000 [ IVILGKIILF 1o F =6 IVILG ilLF10.500 133 I CPPPCPADFF _ ] I[.2 9 TFWRGPVVVA 0.000] 3 ILFLPCISRK

-

F 13 LILFLPCISRK 0]20 11 LSLSSGFTPF 0.1507 FLPCISRKLK 8 II ALSLSLSSGF 10. 00 [0. 2LPCISRKLK S131 LSSGFTPFSC 10.075 PRKR Ii. S211 GSPGLQALSL .07 TablelX-VSB-HLA-AI-10mers. L46 HVSPERVTVM 0.10 0 28 SWDYRCPPPC

.

98P4B6 7 VILGKIILFL I0.050 12] 1 Each peptide is a portion of SEQ D10 5 SIVILGKIIL 0.050 SSGSPGLQALS 0.050 NO: 11; each start position is 18 CISRKLKRIK 0. 361 PCPADFFLYF 0.050 1 specified, the length of peptide is 16 GFTPFSCLSL1 0.025 10 amino acids, and the endLJ RLRK _ _12 SLSSGFTPFS _ .2 position for each peptide is the start F32]1 KSQFLEEGIG I .0 position plus nine. 39 ]1 GIGGTIPHVS I 0.010 1E24 1SLPSSWDYRC 1 2o FIStrII Subsequence IScore 43 TIPHVSPERV I0.010I 20 FSCLSLPSSW I .015 L0 I FSCLSLPSSW '1 ] 00i I18 QTELELEFVF 112,500 11 .. [ KIILFLPCIS 0.010 F141 SSGFTPFSCL7 0.015 -- -1KIFPS 1.1 SITI SSGFTPFSCL ~cIIi 0.15 I~ 120 ELELEFVFLL I 4.500 [33 SQFLEEGIGG l0.007 9 LSLSLSSGFT 0.015 F331SFEGG 1 .0 91_i~If LSLSLSSGFT 1J 0j22 ELEFVFLLTL I4500 ["81 EGIGGTIPHV I00s 18 TPFSCLSLPS P.Ol3 F JEEV38 0.0 1 TPFSCLSLPS 14_11 FADTQTELEL I 2'I0 14 LFLPCISRKL 10.05 7 QALSLSLSSG F16 5 LQALSLSLSSG]f 0] I 1I6 DTQTELELEF 1.250 F36 LEEGIGGTIP I 0.005 1511 GLOASLSL 11_T5' 1211 WREFSFIQIF 1I0.450 11 37 ]f EEGIGGTIPH 1i'0.003 6 LQALSLSLSS F2 O40 Z LQALSLSLSS I ~If5 FSFIQIFCSF 0I1I 0 o3 I LPSIVILGKI ''"0.003 1j0j SLSLSSGFTP 0.0053 jLSVGKj0.3 I] f FT I 12 II CSFADTQTEL I 01 44 IPHVSPERVT 1.003 115 11SGFTPFSCLS] 0.0031 .15 F47 IHSEv S SC 9 11 QIFCSFADTQ I 0.0102 GWEKSQFLEE 3 SPGLQALSLS 0.0 --- 000 FE 11SP S 0I 7 I FIQIFCSFAD 0 .005 4 11 PSIVILGKII I 0.002 1FS 8' IQIFCSFADT 10'.f003 I 9 I1 LGKIIlLFLPC I0.001 F341 PPPCPADFFL .0F 7 F-9 F41f PPPCPADFFL LL 21 LELEFVFLLT I .001 F2I 0023I LKRIKKGWEK .0.001 LQALSLSL 1- 41 EFSFIQIFCS I0.003 17 PCISRKLKRI 10.001 31 YRCPPPCPAD 0.001 - I21 Yr PPPCPA D 0.001 I2471 EFVFLLTLLL II 0.03 1 GKIILFLPCI 0.001I 271 SCSSWDYR 100 I 37 REFSFIQIFC 10.0031 261 IKKGWEKSQF I0.001 27 SSWDYRCP 000 2 SSWDYRCP7 TQTELELEFV 002 341 QFLEEGIGGT 0.001 25 LPSSWDYRCP 0. I1 FCSFADTQTE 0f001 F31I EKSQFLEEGI Io.001i 2I PSSLPP F 0 ] 19 1 TELELEFVFL .I '001 2 7 I KKGWEKSQFL 0.

001 i -9--- - -- 0 6 SI SFIQIFCSFA I 0.001i 8 If ILGKIILFLP II0.00 DYRCPPPCPA

.....

0...... WDYCPPCP 10 IFSFATQ 0.001 F401 IGGTIPHVSP 0.001 29J WDYRCPPPCP 155-_____ _____ ~~[2__I _-23 F LEFVFLLTLL 10.001 F 41[ 1 GGTIPHVSPE I 0.000 . 1 .1 NWREFSFIQI 0.000 128 II KGWEKSQFLE 0.000] TablelX-V5A-HLA-Al-10mers- DTfEEIN 5A-HLA-Al-mers- I ADTQTELELE 0.000 251 RIKKGWEKSQ 0.000 98P486 MT3I FDQE'FI '0 Each peptide is a portion of SEQ ID 13 SFADTQTELE 0 451 PHVSPERVTV 0.0 NO: 11; each start position is 21 f RKLKRIKKGW 0.000 specified, the length of peptide isl0 T a -VS-LA-A ir- 2 SRKLKRKKG I 0.00 amino acids, and the end position for 98P4B6 30 WEKSQFLEEG 11 .000 each peptide is the start position plus Each peptide is a portion of SEQ ID I i 1 KRIKKGWEKS I 0.000 mnne. __ NO: 13; each start position is 147 WO 03/087306 PCT/USO3/10462 TablelX-V6-HLA-AI-10mers- Each peptide is a portion of SEQ ID TablelX-V7C-HLA-Al-10mers 98P4B6 NO: 15; each start position is 98P4B6 Each peptide is a portion of SEQ ID specified, the length of peptide is 10 Each peptide is a portion of SEQ ID NO: 13; each start position is amino acids, and the end position for NO: 15; each start position is specified, the length of peptide is 10 each peptide is the start position plus specified, the length of peptide is 10 amino acids, and the end position for nine. amino acids, and the end position for each peptide is the start position plus Start I Subsequence Score each peptide is the start position plus nine. [100 1 SIDPPESPDR 1100.000 nine. Start Subsequence IScore 67 TAEAQESGIR 9.000 1i start Subsequence I Score 22 1KLKRIKKGWE 0.000 33 LSEIVLPIEW 16.750 106 SPDRALKAAN 0.025 S5 LWEFLLRLLK I 94 DDEAQDSIDP 1 0.022 TablelX-V7A.HLA-Al-10mers. 1 917I VTEDDEAQDS 25 j12 EVLASPAAAW 0]i.020 98P4B6 Il SVEVLASPAA 1 80] 4 IVILDLSVEV 0.020 Each peptide is a portion of SEQ ID 2 STPPPPAMWT 1.250 I 173 ILSKLTQEQK I 0.020 NO: 15; each start position is I 47 I! KIPPLSTPPP i1 specified, the length of peptide is [611 ILDLSVEVLA 1.00 5~ KIPPLSTPPP 0.020 10 amino acids, and the end [168 KLETIILSKL 7 9 113 I AANSWRNPVL 0.020 position for each peptide is the start 103 PPESPDRALK I 72 ESGIRNKSSS 0.015 position plus nine. i127 GVGPLWEFLL I0.500 4~T3 QQDRKIPPLS 0.015 t Subsequence 35 re 1431 AASGTLSLAF .1500 Ii15II ASPAAAWKCL 'i.015] 6 LSETFLPNGI 1 1 VLASPAAAWK I4007 140 KSQAASGTLS ]0015 10o1 FLPNGINGIK [ 200 F5i1 LSTPPPPAMW 0.300 1 LSVEVLASPA 0.1 f5 F 1 ETFLPNGING 1 60 WTEEAGATAE 0J 82 SSQlPWGW 0015 4 KSLSETFLPN 0 157 LGEFLGSGTW 0.225 j155 WSLGEFLGSG . ! 0,015 5 1 SLSETFLPNG I 0020 EAQESGIRNK [105 ESPDRALKAA 0.015 F1 GSPKSLSETF I0 015 97 AQDSIDPPES 0.150 11481 LSLAFTSWSL 0.015 STFLPNGINGI 70005 AQE SGIRNKS 0.135 124 HTNGVGPLWE 0.013 0.00~- F 0 AEGINSF--37 M 2: P SLSETFLPNGIN 01FII78 TQEQKSKHCM 35S [129 GPLWEFLLRL 0.013 I___L I 1178 IITQEQKSKHCM II0.

135 GPWFR' 12 SPKSLSETFL I0. I170! ETIILSKLTQ j 0.125 J 31 GGLSEIVLPI 0.013 3 PKSLSETFLP 0 128I VGPLWEFLLR I0.125 F145 SGTLSLAFTS 0.013 TablelX-V7-HLA-AI-7 VWmersQD1 1R . 185 HCMFSLISGS 0.010 ILAAl-0mes. 37SLAFWQOR T X 8P4B106 14 LASPAAAWKC 0.00 149 SLAFTSWSLG 0.010 Each peptide is a portion of SEQ ID 61 TEEAGATAEA 10.090 1 65 GATAEAQESG 0.010 specified, the length of peptide is 10 I 162 GSGTWMKLET 0.075 1 42 IQAASGTLSLA 0.010 amino acids, and the end position for 7 KSSSSSQPV i~7~ GANILRGGLS 0.010 each peptide is the start position plus 160 FLGSGTWMKL If [0050 1 0a L S 10.010 nine. [ Sc22 CLGANILRG 050 23 CLGANILRGG 0.010 Start Subsequence o KCLGANILRG [ I MAYQQSTLGY 2.0 167[ MKLETIILSK 1 109[ RALKAANSWR10.010 03 STLGYVALLI 1125 38 LPIEWQQDRK 5 176 KLTQEQKSKH 0

.

010 [91[ QSTLGYVALL I[.03 [jh801 SSSSQIPWG 0.030 3 5 EIVLPIEWQQ 0.010 [ F LMA2QT 3[F[791 SSssSQlPW j0.030 175 SKLTQEQKSK 0.010 I2 }1FLNMAYQQST""] 0.010 ' I sSQP I KLEKK F-47~8 .05[SQipWGVVT 0.03 1 AAAWKCLGAN 0.010 [4 ] NMAYQQSTLG ![ 0.005 1 WGVVT J0,0 0l AAAWKCLGAN [ 7 YQQSTLGYVA I 0.003 I ASGTLSLAFT 36 IV IEWQQD i [8 QQSTLGYVAL .0037 81 1 SSSQIPWGV 5 030 5 VILDLSVEVL 0.010 18 IQQSTLGYVAL I!0.003 [SSIW VJ5- [ i =,! I ILNMAYQQSTL 0.003 I 146 GTLSLAFTSW I0275 172 IILSKLTQEQ 0.010 S61 AYIQQSTLGYV 0.1 166 ATAEAQESGI 0.025 156 SLGEFLGSGT 0.010oi 1 LFLNMAYQQS =12 I FTSWSLGEFL 0.025 10 PVLPHTNGVG 0.010 1LIFLNMAYQQS 0I .00 I1 1' IFSs.E_ o05 [] 125_j TNGVGPLWEF 0.025 F1I47T TLSLAFTSWS 0i1o TablelX.VTC.HLA.A.l10mers- I 92i TEDDEAQDSI ] 5 [89[ GVVTEDDEAQ 0.010 98P4B6 17711 LTQEQKSKHC 1 5311 TSWSLGEFLG _ 08 L21 Ii WKCLGANILR 0.025 [] PSIVILDLSV Jf008 148 WO 03/087306 PCT/USO3/10462 TablelX-V7C-HLA-AI-10mers- TableX-Vi-HLA-A0201-9mers. TableX-VI.HLA-AG201-9mers. 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position for Iamino acids, and the end position for each peptide is the start position plus each peptide is the start posiion plus each peptide is the start position plus nine. eight. eight. rStarti Subsequence Score Start Subsequence Score [Start Subsequence Score 11411 SQAAWSGTLSL 0.007 27111 YLAGLLAA.A 152.561 166 YICSNNIQA 113.142 150 LAFTSWSLGE 0.005 2651 TLLSLVYLA 142278 F353 EVWRIEMYIi 3.125 171 PAAAWKCLGA] 0005 4331 VLALVLPSI 40.7921 221 SLATFFFLY 3.121 I1011 IDPPESPDRA I 0.005 442 VILDLQLC 40.518 378 SIPSVSNAL 2937 1t51 ] AFTSWSLGEF 0.00.5 11!2 ILIDVSNNM i34.627 164 QVYICSNNI i]292 1117I! WRNPVLPHTN J.5 360 YISFGIMSL [31.077 268L]] SLVYLAGLL 2.777 42 WQQDRKIPPL 0.003 14031 LLISTFHVL 1 28.2901 396 STLGYVALL 12.525 1 041 PESPDRALKA ]. 3691 GLLSLLAVT 1 6 001 LALVLPSIV I491 24i [LGANILRGGL 1 0.003- 17 CLPNGINGI [23.995 304 QLGLLSFFF 12.377 119 NPVLPHTNGV 0.003 108 LVGKILIDV 23.795 6I LVYLAGLLA ]2.365 111811 RNPVLPHTNG 0 264i ITLLSLWVYL 123.608 371 GSGDFAKSL 173 102 DPPESPDRAL 0.0 2587 TLPIVAITL [ 2 1 .362 3661 MSLGLLSLL 2.017 [53 1 TPPPPAMWTE 1 0.003) 1 QLNFIPIDL 1621.362 17 LSLVYLAGL 2.017 I] LPSIVILDLS [T5 [313 1 AMVHVAYSL 15.428 [242 NQQSDFYKI 2.010 F[4101 VLlYGWKRA I4.358 177 QVIELARQL 1.5 TableX-Vi-HLA.A0201-9mers- [1411 LIVKGFNVV 12 [ 2241 TFFFLYSFV 1.474 98P4B6 305 LGLLSFFFA 12.364 349 WNEEEVWRI 1418 Each peptide is a portion of SEQ ID 44 1 SLTIRLIRC 11.426 1 28 II SNAEYLASL I1.315 NO: 3; each start position is specified, the length of peptide is 9 436 1 LVLPSIVIL 11.0871 -- I HLLVGIILI 13127 amino acids, and the end position for 3971 TLGYVALLI i03 25L KTLPIVAIT h.24 each peptide is the start position plus 386 LNWREFSFI 1110.042 303 II KQLGLLSFF 1238 eight. _ _8_1 ELARQLNFI 9.898 T L TP2PNFVLAL 129 [Start! Subsequence Score I F2 1 IVNKTLPIV 9.75 3 1 GVIGSGDFA 1.172 227 FLYSFVRDV 1789.61 -4047 LISTFHVLI 9.267 216 1 WVAISLAT 1.108 2357 1EMYISFGI 1 MVHVAYSLC 10 49 .8_ I1 TE M F -314 __ 402 A LLISTFHV 115 F4417 IVILDLLQL 7.3097371 LSLLAVS 0.985 307 6 LLSFFFAMV I83.68t 1 21 IVAITLLSL 1 7.309 91 VAIHREHYT] 0.968 1 GLLSFFFAM 2769.748 F209]] FTLWRGPW 6.741] [85 KTNIIFVAI .4 00oo"1 SLWDLRHLL 72962 3681 LGLLSLLAV [133[ LASLFPDSL SFLNMAYQQV 47.909 67 SLGLLSLLA 41 6 425 RFYTPPNFV ] I0.850 140 SLIVKGFNV 40.4021 153 ALQLGPKDA ]4.968 250 IPIEIV75NKT .780 40 S N 27 4 [146 FNWSAWAL I4.811 49 lRCGYHW "0.760 F2031 NLPLRLFTL7 284.974 201 WRGPV 236.68 38911 REFSFIQST 1468 83 LTKTNIIFV I0.727 r2105 TLWRGPVVV 236.6851 [651 FASEFFPHV 131.539 435 II ALVLPSIVI 4.277 r 1321 YLASLFPDS 0.65 1 35[5I SLFPDSLV I l 11871 FPIDLGSL 1 4.4 427 I YTPPNFVLA 0.603 1357 SLPDLI515.1 12741 GLLAAAYQL 79.] 4 1374] LAVTSIPSV 777 171 NIQARQQVI 0.588 1393 FIQSTLGYV 72.344 62 VAITLLSLV 3.777 259 LPIVAITLL 1 0.545 S48 1 RLIRCGYHV I S 299 LQCRKQLGL ] 3.682 4381 LPSIVILDL 0.545 [365 IMSLGLLSL 60325 335 NMAYQQVHA 3.88 r 2781 AAYQLYYGT ] 0.497 [ 511 SMMGSPKSL 1105 I 29 1 FPPWLETWL I3]528 1i7071 INNIQARQQV 0.4] [ 2203 ISLATFFFL 53.163 331 YLFLNMAYQ I 3209 1 385 "ALNWREFSF 0.432i 18I WSAWALQL 3.178 149 WO 03/087306 PCT/USO3/10462 TableX-V2-HLA-A0201-9mers- NO: 11; each start position is 98P4B6 specified, the length of peptide is 9 TableX-V6-HLA-A0201.9mers. Each peptide is a portion of SEQ ID amino acids, and the end position 98P4B6 NO: 5; each start position is for each peptide is the start position Each peptide is a portion of SEQ ID specified, the length of peptide is 9 plus eight. NO: 13; each start position is amino acids, and the end position S rt Subsequence 1{ Score specified, the length of peptide is 9 for each peptide is the start position [ I FTFWRGPW 6.741 amino acids, and the end position plus eight. [ 1I! NLPLRLFTF 0,994 for each peptide is the start position Start I Subsequence I Scor TFWRGPVVV I plus eight. 5 - GLQALS 1S362 F 0 1 "Start[ Subsequence Score 10o r SLSLSSGFT I[ ] 1 7 Il ILGKIlLFL "1459.398] 1 F SLSL 3 1 LPLRLFTFW 0032 27I KGWEKSQFL I 91.350 r' FPS 17S 671 LFTFWRGPV I0.011 7 [ IILFLPC 4.21 F157 SGFTPFSCL 0,3 107 KlFPI 4.8 [T I!SGFTPFSCL 1I ~ ] [T7[ PLRLFTFWR ]j0.003 i : 1 GIGGTIpHV 21.996] 1 SGSPGLQAL 0.32138 GGTPV 296 14 j SGPFC 0.1 4 LRLFTFWRG 0.1 0001 14 FLPCISRKL[1653 ] If SSGFTPFSC 0.1i8 q1FRPVA]oo] __ IRLR __ 8 ALSLSLSSG 0.171 FWRGPVVVA 17 CISRKLKRI 3.299 12 SLSSGFTPF 0.142 LFLEEGIGGT 2.6897 [3 SPGLQALS 0.139 5L IVILGKIIL I1.303 [29 WDYRCPPPC 0.102 4 S 0.5887 PPCPADFFL 0.098 TableX-V5B-HLA-A0201-9mers- 43 IPHVSPERV I 0.378 3_1_ PCPADFFL -- 1 A 22 CLSLPSSWD 0.08298P4B6 - 1 VLPSIVILG t0.291 37 L.___,CPADFFLYF , 07Each peptide isa portion of SEQ ID 46 I VSPERVTVM 0.213 -F37__ NO: 11; each start position is [ -24 SLPSSWDYR I 068 specified, the length of peptide is 9 HVSPERV 0207 S25 LPSSWDYRC ] amino adcids, and the end position F6 II VLGKILF II 0.148 S-6 LQALSLSLS 0.030 for each peptide is the start position .31 KSQFLEEGI 0.117 S23 ILSLPSSWD ][ 0 plus eight. fT12 ILFLPCISR I 0.094 13i LSSGFTPFS 01 tarti Subsequence Score I 1 IILFLPCIS 0.026 20 FSCLSLPSS 0 LELEFVFLL .543,02 9 GKIILFLPC 01013 I7 I SLSLSS 0 04- ) 6 FQIFCSFA 6573 f 21 I KLKRIKKGW 009 11 LSLSSGFTP [ 24] FVFLLTLLL 31.814 35 LEEGIGGTI 0.003 271 SSWDYRCPP j1 22 LEFVFLLTL 22835 [421 TIPHVSPER II 0.002 131I YRCPPPCPA II.003 f QIFCSFADT 7203 32[ SQFLEEGIG I".001 9..... LSLSLSSGF 0003 19 ELELEFVFL 1.072 20[ RKLKRIKKG 0".001 F--9-7 0TEL03 !1257 21 SCLSLPSSW I 0002 17 QTELELEFV 0383 133 I QFLEEGIGG 0.001 FiO I TPFSCSP j[ 0.0I 101 FCSFADTQT 0.224 I 41 GIPHVSPE I GSPGLQALS I1 000 4 FSFIQIFCS 0.110 I3 I VL r33 CPPPCPADF 0 .000 21 ELEFVFLLT If oo0.068 F2 i LPSIVILGK i 0.000 16__] GFTPFSCLS 0 0 o 12 I SFADTQTEL II 06 I26 I[ KKGWEKSQF 1.oo 36 PCPADFFLY 18 TELELEFVF I0052 139 I IGGTIPHVS . 0,000 I 36 71 FCADFL 27 0.067 32[ RCPPPCPAD, 0j. 16 TQTELELEF I 0.031 2 i R IIKKGWEKS 0iQO'.000 44 PGLQALSLS 00 114 ADTQTELEL I 0.030 I [i5 If PCISRKLK I 0.000 I34 PPPCPADFF REFSFIQF 019 13II LFLPCISRK 0.000 19 1PFSCLSLPS 0.0 7 IQIFCSFAD 10.015 i I

'

40 If'GGTIPHVSP if 0.000 623 EFVFLLTLL 0.0 3 28 SWDYRCPPP 0.000 29 WEKSQFLEE 26 PSSWDYRCP_ 0.000. i 3 EFSFIQIFC h0.001J I8! LGKIILFLP 10.000" 1 RESIQ 0.0301 30 DYRCPPPCP 00 2i WREFSFQI 123 KRIKKGWEK 0.00 1i CSFADTQTE 000 137I EGIGGTIPH 0.000 1 3 ' FADTQTELE 3 -0 I21 EKSQFLEEG II 0.000 Tab l eX-V5A-

H

LA-AQ201-9mers- 5I ]1 SFIQIFCSF I00] !44 PHVSPERVT I0.000 98P4B6 9 IFCSFADTQ 0.000 36 EEGIG 0.000 Each peptide is a portion of SEQ ID I 0.000TTELELE 16 PCISRKLKR I 000 150 WO 03/087306 PCT/US03/10462 TableX-V6-HLA-A0201-9mers- TableX-V7C-A0201-9mers. TableX-V7C-A0201.9mers. 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 13; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of pepUtide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight. . plus eight plus eight. StartJ Subsequence S Score Istartl Subsequence Score Starti Subsequence Score 22 LKRIKKGWE 0.000 4I VILDLSVEV j246.631 11 EVLASPAAA 0,121 25[ IKKGWEKSQ 0.000 114811 SLAFTSWSL 160.218 49 PLSTPPPPA 0.109 [18)[ ISRKLKRIK I 0.000 r129l PLWEFLLRL 139.780 178 QEQKSKHCM 0.097 2I8 GWEKSQFLE 0 31I GLSEIVLPI j98.381 59 WTEEAGATA 0.083 L19 SFRKLKRIKK 7M 157 I AMWTEEAGA 29.780 -F17l AAAWKCLGA 069 1231 SIVILDLSV 19.563 F147 LSLAFTSWS 10.064 TableX-V7A-HLA-A0201-9mers- 1 216 GVGPLWEFL 8.564 _ 139 KSQAASGTL 0.063 98P4B6 r5)1 ILDLSVEVL I 6.712 35 IVLPIEWQQ 0.062 Each peptide is a portion of SEQ ID 152 TSWSLGEFL 3.119 129I RGGLSEIVL 11 0.057 NO: 15; each start position is 27 LRGGLSEI 3.100 ANSWRNPVL .- 057 specified, the length of peptide is 9 2 ILRGGLSEI 113 amino acids, and the end position 4 QQDRKIPPL 1.993 20! WKCLGANIL I0.056 for each peptide is the start position 168 LETIILSKL 1.624 I5 LSTPPPPAM] 0.055 plus eight. 12711 VGPLWEFLL 1375 1 775 KLTQEQKSK I 0.052 Start Subsequence ScorI 13 GTWMKLETI 111.355 1 SGTWMKLET I 0.049 1911 FLPNGINGI 110.3791 811 SSQIPWGV 1.044 LDLSVEVLA 043 i4 ! SLSETFLPN .581 165' WMKLETIlL 1.018 3611 VLPEWQQD f 0.043 6 SETFLPNGI II0.203 112 AANSWRNPV L 0.966 10 GANILRGGL .03 3 KSLSIETFLP I0.007 182 SQIPWGW 0.864 [1771 TQEQKSKHC 0.032 LI PKSLSETFL II 0.004] 1341 LLRLLKSQA 0.642 11051 SPDRALKAA I 0.030 5 LSETFLPNG .0 1441 SGTLSLAFT 110.615 1711 llLSKLTQE 11. 8 TFLPNGING II 0.000 133 FLLRLLKSQ ,r 0.583 41_ WQQDRKIPP I 0.028 7- ETF'LPNGIN if 0.00 1 39 IJEWQQDRKIr 0.572 9T SVEVLASPA 0028 [ 71[1SPKSLSETFII 0.000 159! FLGSGTWMK I0 0514 ] F 111 PVLPHTNGV 0.495 1721 ILSKLTQEQ 0.025 TableX-V7B-HLA-A0201-9mers- 18511 CMFSLISGS 0.458 14511 GTLSLAFTS I 0022 98P41B6 781 SSSSSQIPV 0.454 38 LKSQAASGT Each peptide is a portion of SEQ ID SSSSQIPr 7 i [4 WSLGEFLGS 0.01 NO: 15; eah str7oito s191 SSSSQIPW 10.428 [154[ WSLGEFLGS 0[.016 NO: 15; each start position is specified, the length of peptide is 9 83 1 QIPVVGVVI 0.420 1 NKSSSSS amino acids, and the end position 16011 LGSGTWMKL 0403 I 7l DLSVEVLAS I0.013 for each peptide is the start position 155 1 SLGEFLGSG 1 0.347 1149 LAFTSWSL 073 plus eight. Start ISubsequence 1 4Score11 QAASGTLSL II 0297 1116 WRNPVLPHTI 0011 [I I[6 ST n [S 1136 1 RLLKSQAAS I0 276 1 ESPDRALKA 0.010 F6 jYQQSTLGYV 153.3450 17F I 3 II NAYQQSTLV I54 [52Jf TPPPPAMWT II 0.268 I 66 11 TAEAQESGI If 0.009 I 3 MYQSL 15.428 -- 6 I 9 NMAQQSTL 15.428 1141I ASPAAAWKC t 0.243 112511 NGVGPLWEF U 0.008 IF9 - STLGYVALL !2.525 P ]T AAA 125I -0 I1II FLNMAYQQS 110.5i14 [i15 SPAAAWKCL 0.237 [169[ ETIILSKLT I 0.008 2 1 FLNMAYQQST 0.30514 1 81 KSKHCMFSL 0

.

228 11 KLETIILSK .008 [ QSTLGYVAL 0.209 F881[ GVVTEDDEA 0213 26 NILRGGLSE 0.008I 7 SLGYVA 0209 F221 CLGANILRG I 0.171 1140 SQOMSGTLS I 0008 I7 I QQSTLGYVA][ 0.207 [10f VEVLASPA[ TAEA I 4 ~0 VEVLASPAA 0.164 F1 4 -U MAYQQSTLG 0.006 ...... S4 MIAYQQSTLGY 0.006 1142 AASGTLSLA 0.159 1761 LTQEQKSKH I 0.007 50 AYQQSTLGY 04000 .1146 II TLSLAFTSW ! 0.142 1481 KIPPLSTPP 1I0.007 I 1121 VLASPAAAW 1 0.127 I 120 VLPHTNGVG I 0.007 151 WO 03/087306 PCT/USO3/10462 TableX-V7C-AO201-gmers. TableXI-V1-.HLA-A0201.-10mers. TableXI-VI-HLA-AO201-10mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end position amino acids, and the end position for amino acids, and the end position for for each peptide is the start position each peptide is the start position plus each peptde is the start position plus plus eight nine. nine. Strtl SubsequenceI Score Start Subsequence Score Start Subsequence Iscore 16611 MKLETIILS 0.006 1 266 LLSLVYLAGL I83.5271 257 11 KTLPIVAITL II 3.8-42 156 LGEFLGSGT 1 0.005 J 403 LLISTFHVLI t396 [231 FVRDVIHPYA 13.427 158 1 EFLGSGTWM I 0.005 402 ALLISTFHVL 1161.5731 314 1 MVHVAYSLCL 3.178 i 131 II WEFLLRLLK I 0.005 3 6] IMSLGLLSLL 6 [303 KQLGLLSFFF [ 3.121 101 DPPESPDRA 1 0.005 F140 SLIVKGFNW I 54.1811 221 11 SLATFFFLYS 1 2959 I89 VVTEDDEAQ 0 .204 2 58] TLPIVAITLL 149.1341 144 1 KGFNVVSAWA 2.310 1137 LLKSQAASG 0.004 F433 1 VLALVLPSIV I48478 1286 TKYRRFPPWL 1.984 113511 LRLLKSQAA 0.004 I 48 RLIRCGYHW I 42774 147 II NWSAWALQL 1.869 108i RALKAANSW II 0.004 370 LLSLLAVTS/ 4199 REIEN7LPLRL II .03 128'1 LRGGLSEIV II 0.003 1 I 2101 TLWRGPWVA I38884 I4411 IVILDLLQLC I 1.700I 11091 ALKAANSWR 1 0.003 2631 AITLLSLWVYL 37.157 1 38911 REFSFIQSTL I1.537i S18 II AAWKCLGAN 1I 0.003 1 432 I FVLALVLPS I 35.735 1 226 I FFLYSFVRDV l1.437 L911 TEDDEAQDS 1_0.002 01 VALLISTFHV35242 24 GIKDARKVTV 1.372 l164 TWMKLETIl 0.002 1 F207l1 RLFTLWRGPV 133.4551 12011 IENLPLRLFT 1.35 L , IVILDLSVE 0.02 227" FLYSFVRDVI 130852 FSTLGYVA 1.288 1651 ATAEAQESG I 0.002 r 2231 ATFFFLYSFV 1294871 641 KFASEFFPHV I 1.2211 165 FASEFFPHW 28385 152 WALQLGPKDA I. 7 1 364 GIMSLGLLSL 24.9971 3451 IENSWNEEEV 1.127 26171 IVAITLLSLV 723.795 29 LQCRKQLGLL I.1071 435 ALVLPSIVIL 0.145 1631 RQVYICSNNI .058 TableXI-V-HLA-A0201-Omers. 901 FVAIHREHYT 16497 1 1 TPNFVLALV 1.0441 98P4B6 1791 IELARQLNFI 16.1411 2641 ITLLSLVYLA 0.9981 Eachpeptideis a portionofSEQ ID 1427 YTPPNFVLAL 11.929 11131 LIDVSNNMRI F0.975 NO: 3; each start position is 67 SEFFPHWDV 11.509 250 IPIEIVNKTL 0.972 specified, the length of peptide is 10 II 3 KSLTIRLIRC i0.966 amino acids, and the end position for 111 KILIDVSNNM 8- KSLTIRLlRC 0. each peptide is the start position plus F 3035 LGLLSFFFAM I.42 323 1 LPMRRSERYL 0.965 nine. [172 1 IQARQQVIEL I I I424 II YRFYTPPNFV 0.904 [Start ISubsequence Score 2491 KIPIEIVNKT 18.248 1361 IGSGDFAKSL 0.0 2SLWDLRHLLV 2366 8 5 1831 RQLNFIPIDL 8.014 361 ISFGIMSLGL I .877 L~ ~V0 [ LL 5_ _ _ I0 15 r'95 REHYTSLWDL 1 4 II ISMMGSPKSL I0.877 306 GLLSFFFAMV 185.01 F4401 SIVILOLLOL I 336 MAYQQVHANI 0.788 -IIZ 9 I FTLWRGPWV 1 67 1 i139 1 DSLIVKGFNV I0.731 f821 ALTKTNIlFV 879.833 308 [82 ALTKTNIFV 879.83 [308I LSFFFAMVHV 6.568 12 SLSETCLPNG r0703 F304[ QLGLLSFFFA 301.110 i 6.387 1 LLAAAY 0.697 57 V-IGSNPF (-38_ 275 !1LLAAAYQ LYY I 0.697 373 jiLLAVTSIPSV 271.9481-IF069 373 LLAVTSIPSV 271.948 41971 FEEEYYRFYT 5.579 1134 ASLFPDSLIV 0.689 Il1 LLVGKILIDV "I248 [394I IQSTLGYVAL 5.523 121 RINQYPESNA 0.6831 132 YLASLFPDSL 182.973 I i EIVNKLPiv F269 ILWLAGLLAA 15.439 F253 IEWNKTLPlV 0O.676 1219 AISLATFFFL 17032 13131 AMVHVAYSLCI 5.382 F"98 YTSLWDLRHL 0.628 [367 1 SLGLLSLLAV 159.9701 1' FAMHVAYSLI LGYVALLIST 0609 F3851 ALNWREFSFI 106E52 37 IFMHAS 981LYALS M 13851 ALNWREFSFI 1268"1 SLVYLAGLLA l4.9681 F16 1 TCLPNGINGI 05801 298IF WLQCRKQLGL 198.2671 243 I VIL K,.L 137 [92 11 AIHREHYTSL 1 .406 3961 STILGYVALLI 1 o.5361 M437 IVLPSIVILDL 83.527 11 1 U IREYSG 47 I LP L.___ -- 1243I1 QQSDFYKIPI 114.337 356I RIEMYISFGI 0.532 152 WO 03/087306 PCT/USO3/10462 TableXI-V1-HLA-A0201-10mers- TableXI-V2.HLA-A0201-10mers- TableXI-V5B-HLA.A0201-10mers 98P4BS I 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3; each start position is NO: 5; each start position is NO: 11; each start position is specified, the length of peptide is 10 specified, the length of peptide is specified, the length of peptide is amino acids, and the end position for 10 amino acids, and the end 10 amino acids, and the end ach peptide is the start position plus position for each peptide is the start position for each peptide is the start nine. position plus nine. position plus nine. Start Subsequence JScjre ] Star t l Subsequenc Score Start Subsequence Score] 202 ENLPLRLFTL 0.516 361 PCPADFFLYF 0.000 20 ELELEFVFLL I5.198 99i i TSLWDLRHLL ( 1 29 WDYRCPPPCP 0.000 IQIFCSFADT (12.440 27 AGLLAAAYQL [ 0.5 1 28 1SWOYRCPPPC 0.000 3 [ REFSFIQIFC 1.966 332 LFLNMAYQQV i 0.456 35 PPCPADFFLY o.ooo [ 22 ELEFVFLLTL 0.896 25 LPSSWDYRCP 0.000 [14 FADTQTELEL 0.546 F31 YRCPPPCPAD 10.000 [121 CSFADTQTEL 0516 30 DYRCPPPCPA 0.000 [ 611 SFIQIFCSFA 0.072 TableXI-V2-HLA-AO20110mers- 19 PFSCLSLPSS 0.000 [7 FIQIFCSFAD 0.055 98P4B6 2615 PSSWDYRCPP 0.000 FSFIQIFCSF 0.016] Each peptide is a portion of SEQ ID 9II QIFCSFADTQ O014 NO: 5; each start position is 10 IFCSFADTQT .0L9 specified, the length of peptide is 2 EFVFLLTLLL 0.001 10 amino acids, and the end TableXI-V5A-A0201-10mers- EFVFLLTLLL position for each peptide is the start 98P4B6 [1i NWREFSFIQI [0,001 position plus nine. Each peptide is a portion of SEQ ID i1 FCSFADTQTE I 0.000 Start Subsequence I Score NO: 11; each start position is [ 18 QTELELEFVF 0 0 24 ISLPSSWDYRC 4.968 specified, the length of peptide is 10 [ 16 DTQTELELEF 0 00 12 SLSSGFTPFS 1.557 amino acids, and the end position for 4[ - EFSFIQIFCS 0 I2i CLSLPSSWDY M T0.5 each peptide is the start position plus ADTTELELE .......... nine. - .. __ _ __ _ 11311 LSSGFTPFSC ]5 0.320 - [137[SFADTTELE [ 000 Start][ Subsequence Score 13 SFADTQTELE 000 4 SSGFTPFSCL 0.265 6 RLFTFWRGPV 1133.455 | WREFSFIQIF 0 0 I90. LSLSLSSGFT .9 8 FTFWRGPVVV I 6.741 I 571 GLQALSLSLS I70171 2 1 NLPLRLFTFW 10.779 TableXI-V6-HLA.AD201.10mers I2 GSPGLQALSL 10.139 LPLRLFTFWR 74 98P4B6 I34 PPPCPADFFL 0. 98 F7 _ LFTFWRGPVV 0.034 Each peptide is a portion of SEQ ID PP NO: 13; each start position is -51 SLSLSSGFTP I0.086 19 TFWRGPVVVA 0.027I specified, the length of peptide is 8 "ALSLSLSSGF1 0.075 1 1 ENLPLRLFTF 0.002 I 10 amino acids, and the end 16 GFTPFSCLSL 0.01p PLRLFTFWRG 0.002 position for each peptide is the start .6 LQASLSLS 0.013 FWRGPWVAI 0.001 position plus nine. 4 1 PGLQALSLSLSS 0. 0 LRLFTFWRGPWVAI .o000I [Start[ Subsequence I Score 7

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PGLQALSLS i 1 LRLFTFWRGP 7 I VILGKIILFL 233.719 II7 II QALSLSLSS'G ~1 -- [ 1[ TIPHVSPERV I4 5 I SGFTPFSCLS 0.007 TableXI-V5B-HLA-A0201-10mers- 3 LEEGIGGTI 1 LSLSSGFTPF ]0.006 98P4B6 FLEEGIGGTI 1.637 27 SSWDYRCPPP 0.003 Each peptide is a portion of SEQ ID [5 [ SIVILGKIIL II 1.204 23 ILSLPSSWDYR 0.003 NO: 11; each start position is 27 KKGWEKSQFL II 0571 I20 ]FSCLSLPSSW-[ 0.00 specified, the length of peptide is 8 I ILGKIILFLP 0.3381 17 FTPFSCLSLP 0.002 10 amino acids, andtheend r1 ILFLPCISRK I '0.216] 11 [position for each peptide is the start ["i 11 GKIILFLPCI 0 21 SCLSLPSSWD 0.002 position plus nine. 10 GKIILFLPCI 0.127 18 II TPFSCLSLPS 0.002 Start Subsequence Score LVLPSIVILG 0094 3311 CPPPCPADFF 0.001 17 TTELELEFV 13 [38 EGIGGTIPHV 10078 31 1 SPGLQALSLS ] 0.001 I TELELEFVFL 65.849 [,11I FLPCISRKLK 0.069 S32 _ RCPPPCPADF [0.00J 121 LELEFVFLLT 7.1002I KGWEKSQFLE 1.067 111 SGSPGLQALS II0.000 23~ LEFVFLLTLL [ 2 VLPSIVILGK I0.058 153 WO 03/087306 PCT/USO3/10462 TableXI-V6-HLA-A0201-10mers. TableXI-V7A-HLA.A0201.10mers. TableXI.V7C-HLA.A0201-10mers 98P4B6 8P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 13; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 10 10 amino acids, and the end 10 amino acids, and the end amino acids, and the end position for position for each peptide is the start positon for each peptide is the start each peptide is the start position plus position plus nine. position plus nine. nine. Start Subsequence Scoe start Subsequence II Score Start 1 Subsequence S 3 LPSIVILGKI J 0.035 5 SLSETFLPNG I2.670 5 I VILDLSVEVL 35,002 33 SQFLEEGGG 0028 I 9 TFLPNGINGI I 0.062156 I SLGEFLGSGT i 0.553 6 IVILGKIILF 20.025 2 SPKSLSETFL 0.027 27 NILRGGLSEI 12.208 34[ QFLEEGIGGT ] 0.023 [4 KSLSETFLPN 0 012 [ 168 KLETIILSKL 11.006 14 LFLPCISRKL F 6 LSETFLPNGI 0 007 _127 I GVGPLWEFLL 10.841 11 KIILFLPCIS 10.0175 1 FLPNGINGIK 0.0 1 IVILDLSVEV 10.346 46 HVSPERVTVM 81 ETFLPNGING II 0.000 i30 i PLWEFLLRLL [7357I r12 IILFLPCISR II 0.013 F 1 I GSPKSLSETF 05.000 48 LSLAFTSWSL 6.579 _44 I IPHVSPERVT [0.007 3 7I SETFLPNGIN II 0.000 1 58 AMWTEEAGAT 5.807 I GGGTIPHVS 01.01 311 PKSLSETFLP .Ij 9 GPLWEFLLRL 1 S 1 LGKIILFLPC j 0.004 1 152 FTSWSLGEFL 3678 I 17[ PCISRKLKRI 0.003 TableXI.V7B-HLA.A0201.1Omers. [112 f KAANSWRNPV 3.381 i22 KLKRIKKGWE 0.001 98P4B6 [6 ILDLSVEVLA [ 3378 1 !451 PHVSPERVTV 0. 00 1 Each peptide is a portion of SEQ ID '141 SQAASGTLSL 2.1661 I30][" WEKSQFLEEG 1 .1 NO: 15; each start position is 18 F specified, the length of peptide is S [ 4 PSIVILGKII 10001 10 amino acids, and the end [28 I ILRGGLSEIV I1.5 731_ EKSQFLEEGI 1 position for each peptide is the start 78 KSSSSSQPV 1.589 21 RKLKRIKKGW 0.000 position plus nine. 147I TLSLAFTSWS 1.557 411 .GGTIPHVSPE 110.00] Start Subsequence score 1F9 AAWKCLGANI 1.203 1421 GTIPHVSPER l F0I2 I FLNMAYQQST 34.279 [811 SSSQIPWGV 1.044 18 ' CISRKLKRIK_ 0.00 81 QQSTLGYVAL I3.249 14 LASPAAWKC 0.880 1401 IGGTIPHVSP I0.000 0 91 YQQSTLGYVA 1L R1351 LLRLLKSQAA 0.642 116 1 LPCISRKLKR 1 5 [,[3 LNMAYQQSTL [0.877 F1 26 i NGVGPLWEFL 0 639 371 EEGIGGTIPH 0.000 STLGYVALLI 0.536 144 1 ASGTLSLAFT 0.615 321 !KSQFLEEGIG 0.000 I 9I QSTLGYVALL 0321 66 I ATAEAQESGI 0594 [25[ IRIKKGWEKSQO ]1 0.000I4 NMAYQQSTLG] 0.054 -31 G5GLSEIVLPI 0.580 24 1 KRIKKGWEKS 0 I00 61 AYQQSTLGYV 0.016 52 STPPPPAMWT 0.569 231 LKRIKKGWEK 1 15 MAYQQSTLGY 0.006 164 II GTWMKLETII 0.4931 36 LEEGIGGTIP 11 0000 1 LFLNMAYQQS 0.000 177 LTQEQKSKHC 0.481 r191 ISRKLKRIKK 0.000 I119 " NPVLPHTNGV 0.454 26 IIKKGWEKSQF 0.000 138 I LLKSQAASGT 0.443 F26_7_1 SRKKRIKKG F 0.0 TableXI-V7C-HLA-A0201-10mers- 7 201 SRKLKRIKKG 0. 000 98P4B6 79 SSSSSQPVV 0.428 29 I GWEKSQFLEE 0.000] Each peptide is a portion of SEQ ID 181 QKSKHMFSL 0.396 NO: 15; each start position is 83 SQIPWGVVT II 0.310 TableXI-WA-HL.A-A0201-10mers. specified, the length of peptide is 10 137 RLLKSQAASG II 0.276 98P4B6 amino acids, and the end position for 1 KLTQEQKSKH 0.261 Each peptideis a portion of SEQ ID each peptide is the start position plus 16 LETIILSKLT 10.246 NO: 15; each start position is nine. _ _6 specified, the length of peptide is I Start Subsequence 0Score . i ASPAAWKCL 0.237 10 amino acids, and the end I 160 FLGSGTWMKL 167.054 1 1 LSVEVLASPA 0.226 position for each peptide is the start 42 WQQDRKIPPL 93.953 1 1 VEVLASPAAA ' 0.164 position plus nine FTEDDEAQDSI 0.163 N _Statluseu_ M F13471 FLLRLLKSQA 84.55]Q Start Subseuence ScoreSLA 0.159 154 WO 03/087306 PCT/USO3/10462 TableXI-V7C-HLA-AO201-10mers- TableXI-V7C-HLA.A0201-10mers. TableXl-VI-HLA.A3-9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 3; each start position is spedcified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position for amino acids, and the end position each peptide is the start position plus each peptide is the start position plus for each peptide is the start position nine. - nine. plus eight. iStart Subsequence II Score I Sta Subsequence I Score 1 StaraI Subsequence S13 VLASPAAAWK 0.139 1 109 RALKAANSWR 0.004 I SLWo LRLL 3.0 1491 SLAFTSWSLG 0.127 F 97 AQDSIDPPES [ 0.003 ]1 GINGIKOAR 2.700 113 AANSWRNPVL 0.22 43 QQDRKIPPLS [! 0003] 40 LLISTFHVL 2.700 50 PLSTPPPPAM I 0.109 [145 I SGTLSLAFTS IF 0037 2651 TLLSLVYLA 2.70l0 163 SGTWMKLETI !0 077 [49[ PPLSTPPPPA 0.003 1435] ALVLPSIVI 2.7 00 -122 LPHTNGVGPL F8-] DLSVEVLASP I 0.003 r123 NLPLRLFTL 2.700 32j GLSEIVLPIE 10,58" 761 RNKSSSSSQI I0.002 12051 PLRLFTLWR 1i2.400 [1 I WEFLLRLLKSI 104I PESPDRALKA 3 002 I E 1 SISMMGSPK 2.000 821 SSQIPWGW [ 0.058 29[ LRGGLSEIVL II 0.002 2581 TLPVAITL Ii1.800 F162 GSGTWMKLET[ 00493 3 SIVILDLSVE 0.002 1 41 QLNFIPIDL I1.800 123 CLGANILRGG 0.034 127 EVLASPAAAW IFO.002 I397I1 TLGYVALLI 1F.800 1178 ITQEQKSKHCM 0.032 3 SEIVLPIEWQ I 0.002 F IMSLGLLSL 800 24 LGANILRGGL I 0.031 140 KSQAASGTLS 30 0002 1 307 LLSFFFAMV IF 1.800 10 IIl SVEVLASPAA 1 0.028 N1FVAIHR .800 F IVGVVTEDDEA 0o02 TableXII-VI-HLA-A3-9mers- 106I HLLVGKILI 1.80 37 VLPIEWQQDR 0.025I 98P4B6 1433 VLALVLPSI 1.350 1121 1 VLPHTNGVGP 0.025 Each peptide is a portion of SEQ ID 1911 DLGSLSSAR 1.200 1531 TSWSLGEFLG ]I 0.023 1 [NO: 3; each start position is 210 TLWRGP specified, the length of peptide is 9 10 IRGPV .9 105 ESPDRALKAA I .23 I amino acids, and the end position i40 SLIVKGFNV I 0.900 166 I WMKLETIILS 0.020 for each peptide is the start position [17_ 1 CLPNGINGI I 0.900 iF 1 ALKAANSWRN I.20 pluseight, 231 FVRDVlHPY I0.9

[

182 KSKHCMFSLI 1 l0.016 I Stt ubsequence 48I RLIRCGYHV I0.900 2I KCLGANILRG II 0014 I 221 SLATFFFLY I 402 ALLISTFHV 0.900I S36 [IVLPIEWQQD II 0.014 306 GLLSFFFAM 24.300 227 i FLYSFVRDV I.900 172[I IILSKLTQEQ 12941 '"WLETWLQCR 18.000 4171 RAFEEEYYR i0.900 173 ILSKLTQEQK 0.012 281[ QLYYGTKYR 1.Ioo 26 3 I AITLLSLVY i 0.800 2 I2PSVILDLV I.10 249 KlPIEIVNK 9.000 5 I SMMGSPKSL 0.675 iF1 WSLGEFLGSG II 0.009 103][ DLRHLLVGK 9[. 000 369 GLLSLLAVT [0.675 [F115 NSWRNPVLPH 10.009 274 I GLLAAAYQL [8.100 [396I STLGYVALL 0.608 907 VVTEDDEAQD 0.01'09 443 ILDLLQLCR 8.000 303I KQLGLLSFF [0.608 [1021 DPPESPDORAL 0.00 [223 ATFFFLYSF 6.750 0 SLTR C .600 125 TNGVGPLWEF 0.008 304 QLGLLSFFF II 6.000 [3811 SVSNALNWR 0.600 146] GTLSLAFTSW 1 0.0071 5 QLGPKDASR I 6.000 TIRLIRCGY 0.600 47__1 KIPPLSTPPP 310.007 1 5]1 ALNWREFSF ]I 6.000 [219I AISLATFFF 0.600 13971 LKSQAASGTL 1 .007 51 VIGSGDFAK 2 6.00080 [2 1 YQLYYGTKY 0.540 61 TEEAGATAEA O06I [ 4 0I HVLlYGWKR 415.400 11I LIYGWKRAF 0.450 101 IDPPESPDRA 56 WIGSRNPK 4.[500 YLAGLLAAA l 0450 S577 PAMWTEEAGA 10.006 313 AMVHVAYSL 4.050 112 ILIDVSNNM 5 ....... !- rL405 12 ILIDVSNNM II 0.450 1 -59! MWTEEAGATA 110.005 8 ALTKTNIIF I 4.000 I KTNIIFVAI 171 TIILSKLTQE I 005 322 CLPMRRSER II4.000 [90I FVAIHREHY j .400 [84I QIPWGVVTE 2 0.005 275 LLAAAYQLY 14.000 367l SLGLLSLLA I o.400 [165' TWMKLETIIL 0.005 15 [3 SLFPDSLV 3.000 1131 LIDVSNNMR 0.400 155 WO 03/087306 PCT/US03/10462 TableXII-VI-HLA-A3-gmers. NO: 5; each start position is Start Subsequence Score 98P4B6 specified, the length of peptide is 9 NLPLRLFTF 7 .00 Each peptide is a portion of SEQ ID amino acids, and the end position PLRLFTF .00 NO: 3; each start position is for each peptide is the start position PLRLFTFWR 3.600 specified, the length of peptide is 9 plus eight. L FTF.. RGPW J.050 amino acids, and the end position Start Subsequence Score 5 RLFTFWRGP 0.030 for each peptide is the start positon 12 II SLSSGFTPF I o i LPLRLFTFW 0.009 plus eight. I 24 1 SLPSSWDYR 40 9 1 FWRGPVA 0_.001 tIart Subsequence Score 5 GLQALSLSL I3.600 8 71-TFWRGPVVV 0 1481 WSAWALQL II 0.360 I 37 CPADFFLYF LRL0360 FTFR G 0.000 1751 RQQVIELAR 0.360 23 LSLPSSWDY 127 237I LSLPSSWDY II0.135 0.--00TFR0V 1 [217 WAISLATF I 0.300 7 FTPFSCLSL 0.060 184I QVYICSNNI 0.0 7 FTFCS .060 1641 Q IcsrN 1030 I [ 36 PCPADFFLY 0.036 TableXII-V5B-HLA-A3-Smers 400 YVALLISTF I0.300 M 98P4B6 8I ALSLSLSSG 0.030 431I KSLTIRLLR 10.270 22 CLSLPSSWD ii Each peptide is a portion of SEQ ID 441 IVILDLLQL I.270 ] NO: 11; each start position is -268 SWAL 0 1 SLSLSSGFT 03 02 specified, the length of peptide is 9 SIf SLVYLAGLL II 0.270 1 33 CPPPCPADF 0.030 amino acids, and the end position 1801 ELARQLNFI I0.270 i25 LPSSWDYRC 0.018 for each peptide is the start position 3531 EVWRIEMYI 0.270 plus eight. 3581! EMYISFGIM 3.27 1.S ~S Subsequence Score LAAAYQLYY 15 1SGFTPFSCL 0.013 FtaQ 2761 LAAAYQLYY _0.240 24 FVFLLTLLL 0.600 436 LVLPSIVIL 42039 PPPCPADFF 31 ELELEFVFL 0. -1 NMAYQQVHA ]Ti SSGFTPFSC I[FO. [ I003LEFVFLLT IU r335 F-347 PPPCFPAFF 0.003 -2 .7 357 NMAYQQVHA 0.200 212ELEFVFLLT 0.27 15 I! VIGSRNRKF-I o.'l 1 211 SCLSLPSSW"[ 0.003 161 TQTELELEF 1[ h 269 LWLAGLLA 0 l PPCPADFFL 18 QIFCSFADT 0.150A 35PPCPADFFL 0.003 33 3 I FLNMAYQQV FI 0.200 l REFSFIQIF 0.135 16'1 LQALSLSLS I 0.002 2 61 I VAITLLSL 0.10 1 LELEFVFLL 0.19 2251 FFFLYSFVR 0o.180 WJ Yo- 220.2_I LEFVFLLTL 1.081 f 3670 YSFGIMSL27 SSWDYRCPP 10.002 F6 .6 1360I YISFGIMSL IF 0.180 111 6 F11 FIQIF

C

SFA 0.060 1 SGSPGLQAL 0.001 4371 VLPSIVILD 0.180 I7 QALSLSLSS 0.001 1 TELELEFVF 0.041 41 LI STFHVLI 0.18029 WDYRCPPPC .001 QTELELEFV 242 NQQSDFYKI 0.16 LS0 1 5 SFIQlFCSF l.01 242 r ~13 jLSSGFTPFS 0.001 -7 r257 KTLPIVAIT I 0. 1 SSGF S 4 IFSFIQIFCS 0.005 2GSPGLQALS7 0.001 31 YLFLNMAYQ 0.150 1 WREFSFIQI 0.004 r_1671 GFTPFSCLS 0.001 7101 VLIYGWKRA I 0IQFCSFAD 0003 IC GVIGSGDFA P 0.000 IY141 ADTQTELEL 11 LSLSSGFTP 0 .000 L#DQELLI 118-1 LPNGINGIK IF 0.135 10 F RP PAD CSFADQT 32_ RCPPPCPAD_ 0.000 ~5I FSADQ 101 [107J LLVGKILID 0.135 I FSCLSLPSS L I2 ISFADTQTEL 0.001 F4 075~2 F SCLSLPSS 0.00015 000 [1 RNQQSDFYK 1 sWDYRCPP I I CSFADTQTE 0.001 28 SW7DYRCPPP 10.000 4[ ISTFHVLIY 0.120 5 II DTQTELELE 0.000 I'T IIY SLF SII0.10 ___4 PGLQALSLS I0.01_00 132 YLASLFPDS 120 F 30I DYRCPPPCP 1100001 123 IFEFVFLLTLL 0i 428 TPPNFVLAL 0108 I II PFSCLSLPS 00 I FADTQTELE 0.0 F19 PFSCLSP 000 1 53I ALQLGPKDA I 0.100 PSSWDYRCP I "i EFSFIQFC II 0.000 1 08 LVGKILIDV .090 I 9 IFCSFADTQ 0.000"I 3771 SIPSVSNAL FTableXIl-V5A-HLA-A3-9mers 141 LIVKGFNW 10.090 I 98P4B6 ,Mfi LYGTYRR98PBi T a b l e x l l' W H LA 'A3 9 m e rs " 282I LYYGTKYRR F0.090 I Each peptide is a portion of SEQ ID TableXl-V6- A3-9mers-8P46 NO: 11; each start position is "p TableXII-V2-HLA-A3-gmers. specified, the length of peptide is 9 Each peptide isa portion of SEQ ID 98P4B6 amino acids, and the end position NO: 13; each start position is Each peptide is a portion of SEQ DI for each peptide is the start position specified, the length of peptide is 9 Ec peptideiaportio o S Dplus eight. amino acids, and the end position 156 WO 03/087306 PCT/USO3/10462 for each peptide is the start position TableXII-V7C.HLA-A3-Smers plus eight. 9 I98P4B6 I Start Subsequence "Score TableXII-V7A.-HLA-A3-9mers- Each peptide is a portion of SEQ ID 12 ILFLPCISR I60.000 - 98P4B6 NO: 15; each start position is S_ ILGKIILFLj 2.700 Start I Subsequence IScore specified, the length of peptide is 9 6 VILGKlLF 1 Each peptide is a portion of SEQ ID amino acids, and the end position SVILGKIILF NO: 15; each start position is for each peptide is the start position 1 KIILFLPCI j -plus eight. lLPCI 1 - specified, the length of peptide is 9 plus eight. 1_LPSIV__ILGK 0 amino acids, and the end position Start Subsequence Score 42____ TIPHVSPER 0160 for each peptide is the start position 109 ALKAANSWR 4.0 21 j 0.45QJ ~plus eight. 1914.01 [ KLKRIKKGW 0.450 plus eight. SLAFTSWSL 1.800 n 9I FLPNGINGI 0.900 23 KRIKKGWEK 027 15N ILDLSVEVL 1.800 M E 47 SLSETFLPN 0,180 S IVILGKIIL 0.180 SLSETFLPN I 27 I ILRGGLSEI 1.350 F 1 SPKSLSETF 0.020 I VLPSIVILG Jl 0.180 1 ['65IKS WMKLETL [2 .F38 j --- F67 SETFLPNGI 0.002 38 GIGGTIPHV II0.135 SETFLPNGI I . 128 I GPLWEFLLR 1.080 15 _ LPCISRKLK II. KSLSETFLP 0001 57 AMWTEEAGA 1.000IK 7 IETFLPNGIN 0.001 S FLPCISRKL 0 [I GTWMKLETI [0.67 5 1LSETFLPNG 0.000 13 LFLPCISRK 0. 068LSETFLPNG 1 [1467 I TLSLAFTSW I.600 1 8 1 TFLPNGING 1.000 34 FLEEGIGGT 06] 1 F I l[ WEFLLRLLK I 0600 I 171 CISRKLKRI [0451 T21 KCLGANILR 0.540 4"' SIVILGKII 0[045 . 12 VLASPAAAW 0.300 4 SIVILGKII 0.045TableXII-V7B-HLA-A3-9mers- LSA W 19 SRKLKRIKK 0.040 eX-V-HLA-A3-9mers- BP4B6 185 CMFSLISGS I 0.300 45P4 HVSPERV 0.00 13 LASPAAAWK 10300 45 I HVSPERVTV II 0030 Each peptide is a portion of SEQ ID 7 LPW 0.30 41 GTIPHVSP 0. NO: 15; each start position is [ T 37 I7 LPIEWQQDR 31 0.270' 27 J KGWEKSQFL 0.014 specified, the length of peptide is 9 F 128 l GVGPLWEFL 0 .270 16 [PCISRKLKR I 0.012 amino acids, and the end position [38 PIEWQQDRK 0.200 18 _ISRKLKRIK 0-10 for each peptide is the start position LLRLLKSQA 18 I SRKLKRIK 0.01 plsih.134 IILLRLLKSQA 020 _ ~r pluss eight. 31 KSQFLEEGI 1 0.0791 St3 I Subsequence I 1731 LSKLTQEQK 0.100 26 1 KKGWEKSQF 0.006 I 9 STLGYVALL 1 0.608 88 'GVVTEDDEA 0 090 I..11 I lLFLPCIS .o.oI II NMAYQQSTL 11 0.600 691 AQESGIRNK 0.090 '_9 GKIILFLPC 0.005 F7 FLNMAYQQS 0 DLSVEVLAS 10.02 46 VSPERVTVM 0.1 005 I QQSTLGYVA I ! [ SIVILDLSV 0.6 'F-7 0.04 7 71QQSTLGYVA I0.018 ILKQA 24-- RIKKGWEKS 04 L5I AYQQSTLGY [0.008 1 36 LLKSQAAS 0,060 43 IPHVSPERV 0.02 1 QSTLGYVAL o 3 I22I CLGANILRG 05-2060 vs - 8 QSTLGYVAL 110.003 S351 LEEGIGGTI F0-001 6 YQQSTLGYV 0.31 3 151i l FTSWSLGEF I0.045 V 1.0034 I 32 SQFLEEGIG 0.0 4_1 MAYQQSTLG 0.001 1 SLGEFLGSG I004I 29'1 WEKSQFLEE 0.00o0 12 LNMAYQQST ii0.001 1 8 1 0.041I I3 I PSIVILGKI 0.0001 125 NGVGPLWEF 3L I37 'EGIGGTIPH 0.000 TableXII-V7C-HLA-A3-9mers. 49 PLSTPPPPA 0.030 28 GWEKSQFLE 0.000 98P4B6 [4 VILDLSVEV 10030 8 LGKIILFLP 0.000 Each peptide is a portion of SEQ ID 145 GTLSLAFTS I 0.027 33 QFLEEGIGG 0.00-01 NO: 15; each start position is 42 QQDRKIPPL II 0.027 40 GGTIPHVSP 1 0 specified, the length of peptide is 9 3 1 HTNGVGPLW 0.022 amino acids, and the end position STPPPPAMW I39]._ IGGTIPHVS 01 oooo for each peptide is the start position [ STPPPPAMW 0.022 25 IKKGWEKSQ 0.000 _ plus eight. I 133 ,LLRLLKSQ I0022 30 EKSQFLEEG 1 0.000I Subsequene F 351 IVLPIEWQQ 0.020 20 I RKLKRIKKGI 0.000 167[ KLETIILSK 127.oo0 f3 II VLPIEWQQD 0.020 36 EEGIGGTIP 0.000 I 159 I FLGSGTWMK 60.000 72T 1 ILSKLTQEQ 0.020 22 LKRIKKGWE 00 17 KLTQEQKSK 30.000 14 ASGTLSLAF 10020 I44 II PHVSPERVT 0.00 31 GLSEIVLPIt 2300 91 SVEVLASPA 0.020 129[ PLWEFLLRL 15 371 LLKSQAASG 0020 157 WO 03/087306 PCT/USO3/10462 TableXII-V7C-HLA.A3.-9mers. TableXII-V7C.HLA-A3-9mers- TableXIl-V1-HLA-A3-10-98P4B6 98P4B6 9BP4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is specified, the length of peptide is 9 specified, the length of peptide is 9 10 amino acids, and the end amino acids, and the end position amino acids, and the end position position for each peptide is the start for each peptide is the start position for each peptide is the start position position plus nine. plus eight, plus eight. Iti Subseque Score Start Subsequence I Score . ,Start Subsequence Score I 100 SLWDLRHLLV 2.000 82 I G SQIPWGW .051 182 SKHCMFSLI 10.0021 76I VTHHEDALTK 2.000 179 1 EQKSKHCMF i 0.018 160 LGSGTWVVMKL 0.002 3701 LLSLLAVTS 1.800 I 59 I WTEEAGATA ]0.0 115 SWRNPVLPH 0.002 LASLFPDSL 1 831 QPVVGWT 0015 3~31 SEIVLPIEW 0.002 304 QLGLLSFFFA ].800 152 TSWSLGEFL 10015 791 SSSSQIPW 0.0021 15 ALNWREFSFI 1~.oI S176 LTQEQKSKH SPDRALKAA 1 0.002 435 ALVLPSIVIL 1.350 73 GIRNKSSSS 0.012 6L_57 ATAEAQESG 0.0021 3 KQLGLLSFFF 1j.21 141 QAASGTLSL 0012 64 GATAEAQES 0.001 I 7 I LLSFFFAMVH 1.200 1461 KIPPLSTPP 0.009 29 RGGLSEIVL 110.001 1442 VILDLLQLCR 1.200 110Ii EVLASPAAA ]3 1 ANSWRNPVL 280.001 I81 WLQCRKQLGL 1r. 1 I PESPDRALK 0[.009 1 SQAASGTLS II 0.001 365 IMSLGLLSLL 0900 l-00I IDPPESPDR 0.006 410 VLIYGWKRAF 0.900 S"112I AANSWRNPV 10.006 r141 SLIVKGFNW 09 r170I TIILSKLTQ 10.006 TableXll-V1-HLA-A3-10-98P4B6 20 RLFTLWRGPV 0 900R F1201 VLPHTNGVG 0.006 Each peptide is a portion of SEQ ID 25 8 TLPIVAITLL 0.900 S66 pTAEAQESGI 0.006 NO: 3; each start position is specified, the length of peptide is 1 NQYPESNAEY 0.900 26 NILRGGLSE_ 0.006 10 amino acids, and the end I278 AAYQLYYGTK I09 127 VGPLWEFLL 1 0.005 position for each peptide is the start 364 1 GIMSLGLLSL 0.810 I 24 GANILRGGL 0 005 position plus nine. 4271 YTPPNFVLAL 0.810i 142 AASGTLSLA 0.005 startI Subsequence Score 20 ISLATFFLY I 81 SsQ0PVVGV 06151 I13 I SLFPDSLIVK 11450000 22 1 SLATFFLYS ]j.

72 52 TPPPPAMWT 10.005 QLYYGTKYRR 6000 257[ KTLPIVAITL 060 I 3 IVILDLSVE 0.005 i34 GVIGSGDFAK 40.5001 1 FLNMAYQQVH I 11711 IILSKLTQE 056 275 LLAAAYQLYY 124.000 268 SLVYLAGLLA I60 119 PVLPHTNGV 0 21.00571 WLETWLQCRK 1 20.000 3241 PMRRSERYLF 00 I99 I SIDPPESPD 0.005 1 GLLAAAYQLY 118.000 8 ALTKTNIIFV 0.0 168 LETIILSKL I 0.004 CLPNGINGIK 90001 1367 1SLGLLSLLAV 1600 17]! AAAWKCLGA 0I0 21I GINGIKDARK 19.000 20311 NLPLRLFTLW I6 F671 AEAQESGIR 0.004 I ] GLLSFFFAMV 81001 166 YICSNNIQAR I0.600 I_108 RALKAANSW 0.003 271 YLAGLLAAAY 60ooo 219 AISLATFFFL 0.4 SSPAAAWKCL 10.003 11 ILIDVSNNMR 1 6000 F471 I NWSAWALQL .O540 1861 WGVVTEDD 0.003 I 443I ILDLLQLCRY I 1 SAWALQLGPK 150 SAWALQLGPK 0.450 1 77 TQEQKSKHC 0.003 122741 FLYSFVRDVI ]1 4.500 I WIGSRNPKF I 0, 114 ASPAAAWKC 0.003 2101 TLWRGPWVA 4.500 56 r 0 4507 1 APAAWKCII ~o'31 2ml I 417 RA FEEEYYRF 0.40 I' 89 VVTEDDEAQ I 322 CLPMRRSERY 1[400 417 RAFEEE 45 I I LTIRLIRCGY 04 ] 11541 WSLGEFLGS I0.003 155T HIGSRNPK 3.000___ 21 WVAISLATF 0.O4507 L1~3 KSQAASGTL 0.003 402] ALLISTFHVL 2.700 178 VAISLATF 4 157l GEFLGSGTW I 0.003 I [ LLSLVYLAGL 1 2,700QLNF I 5035I LSTPPPPAM 110.002 403 1 LLISTFHVLI !2,700 1 O II S1160 l_3 _ll EIL IJ F4371 VLPSIVILDL rI35708 EMYISFGIMS I 34 EIVIPIFE 0.0I 1 MVHVAYSLCL 036 8 1 PVVGVVTED 40.002 04I LISTFHVLIY 2.400 [4[ M WHVLC 48 RFRCYH 0.300 78 SSSSSQIPVI 0.002 107 ILLVGKILIDV 025 RLIRCGYHw 158 WO 03/087306 PCT/USO3/10462 TableXIi-V-HLA-A3.-10-98P4B6 position plus nine. TableXll-VSA-HLA.A3-10mers. Each peptide is a portion of SEQ ID Start Subsequence Score 98P4B6 NO: 3; each start position is 22 CLSLPSSWDY 1 2.000 Each peptide is a portion of SEQ ID specified, the length of peptide is 8 ALSLSLSSGF 2000 NO: 11; each start position is 10 amino acids, and the end specified, the length of peptide is 10 position for each peptide is the start 24 SLPSSWDYRC J 1.800 amino acids, and the end position for position plus nine. F5 II GLQALSLSLS I0 .180 each peptide is the start position plus Start[ Subsequence I Scoe [12[ SLSSGFTPFS I .2 nine. 317 VAYSLCLPMR 0.300 10 I SLSLSSGFTP 0.060 Fstart II Subsequence Score 331 YLFLNMAYQQ It .3 3 PPCPADFFLY O.057 8I FTFWRGPVVV 0.050 313[t AMVHVAYSLC o.300 [11 LSLSSGFTPF 0.045 4 1 PLRLFTFWRG 0.018 373 LLAVTSIPSV [0.00 I 23 LSLPSSWDYR 0.045 i1 ENLPLRLFTF 0.012 2691 LVYLAGLLAA[ 0.300 33 II CPPPCPADFF i0049 iITFWRGPWVA 0 .05 440 SIVILDLLQL 0.270 1 36 PCPADFFLYF 0.036 10 FWRGPWVAI .004 2221I LATFFFLYSF 0.270 I321 RCPPPCPADF 0.030 7II LFTFWRGPW =00 I154PLGP KDASR 0270 2 GSPGLQALSL 002i I1 LRLFTFWRGP 0.000 L8 'KTNiiFVAIH 10.270 14 I SSGFTPFSCL 0.013 3_ RIEMYISFGI 116I[ GFTPFSCLSL 0.005 406& STFHVLIYGW 13 02 LSSGFTPFSC 0.005 396[ STLGYVALLI 01203 18I TPFSCLSLPS 0.004 432 FVLALVLPSI 10.203 6 LQALSLSLSS I 0.002 217 WAISLATFF ] 0.200 34 IPPPCPADFFL "0.002 1433 VLALVLPSIV I0.200 17 FTPFSCLSLP 0.002I-VB-HLA-A3-1 39 FSFIQSTLGY 0.2001 FSCLSLPSSW 0.001 98P4B6 S3691 GLLSLLAVTS 0.180 3 SPGLQALSLS 0.001 Each peptide is a portion of SEQ ID 12241 TFFFLYSFVR 1 0.180 15 I SGFTPFSCLS 0 .001 NO: 11; each start position is I 49 LIRCGYHWVVI 0.180 [27 SSWDYRCPPP 0.001 specified, the length of peptide is 1_01 DRHLLVGKi j 0.162 21 SCLSLPSSWD I 000 10 amino acids, and the end 103 DLRHLLVGKI 0.2 2 L S SWD 00 position for each peptide is the start i11 KILIDVSNNM 0.135 7 QALSLSLSSG 0.000 position plus nine. 24 1 KIPIEIVNKT 10.135 [9j LSLSLSSGFT o0.000oo StartI Subsequence Score 21 ITLLSLVYLA I 0.13 28I SWDYRCPPPC II .0 20 I ELELEFVFLL 4.860 I5 i SMMGSPKSLS I0.135 4 PGLQALSLSL II 0.000] 221 ELEFVFLLTL I 1.620 I1131 LIDVSNNMRI 0.2 129 WDYRCPPPCP 0.00 I 18 QTELELEFVF 0 0300 2621 VAITLLSLVY ] 0.120] 30 DYRCPPPCPA .000 [ FSFIQIFCSF ! 1 372 SLLAVTSIPS " 0.120 1 SGSPGLQALS 0000 i ! DTQTELELEF 0.0o6o0 3971 TLGYVALLIS "II 0.120 f31 YRCPPPCPAD 0.000 "9 QIFCSFADTQ 0.030 1571 GPKDASRQVYW ] 0120 2 PSSWDYRCPP I .ooo 1 CSFADTQTEL I0.015 _17 i IQARQQVIEL 0.108 251 LPSSWDYRCP 0.000 8 I IQIFCSFADT IF0.013 1243 1 QQSDFYKIPI 0.108] 19 PFSCLSLPSS I0 o.000oo 2 3 LEFVFLLTLL 0.013 -347 NSWNEEEVWR 0.100 117 TQTELLEFV 0.013 39 GDFAKSLTIR I0.090 TableXIII-V5A-HLA-A3.-10mers- F19 TELELEFVFL 0.012 I21781 VAISLATFFF [ 0090 98P4B6 I 14 I FADTQTELEL I 0.012 384 NALNWREFSF 0.090 Each peptide is a portion of SEQ ID 2 I WREFSFIQIF 10.009 285 IGTKYRRFPPW 0.090 eI NO: 11; each start position isREFSFIQIFC specified, the length of peptde is 10 i 3 IF REFSFIQIFC if 0.009 amino acids, and the end position for 2 I LELEFVFLLT I .06 TableXIII-V2.HLA-A3-10mers. each peptide is the start position plus 7 IF FIQIFCSFAD I 0.006 98P4B6 nine. NWREFSFQI 0.005 Each peptide is a portion of SEQ ID [Start Subse uence Score 6 SFIQIFCSFA IF0.001 NO: 5; each start position is L0I RLFTFWRGPV 2I EFVFLLTLLL f 51 specified, the length of peptide is NLPLRLFTFW 0.600 I FFT - 10 amino acids, and the end 11 FCSFADTQTE 1l 0.000 position for each peptide is the start I LPLRLFTFWR 0.540 159 WO 03/087306 PCT/USO3/10462 TableXIII-VSB-HLA-A3-10mers. TableXIII-V6-HLA-A3.10mers. amino adds, and the end position for 98P4B6 98P4B6 each peptide is the start position plus Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID nine. NO: 11; each start position is NO: 13; each start position is Subsequence Score specified, the length of peptide is specified, the length of peptide is 10 5 MAYQQSTLGY 0400 10 amino acids, and the end amino acids, and the end position for QQST position for each peptide is the start each peptide is the start position plus 20 FLNMAYQQST 0.3 position plus nine. nine. STLGYVALLI 03 Start SubsequenceI score Start[ Subsequence 11Score QSTYALL ]0.0 1 FCSFADQT I 0000 F29 GWEKSQFLEE I 0.000 i NMAYQQSTLG 0020 I4~1 EFSFIQIFCS 000 F37[ EEGIGGTIPH 0.000 L218 115 ADTQTELELE 0.0 30I WEKSQFLEEG 00 8 QQSTLGYVAL 0.018 13 SFADTQTELE J 211 RKLKRIKKGW I 0.000 -3 0.002 14[ PSIVILGKII 0.000 1 AYQQSTLGYV 0.0 . TableXIII-V6-HLA-A3-10mers- 1 38I EGIGGTIPHV 0.000 1 il FLNMAY[QQS 0.0l 98P4B6 14 LFLPCISRKL ]0.000 Each peptide is a portion of SEQ ID 41I GGTIPHVSPE [.000 TableXIII-V7C-HLA-A3-10mers NO: 13; each start position is 2 KRIKKGWEKS . 98P4B6 specified, the length of peptide is 10 -24 Each pepde is a poion SEQ ID amino acids, and the end position for F1 EKSQFLEEGI 0.0 NO:15; ach peptide is at position of SEQ ID

-

NO: 15; each start position is each peptide is the start position plus F 44 I IPHVSPERVT 0.000 specified, the length of peptide is 10 nine. 34 I QFLEEGIGGT 0.000 amino adds, and the end position for Start Subsequence Score I 32 KSQFLEEGIG 0.000 each peptide is the start position plus 131 ILFLPCISRK 150.000 36 LEEGIGGTIP 0.000 nine. 1 .VLPSIVILGK 90.000 45 PHVSPERVTV ''.00 St art I Subsequence Score -1511 FLPCISRKLK i10.000 40 IGGTIPHVSP I0 131 VLASPAAAWK I2000 1 42 GTIPHVSPER 7 2,025 [ SRKLKRIKKG 173 1 ILSKLTQEQK I 20.000 121 IILFLPCISR [ 71.800_ VLPEWQQDR I 2oI 16 1 IVILGKIILF 0 900 TableXIII-V7A-HLA-A3-10mers- 1681 KLETIILSKL 4.050 7 VILGKIILFL 0.608 98P4B6 ( 1271 GVGPLWEFLL I 2.430 I35 FLEEGIGGTI ji 0405 Each peptide is a portion of SEQ ID L 160 FLGSGTWMKL I 1.200 lI19 (SRKLKRIK 0.200 NO: 15; each start position is 100l SIDPPESPDR 0.600 181 CISRKLKRIK 0.200 specified, the length of peptide is 176 1 KLTQEQKSKH I0.600 10 amino acids, and the end LPIEWQQDRK 11 S___L_'_'_' ... }"11_80)1 position for each peptide is the start 387- .GWM RI 450 I 8 ILGKIILFLP f0.135 position plus nine. 164 GTWMKLETII 0.40__ 461 HVSPERVTVM i 0.090 I Start I Subsequence Scr 134 1 FLLRLLKSQA I 0.300 16 LPCISRKLKR 0.080 1 0i FLPNGINGIK 19.000 L 6 1 ILDLSVEVLA II 0.300 12311 LKRIKKGWEK 11060 51 SLSETFLPNG 013 281 ILRGGLSEIV j 0.300 1I LVLPSIVILG 0.041 1 GSPKSLSETF 0.0 VILDLSVEVL T7 0.270 1391 GIGGTIPHVS 0271 2_ I SPKSLSETFL 0.006 129 GPLWEFLLRL II 0.243 I 43 11 TIPHVSPERV 0.020 61 LSETFLPNGI 0.003] 1i671 MKLETIILSK 01.203 22 j KLKRIKKGWE .0181 7 I ETFLPNGING 0003 32 GLSEIVLPIE 0.203 11I KIILFLPCIS 0.018 4] KSLSETFLPN 0 -135 - LLRLLKSQAA j0.200 '10 I GKIILFLPCI 0o.0o125 9 TFLPNGINGI ].0 ~I SLGEFLGSGT ]I0.150_ 33 SQFLEEGIGG 0.006 1 SETFLPNGIN 0.000 58 AMWTEEAGA 0.150 3 LPSIVILGKI PKSLETF 146I GTLSLAFTSW 10.135 ?26 l JKKGWEKSQF 0,003 S 27l NILRGGLSEI 0.135 2 IRIKKGWEKSQ If 0.003 l' 166 WMKLETIILS 0.120 Fi27 KKGWEKSQFL 0.002 TableXllI-V7B-HLA-A3-10mers- I 47 TLSLAFTSWS {0.120 28 KGWEKSQFLE 01001 LLKSQAASGT 0.100 F9 LGKiILFLPC o.001 Each peptide is a portion of SEQ ID I 130 1 PLWEFLLRLL IT FI C 1 NO: 15; each start position is 4 S 17 PCISRKLKRI 001_ _ specified, the length of peptide is 10 0.0_8AASGTLSLAF 0 160 WO 03/087306 PCT/USO3/10462 TableXIl.-V7C.HLA-A3-.10mers. TableXIIl-V7C-HLA-A3-10mers- TableXIV-V1 -HLA-A1101-9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position for amino acids, and the end position each peptide is the start position plus each peptide is the start position plus for each peptide is the start position nine. nine. plus eight. Start Subsequence Score Start Subsequence I Score Start Subsequence Score S110 ALKAANSWRN 0.060 78 KSSSSSQIPV i 0.006 249I KIPIEIVNK 1.200 S109] RALKAANSWR 0.060 122 LPHTNGVGPL 0.005 351 VIGSGDFAK 1.200 6611 ATAEAQESGI 0.045 31 S3 IILDLSVE 0.005 751 RQQVIELAR 0.720 111 NSWRNPVLPHI 0.045 36 IVLPIEWQQD 4107005 417 RAFEEEYYR 0.480 159 I EFLGSGTWMK[ I041 123 CLGANILRGG I0 005 3 1 SISMMGSPK [4 131 LWEFLLRLLK 0.040 171 TIILSKLTQE 0005 YQLYYGTK 0[ 400 141 I SQAASGTLSL 0.036 3 f817 SSSQIPVVGV 0.005 136 LFPDSLIVK :400 1152 FTSWSLGEFL 10.030 22 1 i KCLGANILRG I 0004 [3 1 SVSNALNWR I PLSTPPPPAM o.0301 [35[ EIVLPIEWQQ 0.004 241 RNQQSDFYK 0.360 1137 RLLKSQAASG I O030 119 1 NPVLPHTNGV 0.003 [282]1 LYYGTKYRR 0320 4 IVILDLSVEV I 0030 1621 GSGTWMKLET IF 0.003 225 FFFLYSFVR 0.240 111 AAWKCLGANI ]I0.030 142 QAASGTLSLA 00o 2 -Gl GINGIKDAR ]0240 1125 TNGVGPLWEF 0 .0o]27 124 HTNGVGPLWE I 0.003 53 GYHWIGSR 0"'240 42 WQQDRKIPPL 0.027 F 90 VVTEDDEAQD II0.003 87 NIFVAIHR [0~24I S182 1 KSKHCMFSLI 0 i'027 172 IILSKLTQEQ [ 0.003 1 F-[ 7 LPNGINGIK 0,200 31 I GGLSEIVLPI 0. 024 181 QKSKHCMFSL I 0003 4143 ILDLLQLCR 0.1 T60 128 VGPLWEFLLR 0.024 91I LSVEVLASPA o 0002 1 DLRHLLVGK F 0.120 52 oSTPPPPAMWT 0022] 5 LSTPPPPAMW 1 0.0_[ 3 GVIGSGDFA 0,090 1031 PPESPDRALK 0.020 87 - WGWTEDDE [ 002 [322 CLPMRRSER 0 ,080 7-11 SVEVLASPAA ]0 020 [0]LSEIVLPEW 11 LIDVSNNMR 008 1 149 SLAFTSWSLG I 020 [-91I VTEDDEAQDS 0002 I QLGPKDASR 0.00 112 11 VLPHTNGVGP 0020 i 165 TWMKLETilL I0 0012 I3[ AYSLCLPMR 0080I [11211 KAANSWRNPV I 0.018 297 LRGGLSEIVL 0 2691j LVYLAGLLA 0.080 11751 SKLTQEQKSK 110.015 701 AQESGIRNKS 0 0 281 " QLYYGTKYR 0080I 114811 LSLAFTSWSL 0,013 11321 WEFLLRLLKS 1 0002 294 WLETWLQCR 0 08I 1 V2 EVLASPAAAW 10.013 1 [43 1 QQDRKIPPLS F 0.002 [97 ' HYTSLWDLR 0080 [8 U DLSVEVLASP 1 0.013 1 92-- TEDDEAQDSI I 0.002 295 LETWLQCRK 0.060 1691 EAQESGIRNK II 0.013 " 791 SSSSSQPVV 10002] 441! IVILDLLQL 0.060 174 II GIRNKSSSSS 0.012 60 1WTEEAGATAE II 0002 306 GLLSFFFAM 0.054 67 TAEAQESGIR I 0.012 153 j TSWSLGEFLG 0002 99 REIENLPLR 0.054 [831 SQIPWGVVT 0.010 15 ASPAAAWKCL j 00 22[ INGIKDARK 0040 89 11 GVVTEDDEAQ I0.009 148 WSAWALQL ] 0.040 [47 KIPPLSTPPP 0.009 TableXIV-V1.HLA-Ai101-9mers- 77[ THHEDALTK 0040 [1147 LASPAAAWKC 0.009 I 98P4B6 108i LVGKILIDV 0540 S158 I GEFLGSGTWMI 0.009 Each peptide is a portion of SEQ ID 22~3 AFFLYS c040 121 II WKCLGANILR I 00 NO: 3; each start position is 1 2171_ WKCLGANI_ 08 specified, the length of peptide is 9 261 IVAITLLSL 040 177 II LTQEQKSKHC 1 . amino acids, and the end position [18 ICSNNIQAR 0040 I 1179 I QEQKSKHCMF 0.006 for each peptide is the start position [164 QWiCSNNI 0.0[40 113 11 AANSWRNPVL [ 0.006 . plus eight. 143 SLTIRLIR I 0.036 184II QIPWGVVTE I 0.006 Sta rt Subsequence Score 23 RDVIHPYAR 0.036 178 Jj TQEQKSKHCM 0.006 E 56 WIGSRNPK 3.000 4 RLIRCGYHV 1 0.036 I15[ LAFTSWSLGE 0 0.006 409 IHVLIYGWKR 1.200 [ ] GLLAAAYQL 0.036 161 WO 03/087306 PCT/USO3/10462 TableXIV-VI-HLA-A1101-9mers- TableXlV-VI.HLA-A1101.9mers.- TableXIV-V2-HLA.Ai01.9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3; each start position is NO: 3; each start position is NO: 5; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight. plus eight. plus eight. Start I ubsequence [Score ISta Subsequence Score S[ tart Subsequence Score 330 RYLFLNMAY I0.036 1 SLATFFFLY 0.012 18 TPFSCLSLP 0 .00 48 0.030 427T YTPPNFVLA 0.010 2Iol 51 LPSSWDYRC 0.000 15FLI[ KTNIIFVAI 930] 1 l GTKYRRFPP 09009 [ 1 LSLSLSSGF I10.000 436 LVLPSIVIL 0.030 1280 YQLYYGTKY o 009 1 SGSPGLQAL 0.000 303 KQLGLLSFF II 0027 I-397 TLGYVALLI 0.008 1 31 YRCPPPCPA 0.0[00 353 EVWRIEMYI ]0.024 367 SLGLLSLLA 110008 34 PPPCPADFF .o] 1I DLGSLSSAR I0.024 166i YICSNNIQA 0.008 3-07 DYRCPPPCP 0.000 ]254 r IVNKTLPIV J 1 258 TLPIVAITL 0.008 1 11 LSLSSGFTP oa 190101 FVAIHREHY I0.020 317 VAYSLCLPM 0.008 14 SSGFTPFSC 0.0 [151 AWALQLGPK J 0.020 o 100 67I SLWDLRHLL 0.008 1 GSPGLQALS I 0.00ooo0 831 LTKTNIIFV 1 0.020 [210 TLWRGPWV 10.08 191 PFSCLSLPS [ 0.00 [98 1 YTSLWDLRH 0.020 3651 IMSLGLLSL j008 [29 WDYRCPPPC 0.000 231 FVRDVIHPY 10"020 263 AITLLSLVYW 0.008 27 SSWDYRCPP 0.000 400 YVALLISTF I0.020 36011 YISFGIMSL I 3i LSSGFTPFS 0.000 21 WVVAISLATF 0.020 20 ]FSCLSLPSS 0 o S402 ALLISTFHV .018 i TableXIV-V2-HLA-A101-i9mers- 281 SWDYRCPPP I[0.00 [64 KFASEFFPH 0.018 98P4B6 4 PGLQALSLS f . 140 SLIVKGFNV I0.018 Each peptide is a portion of SEQ ID 26 PSSWDYRCP 0.0 214_ GPVWAISL 0.018 NO: 5; each start position is specified, the length of peptide is 9 35 I SLFPDSLIV 0.016] amino acids, and the end position TableXIV-VSA-HLA-A 1101-9mers S205 PLRLFTLWR 0.016 for each peptide is the start position 9BP4B6 209 FTLWRGPW 0.015 plus eight. Each peptide is a portion of SEQ ID 264 ITLLStart I Subsequence Score NO: 11; each start position is ( ~396 ~i2 STLGYVALL F 015 [ SL PSSWDYR l o specified, the length of peptide is 9 _396_ S L Io5amino acids, and the end position 319 YSLCLPMRR L 0.012 1 GLQALSLSL f0024 I or each peptide is the start position 394l IQSTLGYVA 17t1 FTPFSCLSL 0.020 plus eight. F 30 KVTVGVIGS I .21 II SPGLQALSL 0.004] Start Subsequence I F270 I VYLAGLLAA 1 SLSSGFTPF 0.004 3 PLRLFTFWR II 0.024 1 2031 NLPLRLFTL ]37 L l CPADFFLYF I.0 7 1 FTFWRGPVV I 0.020 425 1 RFYTPPNFV 0 .012] [ 2 1 SCLSLPSSW 00 __I1 NLPLRLFTF 0.012 242 NQQSDFYKI I0.012 CPPPCPADF I .002 8 TFWRGPVVV 0.004 287 KYRRFPPWL I0.012 ] r23 LSLPSSWDY I 2 LPLRFTFW 0.003 435 II ALVLPSIVI 10.012 6-1 LQALSLSLS I0001 6 II LFTFWRGPV I 0.002 I265 TLLSLVYLA I0.012 16 i GFTPFSCLS I .0 r 5 II RLFTFWRGP 0.000 | 299 J LQCRKQLGL1 0.012 32 RCPPP 0.001PAD I 9 II FWRGPWVA I 0.000 313 I AMVHVAYSL F 0.012 36 1 PCPADFFLY I 0.00 14 LRLFTFWRG I 0.000 40 DFAKSLTIR 0 35 1 PPCPADFFL I I 0.001 o6il HLLVGKILI 00] [17 QALSLSLSS !0001I TableXIV-V5B-HLA-A11-9mers I42 FYTPPNFVL SLSLSSGFT .0OO 98P4B6 S385 ALNWREFSF 0 012 5 II SGFTPFSCL I Each peptide is a portion of SEQ ID r219 1 AISLATFFFJ 0.012 221 CLSLPSSWD specified, the length of peptide is 9 I 304 ! QLGLLSFFF 0.012 8 I ALSLSLSSG I 0.00 amino acids, and the end psition 162 WO 03/087306 PCT/USO3/10462 for each peptide is the start position TableXIV-V6-HLA.A11i01-9mers. TableXIV-V7AHLA.AI 101-9mers plus eight. 98P486 98P4B6 ista Subsequence Score Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID 24 FVFLLTLLL 0.Io8 NO: 13; each start position is NO: 15; each start position is S6[ TQTELELEF ] 012 specified, the length of peptide is 9 specified, the length of peptide is 9 -- .2.. _4011 amino acids, and the end position amino acids, and the end position 17 QTELELEFV II 0.010i for each peptide is the start position for each peptide is the start position 6 j FIQIFCSFA ] 0.004 plus eight. plus eight. 2 ] REFSFIQIF 0.004 I Start[ Subsequence 1[ Score Star7t][ Subsequence Score 5 SFIQIFCSF 0.003 21 1 KLKRIKKGW ] 0.006 SPKSLSETF 0.002 l7 IQIFCSFAD I 0.003 4 11 GTIPHVSPE I0005 4 SLSETFLPN 0. 001 _ 18 _ TELELEFVF 0003 r 4 SIVILGKII i 0.003 7 ET--FLPNG 0.001 20 ] LELEFVFLL 0.003 18 ISRKLKRIK f 0002 [ 8 TFLPNGING 0.001 22 LEFVFLLTL 0.002 [ 17 . CISRKLKRI 10.002 6 SETFLPNGI 0.001 12I SFADTQTEL 1 0.002 43 IPHVSPERV t0.002 13 KSLSETFLP [0.000 r 1 ELELEFVFL 0.00 321 SQFLEEGIG ] 0. 001 1 2 ! PKSLSETFL 0.000 i2311 EFVFTLL 1 24 RIKKGWEKS 0.001 5 I LSETFLPNG 0.i 00 8 QIFCSFADT i0.001 27 KGWEKSQFL 0.001 1 11471 ADTQTELEL 1 0.000 1I VLPSIVILG 0.001 TableXIV-V7B-HLA-A1101-9mers 1 WREFSFIQI [ 0.000 1 1 26, KKGWEKSQF 0.001 98P4B6 15 I DTQTELELE I 000 L11 IILFLPCIS 0.001 Each peptide is a portion of SEQ ID L21I ELEFVFLLT 0.0000 33 QFLEEGIGG 0.001 NO: 15; each start position is l Ispecified, the length of peptide is 9 9 IFCSFADQ 0.000 31 KSQFLEEGI .1 1 amino acids, and the end position S13 I FADTQTELE 0.000 35 I LEEGIGGTI 0.001 for each peptide is the start position 1i FCSFADTQT l0.000 i 14I FLPCISRKL 0.000 plus eight.

' 4 FSFIQIFCS 1.0 34 [FLEEGIGGT 10.000 Start I Subs equence Score 3 EFSFIQIFC VSPERVTVM 09 STLGYVALL 0.015 1I 17 CSFADTQTE 0 9[ GKIILFLPC t0.000 7 QQSTLGYVA I0.012 28 " GWEKSQFLE 0.000 5EII AYQQSTLGY )I0.0083 TableXIV-V6-HLA.A1101-9mers- 371 EGIGGTIPH i 16 YQQSTLGYV l 006 98P4B6 291 WEKSQFLEE 1. o3I NMAYQQSTL 0.004 Each peptide is a portion of SEQ ID 8 1 LGKIILFLP 0000 1 II MAYQQSTLG 0.000 NO: 13; each start position is 40 GGTIPHVSP 0000 1 specified, the length of peptide is 9 8 GTPHVSP 11 0000 1 II FLNMAYQQS 19 amino acids, and the end position 2 RKLKRIKKG 1 II QSTLGYVAL 0.000 for each peptide is the start position 3 PSIVILGKI 0 000 2 L NMAYQQST 0.000 plus eight. 22 LKRIKKGWE 0 000 Start Subsequence Sco 39 IGGTPHVS 1 000 TableXIV-V7C-HLA-AI101-9mers [ LPSIVILGK 6 0.400EGIGGTIP I I 98P4B6 12- ILFLPCISR 0[2 2 IKKGWEKSQ 0.000 Each peptide is a portion of SEQ ID I 00 30 NO: 15; each start position is 3 I. LFLPCISRK 0.300 [30 EKSQFLEEG 11 0.000 specified, the length of peptide is 9 S23 I KRIKKGWEK II 0.180 44 IPHVSPERVT 00 amino acids, and the end position F115 LPCISRKLK o 0.100 or each peptide is the start position 142 I TIPHVSPER [.08o TableXIV-V7A-HLA-AII01-9mers- pluseight. 5 IVILGKIIL 1 0.0098P4B6 Start Subsequence I Scorel 19 SRKLKRIKK II0.040 Each peptide is a portion of SEQ ID F167 KLETIILSK T 2.400] J45[ HVSPERVTV 0.0 NO: 15; each start position is 159 FLGSGTWMK 0.8001 F10 7 KIILFLPCI 0.018 specified, the length of peptide is 9 F1751 KLTQEQKSK 0100 amino acids, and the end position 21 IKCLGANILR I0.360 I. 16 1I PC!SRKLKR [1 0.012]= for each peptide is the start position I . VILGKIILF [0012 plus eight. 1 GPLWEFLLR 0.360 1387I GIGGTIPHV I 0.012 Start Subsequence 1Score 1 WEFLLRLLK I0.240 7 ILGKllLFL I0.008 FLPNGINGI 0004 13 LASPAAAWK I 200 163 WO 03/087306 PCT/USO3/10462 TabeXIV-V-HLAA1101-9mers TabeVleXIV-VCHLAV7C-HLAAIA1101-mers ab- TableXIV-V7C-HLA-AI101-9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight, plus eight. plus eight. IStart Subsequence - Start Subsequence Score Sub sequence Score i88 GVVTEDDEA 01090 1861 WGVVTEDD 0.002 72 IL-SKL-TQEQ 0.000 I109 j ALKAANSWR 0. 080 142 AASGTLSLA 0.002 I 115 II SWRNPVLPH 1 0.00 691 AQESGIRNK 0.06 1121 AANSWRNPV o.002 [99 SIDPPESPD 000j 11631 GTWMKLETI I 811 KSKHCMFSL 0.2 4911 LAFTSWSLG ]0.000 3711 LPIEWQQDR 03 066 13 6 RLLKSQAAS II 0.002 113 AN-SWRNPVL [000 126 GVGPLWEFL i 0.060 179 EQKSKHCMF 0.002) 155 SLGEFLGSG 0.000 38 PIEWQQDRK] 040 331 SEIVLPIEW 0.002 1371 LLKSQAASG 0.000 [ !2GLSEIVLPl 19 IPLWEFLLRL 0.002] 120l VLPHTNGVG 0000 S173 r LSKLTQEQK J020 170 TIILSKLTQ 0001 1 I 71 SSSSSQPV I 9 11 SVEVLASPA 2 I 731 GIRNKSSSS 1I0.001 r145 GTLSLAFTS 1 21911 RGGLSEIVL 0.001 TableXV-VI-HLA.A1101-1Omers 2 21 SIVILDLSV 467 KIPPLSTPP I0.001 98P4B6 6F AEAQESGIR 41 WQQDRKIPP 0.001 Each peptide is a portion of SEQ ID 151 i FTSWSLGEF 0 0.10 26 NiNLRGGLSE [.0 NO: 3; each start position is 17 LTEQKSKH _ _ SPDRALKAA J0.001 specified, the length of peptide is 10 176 LTQEQ H 1[ 5 ] amino acids, and the end position for 51 STPPPPAMW 0.010 65 ATAEAQESG 0.001 l each peptide is the start position plus I 59 ! WTEEAGATA 15 11 SPAAAWKCL l0.1 00 nine. 1123 HTNGVGPLW j 901 VTEDDEAQD I.01 Start Subsequence Score 1 ! EVLASPAAA 0.0 1589 EFLGSGTWM .1_ 34 GVIGSGDFAK 27.0001 8211 SQIPWGVV lo VEVLASPAA 1 0.0011 [ HI WIGSRNPK 3.000I 108ii RALKAANSW 1 0009 12211 CLGANILRG 0.001 76 1 VTHHEDALTK 2.000I 57 AMWTEEAGA 0 008 185 CMFSLISGS 0.001 135 'SLFPDSLIVK 1.600 116511 WMKLETIIL 1008] 18411 HCMFSLISG 000 21 1 GINGIKDARK 1.0 r148 SLAFTSWSL 008 127' VGPLWEF2L [0.001 [ 9 WLETWLQCRK 0.400 i4 VILDLSVEV 006 I 139 KSQMSGL 10.010 1 278 1 AAYQLYYGTK I0.400 103 I PESPDRALK [ _1125 NGVGPLWEF 1 150 I SAWALQLGPK 0.400 I42I QQDRKIPPL 0.0 [64[ GATAEAQES 0001 17 CLPNGINGIK I[0.400 i 24 I GANILRGGL 0.006 1401 SQAASGTLS 11 0.001 1 281 QLYYGTKYRR I 0320 135 I0VLPIEWQQ 0.06 1711I IILSKLTQE 0.001 442 VILDLLQLCR 0.240I I iILDLSVEVL -- 1496 AQDSIDPPE 0.00 1224 TFFFLYSFVR I0.240 i134I LLRLLKSQA j00 1 LETIILSKL 0.001 407 Il TFHVLIYGWK 0.200 i 100 IDPPESPDR 0.004 1 78[ QEQKSKHCM 0.0 114 LQLGPKDASR 18 F141 QAASGTLSL 00 10o1 DPPESPDRA I0.001 318 AYSLCLPMRR 0.160 271 ILRGGLSEI I00 164 TWMKLET 0 .000 I 1204 LPLRLFTLWR 0.120 I 146( TLSLAFTSW 49 1 PLSTPPPPA [ 0.000 112 ILIDVSNNMR 0.120 j12 LA 0.00vs w I 1871 AAWKCLGAN 0.000 2801 YQLYYGTKYR 10.090 I17 AAAWKCLGA 004 143 ASGTLSLAF 0.000257 KTLPVAITL 090 1'57 GEFLGSGTW 50 3 1150 AFTSWSLGE [0.000 303 KQLGLLSFFF 10.081 __3 IVILDLSVE 003 36[ VLPIEWQQD 0.0 i1661 YICSNNIQAR i0. 119 PVLPHTNGV 0 .00 83 69QIPVVGVVT 0[00 2691 LWLAGLLAA 0.0807 S89 9 0EDDEAQ 00 160 LGSGTWMKL I 03171 VAYSLCLPMR 0.080 166 I TAEAQESGI 10002 52_ TPPPPAMWT 0000 1 240 ARNQQSDFYK 0060 164 WO 03/087306 PCT/USO3/10462 TableXV-Vi-HLA-A 101-10mers- TableXV-V1i-HLA.Alid-1.0mers- Start [Subsequence Score 98P4B6 98P4B6 1 GFTPFSCLSL 110.012 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID [2 CLSLPSSWDY 0.008 NO: 3; each start position is NO: 3; each start position is ]r. specified, the length of peptide is 10 specified, the length of peptide is 10 LSLPSSWDYR amino acids, and the end position for amino acids, and the end position for [3 IFRCPPCPADF 0.006 each peptide is the start position plus each peptide is the start position plus [~ ALSLSLSSGF 0.004 nine, nine.[ ]i P p-- -A - " nine. -nine. 33 CPPPCPADFF 0.002 Star Subsequence I Score StartI Subsequence Score F6[ LQALSLSLSS LI ,321 LCLPMRRSER .060 45j LTIRLIRCGY 0.015 2 GSPG ALSL 0.001 1471 NWSAWALQL ] 0.060 I 209 FTLWRGPVV 0.015 F GLQALSLSLS1 0.001 J183i RQLNFIPIDL 0.054 1[409 HVLIYGWKRA 0.015 10 SLSLSSGFTP ]0 1 '364 GIMSLGLLSL [048 [ 0 FHVLIYGWKR 1 0.012 30 DYRPPPCPA ]0.001 406 STFHVLIYGW 0.040 243 QQSDFYKIPI I 0.012 17 FTPFSCLSLP 0.001 I254I IVNKTLPIVA 0.040 440 SIVILDLLQL 11.012 TPFSCLSLPS . 314 MVHVAYSLCL 0.040 1 [24 I GIKDARKVTV [.012 24 SLPSSWDYRC 0.0 316 3IHVAYSLCLPM I0404 1 QLGLLSFFFA 0.012 [ PPCPADFFLY 3568 RIEMYISFGI 0.036 145I GFNWSAWAL ]0o. 012 I E 1 PPPCPADFFL 0.001 425 RFYTPPNFVL 0.036 359 MYISFGIMSL 3 .012 6 36 PCPADFFLYF 0.000 102I WDLRHLLVGK 0.030 172 IQARQQVIEL 0II .012 I 12 SLSSGFTPFS 0.000 248 YKIPIEIVNK 0.030 [121! RINQYPESNA I 0012 111 L _M~ ~ ~ ~ 1 LSSGFP 0.000QPEN 002 56 WIGSRNPKF 0 .301 3 NQYPESNAEY 1 I SCLSLPSSWD 0.000 285 I GTKYRRFPPW I 0.030J 165 [VYICSNNIQA 012 QALSLSLSSG 0.o000 216 VVVAISLATF l0.030 1071 LLVGKILIDV T 3 PGLALSLS Ii o F, [37 SPGLQALSLS 000 1831 LTKTNIIFVA 0.030 219 I AISLATFFFL 0 012 20 FSCLSLPSSW 0.o2000 85 1 KTNIIFVAIH 0.030 268 SLVYLAGLLA 0 i 1 ISSGFTPFSCL 0.000 396 1 STLGYVALLI 0.3 376! VTSIPSVSNA 0,010 I 4i PGLQALSLSL 432 Ii FVLALVLPSI 0.03 2] ESISMMGSPK I 009 LSSGFTPFSC i0.0001 264 j ITLLSLVYLA 0.030 401 VALLISTFHV 0.009 129 WDYRCPPPCP Ii.000 I 163j RQVYICSNNI j0.027j 214 GPVWAISLA 0.009 2711 SSWDYRCPPP 00 416 KRAFEEEYYR !0.024 218 VAISLATFFF 0.009 15 SGFTPFSCLS 000 86 1 TNIIFVAIHR 0.024 3841 NALNWREFSF 1 9 LSLSLSSGFT 0 [3911 GDFAKSLTIR (0.024 [36771 SLGLLSLLAV 300081 ,1 YRCPPPCPAD 0.0001 41 RAFEEEYYRF 0.024 I 1307 LLSFFFAMVH 0.008 I 19 PFSCLSLPSS 0.00 2L RLFTLWRGPV 1 0.024 1 437 VLPSIVILDL 0.0) LPSSWDYRCP 0.000 7 -125 11 LPSSWDYRCP I .0 217 WAISLATFF 0.020 I [ 227 I FLYSFVRDVI 0.008 28 SWDYRCPPPC 0.000 [2231 ATFFFLYSFV 0.020 42 . AKSLTIRLIR 0.008 J SGSPGLQALS 0.000 400 YVALLISTFH 0I 2 113] LIDVSNNMRI ! 26[ PSSWDYRCPP I.00 261] IVAITLLSLV II 0.020 I2101 TLWRGPVVVA 10.008 I32 TVGVIGSGDF [I0.020 [1781 VIELARQLNF [. i TableXV-V5A.HLAA101-.10mers 1142 IIVKGFNVVSA 0.020 129871 WLQCRKQLGL 9 00 8P4B6 231i I FVRDVIHPYA 0.020 I 404 LISTFHVLIY I 0.008 Each peptide is a portion of SEQ ID 73 I WDVTHHEDA 0.020 82 ALTKTNIIFV 008 NO: 11; each start position is 340 II QVHANIENSW II 0.020 specified, the length of peptide is 10 amino acids, and the end position for 427 1 YTPPNFVLAL I 0.020 TableXV-2V-HLA-Ai101-10mers- ach peptide is the start position plus F399 1 GYVALLISTF 0.018 98P4B6 nine. 11 KILIDVSNNM 110.018 Each peptide is a portion of SEQID [ai "Subsequence iScore I 274- GLLAAAYQLY 0.018 NO: 5; each start position is - LP 01 specified, the length of peptide is ]l PLRLFTFWR 10 I 481 RLIRCGYHW 0.018 10 amino acids, andtheend 6 1 RLFTFWRGPV 0.024I S306 I GLLSFFFAMV 1 0.018 position for each peptide is the start 8 FTFWRGPWV 10.020] 1 0 I SLWDLRHLLV 0I o.1 position plus nine. 1 1 TFWRGPVVVA 0.004 165 WO 03/087306 PCT/USO3/10462 TableXV-V5A-HLA-Al101ii-10mers- TableXV-V6-HLA-A1101-10mers- TableXV-V6-HLA-A1101-i0mers 98P4B6 98P4B6 f98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 11; each start position is NO: 13; each start position is NO: 13; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end position for amino acids, and the end position for amino acids, and the end position for each peptide is the start position plus each peptide is the start position plus each peptide is the start position plus nine. nine. nine. SSubsequence crta rtart I Subsequence lScore Startj Subsequence ]Fre 2 NLPLRLFTFW 0.004 421 GTIPHVSPER I0.900 44 IPHVSPERVT 0.0 7 LFTFWRGPW O002 1 2- 1 VLPSIVILGK 0 0.800 IGGTIPHVSP . I1_ ENLPLRLFTF 1 0.001 1311 ILFLPCISRK I[ i41 PSIVILGKII ]. 10 _ J FWRGPWVA l 0.0o 1 IILFLPCISR 0.240 [20 SRKLKRIKKG 0.000 4 PLRLFTFWRG 0.000 15 FLPCISRKLK 1200 5I[ LRLFTFWRGP I0.6000 18 LPCISRKLKRI 0.080 16 1 IVILGKIILF I0.00 TableXV.V7A.HLA.Ai i 01 TableXV-V5B-HLA-A1101 - 191 ISRKLKRIKK 0.040 mers-98P4B6 10mers-98P4B6 F18I CISRKLKRIK I 0.040 Each peptide is a portion of SEQ ID NO: 15; each start position is Each peptide is a portion of SEQ ID 23 11 LKRIKKGWEK II 0.040 specified, the length of peptide is NO: 11; each start position is specified, the length of peptide is 46 HVSPERVVM I i 10 amino acids, and the end 10 amino acids, and the end I -- 5 1 SIVILGKIIL I 0.12 position for each peptide is the start position for each peptide is the start j 7 VILGKIILFL 110.012 o s nine. position plus nine. 1 LVLPSIVILG 0.006 [Stat Subsequence Score Start I Subsequence [ Score FLEEGIGGTI" 0004 10 - FLPNGINGIK 04 [18 QTELELEFVF I 0.030 1 TIPHVSPERV I 0.004 1 9 TFLPNGINGI 0.003 i 16I DTQTELELEF I33 SQFLEEGIGG 0.002 2 SPKSLSETFL 0.002 171 TQTELELEFV I30006 3 LPSIVILGKI 0.002 8 ETFLPNGING I0.001 14 FADTQTELEL 0 04 F1 KIILFLPCIS . 1 GSPKSLSETF 0001 201 ELELEFVFLL Io004 39 GIGGTIPHVS 01700 5 SLSETFLPNG 0.000 6 SFIQIFCSFA II0 003 8 i 6 f LSETFLPNGI l 0.000 F~~~~ ~ ~ ~ ILGKlLFL 0.001 F47 SLEFN1 .0 -22 ELEFVFLLTL 0.002 22 1 KLKRIKKGWE I1f 4J KSLSETFLPN I 0"00 24I EFVFLLTLLL I0.02 1 7GKIILFLPCI 1 [ I SETFLPNGIN 0000 7 I FIQIFCSFAD 0001 1 25 RIKKGWEKSQ 0.001 PKSLSETFLP 0000 23I LEFVFLLTLL 0001 27 KKGWEKSQFL 0.001 8 IQIFCSFADT 0.001 21 RKLKRIKKGW 0.000 TableXV-V7B-A1101-10mers. 19 I TELELEFVFLI 0.001 28 KGWEKSQFLE I0.000 98P4B6 9 IFCSFADTQ M0.001 37 EEGGGTIPH 0.000 Each peptide is asportion of SEQ ID I 37 EEGIG P NO: 15; each start position is I 3 " _F4IFI _0.001 1 LFLPCSR I0.000 specified, the length of peptide is 10 1 NWREFSFIQI 0.000 34 QFLEEGGGT 0.000 amino acids, and the end position for [12 1CSFADTQTEL 0. 26 IKKGWEKSQF 0.000 each peptide is the start position plus nine. 5 FSFIQIFCSF 0.00 1 PCISRKLKRI 0.000 S ta r t nine.quece So r 13-1 SFADTQTELE 0.000 29 GWEKSQFLEE 0.000 Start Subsequece Score 1 0 IISTLGYVALLI I0.030 S2II WREFSFIQIF II0.000 1 24 I KRIKKGWEKS 0.000 QTLGYVA ___ _______ ___ [7 YQQSTLGYVA 0.a012 11 FCSFADTQTE I 0.000 38I EGIGGTIPHV i 0.000 Qi ( F-107~~~~ lFSATT1MAYQQSTLGY 0.008 _10o9_1 IFCSFADTQT 0I .000I 41 I GGTIPHVSPE I ~o _ ll~o Q1 GGTIPHVSPE 1000[ QQSTLGYVAL 0.006 411 EFSFIQIFCS II 0.000 32 KSQFLEEGIG 0! oooo 211 LELEFVFLLT I0.00 36 LEEGIGGTIP 10.000 [ [ LNMAYQQSTL-- 0. =11 ADTQTELELE 00 3 . Y31Q T1 EKSQFLEEGI I00 [ZL F N Q 0. -- F ~2 1 FMAYQQST f 30 I WEKSQFLEEG II 0.000 4 NMAYQQSTLG 0.000 9 LGKIILFLPC 1 .1 LFLNMAYQQS 0.000 45 7 PHVSPERVTV I. 00 166 WO 03/087306 PCT/US03/10462 TableXV-V7B-A101-10mers- TabIeXV-VTC.A1101-10mers- TabIeXV-V7C-AI 101-10mers. 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end position for amino acids, and the end position for amino acids, and the end position for each peptide is the start position plus each peptide is the start position plus each peptide is the start position plus nine. nine. nine. Start Subsequence IScore Start Subsequence lScore start Subsequence S[core S0QSTLGYVALL .27 I NILRGGLSEI ]6 70 IAQESGIRNKS I0.001 [_178 1 TQEQKSKHCM 0.006 -1 i QKSKHCMFSL I 0.001 TableXV-V7C-A1101-10mers- 42 WQQDRKIPPL [.] 172- IILSKLTQEQ [0.001 98P4B6 6 ILDLSVEVLA 0~04 1_48F 1 LSLAFTSWSL 10.001 Each peptide is a portion of SEQ ID [135 LLRLLKSQAA 0 .004] 65 GATAEAQESG I 0.001 NO: 15; each start position is 1 I I specified, the length of peptide is 10 143 AASGTLSLAF 0.004 GANILRGGLES I0.00 amino acids, and the end position for 19 AAWKLGANI 97 AQDSIDPPES 0.001 each peptde is the start position plus 28 I ILRGGLSEIV 0.004F 43 1' QQDRKIPPLS I0.001 nine. 1158I GEFLGSGTWM 0.492 TEDDEAQDSI 001o [Start][ Subsequence score [36 IVLPIEWQQD 00 611 TEEAGATAEA 0.001 173 ILSKLTQEQK I0.400 1i9 I NPVLPHTNGV 10.003 179~f QEQKSKHCMF oi I13 VLASPAAAWK 1 0.400 I 124 HTNGVGPLWE 0.00] [77j LTQEQKSKHC 0.00101 [38 LPIEWQQDRK 1101 AANSWRNPVL 0.002 [147 TLSLAFTSWS I0.000 109 RALKAANSWR 1[0.180 [122 LPHTNGVGPL 0.002 [121 VLPHTNGVGP 10.000 127[ GVGPLWEFLL 1['.180 [_521 STPPPPAMWT F0 [17 " PAAAWKCLGA 1.O00oo 1 EFLGSGTWMK 180 I 9II VVTEDDEAQD 10.002 [1387 LLKSQAASGT 0.0[0 1F00 SIDPPESPDR I0.080 142 QASGTLSLA 0.002 [2] LRGGLSEIVL I 0.000 I37 I VLPIEWQQDR 1 080 [ 871 WGVVTEDDE 0o.002 53] TPPPPAMWTE 0.000 167 MKLETIILSK ~[060 I 151 I AFTSWSLGEF 0.0 14i LASPAAAWKC J0.

000 i164 [ GTWMKLETII 110.060 31 GGLSEIVLPI F8- _j QIPWGVVTE o.o00 [14611 GTLSLAFTSW 11045 [13 7 3F RLLKSQAASG ]002 50 I PLSTPPPPAM I0. 1"311_ LWEFLLRLLK 1[]0.040 22ff KCLGANILRG 0002 185] HCMFSLISGS F 5I0.000 167 TAEAQESGIR 0.040 17471 GIRNKSSSSS 0.001 [571 PAMWTEEAGA 0.000 4 I IVILDLSVEV 10030 F 47 I KIPPLSTPPP [4o.ool 19 SLAFTSWSLG [0.000 103] PPESPDRALK J[0 F 1321 GLSEIVLPIE ]0.001 33 LSEIVLPIEW I0.000 S SVEVLASPAA 1.020 _76f RNKSSSSSQI 0.001 [156 SLGEFLGSGT 10.000I [129i GPLWEFLLRL [ F [781 KSSSSSQIPV 710.001 175 SKLTQEQKSK 10.015 I 60 WTEEAGATAE I0.oo TableXVI-V1-HLA-A24-9mers. [176 KLTQEQKSKH l10.012 I 91 VEDDEAQDS 98P4B6 1141 SQAASGTLSL 10.012 3 ISQIPWGVV 0. Each peptide is a portion of SEQ ID K68 LETIILSKL 1[0O12 1170 ETIILSKLTQ 0.001 NO: 3; each start position is specified, the length of peptide is 9 _66 IATAEAQESGI 0.010 11i I VEVLASPAAA It _ amino acids, and the end position F 152 1 FTSWSLGEFL II0.010 165 I TWMKLETIIL I 0.001 for each peptide is the start position 1[2 EVLASPAAAW 0.o109 251 TNGVGPLWEF ]F0.001 plus eight. 89]1 GVVTEDDEAQ 10.009 11F 0 j ALKAANSWRN 0.001 FStart I Subsequence Score 160 1 FLGSGTWMKL 0.00 F 166 WMKLETIILS 0.001 287 KYRRFPPWL 400 .000 21 WKCLGANILR 0.008 I 1 NSWRNPVLPH 0.01 426 FYTPPNFVL 240.000 [128 i VGPLWEFLLR 110.008 F 150 LAFTSWSLGE 001 337 AYQQVHANI 105 .000 5 1 VILDLSVEVL 10.006 [58 AMWTIEEAGAT 283 YYGTKYRRF .000 112 KAANSWRNPV 10.061 I3 SIVILDLSVE 228 LYSFVRDVI 70.00 14 l FLLRLLKSQA 10.006 I 1821 KSKHCMFSLI J0.1] [390 EFSFIQSTL [ 28000 69] EAQESGIRNK 10.006 171t TIILSKLTQE 0.0 362] SFGIMSLGL 20000 167 WO 03/087306 PCT/USO3/10462 TableXVI.VI -HLA-A24-9mers. TableXVl-V1-HLA-A24-9mers- TableXVI-1-HLA-A24-9mers 98P486 I9BP4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight. .plus eight. plus eight. start j Subsequence Score Start I bsequenceS ubseque 14181 AFEEEYYRF 18.o000 128 SNAEYLASL 4.800 13717 LSLLAVTSI I1.500[ 330 RYLFLNMAY 18.000 41f FAKSLTIRL353 48 EVWRIEMYI 1.400 31 1 78 SIPSVSNAL i 37 GSGDFAKSL 4 3971 ITLGYVALLI 1.400 1124!1 QYPESNAEY I 9.900 ! R IE 173 4RQQVlE F-44.400 VLALVLPSI 1.4 "399 G ALL 9.000 300] QCRKQLGLL 4.000 1J86 NFIPIDLGS 1.260 177I QVIELARQL 8.640 75 DVTHHEDAL I4.000 1641 QVYICSNNI 1.200 184II QLNFIPIDL 8.400 95L QSTLGYVAL 4.000 180 ELAROLNFI 1.200 258 TLPIVAITL 299 LQCRKQLGL j4000 425 RFYTPPNFV If .200 1313 I AMVHVAYSL 8400 133 1 LASLFPDSL 4-000 386 LNWREFSFI 1200 214 GPVVVAISL 8.400 3651 IMSLGLLSL 14000 246 I DFYKIPIEI 7.700 148 [WSAWALQL 4.000 277 YLAGLLA A 70 360! YISFGIMSL [oo TableXVI-V2-HLA-A24-9mers 359 IMYISFGIMS 261 9IVAITLLSL 4000 98P4B6 268 SLVYLAGLL i7.200 FI9671 SSAREIENL .000 Each peptide is a portion of SEQ ID FPPWLETWL1 7.200 1 NO: 5; each start position is 29 FPPWL L 71 NAEYLASLF 3.600 specified, the length of peptide is 9 366 1 MSLGLLSLL I I7.200 2 i VAISLATFF 3.600 amino acids, and the end position _220 ISLATFFFL f 7.200 I 3 ALNWREFSF 3.0 for each peptide is the start position 403 [LLISTFHVL I 7.200 1 33 VGVIGSGDF I 3.000 plus eight. [303 KQLGLLSFF I 7.200 400 YVALLISTF I Start IIubsequence Score [T436 LVLPSIVIL I 7.200 j 304 QLGLLSFFF F 2.400 5 GLQALSLSL 7.200 2_ EIENLPLRLI[7 F"1383 SNALNWREF 2200 TPFSCLSL 6.000 61 RNPKFASEF 6.600 57 VIGSRNPKF 2.200 1 ISGSPGLQAL .7 I428 TPPNFVLAL 3.000 I23 ATFFFLYSF 12.000 15 SGFTPFSCL 4.800 274 EI GLLAAAYQL 61000411 LIYGWKRAF . 00 1 SPGLQALSL 4I1 . 125 YPESNAEYL 0 I 219 AISLATFFF 2.000 331 CPPPCPADF 3.600 363 1 FGIMSLGLL 6.00 621 NPKFASEFF 210009 LSLSLSSGF Io I r 264 If ITLLSLVYL 6.000 1821 ALTKTNIIF 2.000 371 CPADFFLYF 2~.0 396 STLGYVALL I 6.000 239 YARNQQSDF 2.0 I 112 ISLSSGFTPF "2400 297 TWLQCRKQL i 6.000 217 WAISLATF 2 GFTPFSCLS 0600 259 I LPIVAITLL I000 242 11N DFYKI ]1. DYRCPPPCP I10500] 5f SMMGSPKSL 600~181 DALTKTNII 1j800 IL PPCPADFFL I0'.48 20 NLPLRLFTL 60 117 CLPNGINGI I1.800I 1 PPPCPADFF 0.300 441 i IVILDLLQL 16000 349[ WNEEEVWRI 1.800 23 I LSLPSSWDY I 0.180 1.87i FIPIDLGSL I 6.000 171 NIQARQQVI 1.800 GSPGLQALS I o I 146i FNWSAWAL 6.000 290 RFPPWLETW 180 2I SCLSLPSSW I0.180 7 -! QALSLSLSS 11 0.180 1 267 LSLVYLAGL 6.00 105 RHLLVGKIL 1.680 7 QALSLSLSS 0.180 99 f TSLWDLRHL J 0 F 193 GSLSSAREI 1.650 SGFTPFSC It '100 I SLWDLRHLL 115.760 1112 ILIDVSNNM 1.512 I SLSLSSGFT I F438i LPSIVILDL I5.600 43511 ALVLPSIVI 1. 500ILQALSLSLS I F'857 KTNIIFVAI I5.040 I61 HLLVGKILI 1.500 25 LPSSWDYRC I 0.100 24711 FYKIPIEIV1 5.000 5S34 1G5PS I 423 _ YYRFYTPPN 5.00 253 EVN LP .5_ 0 20 FSCLSLPS 0.100 168 WO 03/087306 PCT/USO3/10462 TableXVI-V2-HLA-A24-9mers- TableXVI-V58-.HLA.A24.9mers. TableXVI-V6-HLAA24-9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 5; each start position is - NO: 11; each start position is NO: 13; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino adcids, and the end position amino acids, and the end position for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight. __ plus eight. plus eight. 1Srt Subsequence c Start Subsequence IStart 1Subsequence Score .19 1 PFSCLSLPS I 0.060 I 12 I SFADTQTEL 26.400 26 KKGWEKSQF 0.400 32 1 RCPPPCPAD 0.036 5 [ SFIQIFCSF I2I 5.200 [~1 KLKRIKKGW 0280 36 ]PCPADFFLY_ 0.08 19 ELELEFVFL 7.2oo00 - 1 PSIVILGKI I .1 24J SLPSSWDYR_ 0.015 24 FVFLLTLLL 4.800 24 1 RIKKGWEKS I0.220 4 PGLQALSLS I 0.015 I 16 I TQTELELEF I 3.168 35 LEEGIGGTI I0.210 I11 ILSLSSGFTP 10.015 20 LELEFVFLL .72 [34] FLEEGIGGT 0.180 r271 SSWDYRCPP 0.012 3 EFSFIQIFC I.7 I 11111 IILFLPCIS I0.180 311 YRCPPPCPA 5 0.012 2 REFSFIQIF 0.480 391 IGGTIPHVS 0.1470 1811 TPFSCLSLP 10.010 14[ ADTQTELEL 0.440 j45 HVSPERVTV 0120 I29 7 I WDYRCPPPC 0.010 j18_ [ TELELEFVF 0.432 3811 GIGGTIPHV 0.100 I8 1 ALSLSLSS G 0.010 22 I LEFVFLLTL 0.400 r43 IPHVSPERV 0.1 28 SWDYRCPPP 0.010 21 ELEFVFLLT I0 .252 [33 OFLEEGIGG ]0.090 1221 CLSLPSSWD 0.010 __ "WREFSFIQI [ 0.180 131 LFLPCISRK 0.090 1261 PSSWDYRCP 70.001 I6 FIQIFCSFA I01i0 142I TIPHVSPER 1. I 17 I QTELELEFV 0i'.150 9 1 GKIlLFLPC 0.022I TableXVI-V5A-HLA-A24-9mers- 18F QIFCSFADT I 0.120 i ii VLPSIVILG 0.021 98P4B6 I 101 FCSFADTQT 0.100 1411 GTIPHVSPE 0.018 Each peptide is a portion of SEQ ID 4 I FSFIQIFCS IF 0100 .28 GWEKSQFLE 1 0.015 NO: 11; each start position is specified, the length of peptide is 9 I 9 IFCSFADTQ I.0 I 3 EGIGTIPH 0.015 amino acids, and the end position IQIFSFAD 0015 LPSIVILGK 0.014 for each peptide is the start position 151 DTQTELELE .0[15 81 LGKIILFLP 0.014 __ __plus eight. 11 II CSFADTQTE I 0.012 18 I0SRKLKRIK 0.012 IStartI Subsequence It Score I 137I FADTQTELE j0 32 I SQFLEEGIG 0.07 II NLPLRLFTF I3.000 401 GGTIPHVSP 1 r8EI TFWRGPVVV I 0.500 TableXVI-V6-HLA-A24.9mers- I 5 LPCISRKLK 0.010 F6 7 LFTFWRGPV 0.500 98P4B6 2 ILFLPCISR 2 0.010 -2 LPLRLFTFW 0.216 Each peptide is a portion of SEQ ID 23 KRIKKGWEK I0.003 17 FTFWRGPW 0.10 NO: 13; each start position is KG 19 FWRGPWVA 0 .100 specified, the length of peptide is 9 20 1 K KR_ I ------- FTW II- amino acids, and the end position PCISRKLKR 0.002 5 RLFTFWRGP 0.020 for each peptide is the start position j 44 IIHVSPERVT 0.0 S i4 LRLFTFWRG 0.002 plus eight. l29I WEKSQFLE 0 S PLRLFTFWR 0.- Sta ISubsequence Sc19 0.001 27 l KGWEKSQFL 11I.520 30 EKSQFLEEG F. TableXVl-V5B-HLA.A24-9mers- 114 FLPCISRKL I9.240 221 LKRIKKGWE I. 98P4B6 5I IVILGKLL 6.00i L25II IKKGWEKSQ 1 Each peptide is a portion of SEQ ID [ ILGKIILFL I 5.60 36 EEGIGGTIP I0.001 NO: 11; each start position is 31 1 KSQLE EGI 1=I 3.60067 specified, the length of peptide is 9 1 SQFLEEG amino acids, and the end position 170r KIILFLPCI I3.000 Tabl eXVI - V7A

-H

LA

-

A24- 9 mer s for each peptide is the start position 6 11 VILGKIILF 3.000 98P4B6 plus eight. 471 SIVILGKII IF1.0 Each peptide is a portion of SEQ ID I Start Subsequence Score 17 1 CISRKLKRI ,1 .00 NO: 15; each start position is 231 EFVFLLTLL 36.000 46 II VSPERVTVM 09 specified, the length of peptide is 9 amino acids, and the end position 169 WO 03/087306 PCT/USO3/10462 or each peptide is the start position TableXVI-V7C-HLA.A24.-10mers- TableXVl-V7C-HLA.A24-10mers. plus eight. 98P4B6 98P4B6 Start Subsequence j Score Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID 1 SPKSLSETF I 2.400 NO: 15; each start position is NO: 15; each start position is 9 FLPNGINGI 1.800 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position 4 SLSETFLPN 0.144 for each peptide is the start position for each peptide is the start position 6 SETFLPNGI [0.144 plus eight. __ lus eight. 7 ETFLPNGIN 0o.100 Startl Subsequence [Score ] Start Subsequence [Score 8 TFLPNGING 090 I L SPAAAWKCL 8 4.000 8- GVVTEDDEA 0.165 t' PKSLSETFL i 0.040 141 QAASGTLSL 4.OOL [14 ASPAAAWKC 0.165_ 3I!l KSLSETFLP J oI 5-- E ILDLSVEVLi 4.000 F 25 ANILRGGLS 5T F5_ 1 LSETFLPNG J I 1651 WMKLETIIL I 4.0001 F72 SGIRNKSSS [ 0.150 F..11311 ANSWRNPVL 4.001 11 EVLASPAAA 0.150 TableXVI-V7B-HLA-A24-9mers- 158 l EFLGSGTWM 13750 81 SSQIPWGV 0.150 98P4B6 2]1 NGVGPLWEF 33oi [177 I TQEQKSKHC i] 5 Each peptide is a portion of SEQ ID 1 ASGTLSLAF 2.400 147 II LSLAFTSWS 0.150 NO: 15; each start position is FT I 04E specified, the length of peptide is 9 151 FTSWSLGEF . 64 GATAEAQES 0.132 amino acids, and the end position I 179 EQKSKHCMF 2.000 1 t I LLRLLKSQA II 0.120 for each peptide is the start position i-164 TWMKLETl 1. 46 TLSLAFTSW I0.120 plus eight. 131_ 1 GLSEIVLPI I1.6801 185 CMFSLISGS 0.120 St Subsequence IScore F661 TAEAQESGI 1i.5oo I182I SKHCMFSLI I 0.120 5 AYQQSTLGY 7.500 1 AWKCLGANI 1.200 58 MWTEEAGAT I 0.120 SSTLGYVALL t 6.000 1 - ILRGGLSELI 1.100 2 EDDEAQDSI 0.120 [8[ IQSTLGYVAL 114.000] 163] GTWMKLETI 1.000 [39 I IEWQQDRKI 0.110 t1 NMAYQQSTL 4.000 132] EFLLRLLKS [ 825 I 1 62 SGTWMKLET 0.110 1I FLNMAYQQS 0180 168 LETIILSKL 0.616 I 17[ AAAWKCLGA 0.100 -2- LNMAYQQST II0180 102 1 PPESPDRAL 0.600 79 II SSSSQIPW I0.100 6 YQQSTLGYV 0.150 50 LSTPPPPAM 0.600 [140 I SQAASGTLS I0100 7 QQSTLGYVA 1i0,120] 1291! PLWEFLLRL 10r480 76 NKSSSSSQI I 0.100 [ ,4, MAYQQSTLG oo 20 _1 WKCLGANIL [0.480 1 4 2 AASGTLSLA I0.100 1081 RALKAANSW _ 105 I SPDRALKAA .10 TableXVl-V7C-HLA-A24-10Omers- IT117 RNPVLPHTN 0.360 5 77 I AMWTEEAGA I 0.100 Each peptd s I 3] RLLKSQAAS 0.300 144 It SGTLSLAFT I .100 Each peptide is a portion of SEQ ID

-

K T 100 NO: 15; each start position is 82 SQIP G 252 18 AAKC .100 specified, the length of peptide is 9 I4 VILDLSVEV I 0.238 I7 DLSVEVLAS Ii 0.100 amino acids, and the end position 123 HTNGVGPLW 0.210 I 787 SSSSSQIPV 10.00 for each peptide is the start position 83I QIPVVGVVT I 0.210 1[2 VLASPAAAW 0.100 plus eight. F104 I ESPDRALKA 0.198 73 1 GIRNKSSSS 0.100 iStartI Subsequence Score I - I511 STPPPPAMW 0.180 7[ 1 ESGIRNKSS I 0.100 391 KSQAASGTL I[20O 1145 GTLSLAFTS T0.180 1787 QEQKSKHCM 0.f075 1RGGLSEIVL I8. i i54I WSLGEFLGS 0.180 t50 AFTSWSLGE 0,050 1 81 KSKHICMFSL II8.000I .. 1-o 1 SHw FSLR '- 681II EAQESGIRN II0.10 46 KIPPLSTPP I 0.043 130 1LWEFLLRLL 720 12471 GANLRGGL I7.200 9 SVEVLASPA 08 167 KLETIILSK 0.042 - 59I WTEEAGATA 0.0 i22I PHTNGVGPL 0.040 I127 I VGPLWEFLL II 6.5000E KCLGANILR - 156 LGFLSG 0.180IL 0.030 F1261 GVGPLWEFL] |5.707 Ii 52I GVGPLWEFL i 5 "52 TPPPPAMWT 0.180 [1 16 WRNPVLPHT I 0.025 1 52 TSWS'LGEFL II 4,80ITPPA 112 AANSWRNPV 0 F [5 IVLPIEWQQ 0.025 160 LGSGTWMKL I! 4.400 L01IVLP 101 D PPESPDRA 0180 LSVEVLASP .025 148 SLAFTSWSL 4.000 2 1777 K S 1.024 Li ~1 SLFTSSL I ~ 2 FT! SIVILDLSV 180hT t7 KSSSSSQIP 0.024 42 QDRIPP 4.00 9EQQDRKIPPL 4 TLSKLT 0.180 11T9 !PVLPHTNGV I0 b.022 170 WO 03/087306 PCT/US03/10462 TableXVI-V7C-HLA-A24-10mers- TableXVII-VI-HLA-A24.10mers. TableXVl-.Vi-HLA-A24-10mers 98P4B S 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end positon amino acids, and the end position for amino acids, and the end position for for each peptide is the start position jach peptide is the start position plus each peptide is the start position plus plus eight nine. nine. [Start I Subsequence core s tart Subsequence Score Start II Subsequence Score 1 37 I LPIEWQQDR II 0.022 [ -E267 LSLWLAGLL [ 7.200 3-3847 NALNWREFSF 3.000 1 PSIVILDLS 40021 6 FYTPPNFVLA 7.200 [410 11 VLIYGWKRAF 000 S6 I LDLSVEVLA I 0.021 [ 402I ALUSTFHVL 216 WVAISLATF 3.000 S32 I LSEIVLPIE 0.0211 53 GYHWIGSRN 7-.000 178 3VIELARQLNF 00 183 11 KHCMFSLIS 0.020 [2471 FYKIPIEIVN 20 i18I VAISLATFFF 3.000 -364 GIMSLGLLSL [ 6.000 F 200 I EIENLPLRLF 3.000 TableXVII-V1.HLA.A24-10mers- 71276 ESNAEYLASL 6.000 L 8 1 DALTKTNIIF 3.0 98P4B6 I1 RNPKFASEFF 1 6.000 r 128I SNAEYLASLF I2.880 Each peptide is a portion of SEQID I 2987 WLQCRKQLGL 6.000 137 IFPDSLIVKGF I2.800I NO: 3; each start position is I 4 j ISMMGSPKSL 6.000 11 KLDSN .2 specified, the length of peptide is 10 F S 2520 amino acids, and the end position for I2 AGLLAAAYQL I 217 [ ILWAISLATF F i 2.400 each peptide is the start position plus 3231 LPMRRSERYL 6.000 16 I TCLPNGINGI 2.160I nine. 147 NWVSAWALQL 11 6.000 f 3277 RSERYLFLNM 11 2.160 Start I Subsequence Score 435 ALVLPSIVIL1 6.000 F [137 LSETCLPNGI J2.160 [ QYPESNAEYL 360000 440 SIVILDLLQL 160003 [396 1 STLGYVALLI 1 2.100 13591 MYISFGIMSL 1300.00058" TLPlVA 3IT 6.0 [432 FVLALVLPSI 1 0

F

399 1 GYVALLISTF 180.000L IF6.001"LA4"V"I I 2.100 282__ LGYVALLIS 100.000 /438 LPSIVILDLL 5.600 354 VWRIEMYISF 2.000 I282 LYYGTKYRRF 100.000 422 EYYRFYTPPN 0 5.0 222 LATFFFLYSF 2.000 A3 YYRFYTPPNF I100.000 219 AISLATFFFL - 3211 TVGVIGSGDF 12.000 290 RFPPWLETWL IFI 86.400 417 RAFEEEYYRF F 385 ALNWREFSFI IF1.800 1 425 RFYTPPNFVL I 40.000 365 IMSLGLLSLL 4.0 1701 NNIQARQQVI 1 1.800 L 18_ NFIPID)LGSL7 --- ..... S NFPIDLGSL [ 197 SAREIENLPL 14800 348 SWNEEEVWRI 1.800 14F GFNWSAWAL i1 30,000 t 172 IQARQQVIEL 400 199 II REIENLPLRL 1.728 40 DFAKSLTIRL 24,000 356 RIEMYISFGI 4.200 403 LLISTFHVLI 1.500 _257 KTLPIVAITL I36 IGSGDFAKSL 4.0003301RYLFLNMAYQ l1.5070 362 1 SFGIMSLGLL 20000 98 YTSLWDLRHL 0 434 LALVLPSIVI I50 213 RGPVVVAISL 10 132 YLASLFPDSL 4.000 [2111 LWRGPVWVAl 1.40 S183 RQLNFIPIDL 16800 ETWLQCRKQL T~336 I MAYQQVHANI 11.4001 377 TSIPSVSNAL 11 %0 266 LLSLVYLAGL 14000 2271 FLYSFVRDVI 1400 131I EYLASLFPDS !10 800 19-5 LSSAREIENL 4.000 103 [DLRHLLVGKI 1.320 F25031 IPIEIVNKTL 1110,080 314 MVHVAYSLCL 4,000 S238 PYARNQQSDF 11 oo 263 AITLLSLVYL/ 4000 TableXVII-V2-HLA.A24-10mers F-27031 VYLAGLLAAA 1 -299 LQCRKQLGLL 4.000 98P4B6 F 437 VLPSIVILDL 8.400 1 92 1 AIHREHYTSL 4.000 Each peptide is a portion of SEQ ID 312 FAMVHVAYSL 8.400 361 1 ISFGIMSLGL 4000] NO: 5; each start position is 279 AYQLYYGTKY 8250 SPKSLSETCL specified, the length of peptide is 165 VYICSNNIQA JL 9 4 10 amino acids, and the end [ 16 VYICSNNI.A .395 QSTLGYVALL 4.000 position for each peptide is the start 176 QQVIELARQL 7.200 3 QSTLGYVAL 4000 position plu s nine. S202 ENLPLRLFTL 47.200 I- 1l RNQQSDFYKI ' 90 Start Subseuence Score 991 TSLWDLRHLL 1 7.200 F1631 RQVYICSNNI ]136003 16 I GFTPFSCLSL 24.000 I427 YTPPNFVLAL I 7.200 3 VSNALNWREF 3 32 RCPPPCPADF 7.200 1303 KQLGLLSFFF I 7.200 5 [ WIGSRNPKF 0 2 I GSPGLQALSL 6000 171 WO 03/087306 PCT/US03/10462 TableXVII-V2-HLA-A24-10 Omers- [Start i Subsequence Score ach peptide is the start position plus S 98P4B6 I 1 I ENLPLRLFTF 3.600 nine. Each peptide is a portion of SEQ ID [r It FWRGPVA Subsequence Score NO: 5; each start position is 7 ILFTFWRGPWI 0.50 1 LFLPCISRKL I55.440 specified, the length of peptide is f .. 7 LIF 05 1 10 amino acids, and the end I9 II TFWRGPWVVVA 0.500 F-!7 I VILGKIILFL 8.400J position for each peptide is the start 2 NLPLRLFTFW 0.216] F 5 SIVILGKIIL 6.000 position plus nine. [I6 RLFTFWRGPV 0.200 --"I IVILGKIILF I3.000 Start ubsequence Score I 8 FTFWRGPVVV 0.100 5 FLEEGIGGTI I 2.520 1301 DYRCPPPCPA[ 5.000 I [f[LLRFFRI is] 11 LPIILK I 30 5.000 LPLRLFTFWR 0.0153 LPSVLGK, 1.540 144 SSGFTPFSCL J I 5 LRLFTFWRGP r0.002 271 KKGWEKSOFL 0.960I !__1i LSLSSGFTPF ! 3.600 I 4 f PLRLFTFWRG 0.001 34 QFLEEGIGGT 1'0.900 16 C0PCPADFF J.oo - ] HVSPERVTVM I. S8 ALSLSLSSGF j 2.400j TableXVII-V5B-HLA-A2410 Omers- 11 KIILFLPCIS 0.360 4 II PGLQALSLSL 0 .720 98P4B6 I 26 l KKGWEKSQF 0 .200 S341 PPPCPADFFL J 0.600 Each peptide is a portion of SEQI I 4 .PSIVILGKII I 80 36 PCPADFFLYF J0360 NO: 11; each start position is 3 ]EGIGGTIPHV 110.150 F9 LSLSLSSGFT [1 specified, the length of peptide is PCISRKLKRI .i5 10 amino acids, and the end __ 51 GLQALSLSLS [0.150 position for each peptide is the start 4 TIPHVSPERV II 0.150 24 SLPSSWDYRC [ .150 position plus nine. 10 GKIILFLPCI 0.150I 1 SGSPGLQALS I StartI Subsequence I Score 91 LGKIILFLPC iio.1441 SLQ'LSLSLSS [ 020 F2471 EFVFLLTLLL IF0 1 GIGGTIPHVS I0140 2 1 FSCLSLPSsw 0120 122 ELEFVFLLTL 6.000 1 EKSQFLEEGI J0.1 18 TPFSCLSLPS 0.120 20 7 ELELEFVFLL 1 6.00 44 iPHVSPERVT I0. 15] SGFTPFSCLS 0.100 12 CSFADTQTEL II 4.400 21 RKLKRIKKGWF 1142 12 SLSSGFTPFS [ 0.100 14 1 FADTQTELEL J 4.400 I KRIKKGWEKS I 0033] 28 SWDYRCPPPC [ .1 16 ! DTQTELELEF I3.960 32II KSQFLEEGIG I 0.030 13 LSSGFTPFSC 0.100 18 QTELELEFVF 3.600 42 GTIPHVSPER 0.028 3]1 SPGLQALSLS 01I00 5 I FSFIQIFCSF 3.360 I !LVLPSIVILG 0.02 22 ! CLSLPSSWDY 0.1001 NWREFSFQI 1.440 1 281 KGWEKSQFLE 110.024 1i9 PFSCLSLPSS [0.050 19 TELELEFVFL 0.86 2! VLPSIVILGK I0.021 23 LSLPSSWDYR i 0.018 I 6 SFIQIFCSFA II 0.750 251 RIKKGWEKSQ IF0.020 71 QALSLSLSSG r 0.01 4 EFSFIQIFCS 1 0. 500 1 KLKRIKKGWE 0.0I20 17 FTPFSCLSLP i0.015 10 IFCSFADTQT Ii 0.5001 29 GWEKSQFLEE 0.020 121 SCLSLPSSWD 0i. 23 LEFVFLLTLL 0.480 12 IILFLPCISR I o.o15I 35 PPCPADFFLY 014 I L: WREFSFIQIF 0.360 15 FLPCISRKLK II .015 27 Ji SSWDYRPPPP .871 IQIFCSFADT i 0, 180] 8 1 ILGKIILFLP 0014I 25 LPSSWDYRCP 0.010 17 QTELELEFV 0.120 I 181 CISRKLKRK [ 0.0121 10 SLSLSSGFTP 0.010 [137 SFADTQTELE 10.060 1 LPCISRKLKR ]0.011 31! YRCPPPCPAD 21 1 LELEFVFLLT II 0.030 19 ISRKLKRIKK Ii.0f1 [29 I WDYRCPPPCP o.o1l 3 REFSFIQIFC 11 0.028 133 SQFLEEGIGG 0.01 0 2 ] IPSSWDYRCPP 0.001 I 7 FIQIFCSFAD I 0015 41I GGTIPHVSPE I0.010 S 11 i FCSFADTQTE .12 4 IGGTIPHVSP !. 9 QIFCSFADTQ I o.oio 13 ILFLPCISRK ,0.010 TableXVII-VSA-HLA-A24-10mers- I15 ADTQTELELE 10 361 LEEGGGTIP 0.002 98P4B6 ....... 45 PHVSPERVTV I.02 Each peptide is a portion of SEQ ID 51PVPEvv .0 NO: 11; each start position is TableXVII-V6-HLA-A24-10mers- 201 SRKLKRIKKG .0i] specified, the length of peptide is 10 98P4B6 = [771 amino acids, and the end position for Each peptide is a portion of SEQ ID 23 II LKRIKKGWEK o.0 each peptide is the start position plus NO: 13; each start position is37 EEGGGTIPH 0.001 nine. specified, the length of peptide is 10 amino acids, and the end position for 172 WO 03/087306 PCT/US03/10462 TableXVII-WV7A-HLA-A24-10mers- TableXVll.-V7C-HLA.A24-10mers. TabIeXVII-V7C-HLA-A24.-10mers. 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is specified, the length of peptide is 10 specified, the length of peptide is 10 10 amino acids, and the end amino acids, and the end position for amino acids, and the end position for position for each peptide is the start each peptide is the start position plus each peptide is the start position plus position plus nine. nine. nine. Start I ubsequenc core Sa Subsequence I Score I Startl Subsequence IScore 9 TFLPNGINGI 10800 1261 NGVGPLWEFL 7.200 I 52 STPPPPAMWT 0.180 211 SPKSLSETFL 4.000 211 DPPESPRA ]l 177 J LTQEQKSKHC 0.180 i1 GSPKSLSETF II 3.600 I 113 AANSWRNPVL "6.000 1'47 FLLRLLKSQA I0.180 I 6 _ LSETFLPNGI 2.160 11291 GPLWEFLLRL I 6.000 .

185 IHCMFSLISGS 0.180 4 KSLSETFLPN 0.360 1 481 1 LSLAFTSWSL II 6.000 146I GTLSLAFTSW F0.180 10 FLPNGINGIK 0.021 [15 ASPAAAWKCL 6.000 39 I PIEWQQDRKI I0.165 5 l SLSETFLPNG 10.012 165 _ TWMKLETIIL 6000 _88 I VGVVTEDDEA 0.1657 7[ SETFLPNGIN 0.010 2411 LGANILRGGL 4.800 10 SVEVLASPAA 0.15 8 I ETFLPNGING 10 [20 AWKCLGANIL 4.800 I73I SGIRNKSSSS !0.150 31 PKSLSETFLP 0.00 l [127 I GVGPLWEFLL f 4.800 25I GANILRGGLS ]0~1 [152 I FTSWSLGEFL 4800 1.57i LGEFLGSGTW "0.150 TableXVII-V7B-A24-10mers- 1 160 I FLGSGTWMKL 4.400 iz EVLASPAAAW 0.150 98P4B6 [122 7 LPHTNGVGPL 1 4.000 156 SLGEFLGSGT 0.144 Each peptide is a portion of SEQ ID [141 I SQAASGTLSL I1 4.000 1 [ LPSIVILDLS IF0.140 NO: 15; each start position is r1 S F '2__D E _o4 specified, the length of peptide is 182 SKHCMFSL 1 2.400 61 ILDLSVEVLA 0.140 10 amino acids, and the end [1i43 F AASGTLSLAF 2. 400 IT11 SWRNPVLPHT 0.140 position for each peptide is the start [125 I TNGVGPLWEF 2.200] 43 QQDRKIPPLS 10.140 position plus nine. l31 GGLSEIVLPI 1 2.100 64 AGATAEAQES I 0.132 Start Susequence ISCore 76I RNKSSSSSQI 1 2.000 I4 iLASPAAAWKC 0.132 6i AYQQSTLGYV I~50I 27I NILRGGLSEI 1.650 174 LSKLTQEQKS 1 0.132 3]I LNMAYQQSTL I 6.0 [164 I GTWMKLETII 11.200 51i LSTPPPPAMW 0.120 18 QQSTLGYVAL 14.000 [19 II AAWKCLGANI 1.200] 92[ TEDDEAQDSI J 0.120 I QSTGYVALL6 ATAEAQESGI I1.200 I1 LLRLLKSQAA 0.120 1J10 STLGYVALLI 1 2.10 163 I SGTWMKLETI I.000 '106 SPDRALKAAN "0.120 i I LFLNMAYQQS ] 0.900 IF1 78 I TQEQKSKHCM II 0.750 59 MWTEEAGATA Io0.120 7 I YQQSTLGYVA 01 18 01301 PLWEFLLRLL l 0.5761 28 ILRGGLSEIV I01 12 FLNMAYQQST 1 0.180 29 LRGGLSEIVL 4.400 1i 4 SWSLGEFLGS 0.120I i5 MAYQQSTLGY ooo 181I QKSKHCMFSL 0I.400 1 SGTLSLAFTS I 4 NMAYQQSTLG 0.010I 139 I LKSQ:AASGTL 1.400 162 J GSGTWMKLET 01 F179 I QEQKSKHCMF I01300 97 AQDSIDPPES I0.110 TableXVII-V7C-HLA-A24-10mers. [140 I KSQMAASGTLS I 0.300 [ 147 TLSLAFTSWS i0.100 98P4B6 98P4B[ If70 AQESGIRNKS I0.277 I I 180 II EQKSKHCMFS i'0.100 Each peptide is a portion of SEQ ID F7 SGV 0J SSQP 01 NO: 15; each start position is [83 1 SQlPWGVT 0.5 _ 79 I SSSSSQIPVV1 0.100 specified, the length of peptide is 10 112 II KAANSWRNPV 0.240 4I Ii721 QAASGTLSLA II 0.100 amino acids, and the end position for [91f VTEDDEAQDS I 0.216 18 AAAWKCLGAN I 0.100 each peptide is the start position plus [9 I LSVEVLASPA I 0.216 38 LLKSQAASGT I0.100 nine. b 82 SSQIPVVGW 0.210 1 iioj ALKAANSWRN IF0.100 Start Subsequence Score ss IP I oi ASTSR T 168 I KLETIILSKL [18.4801 78 1 KSSSSSQIPV ]1 0.200 144 ASGTLSLAFT 0.

100 ! 471 IVILDLSVEV I 198 7 4 GIRNKSSSSS J1 0.100 5 VIITS LF I3371 LSEIVLPIEW 0198 1SSSQPVVGV ]F_000 I5 IIVILDLSVEVL [i7.200[ 217.200 19 NPVLPHTNGV 18 166 WMKLETIlLS ,0.100 r42 W[VQQDRKIPPL 7 20 05 IESPDRALKAA 01I8 72 I ESGIRNKSSS 0.1 173 WO 03/087306 PCT/US03/10462 TableXVIl-V7C-HLA-A24-10mers- TableXVIII-VI-HLA-B7-9mers- TableXVIII-Vi-HLA-B7-9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position amino acids, and the end position each peptide is the start position plus for each peptide is the start position for each peptide is the start position nine. plus eight plus eight. start Subsequence [Score Start Subsequence Score Start Subsequence i core 58 ] AMWTEEAGAT 0.100 [220 ISLATFFFL 4.000 328 SERYLFLNM I1.000 1337 EFLLRLLKSQ I 0.090 187[ FIPIDLGSL 4.000 3 106 GLLSFFFAM 1000 159 EFLGSGTWMK 0 .05 128 SNAEYLASL 4.000 278 AAYQLYYGT I 0.90oo0 1 58 GEFLGSGTWM 0.050 363 I FGIMSLGLL I 4.000 I 0 2 [LLISTFHV 0.6D00 5o II PLSTPPPPAM I0.050 [274][ GLLAAAYQL 4.000 [297 TWLQCRKQL 1 0.600 S4771 KIPPLSTPPP 0.036 [365 IMSLGLLSL 1[ 4.000 1 F262 I VAITLLSLV I 0,600 22 KCLGANILRG o.030 3 66[1 MSLGLLSLL 4.000 [239 [YARNQQSDF 0.600 F 118 RNPVLPHTNG" 0.030 [18 QLNFIPIDL [4.000 434I LALVLPSIV [ 11091 RALKMAANSWR I030 9_3 IHREHYTSL I 4.0001 [5 FASEFFPHV 0.00 1371 RLLKSQAASG II 0.030 324 PMRRSERYL 4.000 1t61]1 ASRQVYICS 0.600 __ 9 EAQDSIDPPE ][.025 [395 I QSTLGYVAL 4.000 [ 26 F YTPPNFVL 0I .6 17J IILSKLTQEQ 10.024 267 LSLWLAGL =4.000 _374 LAVTSIPSV - 268 SLVYLAGLL 4.000 [314 MVHVAYSLC 0.500 TableXVIII-VI-HLA-B7-9mers. 1 i360 YISFGIMSL 14.000 34 GVIGSGDFA I 0500 98P4B6 196~ SSAREIENL 4.000 216 VVVAISLAT I0.500 Each peptide is a portion of SEQ ID 378 I SIPSVSNAL II 4.000 I 269 LWLAGLLA I 0.500 NO: 3; each start position is specified, the length of peptide is 9 F.. TLPIVAITL 2 . amino acids, and the end position 299 LQCRKQLGL II 4.00071 I LSLLAVTS II 0.400 for each peptide is the start position [99 TSLWDLRHL II 4.000 85 It KTNIIFVAI I . plus eight. 403"1 LLISTFHVL II 4.000 39 I EFSFIQSTL ]0.400 S1r1 Subsequence [Score 37I GSGDFAKSL IIT0 I 439 PSIVILDLL [0.400 173- QARQQVIEL 120.ooi 203 NLPLRLFTL I'4.000 397 TLGYVALLI_0.0 214] GPVWAISL 80.000 264 I ITLLSLVYL I 4.000 30 PNFVLALVL I0400 259 L26V4TL 80.000 "0.400 259 1 LPIVAITLL JI 80.00 1 396 STLGYVALL I4.000 [362 SFGIMSLGL 0.400 428 TPPNFVLAL 80.000 287I KYRRFPPWL I4.000 1 71II NIQARQQVI 0.400 438 LPIID .. 80000O 438 LPSIVILDL 800 157 JGPKDASRQV II4.000 [180 I ELARQLNFI .400 291 FPPWLETWL 80000 317 VAYSLCLPM 3.000 3 GSLSSAREI 0.400 300 QCRKQLGLL I4000 9" SPKSLSETC I2.000 38 LNWREFSFI 0.40 125 YPESNAEYL 24,000 250 IPIEIVNKTI 2.000I 204L P L l 177]! QVIELARQL I0 2o353 EVWRIEMYI 2.000 [429_t PPNFVLALV 0.400 148 WSAWALQL 20,000 49 LRCGYHVV .000 1 188 I IPIDLGSLS I 0.400 1226]1 IVAITLLSL 20000 1-6I QVYICSNNI 2.000 I79 IPSVSNALN 0.400 75 DVTHHEDAL "20,000 i34I ASLFPDSLI II.800 i2 NPKFASEFF II 0.400 F441 IVILDLLQL 20,0001 435 ALVLPSIVI II .800 [326 RRSERYLFL I0.400 1436 LVLPSIVIL 120.00 200( EIENLPLRL I1.20I 4[ VLALVLPSI 0.400. 41 ]I FAKSLTIRL 12.00o0 81 1 DALTKTNII 1 .200 I 253 EIVNKTLPI 0.400 31 AMVHVAYSL 12,000 [323]t LPMRRSERY 12~ 1i6 HLLVGKILI I0.40 1331 LASLFPDSL 12]0 108 I LVGKILIDV I I .000I 5s ! SMMGSPKSL 12.000 358I EMYISFGIM 11.000 I TableXVIII-V2-HLA-B7-9mers 127_ DARKVTVGV 6.000 1 ILIDVSNNM 1.0 98P4B6 [_100] SLWDLRHLL 6 0 1254 IVNKTLPIV I1.0 Each peptide isa portion of SEQ ID 1146 FNWSAWAL 4.000 1 23 FVRDVIHPY II1.000 NO: 5; each start position is 174 WO 03/087306 PCT/US03/10462 specified, the length of peptide is 9 Start I Subsequence Iplus eight.

amino acids, and the end position [2 LPLRLFTFW 0.400 [Start IISubsequence Score for each peptide is the start position FTFWRGPW ... 00 Str S e ncIVILGKL _r plus eight. FTFWRGPWF 20.20 5 IVILGKL 20.00 Start Subsequence Score 9 FWRGPVVVAI 0.150 FLPCISRKL SPGLQALSL 80.000 6 LFTFWRGPV 0.030 4311 IPHVSPERV 4.000 I35 PPCPADFFL I8.000 II8 TFWRGPWV 0.020 [7 ILGKIILFL 14.000 15 SGFTPFSCL 6.00 NLPLRLFTF 0.020 [27 KGWEKSQFL 4.000 1 SGSPGLQAL 4.000 1 PLRLFTFWR 0.010 45 I HVSPERVTV 1.500 17 FTPFSCLSL j4.000 5 II RLFTFWRGP 0.010 F 46II VSPERVTVM i1.000 1 5 ,~ GL ALS LSL )[ [* ,4 II ~ LRLFTFWRG [! 0.001 31 KSQFLEEGI i" 0.400 GLQALSLSL 0 J[..001 31 25 LPSSWDYRC 2.000 4 S.I.II [ 0.400 37 CPADFFLYF ] 0.400 TableXVIll-V5-HLA-B7-9.mers. 17 1 CISRKLKRI ._ 33 CPPPCPADF 0.400 98P4B6 10 KIILFLPCI 18 ITPFSCLSLP 0.200 Each peptide is a portion of SEQ ID LPCISRKLK 0.300 .... 1. TPFSCLSLP NO: 11; each start position is 1- R 1i ' SLSLSSGFT 10.100 specified, the length of peptide is 9 38 GIGGTIPHV 0.200 14J SSGFTPFSC ]0.100 amino acids, and the end position [2 LPSIVILGK 0.200 L7'u 1 QALSLSLSS ]I of~ for each peptide is the start position 1 ISRKLKRIK 0.100 4 PPPCPADFF plus eight. 3 PSIVILGKI 0.040 8 L S S 0.030 Start Subsequence S lGrG 0.030 S8 ALSLSLSSG !.03o 24[ FVFLLLLL IILFLPCIS 23 LSLPSSWDY 0.2 11 IlFLCI 0.020 12 S G F 014 ADTQTELEL 1.200 3 IGGTIPHVS 12 i] SLSSGFTPF jIoo [ I[ ELELEFVFL 0I020 199 1 I0.2 21 j SCLSLPSSW 0.020 F12 EL EL 6 VIG [ 0.020 1 LQALSLSLS 0.020 FTL I f2 RIKKGWEKS 11020 13 LQSGFTPFS 0.020 23 EFVFLLTLL I0.400 1211 KLKRIKKGW 0. 22 LEFFLLTL 0.400 F GSPGLQALS 14 0 LEFVFLLTL "4[ GGTIPHVSP 0.015 20 LELEFVF LL 0.0 015E LSLQLSSGF ELEFLL I 12 1!ILFLPCISR 0.015 20I 9 LSLSLSS .020 l FCSFADTQT 3II 1 LEEGIGGTI 0.012 S20_ ] FSCLSLPSS 11 0.02J 11 8 ][ QIFCSFADT I 0.100 1 EGIGGTPH ]I 0. 32 1 RCPPPCPAD 0.015 37 EGIGGTIPH 0.010 .22 . CLSLPSSWD 0.015 FIQIFCSFA, 0.100 22i LKRIKKGWE T0.010 2 flI CLSLPSSWD II 0.0iT]QTELELEFV 0.06 0o.I[ LGKIILFLP 31 YRCPPPCPA Io.015 21 EEF3LL 8,LGllLFLP 0.1 30 JEI DYRCPPPCP_ 1 I ] FF L 0I SQFLEEGIG 1 0.010 17 SSWDYRCPP 0015 "I FSFIQ4FCS t GTIPHVSPE 0.1 S29 WDYRCPPPC 0.0I0 1 TQTELELEF 11 0.020 1 I VLPSIVILG 0.010 I 24 II SLPSSWDYR 0o.00 i ,1 WREFSFIQI 0.012 F97 GKIILFLPC 10 11SLPSSWDR II 07 I [11 CSFADTQTE II .1 I -42 -' TIPHVSPER 0.010I 3 EFSFlQIFC 0.010 SLSLSSGFTPCPADFFLY 0.002 I 1 EFSFIQIFC 0. F 1 KKGWEKSQF 0.002 ['L'3'6 II PCPADFFLYjj ~i[ IQIFCSFAD I 5oo] 1 1 ' SRKLKRIKK I[ o5oo 16 GFTPFSCLS I19 .0SRiL DKTELELE RKi 19 PHSPRVl [ 0.002 4 PGLQALSLS 0. 002 44 PHVSPEELERVT 0.002 2]6 PSSWDYRCP 10 FADTQTELE 10.009 EEGIGGTIP I0.001 28 1I SWDYRCPPP t i1 SFIQIFCSF 0.002 i ] RKLKRIKKG 0.001 PFSCLSLPS 0.000 12] REFSFIQlF II0.002 291 WEKSQFLEE 0~0 S TELELEFVF . LFLPCISRK ]0.001 . 1 IFCSFADTQ 7 .0 ] ~KKWKQI .0 TableXVIII-V5A.HLA.B7.-9mer--' 25 IKGES 98P4B6 30 EKSQFLEEG I0.001 Each peptide is a portion of SEQ ID TableXVl-V6-HLA-B7-9mers- F3 QFLEEGIGG I o00 on48 of S RKGE I 0.00 1] NO: 11; each start position is 98P4B6 23 KRIKKGWEK 0.001 specified, the length of peptide is 9 Each peptide is a portion of SEQ ID C6

'

ISRKLKR I .001 amino acids, and the end position NO: 13; each start position is I.00 for each peptide is the start position specified, the length of peptide is 9 2. _ GWEKSQFLE 0.000 plus eight amino acids, and the end position for each peptide is the start position 175 WO 03/087306 PCT/USO3/10462 TableXVIII-WA-HLA-B7-9mers- TableXVIll-V7C.HLA.B7.9mers. TableXVIII-V7C-HLA-B7-9mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 9 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position amino acids, and the end position amino acids, and the end position for each peptide is the start position for each peptide is the start position for each peptide is the start position plus eight, _plus eight. plus eight. IStart Subsequence Sta i ubsece Sc uence II Score I Start Subsequence Score 9 I FLPNGINGI 0.400 I148I SLAFTSWSL 114.000 11 LPHTNGVGP 0.200 r17 SPKSLSETF .400 i 181 KSKHCMFSL 4.000 18 AAWKCLGAN 0.180 6]1 SETFLPNGI 0I. I29! RGGLSEIVL tl4000 ] 9 1 SVEVLASPA 0.1507 2 ] PKSLSETFL If1 0.040 1391 KSQAASGTL II 4.000 L I4 TWMKLETI 0.120 7 1 ETFLPNGIN r 0.030 [271 ILRGGLSEi 114000] i AWKCLGANI .120I 4 SLSETFLPN .20 165 WMKLETIIL 14.000 130 LWEFLLRLL! 0.120 .3_ 1 KSLSETFLP 10ol 11 TSWSLGEFL 000 1041FESPDRALKA 0.1001 F57 LSETFLPNG I0.03 1601 LGSGTWMKL 4.000 158 EFLGSGTWM I0.100 1 TFLPNGING II 0.001 102 I PPEsPDRA 3600 SGTWMKLET If . 5[2 I TPPPPAMWT II 3.000 169 ETIILSKLT 0.100 TableXVIII.V7B-HLA.B7-9.gmers- [112 If AANSWRNPV 2.7 83 QIPWGVVT 0.100[ 98P4B6 [101 DPPESPDRA 12.00 78I]I QEQKSKHCM t0.100I Each peptide is a portion of SEQ ID 50 LSTPPPPAM 144 SGTLSLAFT 0.100 NO: 15; each start position is 5L_ ILDL.SVEVL 1i .200 1 1 PVLPHTNGV II0.100 specified, the length of peptide is 9 L1. 200 l-19 ]I PVLPHTNGV 1 I amino acids, and the end position 42 1.200 143 ASGTLSLAF 0.060 for each peptide is the start position 134 I LLRLLKSQA 1.000 64 GATAEAQES I. plus eight. 1 42 I AASGTLSLA I0.900 68 1 EAQESGIRN 0.060 I FStart Subsequence Score 1471 AAAWKCLGA 10 l 25 ANILRGGLS 060I 0 SLGYVALL 0 SPDRALK1A 106001 108 RALKAANSW 0.060 8II QSTLGYVAL I 4.000 EVLASPAAA 0.500 135 IVLPIEWQQ 0.050I 311 NMAYQQSTL 4.000 GVTEDDEA 0 86 WGVVTEDD I00 5 2 LNMAYQQST 0I0 r--- FT 0NMAYQQST 15I31 F GLSEIVLPI 0400 1 IVILDLSVE 0.50 6I YQQSTLGYV o20 20 I WKCLGANIL 0 19 VVTEDDEAQ [5 711 QQSTLGYVA Io0o 168 LETIILSKL 0400 F1221 PHTNGVGPL 0.04o 4 MAYQQSTLG 0.030 163 GTWMKLETI 04001 76 NKSSSSSQI ] 0.040 I 1l FLNMAYQQS II 129 PLWEFLRL 0 821 SKHCMFSLI IO.040 SAYQQSTLGY 0.006 66 [ TAEAQESGI 360 39I IEWQQDRKI 0.040 [1 SSQlPVVGV 0.0 [1 VLASPAAAW [0.030 TableXVIII-V7C-HLA-B7-9mers. 578 [ AMWTEEAGA 0.300 162 EAGATAEAQ 0030 98P4B6

-

-00 98P46614 ASPAAAWKC 1251 NGVGPLWEF 0.030 Each peptide is a portion of SEQ ID I18 NO: 15; each start position is - I -18INLHG .0 LASPAAAWK 0.030 specified, the length of peptide is 9 PGVVT 0.200] 109 ALKAANSWR II 0.030 amino acids, and the end position 79 SSSSQIPW 200 163 AGATAEAQE I03o for each peptide is the start position 55 PAMTEEA 0200 95 EAQDSIDPP 0.030 I plus eight. - 11 puseight.e_- r82 [ SQIPWGW 1I0.2001 6511 ATAEAQESG 110.030 7Start LPIEWQQDR 0.200 149 LAFTSWSLG I .3 F151 SPAAAWVKCL 8000 - 0.0 II SPAAAWKCL I 78 SSSSSQlPV 0.0 I KAANSWRNP "0.030 1 26 GVGPLWEFL 120.000 -I 24 GANLRGGL II 73 GIRNKSSSS 10.200 STPPPPAM [i II~ GANRGPVL 1.0 411 VILDLSVEV I.2 1841 HCMFSLISG 0.030 113 ANWRPV 12.0004IF 11 ANSNLVL f112.ooo 2 II SIVILDLSV 0.200I 1591 WTEEAGATA f030_ F141 jQAASGTLSL 112.000 SVLE737 1 1 SGPLSL I4.000 471 IPPLSTPPP I0.200 I 15 LGEFLGSGT I 0.030 1227 VGPLWEFLL 4.000 " G L ..... 0 I 128][1 GPLWEFLLR 0.200 1'7711 TQEQKSKHC I (.00 176 WO 03/087306 PCT/US03/10462 TableXVIll-V7C-HLA-B7-9mers- TableXIX-VI-HLA-B.7-10mers. TableXIX-VI-HLA.87-.0mers 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is specified, the length of peptide is amino acids, and the end position 10 amino acids, and the end 10 amino acids, and the end for each peptide is the start position position for each peptide is the start position for each peptide is the start plus eight. position plus nine. position plus nine. Start Subsequence ][c [startI Subsequence Score I Start Subsequence Score 1140i SQAASGTLS [0.020 195 LSSAREIENL II4.000 1255 VNKTLPIVAI 0.600 48__ PPLSTPPPP ][0.020 257] KTLPIVAITL j[4.000 F401 VALLISTFHV 0.600 [71 ESGIRNKSS ]0020] 377[ TSIPSVSNAL 4.000 [125 ' YPESNAEYLA 0.600 123 jJ HTNGVGPLW 0.020 266 LLSLVYLAGL 4.000 157 GPKDASRQVY 0.600 F72 SGIRNKSSS F0020 202I ENLPLRLFTL II4.000 [227 I FLYSFVRDVI 0.600 179 EQKSKHCMF 0.020 F132[ YLASLFPDSL 4,000 82 ALTKTNIFV 0.600 18511 CMFSLISGS II0.020 29 LQCRKQLGLL 4.000 425 RFYTPPNFVL 0.600 54 PPPAMWTEE 110.020] 761 QQVIELARQL 4 I000 65I FASEFFPHVV I0.600 [147 I LSLAFTSWS I 0.020 14 YPPNFVLAL [ 4 I ASLFPDSLIV i 0.600 1 281 LRGGLSEIV 1.02 I 394I IQSTLGYVAL 4.000 223 ATFFFLYSFV __ S213 RGPVVVAISL 4.000 269 LVYLAGLLAA I 0.500 I TableXIX-V1-HLA-B7-10mers- 136511 IMSLGLLSLL II4.000 [142 IVKGFNWSA 10t.500 S 98P4B6 "49 1 LIRCGYHWI 4.000 [7 DVTHHEDALT [ 0.500 Each peptide is a portion of SEQ ID [ 428 TPPNFVLALV 4.000 441 i IVILDLLQLC 0.500 NO: 3; each start position is 1i LLVGKI specified, the length of peptide is 13 DLRHLLVGK 4.000 HVLYGWKRA 0.500 10 amino acids, and the end I36 IGSGDFAKSL I 4.000 1 25i IVNKTLPIVA I .500 position for each peptide is the start 198 YTSLWDLRHL J 4.000 1 [ !1 FVAIHREHYT 0.500 position plus nine. 298 WLQCRKQLGL II 4.000] 37-5I AVTSIPSVSN 10.450 [art S euence IScore I3251RRS ERYLFL 4.9000 1 9 REIENLPLRL i .400 323 LPMRSERYL 2 361 I ISFGIMSLGL I 4.000 [ 95i REHYTSLWDL 0.400 i197 I SAREIENLPL 1000 1258 TLPIVAITLL 4.00 379 I IPSVSNALNW 0.400 438 i [ LPSIVILDLL i8.0 117211 IQARQVIEL 0 259 I LPIVAITLLS 0.400I F 9I SPKSLSETCL 1180.000 1 IR E F 11 LPVAIl 0.400 250 I PiKEVNKTL 127 ESNAEYLASL 4.000 211I LWRGPVWAI .400 2 ENKTL 0J 440 SIVILDLLQL 4 1 [163 i RQVYICSNNI ][1 0 31 2MVH VAYSL 1183 RQLNFPIDL 40 145 GFNWSAWAL I0.4001 [147II NWVVSAWALQL 120.000 67 LSLVYLAGLL 1 87618 l NFIPIDLGSL 0.400 [314VHV AYSLCL 20.000 1437 VLP SIVILDL " 188 IPIDLGSLSS 0.400I 364 GIMSLGLLSL 2000 13951 QSTLGYVALL 4.000 [ 370 LLSLLAVTSI 0.400 263I AITLLSLWL 12.000 1731 QARQQVIELA 3.II 000ooo 359 I MYISFGIMSL 1F F219[ AISLATFFFL i12000 1432 FVLALVLPSI 2.000 16 i TCLPNGINGI 0.400 r4021 ALLISTFHVL 12.000 214 GPVVVAISLA 2.000 24P ESNAEYL 0.400i 43511 ALVLPSIVIL 2.000 I434 LALVLPSIVI 1.800 [170 NNIQARQQVI 0.40I [273][ AGLLAAAYQL i12.000 133 LASLFPDSLI I1.800 [243i QQSDFYKIPI I 04 F 71ISMMGSPKSL 12.00 -ALPSI .00 M IIO4 3ISMMGSPKSL 8i 51 I15~ ALNWREFSFI 1.200 F241 I RNQQSDFYKI 0.40 A92 AIHREHYTSL i12.000 33 MAYQQVHANI .200 74 I VDVTHHEDAL 0.40oI 27 DARKVTVGVI 12.0001 F41 FAKSLTIRLI 1.200 181I LARQLNFIPI 12.000o I1l KILIDVSNNM 1.000 42 II PPNFVLALVL 1 8.000 2611 IVAITLLSLV 1. TableXIX-V2-HLA-B7-10mers- 1 [296 F ETWLQCRKQL i 6.0305 LGLLSFFFAM 1. - 00 98P4B6 I 99 TSLWDLRHLL 11 6.000 21 7 AYQLYYGT 0.0 Each peptide is a portion of SEQ ID 1 YSLCLPM I NO: 5; each start position is 11A P 5.000 I 61 II ASRQVYICSN II 0.60 specified, the length of peptide is [231 FVRDVHPYA i 5.000 I 239 IYARNQQSDFY 0.60 10 amino acids, and the end 177 WO 03/087306 PCT/USO3/10462 position for each peptide is the start TableXIX-VA-HLA-7-10mers- TableXIX-V6-HLA-B7-10 Omers pi position plus nine. 981P4B6 98P4B6 SStart I Subsequence I Score Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID S34 I PPPCPADFFL [8.000 NO: 11; each start position is NO: 13; each start position is 14 SSGFTPFSCL I 6.000 specified, the length of peptide is specified, the length of peptide is 10 10 amino acids, and the end amino acids, and the end position for I 2 [ GSPGLQALSL 4000 I position for each peptide is the start each peptide is the start position plus 33 CPPPCPADFF [ 0.600 position plus nine. nine. 18 11[ TPFStLSLPS 0[400 ar Start II Subsequence Score]( .16 11 GFTPFSCLSL 80.400 FTFWRGPVW r 0.200 [3] LPSIVILGKI 8.0 0-1 3 SPGLQALSLS [0.400 3 lLPLRLFTFWR 0.200 HVSPERVVM ~oj 4 PGLQALSLSL 0.400 2 NLPLRLFTFW 0.020 51 SIVILGKIIL 4.000 25 LPSSWDYRCP 0.200 1 7 LFTFWRGPVV .020 F7 VILGKIILFL 4.000 30 DYRCPPPCPA 0.150 1[1 ENLPLRLFTF 0I.02o 44 IPHVSPERVT 13.000 24 SLPSSWDYRC 0.100 9 TFWRGPWVA 0o.015 14i LFLPCISRKL 0.40] 13 LSSGFTPFSC 0100 4 PLRLFTFWRG I 0.010 27 KKGWEKSQFL 0.400 F9 I LSLSLSSGFT 5.1 5 LRLFTFWRGP 0001 16 11 LPCISRKLKR I0.200 8 ALSLSLSSGF I 060- 43 TIPHVSPERV 0.200 S357 PPCPADFFLY I 0.040 TableXIX-V5B.HLA-B7.-10mers. 38 EGIGGTIPHV ]0.200 S7 Q! OALSLSLSSG 0.0 30 98P4B6 [I ISRKLKRIKK 01 152 SGFTPFSCLS 0.020 Each peptide is a portion of SEQID 35 FLEEGIGGTI 0.120 22 CLSLSSWDY NO: 11; each start position is 97 L - j L P _WY_ 0. 020specified, the length of peptide is _9 LGKIILFLPC .1 11 J LSLSSGFTPF 0.020 10 amino acids, andtheend 6 IVILGKIILF 0.100 S6 LQALSLSLSS [ 0.020 position for each peptide is the start 1I LVLPSIVILG 0.050 I 32 I RCPPPCPADF 1 0.020 position plus nine. [ 10 GKIILFLPCI 0.040 I 1 II SGSPGLQALS 0.020 Start Subsequence Score 4 PSIVILGKII I.4 20I FSCLSLPSSW [ ooATE_0 [14.- -311 EKSQFLEEGI 0.040 L12[ SLSSGFTPFS FADTQTELEL I3.60 T PCISRKLKRI 00__40 F5, GLQALSLSLS 0.020 20 7 ELELEFVFLL 1.200 i1 KLFLPCIS 0.020 121[ SCLSLPSSWD 10.015 ] ELEFVFLLTL T~ -9i GIGGTIPHVS 0.020 7 0 SLSLSSGFTP [ 0.4 1 FLPCISRKLK 0 015 I1 1 FTPFSCLSLP I 01004I0 NWR 0 40 IGGTIPHVSP I 0.015 27 SSWDYRCPPP TELELEFVFL ~o 1 IILFLPCISR IF.015 23 LSLPSSWDYR 24 EFVFLLTLLLj 0.400 341 QFLEEGIGGT 0.010 281 SWDYRCPPPC 0003 17 TQTELELEFV 0200 11 VLPSIVILGK 0.010 1 36 PCPADFFLYF I 0.002 1 IQIFCSFADT 0.100 33I1 SQFLEEGIGG 0.010 26 PSSWDYRCPP I0002 Z FSFQIFCSF l~ j~ RIKKGWEKSQ 0.1 131] YRCPPPCPAD 1 0 16 DTQTELELEF 0.020 32 KSQFLEEGIG 0.010I 29 1WDYRCPPPCP 0 i IFCSFADTQT I.00 1 ILFLPCISRK I01 19 PFSCLSLPSS 0.000 21 LELEFVFLLT 0.010 22 KLKRIKKGWE 0.010 6 SFQIFCSFA I0 ILGKIILFLP 1 TableXlX-V5A-HLA-B7.-10mers. 13 REFSFIQ 0.010 411 GGTIPHVSPE 0.010] 98P4B6 9 QIFCSFADTQ 1 18 CISRKLKRIK 0.010] Each peptide is a portion of SEQ ID 7 II FIQIFCSFAD J 1 28 1 KGWEKSQFLE 0.010 NO: 11; each start position is 1111 FCSFADTQTE 0015 421 GTIPHVSPER .1-0 specified, the length of peptide is 1 QTELELEFVF - .o6576__ 10 amino acids, and the end 18 06[QTELELE 001 LKRIKKGWEK 0.010T position for each peptide is the star 15 ADTQTELELE 0.003 PHVSPERVTV 0.003 position plus nine. 4 1 EFSFIQIFCS 0.002 24 J KRIKKGWEKS I0.002 Start Subsequence Score ] SFADTQTELE 0001 F i IKKGWEKSQF 0.002 S FWRGPWVA 0400 0

-

0 0 1 2U 1 RKLKRIKKGW 1 0.002 6 RLFTFWRGPV 0.300

~

0 SRKLKRIKKG 0.001 178 WO 03/087306 PCT/USO3/10462 TableXIX-V6-HLA-87-10mers- TableXIX-V7C-HLA-B7-10mers. 98P4B6 TableXIX-V7C-HLA-B7-10mers- 98P4B6 Each peptide is a portion of SEQ ID 98P4B6 Each peptide is a portion of SEQ ID NO: 13; each start position is Each peptide is a portion of SEQ ID NO: 15; each start position is specified, the length of peptide is 10 NO: 15; each start position is specified, the length of peptide is 10 amino acids, and the end position for specified, the length of peptide is 10 amino acids, and the end position for each peptide is the start position plus amino acids, and the end position for each peptide is the start position plus nine. each peptide is the start position plus nine. Start[ Subsequencel Score nine. Startl1 Subsequence Score 37l EEGIGGTIPH 0[00 StartI Subsequence Score 178 TQEQKSKHCM 0.300 F30 1I WEKSQFLEEG ].0 1 02 DPPESPDRAL 1120.000 161 SPAAAWKCLG 10.200 f29 I GWEKSQFLEE 0. F122 I LPHTNGVGPL 80000 [85 IPWGVVTED 1.200 S36 LEEGIGGTIP J 0.000 i 129 i GPLWEFLLRL 80.000 I 82 SSQIPVVGW 0200 F1137[ AANSWRNPVL 1 36-000 487 IPPLSTPPPP "0.200 TableXIX-V7A-HLA-B7-10mers- 127 GVGPLWEFLL 20.000 I 55]PPPAMWTEEA i 0.200 98P4B6 15 ASPAAAWKCL f12.0001 78 KSSSSSQIPV 10.200 Each peptide is a portion of SEQ ID (24 LGANILRGGL I 7 I SSSSSQPVV I 0.200 NO: 15; each start position is F152f FTSWSLGEFL 11 4.000 F 741 GIRNKSSSSS 0.200 specified, the length of peptide is 4 WQQDRKIPPL 10 amino acids, and the end 42 I WQQDRKPPL TPPPPAMWTE I0.200 position for each peptide is the start 16 1 FLGSGTWMKL I4.000 38 LPIEWQQDRK 0.200 position plus nine. I5 If VILDLSVEVL 4000 IAWKCLGAN11 0.180 ri t Subsequence I Score F126If NGVGPLWEFL 0 4000143 1 AASGTLSLAF F8 7 F2 SPKSLSETFL 80.000 1 [1411 SQAASGTLSL 14.0 501 PLSTPPPPAM _. [6_ ILSETFLPN1Gi 191 NPVLPHTNGV 11.000 1 SVEVSP 110150 I 9 TFLPNGING II 0.040 1 1481 LSLAFTSWSL 4.000 52 1STPPPPAMWT 0 150 1 IGSPKSLSETF 0. 020 19 AAWKCLGANI 3.600 44[ QDRKIPPLST ~5f 4 I KSLSETFLPN 1.020 28 ILRGGLSEIV 2.000 2 EVLASPAAW ElW 15 1 FLPNGINGIK I 0.010 1 68f KLETIILSKL 11 200 I 106 [SPDRALKAAN 020 S5II SLSETFLPNG I.0 20 AWKCLGANIL i 1.2001 581 GEFLGSGTWM 10 8l ETFLPNGING . I0F0165 TWMKLETIIL I 1.200 I 156_ S EFG T _1 l SETFLPNGIN 0.003 66f ATAEAQESGI 1.200 162 GFSGTWMKLET 0.100 3_. PKSLSETFLP [0.000 4f IVILDLSVEV 1.000 88 VGVVTEDDEA 0.100 135 LLRLLKSQAA 11.000 134 FLLRLLKSQA 0.100 STableXIX-V78-HLA.B7-10mers- 1 TIT KAANSWRNPV 0.008 LLKSQAASGT 0.100 98P4B6 164f GTWMKLETII 0.400 177 LTQEQKSKHC 0.100 Each peptide is a portion of SEQ ID 1 139 I LKSQAASGTL 01 I83 SQIPWGVVT 0.100 NO: 15; each start position is l1-1 L _ 0,0 specified, the length of peptide is 10 181 QKSKHCMFSL 0400 105iESPDRALKAA 0.100 amino acids, and the end position for 76 1 RNKSSSSSQI 11 0.400 116 [SWRNPVLPHT 0.100 each peptide is the start position plus 29 LRGGLSEIVL II 0400 9 LSVEVLASPA 0.100 e one. el I LPSIVILDLS 0.400 I57 1 PAMWTEEAGA 0.090 Start Subsequence Score 13o0f PLWEFLLRLL 0,400 185.. HCMFSLISGS 06 [T [2LNMAYQQSTLIf00 12 f NILRGGLSEI jf 0.400"1 11[ ALKAANSWRN 0.60 I8 I QQSTLGYVAL 00014.oAG GGLSEIVLPI 0400 1GANILRGGLS 9 If QSTLGYVALL 4.000 183 I SGTWMKLETI 4 0.400 1 64 1AGATAEAQES 10, STLGYVALLI 11 0.4O' .V 00 10 STLGYVALLI 0400 182f KSKHCMFSLI 0,400 36 IVLPIEWQQD 0.050 rI 7MYQQSTLGYVA I0. !" T4 ASGTLSLAFT 0.3001 87 WGWTEDDE 0.050 RI2 FLNMAYQQST I I0.100 4 1 PPLSTPPPPA 1031 I VVTEDDEAQD 0.0 I6 i AYQQSTLGYV If0.0670 871 i SSSQIPWVVGV I10300 89-- GVVTEDDEAQ 0.050 5 MAYQQSTLGY i0.060 iI QAASGTLSLA 1031 f 01] LAFTSWSLGE] I 4 If NMAYQQSTLG If o1o 1 I ( LASPAWKC [I 03001 TNGVGPLWEF 40.01 SS7 APAWK1F2 E I f LFLNMAYQQS 0.002 I 8 AMWTEEAGAT I RALKANSWR I030 179 WO 03/087306 PCT/US03/10462 TableXIX-V7C-HLA-B7-10mers- TableXX-VI.HLA.B3501.9mers. TableXX-VI-HLA-B3501-9mers. 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 10 specified, the length of peptide is 9 specified, the length of peptide is 9 amino acids, and the end position for amino acids, and the end position amino acids, and the end position ach peptide is the start position plus for each peptide is the start position for each peptide is the start position nine. _ plus eight. plus eight. Start Subsequence Score eStart rt Subsequece S e Subsequence 961 EAQDSIDPPE II 0.030 196 SSAREIENL I7.500] 65 i FASEFFPHV I1 _63 EAGATAEAQE I 0.030 9 t SPKSLSETC 6.000 365 0MSLGLLSL 100 26 ANILRGGLSE I0.030 1 317 VAYSLCLPM I F5 1847F QLNFIPIDL i1.000 51 LSTPPPPAMW ] 0.030 276 LAAAYQLYY 6.000 385 ALNWREFSF I1.0070 F69[ EAQESGIRNK 0.030 272 II LAGLLAAAY 116.0000 148 WSAWALQL 1.000 S171 PAAAWKCLGA ]0 12 YPESNAEYL 1600 274 GLLAAAYQ ]1 f65 [ GATAEAQESG .030] 46 TIRLIRCGY IF 144i KGFNWSAW 11.000 F114[ ANSWRNPVLP I 2671 LSLVYLAGL i5000 461 FNWSAWAL 1700 6 li ILDLSVEVLA 10 395 QSTLGYVAL 5.000 1 3 83 I SNALNWREF 18300 707[ AQESGIRNKSI 0.027 3661 MSLGLLSLL I. IL QLGLLSFFF I100 1147 I TLSLAFTSWS 0.020 220 11 ISLATFFFL 50 1 363 FGIMSLGLL 1.000i F1461 GTLSLAFTSW o.2 2501 IPIEIVNKT 14.000 217 WAISLATF 11 000 S140 KSQAASGTLS 0.020 11 2 1 ILIDVSNNM 4.000 57 i VIGSRNPKF .000 F180 EQKSKHCMFS 1'W [188 IPIDLGSLSj 4.000 [313 AMVHVAYSL 1 5 [ PPAMWTEEAG 10.020] 347 1 NSWNEEEVW 3.750 411 LYGWKRAF 1,000 145 SGTLSLAFTS 1"0.020 1133 LASLFPDSL II 3.000 i 3781 SIPSVSNAL ]000I F72I ESGIRNKSSS 10.020 300 QCRKQLGLL 3 000 I1264 ITLLSLVYL 1.000 218 I VAISLATFF 3.000 II DVTHHEDAL 1. TableXX-V1-HLA-B3501-gmers- [ 11 QVIELARQL 2000 436 LVLPSIVIL 000 98P4B6 303 KQLGLLSFF I2.000 8 72 ALTKTNIIF 1.0007 Each peptide is a portion of SEQ ID [ 371 LSLLAVTS I 2.000 [403' LLISTFHVL 1.000I NO: 3; each start position is I -I K__ specified, the length of peptide is 9 [12811 SNAEYLSL 1 1 r LQRKLG i: ] amino acids, and the end position [275 ] LLAAAYQLY 2.000 F400 I YVALLISTF 000I for each peptide is the start position 61 RNPKFASEF 2.000 258 I TLPIVAITL 1 1.000 1 "plus eight 1o0 SLWDLRHLL 2 .000 268 SLVYLAGLL 1.000 S Subsequence oiI HPYARNQQS 2.00 5i SMMGSPKSL 11.0001 I 62]1 NPKFASEFF 6 [ 379 IPSVSNALN 2.0001 [223II ATFFFLYSF i.000 323 I LPMRRSERY 140.000 [117 SNNMRINQY 112.000 33 1 VGVIGSGDF 1.000 157I GPKDASRQV I24.000 F 3061 GLLSFFFAM 2.00 [396I1 STLGYVALL I.000 191 LPIWITLL 2 0 [134 r ASLFPDSLI 2.0 2E61E IVAITLLSL 1.000 428 F TPPNFVLAL 120.000o 221 SLATFFFLY T.000 136 YISFGIMSL 1.000 FI291j FPPWLETWL [1 i l193I GSLSSAREI -2.000 219 1i AISLATFFF 1.000 438 LPSIVILDL 20.00 263 AITLLSLVY 2.000 1203 NLPLRLFTL 1.000 1 GPVWAISL [0R 90 FVAIHREHY I2.000 [ 129!1 NAEYLASLF 0.900 2371 FVRDVIHPY i12000 280 1 YQLYYGTKY 2.000 185 II KTNIIFVAI 0.800 1 GSGDFAKSL i10.000 13581 EMYISFGIM 2.000 1 127 ESNAEYLAS 10.750 405 ISTFHVLIY 7-10 000 -277 DARKVTVGV 1.800 386 LNWREFSFI 10.600 120411 LRLFTLW IVILDLLQL ] s15 ~ :L VLPSv 7 I.00 4L 239 I YARNQQSDF 900 16i ASRQVYICS I 4 16 KAFEEE YY 0.600 F41 FAKSLTIRL 90 1 411 FAKSLTIRL_1[ oo0! f jI GSRNPKFAS ][ I ~ 38 SERYLFLNM II 0.600 I 7 137 QARQQVIEL I9.00 I 1871 FIPIDLGSL i 1.500 KYRRFPPWL ][0.600 799 TSLWDLRHL 1 [2 DALTKTNII 1[.200 L41 GIKDARKVT 0.600 180 WO 03/087306 PCT/USO3/10462 NO: 11; each start position is Each peptide is a portion of SEQ ID TableXX-V2-HLA-B3501-9mers- specified, the length of peptide is 9 NO: 13; each start position is 98P4B6 amino acids, and the end position specified, the length of peptide is 9 Each peptide is a portion of SEQ 10D for each peptide is the start position amino acids, and the end position NO: 5; each start position is plus eight. for each peptide is the start position specified, the length of peptide is 9 I Start 1 Subsequence I Score I plus eight amino acids, and the end position [ lu e t.____ amino acids, and the end position 2 LPLRLFTFW I10.000 Start Subsequence Score for each peptide is the start position 1 NLPLRLFF 1 .000 46 2000 plus eight. 1 f NLPLRLFTF If F46 VSPERVTVM 1120000 I Start ubseuence II I FTFWRGPW 0.200 I 27 KGWEKSQFL 4.000 FStar Subsequence Score SCP9DFFLYF 1140.000 FWRGPWVA Ii 0.030 43 IPHVSPERV 4.000 F37 ICPADFFY 40.000 M 33 CPPPCPADF 112000 LFTFWRGPV 0.020 F-31 KSQFLEEGI 4.000 33 1 CPPPCPAF 20.000 r6 I 3!SPGLQALSL I I15 RLFTFWRGP 0.020 21 KLKRIKKGW 3.00 877 TFRGW 0.2 14 FPS R 1000 23 LSLPSSWDY 1110.0001 F 1 TFWRGPV .2 [ LPCISRKL I I ~ '3SLSLSSGF I 1O PLRLFTFWR E 0.0603 6[ VILGKIILF 11.000 r_35 PP_ _,00__I4 _! LRLFTFWRG 0.001 IVILGKIL 1 I35 PPCPADFFL tPPi-71 LKLL ][ 5I 7_Zd iLGKIlLFL 1.00 F34 PPPCPAFF 2 000 257 __ TabeXX-V5B-HLA-B3501-9mers- 1 KILFLPCI 0.800 15 SFSYC I Eachpopide98P4B6 20] RIKKGWEKS 0.600 I SGFTPFSCL P 0 Each peptide is a portion of SEQ ID 1 CISRKLKRI 1.400 F1 SGSPGLQAL NO: 11; each start position is [ IF SIVILGKII [ 0.400 I 12 SLSSGFTPF 1 .000 1 specified, the length of peptide is 9 r i F451 HVSPERVTV .0 5I GLQALSLSL ]1 amino acids, and the end position I VER 0.300 I 1 FTPFSCLSL 100for each peptide is the start position KKGWEKSQF 0.300 plus eight. 2 LPSIVILGK 110.200 20 FSCLSLPSS71vzv CSSS I ~ Start 1Subsequence ] Score I F15 LPCISRKLK 0.20 2 GSGLAL 67 5006 8 2 16 TQTELELEF 1120001 - 31 GIGGTIPHV I0.200 S SSGFTPFS24 FVFLLTLLL 11.0001 i 'T PSIVILGKI 0.200 14 SSFTFS 5007 F4 i]4 I! FSFIQIFCS I 0.:5001 [ 18 ]I ISRKLKRIK 11 0.150 21 SCLSLPSSW 0 5000 S SLSLSS U00 19 ELELEFVFL 0.450 1 39 IGGTIPHVS 0.o10 1 l Q SLS ~ i"i12 SFADTQTEL 0.20 I1 lIIILFLPCIS 3100 36 PCPADIFI.Y 0.300 1F -F IIICS7 18 C FLI j18 TELELEFVF 0 0200 L34 FLEEGIGGT l0.060 IC2 I I LELEFVFLL 10.2001 81 LGKIILFLP 0.o30 6 LQALSLSLS 0 100 REFSFIQIF I0.200 132 SQFLEEGIG I0.015 10 SLSLSSGFT 0,100 F2 f E F3 22F LEFVFLLTL I 0.100 35 LEEGIGGTI 1 i F277 SSWDYRCPP 0.100 370.1 [ 27 jf SSWDYRP 0100_]10 FCSFADTQT II 0.100 ] I 37 EGIGGTIPH I0 I1 11 LSLSSGFTP 0,050F I SL T I f1 QIFCSFADT 0 100 1 I GTIPHVSPE" J 0.010 F32 RCPPPCPAD r0 020 RP i23 EFVFLLTLL .1i0 40 GGTIPHVSP 0#h~ 8 -]ALSLSLSSG 0,010 23F40 E22 ALSLSSSG 0 1 1 FIQIFCSFA i0.100 1 VLPSIVILG 0. I 11 CSLPSrW I01141 ADTQTELEL I 0.1001 9 1 GKIILFLPC 0.010 29 Wr P 1 I SFIQIFCSF U 0 0.100 12 ii ILFLPCISR .10 24 SLPSSWDYR 0.010 S11 QTELELEFV 0.090 F 42 TIPHVSPER1 4 AL 0.010 l11 CSFADTQTE I0075 133I QFLEEGIGG I0.003 4 G 3LoI000 I 29 II WEKSQFLEE II 0.003 [16 GFTPFSCLS 0,010 16] C I 1 DTQTELELE II 0.015 I 2 K I KGWEKSQ ," 0.003 I [3C S01.03 T1 WREFSFIQI 0.012 22 LKRIKKGWE I 0.003 SF~Y Ft371 IQIFCSFAD o0.00 193 SRKLKRIKK 0.003I 19 EPFSCLSLPS 0.001-IF D I___ PFSCLSLPS [I0 ]~3 EFSFIQIFC 0.01 o20 RKLKRIKKG 0.0021 28 1SWDYRCPPP 0.000 3 siQp ovF200.2 WD1P3-l FADTQTELE I.0o09 2 3 'KRIKKGWEK l0.0 90mr. IFCSFADTQ 30001 4 I 4 I3 PHVSPERVT 110.001] TableXX-VSA.HLA-B3501-9mers- 44 PISRK] 98P4B6 13 LFLPCISRK 0.00 D TableXX-V6-HLA-B3501-9mers- M30 EKSQFLEEG .001 ] Each peptide is a portion of SEQ IDI 98P4B6 6 0.001 181 WO 03/087306 PCT/US03/10462 TableXX-V6-HLA.B3501 -9mers. specified, the length of peptide is 9 TableXX-V7C-HLA-B3501-9mers. 98P4B6 amino acids, and the end position 98P4B6 Each peptide is a portion of SEQ ID for each peptide is the start position Each peptide is a portion of SEQ ID NO: 13; each start position is plus eight. NO: 15; each start position is specified, the length of peptide is 9 Start Subsequence [ Score specified, the length of peptide is 9 amino acids, and the end position [181 KSKHCMFSL II 30.000 amino acids, and the end position for each peptide is the start position 15 j SPAAAWKCL [2.000 for each peptide is the start position .. plus eight. 139 KSQAASGTL - plus eight. start. Subsequence Score I Start [ Subsequence I Score 36 EEIGGTI 0. 150 LSTPPPPAM 10.000 [ 36 ~ G TIP1 0.001 --- LSTPPPPAM 1 42 ![ QQDRKIPPL I0.300 [_?8 _I 152 ~~TSWSLGEFL 5.000 F4 QRIP _300 28 GWEKSQFLE 0.0007 13 TSWSLGEFL 5.000 F 73[ GIRNKSSSS I 0.300 1I3I ASGTLSLAF I 5.000Gi 165 MKLTIIL 4.50 F177 AAAWKCLGA 0.300 TableXX-V7A.HLA.B3501-9mers. 165 WMKLETL II 4.500 1421 AAMSGTLSLA 1 0.300 98P4B6 F101 I DPPESPDRA 1 4. 128 GPLWEFLLR 0.300 Each peptide is a portion of SEQ ID [179 I EQKSKHCMF II 3.000 1 18 ) WKCLGAN 03001 NO: 15; each start position is 24 GANILRGGL 113.000 specified, the length of peptide is 9 14 1 il QAASGTLSL 3.000 15 I LDLSVEVL [ 0.300 amino acids, and the end position 0 136 RLLKSQAAS 0 for each peptide is the start position 1.8 R ALKAASW .000 82 IPSQlPWGVV 0.200 plus eight. 29 !RGGLSEIVL 42.000 IPPLSTPPP startI Subsequence Score 52I TPPPPAMWT 2000 5I 57I PPAMTEEA 10.200 SPSST 60.00 275I PMTEAI .0 1 SPKSLSETF 60.000 27 I ILRGGLSEI I12 121 LPHTNGVGP 0200 L9 FLPNGINGI 0 .400 [78 SSSSSQIPV M1.o00 129 PLWEFLLRL 0.200 1 1 SLSETFLPN 0.200 126 1 GVGPLWEFL I1.000I 8 QEQKSKHCM 1F0200 311 KSLSETFLP 0150 1131 ANSWRNPVLI 1.000 117 RNPVLPHTN 0.200 7 i ETFLPNGIN J0. O 14 IIESPDRALKA 1.000 7 ETFLPNGIN 1 [ S A .000 2 SIVILDLSV 0.200 F6 I SETFLPNGI 0.040 160 LGSGTWMKL I1.000 l58 EFLGSGTWM I0.2 ' 57 LSETFLPNG 0.015 I 2 VGPLWEFLL 11.04 IPVVGTE 0.200 2 7PKSLSETFL 0.010 SSSSQIPW I1.o000 118I NPVLPHTNG '0.200 811 TFLPNGING 0.001 F 148 SLAFTSWSL 57 1.7 1 AMWTEEAGA II 0.150 151 FTSWSLGEF 1l SKLTQEQK II 015 Ta beXX-V7-HLA-B3501-9mers. 1257 NGVGPLWEF 1.000IFE 7_L~ DLSVEVLAS II0.150 98P4B6 F 1 SSQIPVVGV 1.000 881 GVVTEDDEA 10.150 Each peptide is a portion of SEQ ID F 31 [ GLSEIVLPI I 0.800 1 AWKCLGAI NO: 15; each start position is i154 WSLGEFLGS 0750 0,120 specified, the length of peptide is 9 0 54 r EF F98 DSIDPPESP 0.00 amino acids, and the end position 1 2 I PPESPDRAL I0.600 1f45 GTLSLAFTS 0.100 for each peptide is the start position I 112 AANSWRNPV 80.600 3[]! QIPWGVVT 0.100 plus eight. I 105 SPDRALKAA 0.600 I8 LSVEVLASP 0.100 Start [1 Subsequence 11 Score 68 EAQESGIRN 10.600 I 811 LSVEVLASP I0.100 8 1 QSTLGYVAL 50 151 STPPPPAMW 0.500 169 ETIILSKLT 0.100 S9 STLGYVALL 1.000 147[ LSLAFTSWS ) 0.500 169 ESG KLT 01 I3 7 NMAYQQSTL I1F.0 I' [ 46 TLSLAFTSW 0.500 62i SGTWMKLET 0.100 [6 7 YQQSTLGYV 0.200 12 VLASPAAAW 0.500 1211 ANILRGLS 0.100 5 AYQQSTLGY I 0.200 V71 ESGIRNKSS 0.500 12 SGIRNKSS 0.0 72 SGIRNKSSS 0.0 17 QQSTLGYVA l 123)1 HTNGVGPLW I 0.500 1r T L F FLNM QS 0500 F144 SGTLSLAFT 0.100 1 "]h FLNMAYQQS 1i oTool 114 ASPAAAWKC'""WI 0.500 [T FR71GATAAOES1 0.50 1 40 SQAASGTLS 0.100 I121i[ LNMAYQQST 110.100 4I ! GATAEAQES ]1KS0.450 0.40 F_77 KSSSSSQIP 0.100 I4 I MAYQQSTLG 0.030 163 GTWMKLETI I I 0.400_ KSSS __P r1851 CMFSLISGS 0.100 37 LIEWQQDR 0.400 .A-B501-mers 4 ETP20 WVKCLGANIL 0.100 TableXX-V7C-HLA-B3501-9mers- 4 VILDLSVEV 0.400 98P4BS 951 EALVV 1~~ QDSIDPP 10.060) ,Each peptide is a portion of SEQ ID ' ' 34 ! LLRLLKSQA 110.300 I KANWRP 0060 NO: 15; each start position is 7 RNKSSSSSQ 0.060 182 WO 03/087306 PCT/US03/10462 TableXX-V7C-HLA-B3501-9mers- Table XX-V1-HLA-83501-10mers- TableXXI-VI-HLA.B3501-10mers. 98P4B6 98P486 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 3; each start position is NO: 3; each start position is specified, the length of peptide is 9 specified, the length of peptide is 10 specified, the length of peptide is 10 amino acids, and the end position amino acids, and the end position for amino acids, and the end position for for each peptide is the start position each peptide is the start position plus each peptide is the start position plus plus eight. nine. nine. Start Subsequence Score Start Subsequence Score Start Subsequence Score I591 WTEEAGATA I0060 F 1271 ESNAEYLASL I5-7 F49 ,LIRCGYHWI 1.200 SPSIVILDLS j'0.050 141 ISMMGSPKSL 1434_ LALVLPSIVI 1.200 S80 I SSSQIPVVG II 0.050 382 I VSNALNWREF I5.000 133 LASLFPDSLI 1.200 1157 GEFLGSGTW 377 11 TSIPSVSNAL 0 24 GIKDARKVTV 1.20 S33] SEIVLPIEW I 050 428 TPPNFVLALV 4.000] 241 RNQQSDFYKI [1.200 161 GSGTWMKLE I 0.0501 18871 IPIDLGSLSS 4.000 32 TVGVIGSGDF 1.000 114 NSWRNPVLP II 0.050 I 111 I KILIDVSNNM 14.000 i4357 ALVLPSIVIL I1.000 76 NKSSSSSQI 0.040 181 LARQLNFIPI 13.600 273) AGLLAAAYQL 1.00 I164 TWMKLETII I 040 27 DARKVTVGVI 1 3.600 l361 IGSGDFAKSL 1.000 182 SKHCMFSLI II 0.040 41 FAKSLTIRLI 3.600 I 308 LSFFFAMVHV 1.00 39 IEWQQDRKI I 0.040 384 NALNWREFSF 3.000 56 VVIGSRNPKF 1.000 58 MWTEEAGAT 0.030 3121 FAMVHVAYSL 13.000 1761 QQVIELARQL [i1.00 89_ VVTEDDEAQ 0.030 [222q LATFFFLYSF r3.000 1296 ETWLQCRKQL I[1 [81 Jj DALTKTNlIF 3.000 43 i KSLTIRLIRC ][. I TableXXI-VI-HLA-B3501-10mers- 218 VAISLATFFF IF 3.000 202i ENLPLRLFTL 1.000 98P4B6 1 322 CLPMRRSERY 112.000 F 147 NWSAWALQL I1.000 I Each peptide is a portion of SEQ ID 429 PPNFVLALVL I 2.000 217 WASLATFF 1.ooo NO: 3; each start position is _ speciied, thelenthofpepdeis 10 316 HVAYSLCLPM 2.000 216 1 VVVAISLATF IF 1.000 I specfe, thegtho peptide is10 -7M amino acids, and the end position for F61 RNPKFASEFF 1 2.000 13 I YLASLFPDSL 1.000 each peptide is the start position plus [ 257 KTLPIVAITL II 2.000 364 GIMSLGLLSL 1 .000 nine. 1259 LPIVAITLLS 12.000 3651 IMSLGLLSLL I1I.000 Sta Subsequence I core 45 LTIRLIRCGY 2.000 9271 AIHREHYTSL I1.00oj 157 ] GPKDASRQVY 240.000 276 LLAAAYQLYY 2.000 314 MVHVAYSLCL 1.0 9 1 SPKSLSETCL 60.00 274 ~~GLLAAAYQLY ~2001 VLIYGWKRAF 1.000 1250 IPIEIVNKTL 40.0001 3031 KQLGLLSFFF .5 29971 LQCRKQLGLL 1.000 197 SAREIENLPL II 27.000 128 SNAEYLASLF F2.000 394 IQSTLGYVAL 1.000 S323 1 LPMRRSERYL II 2Noo2 NQYPESNAEY [ 20 11 KSLSETCLPN 1.000 I S438 1 LPSIVILDLL II 20.000 305 LGLLSFFFAM 263 ] AITLLSLWL I. I 239 YARNQQSDFY 18.o000 44[ LISTFHVLIY 2 0- 14 72 0 IQARQQVIEL 1I 4171 RAFEEEYYRF 118.0001 12137 RGPWVAISL I2000 219 AISLATFFFL 1.000I 1379 IPSVSNALNW 10.000 [271 [YLAGLLAAAY I 2.0 298 WLQCRKQLGL 1.000 1161 VSNNMRINQY 110. 000 183 RQLNFIPIDL 2.000 I 37 GSGDFAKSLT 1.000 1 FSFIQSTLGY 1 10.000 1 4I[ GPVWAISLA II 0.000 2 ALLISTFHVL 1.000 22071 ISLATFFFLY I 1134 II ASLFPDSLIV 1.500 I 258 TLPIVAITLL 1.0 11951 LSSAREIENL 4 7.5 4 SIVILDLLQL I 1.500 427 I YTPPNFVLAL 1.000I 137 FPDSLIVKGF 6.000 98 TLDR 11.0 27 1 FPDRSERYLFLNM I6000 9I YTSLWDLRHL 1 .500 1139 DSLIVKGFNV 1.000 I 1 RSERYLFLNM EMT I 1 !ASRQVYICSN II 1.5 437 VLPSIVILDL I[.0 I 262 1I VAITLLSLW 6.000 285 IGTKYRRFPPW I11.500 [266 LLSLWLAGL 1.000I S361 ISFGIMSLGL 5.000 DLRHLLVGKI 1.200 395 QSTLGYVALL I5.000 336 iMAYQQVHANI 1.200 TableXXI-V2-HLA-B3501-10mers S267 LSLWLAGLL 2555.00 VNKTLPIVAI I . _98P41B6I 99 TSLWDLRHLL 5.000 651 FASEFFPHW II [ Each peptide is a portion of SEQ ID 183 WO 03/087306 PCT/US03/10462 NO: 5; each start position is Start Subsequence [Score amino acids, and the end position for specified, the length of peptide is [1 ENLPLRLFTF [1.000 ach peptide is the start position plus 10 amino acids, and the end -- ER1 nine. position for each peptide is the start NLPLRLFTFW 1 position plus nine. [6I1' RLFTFWRGPV TII0.40 L _tart ________e uen~ core r~ubegue... ....... 3 LPSIVILGKI 8.000 Start Subsequence I [ J FTFWRGPWVV 0[.20j 0 LPSIVLGKI [ 3 PCADFF 3_ LPLRLFTFWR 10.044 IPHVSPERVT J2. 000 33j CPPPCPADFF 2000 _3 LPLRLFTFWR 0.200 F-6- -- r46 jHVSPERVTVM 2.000 35 [ PPCPADFFLY 000 10 FWRGPWVAI 0.120 HVSPERVVM 1000 14 SSGFTPFSCL 5.000 7 7 LFTFWRGPW 0,020 6 IVILGKIILF 1[ 1.000 -11 LSLSSGFTPF 5.000 9 TFWRGPVVVA 0.010 I -7 VILGKIILFL 1000 5 SIVILGKIlL 1M00 2 GSPGLQALSL 50 4LJ[ PLRLFTFWRG 10003 '" I LGKL F5100 I20I FSCLSLPSSW I I[500 LRLFTFWRGP I 26 IKKGWEKSQF [0.450 PPFF j RLFTFWRGP [109 I LGKIILFLPC [10300 34 PPPCPADFFL 1 2,000 1 3! SPGLQALSLS 2.0 TableXXI-VSB.HLA-3501-10mers.

[-J

35 FLEEGIGGTI 10.240 22 CLSLPSSWDY 12.0 98P4B6 0.42300 TIPHVSPERV .200 S32 RCPPPCPADF 2.000 Each peptide is a portion of SEQ ID [ I KIILFLPCIS 0200 181 TPFSCLS ]2,000 NO: 11; each start position is 27[ KKGWEKSQFL 10.200 STPFSCLSLPS specified, the length of peptide is r 38 IEGIGGTIPHV 0.200 SALSLSLSSGF 10 amino acids, and the end LPCISRKLKR 116 IILPCISRKLKR I0.200 9 LSLSLSSGFT 0.500 p osition for each peptide is the start PSIVGKII 13 I LSSGFTPFSC 0.00 position plus nine. . 200........ I25 71 LPSSWDYRCP I Start I Subsequence ] 27 [32 KSQFLEEGIG 0.150 [4[ PGLQALSLSL" 5i0 I -12] CSFADTQTEL ]5.000 F19 ISRKLKRIKK 0.150 JJ SGFTPFSCLS 5 FSFlQFCSF1 5.000 39 GIGGTIPHVS 10100 r1 SsWDYRCPPP! 0.100 .... 6 DTQTELELEF 1.000 LFLPcsRKL . 16] GFTPFSCLSL 0. 14 FADTQTELEL I.900 21 RKLKRIKKGW 0100 -67 LQALSLSLSS TQTELELEFV .6250 RIKKGWEKSQi 0.060 F 1 SGSPGLQALS 0.100 I V F 11 00 22 LKRIKKGWE 0.060 24 SLPSSWDYRC .. 18 QTELELEFVF II 50.300 10 GKIILFLPCI 0.040 SPCPADFFLYF 0.100 2 ELELEFVFLL 1 0.300 [I287( KGWEKSQFLE 0.040 I T 3 ! GCP DF LLS 010100G319S TELELEFVFL1~~ 0.300 i II PCISRKLKRI 10.040 EKSQFLEEGI 0.4 112 SLSSGFTPFS I 1 NWREFSFIQI 0.240 [ EKSQFLEEGI 1040 723 LSLPSSWDYR I 0.050 I I IQIFCSFADT I0.100 24 KRIKKGWEKS II0.020 24 EFVFLLTLLL 0.100 33 SQFLEEGIGG 0.015 F771 QALSLSLSSG II oG30 -7 -1 ILEV TLL II010 ) I SQFLEEGIGGI0.2 I30I DYROPPPCPA 0030 FVFLLTL 0.100 I 337 fli2 FTPFSCLSLP I OO3 1 I WREFSFIQIF I0.030 13 ILFLPCISRK I0.010 177 FTPFSCLSLP 0.010 I3 SLSLSSGFTP I 0. 1 1 REFSFIQIFC II 0.020 ] 18I CISRKLKRIK 0.010 10 SLSLSSGFTP 001 F: SCLSLPSSWD 0,iO -21 LELEFVFLLT I 0.020 . .8 1 ILGKIILFLP I0.010 I 26 I![PSSWDY RCPP !1[011 FCSFADTQTE 0.01 5 I 2 ! VLPSIVILGK 0.010 267 PSSWDYRCPP 0.005 F17F27 IPSVLK Ini F 128SWDYRCPPPC I0.03J 1 IFCSFADTQT 1 0.010 40 IGGT-IPHVSP 0.010 E 77WDYRCPPPCP_ 0o 7 FIQIFCSFAD 0.010 15 I FLPCSRKLK 0.010 2WDYRCPPPCP 0.001 19 IPFSCLSLPSS .1 04001.i I17 GGTIPHVSPE i 31 I YRCPPPCPAD 0.0 9 QIFCSFADTQ 0.010 LVLPSIVILG 0010 i1 SFIQIFCSFA 0.010 r 427 GTIPHVSPER 0.010 13 SFADTQTELE 0002 I121 IILFLPCISR 0.010 TableXXI-V5A-HLA.B3501-10mers- 1 ADTQTELELE 0002 45 PHVSPERVIV 0.003 98P4B6 20 SRKLKRIKKG 0. Each peptide is a portion of SEQ ID I 3 WEKSQFLEEG 0.003 NO: 11; each start position is TableXXl-V6.HLA-B3501.-10mers. I 23 1 LKRIKKGWEK 0.003 specified, the length of peptide is 10 98P4B6 I 371 EEGIGGTIPH 0.001 amino acids, and the end position for Each peptide is a portion of SEQ ID 3 II EEGIGGTIP 0.000 each peptide is the start position plus NO: 13; each start position is __36 _1 _________ [L nine. specified, the length of peptide is 10 I29 iGWEKSQFLEE 0.000 184 WO 03/087306 PCT/USO3/10462 TableXXI-V7C-HLA-B3501-10mers- TableXXI-V7C-HLA-B3501-10mers. TableXXI-VA-HLA-3501-10mers- 98P4B6 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 15; each start position is NO: 15; each start position is NO: 15; each start position is specified, the length of peptide is 10 specified, the length of peptide is 10 specified, the length of peptide is amino acids, and the end position for amino acids, and the end position for 10 amino acids, and the end each peptide is the start position plus each peptide is the start position plus position for each peptide is the start nine. nine. position plus nine. Start I Subsequence ie Start 1 Subsqece Score SSube sequence 31 LWEFLLRLLK 4500 94 DDEAQDSIDP 0022 f-2 7 SPKSLSETFL 60.000 2.5 12 0.020 1~h PKSLSETF 160000 VTEDDEAQDS I2,250 12VT3 EVLASPAAAW Ir10203 l iF GSPKSLSETF !5.00 SVEVLASPAA 1.800 4 IVILDLSVEV j0.020 P4 IF 55671____ F-527 i i r 4 KSLSETFLPN . 52 F71 STPPPPAMWT 1.250 173 ILSKLTQEQK .020 6 LSETFLPNGI 0.600 6 1.000 47 KIPPLSTPPP 0.020 STFLPNGINGI 5 168 KLETiILSKL 0.900 113 AANSWRNPVL 0.020 5i SLSETFLPNG I0.020 l PPESPDRALK 2 E SISSS 015 F10 FLPNGINGIK 10.010 271 GVGPLWEFLL 1 0 43 QQDRKIPPLS 7 SETFLPNGIN 0.010 143 AASGTLSLAF . 15 ASPAAAWKCL 0.015 8 ETFLPNGING I 10.030 1 VL7 [1 KSQAASGTLS ]3.315 3 i PKSLSETFLP i 0.000 I [ LSTPPPPAMW 0.300 9~[ LSVEVLAS IFPA 0.015 F601 WTEEAGATAE 0.225 [82 ISSQIPVVGW l0.015 B-HLA-B3501 0mers- [157 LGEFLGSGTW 0.225 3 F 1557[ WSLGEFLGSG jf 0.015 3 TableXXI-V7B-HLA-B350110mersE L 98P4B6 691 EAQESGIRNK 110.200 ESPDRALKAA I.0-15 Each peptide is a portion of SEQ ID 97 AQDSIPPES 0.150 [ 148 II LSLAFTSWSL 0.015 NO: 15; each start position is [70 AQESGIRNKS [ 0.135 1 124 oHTNGVGPLWE 0.013 specified, the length of peptide is 10 TQEQKSKHCM 1 0.135 11 GPLWEFLLRL i 0.013 amino acids, and the end position for 170 ETlSKT 011 GGLSEIVLPI 0.013 each peptide is the start position plus ES 128 VGPLWEFLLR 4 SGTLSLAFTS 0.013 SStart Sub ce I Score [ VLPIEWQ QDR .10 185 II HCMFSLISGS 0010.010 5 L71MAYQQSTLGY 6.000 14 LASPAAAWKC 10.1001 F1491 SLAFTSWSLG I1I 9 QSTLGYVALL 1 5.000 IF6 1 TEEAGATAEA 0.090 65 IGATAEAQESG 0017 I3II LNMAYQQSTL 1.000] I 391 PIEWQQDRKOO I 0.090 I 112 1 KAANSWRNPV o. I 87 QQSTLGYVAL I1.00 16211 GSGTWMKLET 110.075 142 QAASGTLSLA f0.010 I10 STLGYVALLI 0.400 7871 KSSSSSQIPV 0.075 125 GANILRGGLS I0.010 71_ YQQSTLGYVA 0. 10 160I FLGSGTWMKL I 0.050 1 I59 EFLGSGTWMK 0.010 i 1 FLNMAYQQST 1MS 100 2 KCLGA NILRG 0.050 [23 CLGANILRGG 0.010 I6l AYQQSTLGYV i0.020 F6711 MKLETIILSK 10.050 I 1097 RALKAANSWR II 010 400 NMAYQQSTLG 1 381 LPIEWQQDRK 0.050 176 1 KLTQEQKSKH 0.010 I 11 LFLNMAYQQS 0.010 80 SSSSIPWG 351 EIVLPIEWQQ 1 0.010 F SSSSSQPVV 0.030 1751 SKLTQEQKSKf 0.010 TableXXI-V7C-HLA-B3501-10mers.i SQIPWGVVT 0.030 8 AAAWKCLGAN 0.o0 98P4B6 F 1441 ASGTLSLAFT 0.030 36 IVLPIEWQQD ] 0,010 Each peptide is a portion of SEQ ID F 81 I SSSQIPVVGV 0.030 5 VILDLSVEVL 0.010 SNO: 15; each start position is [14611 GTLSLAFTSW 1 0.025 1721 IILSKLTQEQ 0.010 specified, the length of peptide is 10 661 ATAEAQESGI 0.025 156 )ILGEFLGSGT 1 amino acids, and the end position for 5 0 each peptide is the start position plus F1527 FTSWSLGEFL 0.025 120 PVLPHTNGVG 0 .010 nine. 1251 TNGVGPLWEF 0.025 14 TLSLAFTSWS I0.010 Start Subsequence Score F 92 ] TEDDEAQDSI 8 0.025 89 GVVTEDDEAQ 0.010 100 SIDPPESPDR 100000 177 LTQEQKSKHC 10.025 1531 TSWSLGEFLG 0.008] 67 TAEAQESGIR 9.000 [ 1 WKCLGANILR 2 PSIVILDLSV .008__ 33 ILSEIVLPIEW 6.750N I2 5 141 11 1 0.0071 185 WO 03/087306 PCT/USO3/10462 TableXXl-V7C-HLA -B3501-.10mers- Table VIII-V13.HLA.A1.9mers. 5 l QEQKTKHCM 0 .000 98P4B6 98P4B6 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID Table VllI-V25-HLA-A1-9mers. NO: 15; each start position is NO: 27; each start position is 98P4B6 specified, the length of peptide is 10 specified, the length of peptide is 9 Ee p amino acids, and the end position for amino acids, and the end position Each peptide is a portion of EQ I each peptide is the start position plus for each peptide is the start position NO: 51; each start position is nine. lus eight specified, the length of peptide is 9 rt I ne 1 Subsequence e Scor amino acids, and the end position Start Subsequece Score core for each peptide is the start position 150 f LAFTSWSLGE 0.005 7 ETFLPNGIN 0.025 plus eight. FI 17[ PAAAWKCLGAFO [s 0a TFLPNGING 0.025 Starti Subsequence Score 101 IDPPESPDRA 50.005 9 FLPNGINGI I 0.010 2 f LFLPCISQK 0.100 !151i AFTSWSLGEF 1 0.00 3 i KSLS 0.007 1 ILFLPCISQ 0.050 11 7 WRNPVLPHTN I0.005 1 SPKSLSETF 0.003J II PCISQKLKR 0I 5 42f WQQDRKIPPL f 0003 [6 SETFLPNGI 0.0011 L ii LPCISQKLK I0.050 104 PESPDRALKA 0.003 _ 2 PKSLSETFL 0.00 7 I ISQKLKRIK 0.030 [ 24 LGANILRGGL i 0.003 8 SQKLKRIKK IF 0.015 S119f NPVLPHTNGV I 003 Table VIII-V14-HILA-A1- I II FLPCISQKL F 0.010 118 [ RNPVLPHTNG I 9mers-98P4B6 6 CISQKLKRI F0 010 10 1 DPPESPDRAL 0.003 Each peptide is a portion of SEQ ID 9 QKLKRIKKG I53 TPPPPAMWTE I 0.003 NO: 29; each start position is specified, the length of peptide is 9 ........ specified, the legamino acids, and the end position Table IX-V8-HLA.Al-10mers for each peptide is the start position 98P4B6 Table VIII-V8-HILA-AI-9mers- plus eight. Each peptide is a portion of SEQ ID 98P4B6 Start[ Subsequence I Score NO: 17; each start position is Each peptide is a porton of SEQID i4 NLPLRLFTF 1 0.500 specified, the length of peptide is NO:. 1;ecsato 10 amino acids, and the end NO: 17; each start position is r___ FTFWRGPVVI 0.050osition for each peptide is the start specified, the length of peptide is 9 3] PLRLFTFWR I 0.005 p osition h plueptie s the start amino acids, and the end position f 1 pst pus ne for each peptide is the start position 5 5I RLFTFWRGP 0.001 StartL Subsequence plus eight. F6 LFTFWRGPV 0.001 5I FLEEGMGGTI 0.900 Start I Subsequence Score 4 ILRLFTFWRG Io.001 2 KSQFLEEGMG I .05 I 4 1 FLEEGMGGT f 10.900 2 LPLRLFTFW 0.0001 3 1 SQFLEEGMGG 0.007 F5 LEEGMGGTI 0.045 9 IFWRGPVVVA 0.0001 I8 EGMGGTIPHV [ 0.005 1 L1 I KSQFLEEGM T0.015 TFWRGPVVV! 0.000 9 GMGGTIPHVS IF 000 [ EGMGGTIFPH .013 LEEGMGGTIP 0.005 GMGGTIPHV 0.010 Table VIlI-V21-HLA-Al-gmers. - 7 ] EEGMGGTIPH 0.003 S9f MGGTIPHVS 98P4B6 II QFLEEGMGGT f . 001 0 i 31 QFLEEGMGG f- 031 Each peptide is a portion of SEQ IDl GGTIPHVSP I SfQFLEEGMG f 0.00 NO: 43; each start position is 1 F2 1 SQFLEEGMG .00 specified, the length of peptide is 9 I 1 I EKSQFLEEGM II 0.001 6 EEGMGGTIP 0.000] amino acids, and the end position for each peptide is the start position Table IX.V13-HLA.AI-10mers Table VIII-V13-HLA-AI-9mers- plus eight. 98P4B6 98P4B6 Itartl Subsequence I Score Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID F2 7 KLTQEQKTK I 0200 NO: 27; each start position is NO: 27; each start position is 4 II TQEQKTKHC 135 specified, the length of peptide is specified, the length of peptide is 9 3 I LTQEQKTKH I0 025 10 amino acids, and the end amino adds, and the end position i 8 II KTKHCMFSL position for each peptide is the start for each peptide is the start position I position plus nine. plus eight. II EQKTKHCMF 2 I Start Subsequence Score I Start Subsequence co I TKHCMFSLI .0I 6-1 LSETFLPNGI 1.350 5 LSETFLPNG 2,700t E SKLTQEQKT I i0.001 10 FLPNGINGIK 0.200 .4 _ SLSETFLPN 0.05 0 QKTKHCMFS It0.000 i8 I ETFLPNGING 0.1251 186 WO 03/087306 PCT/USO3/10462 Table IX-V13-HLA-Al-10mers- LSKLTQEQKT 02 Table X-Vi 3-AO201-9mers-8P4B6 91P4B6 7 I EQKTKHCMFS I0.001 I Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID 6

'

QEQKTKHCMF 0.001 NO: 17; each start position is NO: 27; each start position is I-8 QKTKHCMFSL 0.000 specified, the length of peptide is 9 specified, the length of peptide is amino acids, and the end position for 10 amino acids, and the end each peptide is the start position plus position for each peptide is the start -eight. position plus nine. Table IX-V25-HLA-AI-10mers- start Subsequence Scor Start Subsequence Score 98P4B6 1 FLPNGINGI 379 1 I4 KSLSETFLPN 0.075 Each peplide is a portion of SEQ ID I KLSTFPN . .04 I-SLSETFL.PN ""0.581 5 SLSETFLPNG 0120 NO: 51; each start position is SLSETFLPNI 0.581 - specified, the length of peptide is SETFLPNGI 02 1I: GSPKSLSETF 10.015 10 amino acids, and the end 3 KSLSETFLP I0.007 9 TFLPNGINGI I 0.005 position for each peptide is the start PKSLSETFL 7 SETFLPNGIN 10I position plus nine. 5 LSEFLPNG I o. I 2 SPKSLSETFL 0.000 Start Subsequence II Scorel F TFLPNGING II oo E 8 TFLPNGING 0.000 3 PKSLSETFLP 7 CISQKLKRIKI 0.20 7 ETFLPNGIN 000 4 II FLPCISQKLK 70.200 SPKSLSEF 2 ILFLPCISQK -0.20 Table IX-V14-HLA-Al-10mers. 18 ISQKLKRIKK 0.150 98P4B6 5 LPCISQKLKR 0.125 Table X-V14-AO201-9mers-98P4B6 Each peptide is a portion of SEQ CID 1 ISLFLP Q 0.05 Each peptide is a portion of SEQ ID NO: 29; each start position is I31 LFLPCISQ I NO: 29; each start position is specified, the length of peptide is 3 LFLPCISQKL I 0.005specified, the length of peptide is 9 10 amino acids, and the end 16 II PCISQKLKRI 0.001 amino acids, and the end position for position for each peptide is the start F9 SQKLKRIKKGf 0.000 each peptide is the start position plus Istarit SbseqenceI[~~) - E ~eight. Scr position plus nine. I I QKLKRIKKGW I0.000 Subsequence ight. Start] Subsequence Score Str Subsequence-Score I1l ENLPLRLFTF _1[0 7 FTFWRGPW 1 6.741 8 iFFWRGPVVV 0 5 Table X-VS-A0201-9mers-98P4B6 i NLPLRLFTF 0.994 [ LPLRLFTFWR . o013 Each peptide is a portion of SEQ ID -~ 8 TFWRGPWV 0.164 21 NLPLRLFTFW I0.010 NO: 17; each start position is [5 RLFTFWRGP 110.071 6 RLFTFWRGPV 0.1 specified, the length of peptide is 9 [_2 LPLRLFTFW 0.0321 __7__I_____WR __ Jamino acids, and the end position 1 6-7 LFTFWRGPV 11I 7~ LFTF RGPW ][ 0CO 1 for each peptide is the start position i PLRLFTFWR 4 [PLRLFTFWRG I1.0 plus eight.3 PLRLFTFWR 0.003 FL10[ FWRGPVWVAI St t Subsequence I sc 441 LRLFTFWRG 0.001 5II LRLFTFWRGP ] I I GMGGTIPHV 1134 _ 9 I FWRGPVVVA 0o.0 E9][ TFWRGPWVA 0 ~41 FLEEGMGGT 2.689 _ 11 KSQFLEEGM 0.056 Table X-V21-AD201.9mers. Table IX-V21-HLA-Al-10mers- F2J[ SQFLEEGMG 1 0.004 . 9846 98P4B6 ELEEGM Each peptide is a portion of SEQ ID Te. NO: 43; each start position is Each peptide is a portion of SEQ ID [3 _ QFLEEGMGG i0.001 specified, the length of peptide is 9 NO: 43; each start position is NO: 43; each start position is 9 ' MGGTIPHVS 0.000 amino acids, and the end position spe10 amino acids, and theend [ i EGMGGTJPH 0.000 for each peptide is the start position 10 a inoacis, nd te ed E MGGIPHplus eight. positionn or each peptide is the star Star Subsequenc II io o ta] position plus nine. Subseuence Score Start I KTKHCMFSL f0.485 Table X-V13-A0201.9mers98P4B61 II QEQKKHCM I0.97 5 I1 TQEQKTKHCM I0135 Each peptide is a portion of SEQ ID TQEQKTK JI 0.052 4 LTQEQKTKHC F0.025 NO: 17; each start position is 2 KL 3 KLTQEQKTKH 0.010 specified, the length of peptide is9 1 SKLTQEQKT 0.038 2 ]SKLTQEQKTK 0 amino acids, and the end position for '4 I TQEQKTKHC 0.032 ][ KTKHCMFSL 10.003 I each peptide is the start position plus E T TKHCMFSLI 0.028 I eight. ~~TKHCMFSLIS 1 eight. Sc 3 I LTQEQKTKH I 0.007 JI_ II [~Start Subseuence 187 QKTKHCM 0 187 WO 03/087306 PCT/USO3/10462 Table X-V21-A0201-9mers- NO: 27; each start position is 7 EQKTKHCMFS 0.001 98P4B6 specified, the length of peptide is 6 QEQKTKHCMF 0.001 Each peptide is a portion of SEQ ID 10 amino acids, and the end I 81 QKTKHCMFSL 10.000 ] NO: 43; each start position is position for each peptide is the start __ specified, the length of peptide is 9 position plus nine. IX amino acids, and the end position I Start j Subsequence Iscore Table X-V25-HLA-A0201-10mers for each peptide is the start position 5 1 SLSETFLPNG 2.670 98P4B6 plus eight I 9II TFLPNGINGI I 0062 Each peptide is a portion of SEQ ID Start Subsequence o NO: 51; each start position is 6~E~KITM 0000 2 SPKSLSETFL 0.027 specified, the length of peptide is [_ EQTKHC 0.00 1 4 KSLSETFLPN 0.012 10 amino acids, and the end 6 1 LSETFLPNGI 0.007 position for each peptide is the start Table X-V25-A0201-9mers- 10 FLPNGINGIK 0 004 position plus nine. ,, 98P4B6 FI -7 F IEFPGIGJ Start]

!

SbeuneJ Score Each peptide is a portion of SEQ ID I 81 ETFLPNGING II 0I LISq 0 NO: 51; each start position is 1 GSPKSLSETF 0.000 specified, the length of peptide is 9 F7 ESETFLPNGIN . I .LFLPCISQKL ifO.093 amino acids, and the end position 3 I PKSLSETFLP If ~_00 FLPCISQKLK 0 for each peptide is the start position J IILFLPCISQ 110.013 pluseight. X-V14HLA A0201-mers PCISQKLKRI I0.003 start l Subsequence Scre Table X-Vi4HLAA201-10mers-.R 1111 CS sco8e98P4B6 ji SQKLKRIKKG 0.001 3 1 FLPCISQKL"l 97 Each peptide is a portion of SEQ ID 10 QKLKR~KKGW .5000 [6 l CISQKLKRI I 3299 J NO: 29; each start position is L7 I CISQKLKRIK 1 0.000 I1 ILFLPCISQ _ specified, the length of peptide is F[8 ISQKLKRIKK [.00 9 [ QKLKRIKKG 0I00 10 amino acids, and the end 5 LPCISQKLKR 1'0.000 1 4 LPCISQKLK I0 000 position for each peptide is the start I position plus nine. F2 LFLPCISQK 01 00001 r-a Ir Subsequence 8 SQKLKRIKK il0 [000S Table Xll.V8-HLA-A3-9mers 6 87 RLFTFWRGPV J 33.455 .V8-HLAA39me 7l ISQKLKRIK II060 IFFRP I671I98P4B6 ISQKL ~ 8 11FTFWRGPVVV 6.7413 5I PCIISQKLKR oI FTFW 7790 0Each peptide is a portion of SEQ ID 2 0779 NO: 17; each start position is 1 3 1 LPLRLFTFWR 0.074 I specified, the length of peptide is 9 7 7H 2 LFTFWRGPW 0.034 amino acids, and the end position Table X-V8-HLA-A201-1 9 TFWRGPVVVA [ 0.027 for each peptide is the star position I8 plus eight. Each peptide is a portion of SEQ ID I II ENLPLRLFTF 0.002us e NO: 17; each start position is 4 __1 PLRLFTFWRG [ 02 I GMGGTIPHV 5 specified, the length of peptide is I 10 1 FWRGPWVA 0.001 GMGGT0IPHV .3 10 amino acids, and the end 4 FLEEGMGGT 0.0 position for each peptide is the start LRLFTFWRGP 0.000 KSQFLEEGM J 0.003 position plus nine. I2 ii SQFLEEGMG J0.00 Start Subsequence Score Table X.V21HLA-AO201-10mers- 5[ LEEGMGGTI 0.001i 5 FLEEGMGGTI J 1.637 98P4B6 EGMGGTI 0.00 8F-B EGMGGTIPHV i Each peptide is a portion of SEQ ID EGMGGTIPH NO: 43; each start position is 3 QFLEEGMGG 0 F3 SQFLEEGMGG .028 specified, the length of peptide is 9JI MGGTIPHVS ]Fo.00] S4 IIQFLEEGMGGT 0.023 10 amino acids, and the end 8 EEGMGGTIP 0.000 S9F GMGGTIPHVS 0022 position for each peptide is the start 1 EKSQFLEEGM TIa XVm position plus nine. ers I 2 II KSQFLEEGMG JI o start Subsequence 11 s Table XIIV13.HLA.A3.mers.6 51 MGGTIPHVSP 1 I TQEQKTKHCM 0135 Each peptide is a portion of SEQ ID 7 I EEGMGGTIPH 0 00 4 II LTQEQKTKHC II 0.025 NO: 27; each start position is I6 II LEEGMGGTIP 0.000 3 KLTQEQKTKH 010i specified, the length of peptide is 9 I2 I SKLTQEQKTK I0.010 amino acids, and the end position Table X-V13-HLA-A0201.mersl I 9 I KTKHCMFSLI o ofor each peptide is the start position T e 1 2 01-10mers - 9 TKHCM 0.003 plus eight. 98P4B6 J 1101I TKHCMFSLIS 10,0031- Score] !Start E Subsequence Scr Each peptide is a portion of SEQ ID I 1I LSKLTQEQKT I 0.002 188 WO 03/087306 PCT/US03/10462 Table XII-V13-HLA-A3-9mers- 9 TKHCMFSLI 0.002 Table XI-V13-HLA-A3-10mers. 98P4B6 I 5 QEQKTKHCM I0.001 1 98P4BB Each peptide is a portion of SEQ ID 1 I] SKLTQEQKT 0.000 Each peptide is a portion of SEQ ID NO: 27; each start position is QKKHC 0.000 NO: 27; each start position is specified, the length of peptide is 9 [.0 specified, the length of peptide is amino acids, and the end position 10 amino acids, and the end for each peptide is the start position Table XII-V25-HLA-A3-gmers- position for each peptide is the start plus eight 98P4B6 position plus nine. r Subsequence Sco] Each peptide is a portion of SEQ ID Start Ssi u Score 97 FLPNGINGI 0.900T NO: 51; each start position is N e I 9.000 _ SiSETFLPN ) 0. specified, the length of peptide is 9 ai FLPNG 4 SLSETFLPN 0.180 5 SLSETFLPNG 0.135 amino acids, and the end position F_7 1 SPKSLSETF I 0.020 for each peptide is the start position 1 GSPKSLSETF IF0030 6 SETFLPNGI 0.002] plus eight. FL 1 0 3 KSLSETFLP I0.001 I Startl Subsequence 1Score 6 L ~GL I 0.003 7 ETFLPNGIN I0.001 8 SQKLKRIKK I 1.200 ETFLPNGING ]0.003 5 LSETFLPNG I0.000 3 FLPCISQKL I0.900 I4[ KSLSETFLPN 10.003 8 If TFLPNGING ]0.000 1 1 ILFLPCISQ 10.300 91I TFLPNGINGI 0.002 2 1 PKSLSETFL ~. 4 [[ LPCISQKLK 0.100 I 7L SETFLPNGIN 0.000 2 LFLPCISQK 0.068 31 PKSLSETFLP I0.000 r_6i , CISQKLKRI 0.045 Table XII-V14-HLA-A3-gmers- 5 PCISQKLKR 1 0.012 Table XIll-V14-HLA-A3-10mers. 98P4B6 9812437 F ISQKLKRIK 0.010 98P4B6 Each peptide is a portion of SEQ ID [ ISQKLKRIJ .1 NO: 29; each start position is [ QKLKRIKKG 1 0.000 Each peptide is a portion of SEQ ID O NO: 29; each start position is specified, the length of peptide is 9 specified, the length of peptide is amino adcids, and the end position Table XIII-V8-HLA-A3-10mers- 10 amino acids, and the end for each peptide is the start position 98P4B6 position for each peptide is the start plus eight. Each peptide is a portion of SEQ ID position plus nine. Start Subsequence I Score NO: 17; each start position is S tartl Subsequence IS 1 f[ NLPLRLFTF ]. specified, the length of peptide is 6 RLFTFWRGPV 0900 3 PLRLFTFWR 3.600 10 amino acids, and the end position for each peptide is the start [2 I NLPLRLFTFW I000 II fFTFWRGPVV II 000 ]position plus nine. 3 II LPLRLFTFWR 1 040 5 l RLFTFWRGP I0.030 Startl Subsequence II Score f78 FTFWRGPVVV I 05 2I: I LPLRLFTFW 0.1009 9 ] GMGGTIPHVS F-502705 [4 ] PLRLFTFWRG 0i018 I9 9 FWRGPWVA 0.001 I FLEEGMGGT I1 0.270 1 I ENLPLRLFTF Ii 0012 I 8-- TFWRGPWV 13 SQFLEEGMGG 10.006 9f TFWRGPVA 0.05I 4 ILRLFTFWRG r0.000 I EEGMGGTIPH 0.000 10 WRGPVVVA 0.004 6I LFTFWRGPV 00I 8 EGMGGTIPHV I0.000 "7 I LFTFWRGPW II0.0001 4_T QFLEEGMGGT 1"0.000 1 5I LRLFTFWRGP II.000 I 98P4B6 1 [6 IfLEEGMGGTIP 0.000P4B Table XII-V21-HLA-A3-9mers- 6 LEEGMGGTIP 10.0oo 98P4B36 2 I KSQFLEEGMG !0.0 Table XIII-V21-HLA-A3-10mers Each peptide is a portion of SEQ ID 11 EKSQFLEEGM [0.000 98P4B6 NO: 43; each start position is MGGTIPHVSP 11 0.000 Each peptide is a portion of SEQ ID specified, the length of peptide is 9 NO: 43; each start position is amino acids, and the end position Table 1 specified, the length of peptide is for acpidis the sn position Table XIII.V3-HLA-A3-1Omers- 10 amino acids, and the end plus eight. 98P4B6 J position for each peptide is the start IStart[ Subsequengh s[ I Each peptide is a portion of SEQ ID position plus nine. _ _ S e nNO: 27; each start position is IStartl Subsequence tScore I KLTQEQKTK 30,000 I specified, the length of peptide is 3 KLTQEQKTKH 0.600 I a] KTKHCMFSL 0.405 1 0 amino acids, and the end I KL KTKH_ I o.270 6 EQKTKHCMF 0.018 position for each peptide is the start I KTKHCMFSL 0.270 I 3I LTQEQKH position plus nine. 2 21 SKLTQEQKTK 0 .015 I I TQEQKKH I Start Subsequence Score T LTQEQKTKHC 0.007 S TQEQKKHC 10.00389 189 WO 03/087306 PCT/US03/10462 6 QEQKTKHCMF 0.0061 plus eight. Each peptide is a portion of SEQ ID 5 TQEQKTKHCM [0.00 6 Startl Subsequence ]tScre NO: 51; each start position is 8 7 QKTKHCMFSL 0.003 9 FLPNGINGI [ 0.004 specified, the length of peptide is 9 Samino acids, and the end position I7 1 EQKTKHCMFS [0.001 l II SPKSLSETF )I 0.002 for each peptide is the start position I1 II LSKLTQEQKT I0.001 1411 SLSETFLPN I 0.001i plus eight. I101 TKHCMFSLIS [0.000 [7 ETFLPNGIN 0.00t IStartl Subsequence Score ] 8 TFLPNGING 0.001 8 SQKLKRIKK 1.200 Table XII.V25-HLA-A3-10mers. 6 I SETFLPNGI 170.001 2 [ LFLPCISQK 0.300 98P4B6 3 I KSLSETFLP 0.000 4 II LPCISQKLK I 0.100 Each peptide is a portion of SEQ ID 2 PKSLSETFL [ 0.000 5 PCISQKLKR 0.012 NO: 51; each start position is I TFLN 3 specified, the length of peptide is 5 LSETFLPNG 0.000 3 FLPCISQKL .004 10 amino acids, and the end 7 ISQKLKRIK 0.002 position for each peptide is the start Table XIVV14-HLA-A1101- 16 CISQKLKRI [0.00 position plus nine. 9mers-98P4B6 _1 ILFLPCISQ 0.002I artl Subsequence Score Each peptideisa portion of SEQ ID I9 QKLKRIKKG 10.000 2I ILFLPCISQK 1150.000 NO: 29; each start position is 4 I FLPCISQKLK i10.000 specified, the length of peptide is 9 I I K Kamino acids, and the end position S ISQKLKRIKK 0.200 for each peptide is the start position Table XV-8HLA-A11-10mers F7 CISQKLKRIK 0 .200 plus eight. 98P4B6 S5 LPCISQKLKR 0.[ 0080 Start Subsequence Score Each peptide is a portion of SEQ ID 1I[ IILFLPCISQ 0.009 3 PLRLFTFWR I .0 NO: 17; each start position is __3 _ 0002 r7 FTFWRGPVV ~specified, the length of peptide is IT [LFLPCISQKL 0.00 7__ __TFWRGPVV_ 0.00_0amn I 1FPSK_____ L _ 000 10 amino acids, and the end 6 PCISQKLKRI 0.001 NLPLRLFTF I01 position for each peptide is the start 9 I SQKLKRIKKG ][.000 8 TFWRGPVVV 004 position plus nine. 1I QKLKRIKKGW 2]f LPLRLFTFW 10.003 i Subsequence I Score 6 LFTFWRGPV 1 0002 5 FLEEGMGGTI 0.000 TableXlV-V8.HLA.Al101.9mers. 5] RLFTFWRGP 0.000 3 SQFLEEGMGG 0.2 98P4B6 9 FWRGPWVA 00 9 I GMGGTIPHVS 0.001 Each peptide is a portion of SEQ ID 00 LRLFTFWRG ]1I7 I EEGMGGTIPH II o. NO: 17; each start position is -1 QFLEEGMGGT lfT specified, the length of peptide is 9 .... T. . amino acids, and the end position Table XIV-V21-HLA-A1101. 8 EGMGGTIPHV .00_ for each peptide is the start position 9mers-98P4B6 2 KSQFLEEGMG I 0.000 1 plus eight. Each peptide is a portion of SEQ ID 6 LEEGMGGTIP I 0.000 start Subsequence Score NO: 43; each start position is V1 EKSQFLEEGM I0. 8 GMGGTIPHV I1,350 specified, the length of peptide is 9 MGGTIPHVSP 8 GMGGT amino acids, and the end position I i I FLEEGMGGT I 0.068 for each peptide is the start position 1 KSQFLEEGM 0.003] plus eight Table XV-V13-HLA-Al1-10mers I2 SQFLEEGMG I 0.001 Fstart Subsequence I Score 98P4B6 5 LEEGMGGTI 0.001 2 KLTQEQKTK f 0.600 Each peptide is a portion of SEQ ID 7 EGMGGTIPH I 0000 I81 KTKHCMFSL 0.090 ] NO: 27; each start position is _3_______ _ -E specified, the length of peptide is 3 QFLEEGMGG 1 000 LTQEQKTKH I 0.010 10 amino acids, and the end 91_I MGGTIPHVS 6[ iooo LII[ EQK[KHCMF 0 .002 position for each peptide is the start 6 I1 EEGMGGTIP 0.000 i 5i QEQKTKHCM 0.001 position plus nine. 4 II TQEQKTKHC Start Subsequence I Sco fTable XIVV13-HLA.A1101-. 91 TKHCMFSLI Io.o 1l FLPNGINGIK I0.0 9mers-98P4B6 rC 7! 09 TFLPNGINGI I.03 Each peptide is a portion of SEQ ID TE S .02 I SPKSLSETFL II 0.002 1 NO: 27; each start position is 8i ETFLPNGING I.001 specified, the length of peptide is9 8 1 I G NPILSETF I 0 0017 amino acids, and the end position Table XIV-V25-HLA-A1101- GSPKSLSETF 001 for each peptide is the start position 9mers98P4B6 I SLSETFLPNG I I0.000 190 WO 03/087306 PCT/USO3/10462 6 I LSETFLPNGI 0.000 Start[ Subsequence I Score Eachpeptideis a portionof SEQ ID 4 KSLSETFLPN I 0.000 ILFLPCISK NO 29; each start position is S SETFLPNGIN 0.000 2F specified, the length of peptide is 9 IiI4 I FLPCISQKLK 0.200 amino acids, and the end position 5 LPCISQKLKR 0.080 r each peptide is the start position plus eight. Table XV-V14-HLA-A11-10mers- ISQKLKRIKK s.040 Startl Subsequence I Score I 98P4B6 7 CISQKLKRIK I I 0.040I NLPLRLFTF II3.000 Each peptide is a portion of SEQ ID LFLPCISQKL 0.003 TFWRGPVVV 0.500 NO: 29; each start position is I1 IILFLPCISQ 0 o.oo001 [ i LFTFWRGPV specified, the length of peptide is g] SQKLKRIKKG 00 0 L LPLRLFTFWRGPV 0.500 10 amino acids, and the end QKLKRK LPLRLFTFW 1 0.216 position for each peptide is the start KKRIKKGW . 7 FTFWRGPVV 0.] position plus nine. __ E:]I PCISQKLKRI 0.000~ FWRGPWVA JIT Ire 5 RLFTFWRGP 0VA . 3 LPLRLFTFWR 0.18-0 Table XVI-VB-HLA-A24-9mers- 4_1 LRLFTFWRG 0.002 6 RLFTFWRGPV 0024 98P4B6 8 FTFWRGPVVV 002 Each peptide is a portion of SEQ ID 3 PLRLFTFWR 0.001 I NO: 17; each start position is 91 TFWRGPVVVA T . specified, the length of peptide is 9 Table XVI-V21-HLA-A24-9mers I2- NLPLRLFTFW 1 0.004 amino acids, and the end position 981P4B6 17 LFTFWRGPVV [ 0.002 for each peptide is the start position Each peptide is a portion of SEQ ID l 1 7I ENLPLRLFTFJ 0.00] plus eight. NO: 43; each start position is 10) FWRGPWVVVAI 0 [000 StartI Subsequence Score specified, the length of peptide is 9 S4 I PLRLFTFWRG .0 0 I 1 KSQFLEEGM 1.800 amino acids, and the end position l LRLFTFWRGIt ! _FLEEG_ GT 08 for each peptide is the start position F FLEEGMGGT 0.150 pl vus eight_ _ [51 LEEGMGTi0. I 10 start Subsequence I Score TableXV-V21-HLA-A11.10mers- 9 MGGTIPHVS 0.140 r 8 KTKHCMFSL 8.0 98P4B6 _.8 _ GMGGTIPHV I oF6 EQKTKHCMF i2.000 Each peptide is a portion of SEQ ID I1 QFLEEGMGG I.9 1411 TQEQKTKHC 0. NO: 43; each start position is [ 7 EGMGGTIPH 0.015 1 TKHMFSLI I specified, the length of peptide is 21 SQFLEEGMG I QETKHCMFSLI 0.120 10 amino acids, and the end 5 QEQKTKHCM 0.075 position for each peptide is the start - EGMGGTP I KLTQEQKTK 0.020 position plus nine. [II SKLTQEQKT 0.020 [Score Table XVI-V1 3-HLA.A24-9mers- 3 LTQEQKTKH 0.020 I9t KTKHCMFSLI 0.030 98P4B6 .P... 2 ISKLTQKTKHCFSI 0. Each peptide is a portion of SEQ ID QKTKHCMFS S 27 IKLTQEQKTK 1 0.015 NO: 27; each start position is S31 KLTQEQKTKH 12 specified, the length of peptide is 9 Table XVI-V25-HLA-A24-9mers 5 TQEQKTKHCM I 0.006 amino acids, and the end position 98P4B6 I 8 QKTKHCMFSL 0.001 for each peptide is the start position Each peptide is a portion of SEQ ID r . II QEQKTKHCMF 0.001 I plus eight. NO: 51; each start position is 4 LTQEQKTKHC I 0.001 Stat Subsequence Fi Score specified, the length of peptide is 9 I 7 EQKTKHCMFS ] 0.000 1 t SPKSLSETF ! 2.400 amino acids, and the end position KIl __TKHCMFSIl 9 FLPNGINGI 1.800 for each peptide is the start position TKHCMFSLIS 0 4 plus eight. S LSKLTQEQKT 0.000 4 SLSETFLPN 0.1 start Subsequence 1 Score 6 ( SETFLPNGI I 4 13 FLPCISQKL 111.088 Table XV-V25-HLA-AlI-10mers. 7 ETFLPNGIN 00 6I CISQKLKRI 1 T0 98P468 0.090 2 LFLPCISQK .0 Each peptide is a portion of SEQ ID 2 PKSLSETFL 0.040 i7 I SQKLKRIK I 0.018" NO: 51; each start position is 3 KSLSETFLP 0.0301 SQKLKRIKK] specified, the length of peptide is 5 L LSETFLPNG 01 8 SQKLKRIK0 .011 10 amino acids, and the end - 1L ILFLPCISQ 0.010 position for each peptide is the start r-4 I LPCISQKLK 10.010 position plus nine. TableXVI-V14-HLA-A24-9mers- QKLKRIKKG L0.002 191 WO 03/087306 PCT/USO3/10462 Table XVI-V25-HLA-A24-9mers- Each peptide is a portion of SEQ I 7 E CISQKLKRIK 10.012 I 98P4B6 NO: 29; each start position is SQKLKRIKKG 0.011I Each peptide is a portion of SEQ ID specified, the length of peptide is !5 LPCISQKLKR 0.0I11 NO: 51; each start position is 10 amino acids, and the end 0-11 specified, the length of peptide is 9 position for each peptide is the start 11 ILFLPCISQK 0.010 amino acids, and the end position position plus nine. for each peptide is the start position Start Subsequence Score Table XVIII-V8-HLA-97-9mers. plus eight. 1 II ENLPLRLFTF II 3.60098P4B6 Start Subsequence I Score [i FWRGPVVVAI 1.400 Each peptide is a portion of SEQ ID S PCISQKLKR 0 .002 _ _ LFTFWRGPW 0. 50 NO: 17; each start position is specified, the length of peptide is 9 I9 [ TFWRGPVVVA t 0 amino acids, and the end position TableXVIIVHLAA24-10mers 2 NLPLRLFTFW 0.216 for each peptide is the start position 98P4B6 RLFTFWRGPV 0.200 plus eight. Each peptide is a portion of SEQ ID B_ RLFTFWRGPV I0 I - ii NO: 17; each start position is FTFWRGPVVV It Subsequence specified, the length of peptide is _ 1 LPLRLFTFWR 0.015 1 [KSQFLEEGM I00 10 amino acids, and the end 5 j LRLFTFWRGP 0.002 I8 GMGGTIPHV [ 0.200 position for each peptide is the start 4 PLRLFTFWRG 0001i I 7 EGMGGTIPH 0.030 position plus nine. I 4: i FLEEGMGGT I 0.030 Start SubsequenceI Score Table XVII-V21-HLA-A24-10mers-] 9 MGGTIPHVS F9 0.020 5 FLEEGMGGTI 111.8007 98P4B6 5 [ LEEGMGGTI 0012 T -1 QFLEEGMGGTI 0-900 Each peptide is a portion of SEQ ID i 2 7 SQFLEEGMG I .010 81 EGMGGTIPHV" 0.150] NO: 43; each start position is 6 [ EEGMGGTIP t 0.001 S9] GMGGTIPHVS 0I .140i specified, the length of peptide is I1 EKSQFLEEGM I.6 10 amino acids, and the end I 3 QFLEEGMGG 0.001 - position for each peptide is the start r 21 KSQFLEEGMG 0.030 position plus nine. Table XVIII-V13-HLA-B7-9mers [101 MGGTIPHVSP 0.010 start[ Subsequence II Score I 98P4B6 SSQFLEEGMGG 0.010 9 KTKHCMFSLI 2.400 Each peptide is a portion of SEQ ID 61 LEEGMGGTIP I0.002 LI TQEQKTKHCM 0.750 NO: 27; each start position is 7 rEEGMGGTIPH 0.001 8 KTKHC specified, the length of peptide is 9 ,,TKHCMFSL 0400 amino acids, and the end position ITableXVIIV36 QEQKTKHCMF 0.300 for each peptide is the start position TableXVi-V13-HLA-A24-10mers7 i LTQEQKTKHC 0.180 - plus eight. 98P4B I LSKLTQEQKT 0.132 1 Start [Subsequence Score Each peptide is a portion of SEQ ID

-

EQKTKHCMFS 1I 9 FLPNGINGI I NO: 27; each start position is J _09 specified, the length of peptide is .3 iKLTQEQKTKH 0.022 1 ] SPKSLSETF I0.400 10 amino acids, and the end I I TKHCMFSLIS 0.01 6[ SETFLPNGI 1[0.040 position for each peptide is the start I 2 SKLTQEQKTK 0.002 2 PKSLSETFL 0.040 position plus nine. -I 7 I1 ETFLPNGIN 0.030 Start Subsequence Score Table XVII-V25-HLA-A24-10mers. [4 0 SLSETFLPN II0 1 TFLPNGINGI .800 98P4B 3I KSLSETFLP t 0: 2 SPKSLSETFL r.0 Each peptide is a portion of SEQ ID -5 I LSETFLPNG I 0.003 1 ]GSPKSLSETF [3.600 NO: 51; each start position is TLPNGING I 00 6 LSETFLPNGI I2.6 specified, the length of peptide is 4 KSLSETFLPN 06 10 amino acids, and the end position for each peptide is the start 10 FLPNGINGIK 0021 position plus nine. S5 1 SLSETFLPNG 0012 I Start Subsequence" Score 7 SETFLPNGIN I I0.010 3 IF LFLPCISQKL I66.528 Table XVIII-Vi4-HLA.B7-9mers 81 ETFLPNGING I6 PCISQKLKRI [ 0.150 I 98P4B6 3 PKSLSETFLP U.000 I -10 QKLKRIKKGW 00 Each peptide is a portion of SEQ ID 8 1 ISQKLKRIKK I0.017 NO: 29; each start position is Table XVII-V14-HLA-A24-10mers-. 4_ r FLPCISQKLK i0. ! specified, the length of peptide is 9 98P4BS amino acids, and the end position B1 [IILFLPCISQ I0.015 for each peptide is the start position 192 WO 03/087306 PCT/US03/10462 plus eight. 98P4B6LFTFWRGP 0.020 Start Subseuence Score Each peptide is a portion of SEQ ID 1 ENLPLRLFTF 0.020 LPLRLFTFW 0.400 NO: 17; each start position is 9 TFWRGP 0015 FWRGW 0.200 specified, the length of peptide is 11 PL1F0101 E 10 amino acids, and the end 9 FWRGPVVVA 50 position for each peptide is the start L1 6 LFTFWRGPV 0.030 position plus nine. SsTFWRGPVVV 0020 Startl Subsequence IScore Table XlX-V21.HLA.B7-10mers 1 NLPLRLFTF 0.020 8 EGMGGTIPHV 0.600 98P4B6 3 PLRLFTFWR I0.010 5 IFLEEGMGGTI 0.120 Each peptide is a portion of SEQ ID RLFTFWRGP IJ EKSQFLEEGM NO: 43; each start position is 5 RFTFRGP 0.00 1 EKSQFLEEGM 0.100 LQFFW P 0.10 ______specified, the length of peptide is LRLFTFWRG 1 11 GMGGTIPHVS 0.020 10 amino acids, and the end 110 1 MGGTIPHVSP ]0.015 position for each peptide is the start Table XVIII-V21-HLA-B7-9mers. 4 QFLEEGMGGT 0.010 position plus nine. 98P4B6 3LLI SQFLEEGMGG 0 .010 stI Subsequence 11Score Each peptide is a portion of SEQ ID 2 KSQFLEEGMG 010 [ 9]1 KTKHCMFSLIU .400 NO: 43; each start position is 7 EEGMGGTIPH 0.001 QKTKHCMFSL .400 specified, the length of peptide is 9 i0 0MGGiP 1I 0.01 TEQKTKHCM ][ 0.400 3 amino acids, and the end position LEEGMGGTIP 5 TQEQKTKHCM 0.300 for each peptide is the start position LSKLTQEQKT [0.10 pSi Table X IX-V13-HLA-BT7-10mers- [4 LTQEQKTKHC o0.100oo Start Subsequence Score 98P4B6 7 1 EQKTKHCMFS 0.020 8 KTKHCMFSL 4.00 Each peptide is a portion of SEQ ID 3 KLTQEQKTKH 0.010 5 QEQKTKHCM [T NO: 27; each start position is 10 TKHCMFSLIS 0.002 !THMSI specifiedie, the length of peptide is QEQKTKHCMF 0002 ................ .... 0.. 10 amino acids, and the end 4 TQEQKTKHC 0.030 position for each peptide is the start 2 II SKLTQEQKTK 0II 1 I 6 I EQKTKHCMF I 0.020 position plus nine. S LTQEQKTKH 0.010 Istart I Subsequence IFScore Table XIX-V25.HLA.B7-10mers. 1 ]1 SKLTQEQKT I 0010 EI1 SPKSLSETFL 180.000 98P4B6 2 KLTQEQKTK 0.010 LSETFLPNGI 0.120 Each peptide is a portion of SEQ ID 71 QKTKHCMFS K 0.002 I 9 TFLPNGINGI 0.040 NO: 51; each start position is I specified, the length of peptide is 1 GSPKSLSETF I0.020 10 amino acids, and the end Table XVIII-V25-HLA-B7-9mers. 4 KSLSETFLPN 0.020 position for each peptide is the start 98P4B [10 FLPNGINGIK 0.010i position plus nine. Each peptide is a portion of SEQ ID 1 SLSETFLPNG 0.01i0 SI7tart I Subsequence ,I Score NO: 51; each start position is -i ETFLP 13 LFLPCISQKL U0.400 specified, the length of peptide is 9 FLPNGI I I LCSQKL .0 amino acids, and the end position LPCISQKLKR 0.200 for each peptide is the start position [T j PKSLSETFLP II 0.000 i 6 PCISQKLKRI I 0.040] plus eight. 181 ISQKLKRIKK 0.015 Start Subseuenc [Score] Table XIX-V14-HLA-B7.-10Omers. M I IILFLPCISQ 0.15 3 FLPCISQKL I 4.000 98P4B6 7 CISQKLKRIK I 0.010 E6 II CISQKLKRI 0.400 Each peptide is a portion of SEQ ID I4 1 FLPCISQKLK '0.00 T LPCISQKLK I NO: 29; each start position is I9 11 SQKLKRIKKG 0.i1I 11 SQKLKRIKK I Ospecified, the length of peptide is ILFLCISQK 10 amino acids, and the end I _I SK I 1 F-1 ILFLPCISQ 0015 position for each peptide is the start I 1 I QKLKRIKKGW I0.002] S7 II ISQKLKRIK 0.010 position plus nine. 19 I QKLKRIKKG 0.001 Sta Subsequence Score Table XX-V8-HLA-B3501-9mers 2 1 LFLPCISQK I0.001 10 FWRGPWVA 0.400 98P4B6 I 5 PCISQKLKR 6 RLFFWRGPV 00 Each peptide is a portion of SEQ ID S FTFWRG I NO: 17; each start position is specified, the length of peptide is 9 3II LPLRLFTFWR II 0.20_0 amino acids, and the end position Table XIX-V8-HLA-B7-10mers- 2 1 NLPLRLFTFW I 02 for each peptde is the start position 193 WO 03/087306 PCT/USO3/10462 plus eight. Each peptide is a portion of SEQ ID E7 ' EEGMGGTIPH 0.001 Start Subsequence [Score NO: 43; each start position is LEEGMGGTIP 0.000 1 KSQFLEEGM 20.000 specified, the length of peptide is 9 1 E [amino acids, and the end position 81 GMGGTIPV _ 0.200 for each peptide is the start position TableXXl-V13-HLA-B35-10m Oers g 9 MGGTIPHVS I0.00 plus eight. 98P4B6. . _ FLEEGMGGT [ 0.060 St art Subsequence IIScore Each peptide is a portion of SEQ ID 1 SQFLEEGMG 1i IKTKHCMFSL !.001 NO: 27; each start position is I ____I _ LO 01 I 11 __-rCM II 3.60specified, the length of peptide is 5 LEEGMGGTI 0012 61 EQKTKHCMF 3.000 10 amino acids, and the end 7 EGMGGTIPH 5 010 1 QEQKTKHCM 0.200 1p osition for each peptide is the start 3 QFLEEGMGG 0103 TKHCMFSLI ].040 position plus nine. 2EEGMGGTIP 0 2 KLTQEQKTK Start Subsequence Score 4 1 - 1 2 1! SPKSLSETFL 11600001 4 TQEQKTKHC 0.030 2 SPKSLSETFL 6000 Table XX-V13-HLA-B3501-9mers- F 3 LTQEQKTKH] j I GSPKSLSETF 5000 98P4B6 J 7 QKTKHCMFS 0 1 KSLSETFLPN I1.0 Each peptide is a portion of SEQ ID SKLTQEQKT 6 I LSETFLPNGI I 0.600 NO: 27; each start position is I TFLPNGINGI I 0.040 specified, the length of peptide is 9G amino acids, and the end position Table XX-V25-HLA-83501-9mers.- 5 ii SLSETFLPNG 0.020 for each peptide is the start position 98P4B6 110 1 FLPNGINGIK 0.010 plus eight. Each peptide is a portion of SEQ ID 7 1 SETFLPNGIN I 0.10 StartI Subsequence [Score NO: 51; each start position is 8 ETFLPNGING L01 I SPKSLSETF 60.0001 specified, the length of peptide is9 KSLSETFLP S SS amino acids, and the end position I I J FLPNGINGI I[ 0400] for each peptide is the start position I4 SLSETFLPN 0.200 _ plus eight. Table XXIJ-V14-HLA-B35-10mers 3 KSLSETFLP I o0.150 starti Subsequence S cr 98P4B6 7 ETFLPNGIN I o.o100 3 I1 FLPCISQKL 1.000 Each peptideis a portion of SEQ ID 161 6!1 tSQLKR I! NO: 27; each start position is 6 SETFLPNGI 0.040 6 CISQKLKRI 0.400 NO: 27; each start position is 001 specified, the length of peptide is 5 LSETFLIPNG 0. 01 5 4 LPCISQKLK 0201 J LSETFLPNG II oo_ I L C I SQKLK_ 0 10 amino acids, and the end I 2 II PKSLSETFL 00107 7 ISQKLKRIK 0.50 position for each peptide is the start 18 II TFLPNGING I . 8 SQKLKRIKK ] 9 positionin plus nine. _ F1l ILFLPCISQ 0.010 Start[ Subsequence ScoreI Table XX-V14-HLA-B3501-9mers- I 9 QKLKRIKKG 001 I 1 ENLPLRLFTF 1 .000 98P4B6 2 2 LFLPCISQK 1 0.001 1 NLPLRLFTFW 0.500 Each peptide is a portion of SEQ ID 5 I PCISQKLKR RLFTFWRGP NO: 29; each start position is -'"8 I FTFWRGPWV I 0200 specified, the length of peptide is 9 I FTFW amino acids, and the end position Table XXI-V8-HLA-B35-10mers- LPR T 0.200 for each peptide is the start position 98P4B6 I 10 I FWRGPWVAIl 0.120 plus eight. Each peptide is a portion of SEQ ID I I LFTFWRGPVV I o.020 I Start Subsequence S NO: 17; each start position is 1 TFWRGPVVVA I0. 2 LPLRLFTFW I 10.000 specified, the length of peptide is PLRLFTFWRG 0.003 10 amino acids, and the end .. 1 NLPLRLFTF 1.000 position for each peptide is the start [5 LRLFTFWRGP I 0.001 17 FTFWRGPVV I 0.200 I position pus nine. S9 II FWRGPVVVA I 0.030 ta Subsequence II Score Table XXI-V21-HLA-B35-1 Omers 16 1 LFTFWRGPV I 0.020 [51 FLEEGMGGTI [0.240 98P4B6 IF I RLFTFWRGP I 0.0201 [ 8 EGMGGTIPHV 0 o.200oo Each peptide is a portion of SEQ ID I TFWRGPWV 0.020 1 EKSQFL'EEGM I0.200 NO: 43; each start position is 8- 1 - __ _0.020 1 __ Ispecified, the length of peptide is I PLRLFTFWR I2 0.003 2 - 11" KSQF LEEGMG I 0.150 10 amino acids, and the end 4I -I LRLFTFWRG II 0.001 19 ]1 GMGGTIPHVS I 0.00 position for each peptide is the start 4,-i] QFLEEGMGGT I0.020 position plus nine. Table XX-V21-HLA-B3501-9mers- 13 SQFLEEGMGG Si 1 Itart Subsequence Score 98P4B6 I o1 MGGTIPHVSP I0. o jKTKHCMFSLI [2.400 194 WO 03/087306 PCT/USO3/10462 1 LSKLTQEQKT ] 15 Table XXI-V25-HLA-B35-10mers- 187 ISQKLKRIKK 0.050 II TQEQKTKHCM 0.600 98P4B6 10 QKLKRIKKGW 050 7 EQKTKHCMFS 0.300 Each peptide is a portion of SEQ ID 6 PCISQKLKRI I0.040 4 LTQEQKTKHC IM NO: 51; each start position is 9 "1 SQKLKRIKKG 0 specified, the length of peptide is 6 QEQKTKHCMF 0.100 10 amino acids, and the end 4l FLPCISQKLK 0.010 8 QKTKHCMFSL 0.1001 position for each peptide is the start 7 CISQKLKRIK 0.010 3! KLTQEQKTKH 0.020 position plus nine. 21 ILFLPCISQK 0.010 I o10I TKHCMFSLIS [.1 1art Subeee S IILFIPCISQ 0010 i"I SKLTQEQKTK 11521 5 LPCISQKLKR 0.200

L

3 _Z LFLPCISQKL 0100 195 WO 03/087306 PCT/USO3/10462 Tables XXII - XLIX: TableXXII-VI-HLA-AI- position is specified, the TableXXII-V6-HLA-Al 9mers-98P4B6 length of peptide is 9 amino 9mers-98P4B6 Each peptide is a portion of acids, and the end position Each peptide is a portion of SEQ ID NO: 3; each start for each peptide is the start SEQ ID NO: 13; each start position is specified, the length position plus eight. position is specified, the of peptide is 9 amino acids, Pos 123456789 score length of peptide is 9 amino and the end position for each 23 LSLPSSWDY 23 acids, and the end position peptide is the start position 36 PCPADFFLY 20 for each peptide is the start plus eight. 17 FTPFSCLSL 13 position plus eight. Pos 123456789 score 28 SWDYRCPPP 12 Pos 123456789 score 158 PKCDASRQVY 27 6 VILGKIILF 8 419 FEEEYYRFY 27 TableXXII-V5A-HLA-A1- 16 PCISRKLKR 8 405 ISTFHVLIY 26 9mers-98P4B6 7 ILGKIILFL 7 221 SLATFFFLY 23 Each peptide is a portion of 37 EGIGGTIPH 7 263 AITLLSLVY 23 SEQ ID NO: 11; each start 46 VSPERVTVM 7 392 SFIQSTLGY 23 position is specified, the length 3 PSIVILGKI 6 276 LAAAYQLYY 22 of peptide is 9 amino acids, 5 IVILGKIIL 6 280 YQLYYGTKY 21 and the end position for each 12 ILFLPCISR 6 244 QSDFYKIPI 19 peptide is the start position 101 LWDLRHLLV 18 plus eight. TableXXII-V7A-HLA 189 PIDLGSLSS 18 Pos 123456789 score A1-9mers-98P4B6 198 AREIENLPL 18 7 FTFWRGPVV 1 9 Each peptide is a portion of 231 FVRDVIHPY 18 9 FWRGPVVVA 5 SEQ ID NO: 15; each start 240 AR!NQQSDFY 18 position is specified, the 275 LLAAAYQLY 18 TableXXII-V5B-HLA- length of peptide is 9 amino 311 FFAMVHVAY 18 Al-9mers-98P4B6 acids, and the end position 90 FVAIHREHY 17 Each peptide is a portion of for each peptide is the start 117 SNNMRINQY 17 SEQ ID NO: 11; each start position plus eight. 327 RSERYLFLN 17 position is specified, the Pos 123456789 score 388 WI EFSFIQS 17 length of peptide is 9 amino 5 LSETFLPNG 14 427 YPPNFVLA 17 acids, and the end position 4 SLSETFLPN 12 443 ILDLLQLCR 17 for each peptide is the start 8 TFLPNGING 9 444 LDLLQLCR 17 position plus eight. 7 ETFLPNGIN 8 46 TIRLIRCGY 16 Pos 123456789 score 3 KSLSETFLP 6 66 ASEFFP V 16 21 ELEFVFLLT 24 - _ ___ 66 A SEFFPHVV 16 124 QYPESNAEY 16 1 WREFSFIQI 17 TableXXII-V7B-HLA-Al 200 EIENLPLRL 16 17 QTELELEFV 16 9mers-98P4B6 200 EIENLPLRL 16 1 330 RYLFLMAY 16 13 FADTQTELE 15 Each peptide is a portion of 352 EEVWRIEMY 16 19 ELELEFVFL 14 SEQ ID NO: 15; each start 352 EEVWRIEMY 16 - 272 LAGLLAAAY 15 position is specified, the TableXXIXH-V6-HLA-AI- length of peptide is 9 amino 323 LPMRRSERY 15 9mers-98P4B6 acids, and the end position for 351 EEEVWRIEM 15 Each peptide is a portion of each peptide is the start 415 WIKRAFEEEY 15 SEQ ID NO: 13; each start position plus eight. 416 K]AFEEEYY 15 position is specified, the Pos 123456789 score 13 LSETCLPNG 14 length of peptide is 9 amino 5 AYQQSTLGY 22 38 SGDFAKSLT 14 acids, and the end position 9 STLGYVALL 13 98 YTSLWDLRH 14 for each peptide is the start 178 VIELARQLN 14 position plus eight. TableXXII-V7C-HLA-A1 406 STFHVLIYG 14 Pos 123456789 score 9mers-98P4B6 94 HREHYTSLW 13 34 FLEEGIGGT 14 Each peptide is a portion of 135 SLFPDSLIV 13 28 GWEKSQFLE 12 SEQ ID NO: 15; each start 137 FPDSLIVKG 13 35 LEEGIGGTI 12 position is specified, the length 251 PIEIVNKTL 13 29 WEKSQFLEE 11 of peptide is 9 amino acids, 396 ISTLGYVALL 13 41 GTIPHVSPE 11 and the end position for each I VLPSIVILG 9 peptide is the start position TableXXII-V2-HLA-Al- 9 GKIILFLPC 9 plus eight. 9mers-98P4B6 19 SPRKLKRIKK 9 Pos 123456789 score Each peptide is a portion of 2 LPSIVILGK 8 591 WTEEAGATA 17 SEQ ID NO: 3; each start 196 WO 03/087306 PCT/USO3/10462 TableXXII-V7C-HLA-A1- acids, and the end position _ position plus eight. 9mers-98P4B6 for each peptide is the start Pos 123456789 score Each peptide is a portion of position plus eig ht. 5 PCISQKLKR 10 SEQ ID NO: 15; each start Pos 123456789 score 8 SQKLKRIKK 9 position is specified, the length 4 FLEEGMGGT 14 1 ILFLPCISQ 6 of peptide is 9 amino acids, 5 LEEGMGGTI 12 2 LFLPCISQK 4 and the end position for each 7 EGMGGTIPH 7 3 FLPCISQKL 4 peptide is the start position 7 ISQKLKRIK 4 plus eight. Pos 123456789 score TableXXII-V13-HLA 90 VTEDDEAQD 17 A1-9mers-98P4B6 TabIeXXIl-VI-HLA 99 SIDPPESPD 17 Each peptide is a portion of A0201-9mers-98P4B6 167 KLETIILSK 17 SEQ ID NO:27; each start Each peptide is a portion of 32 LSEIVLPIE 16 position is specified, the SEQ ID NO: 3; each start 51 STPPPPAMW 14 length of peptide is 9 amino position is specified, the length 154 WSLGEFLGS 14 acids, and the end position of peptide is 9 amino acids, and 5 ILDLSVEVL 13 for each peptide is the start the end position for each 69 AQESGIRNK 13 position plus eight. peptide is the start position plus 9 SVEVLASPA 12 Pos 123456789 score eight. 38 PIEWQQDRK 12 5 LSETFLPNG 14 Pos 123456789 score 60 TEEAGATAE 12 4 SLSETFLPN 12 365 IMSLGLLSL 29 66 TAEAQESGI 12 8 TFLPNGING 9 271 YLAGLLAAA 28 93 DDEAQDSID 12 7 ETFLPNGIN 8 433 VLALVLPSI 28 104 ESPDRALKA 121 3 KSLSETFLP 6 227 FLYSFVRDV 27 105 SPDRALKAA 12 360 YISFGIMSL 27 123 HTNGVGPLW 12 TableXXII-V14-HLA-Al- 396 STLGYVALL 27 130 LWEFLLRLL 12 9mers-98P4B6 17 CLPNGINGI 26 96 AQDSIDPPE 11 Each peptide is a portion of 100 SLWDLRHLL 26 102 PPESPDRAL 11 SEQ ID NO: 29; each start 135 SLFPDSLIV 26 128 GPLWEFLLR 11I position is specified, the length 203 NLPLRLFTL 26 143 ASGTLSLAF 11 of peptide is 9 amino acids, 402 ALLISTFHV 26 156 LGEFLGSGT 11 and the end position for each 436 LVLPSIVIL 26 42 QQDRKIPPL 10 peptide is the start position 128 SNAEYLASL 25 78 SSSSSQPV 10 plus eight. 140 SLIVKGFNV 25 82 SQIPVVGVV 10 Pos 123456789 score 187 FIPIDLGSL 25 91 TEDDEAQDS 10 7 'WRGPVV 9 210 TLWRGPVVV 25 - 9 FWRGPVVVA5 92 EDDEAQDSI 10 FWRGPVVVA 261 IVAITLLSL 25 115 SWRNPVLPH 10 403 LLISTFHVL 25 TableXXII--V-21-HLA-Al 176 LTQEQKSKH 10 9mers-98P4B6 5 SMMGSPKSL 24 177 TQEQKSKHC io 9mers-98P4B6 24ILSVL 2 177 TQEQKSKHC 10 Each peptide is a portion of 264 ITLLSLVYL 24 26 NILRGGLSE 9 SEQ ID NO: 43; each start 274 GLLAAAYQL 24 50 LSTPPPPAM 9 position is specified, the 307 LLSFFFAMV 24 79 SSSSQIPWV 9 length of peptide is 9 amino 369 GLLSLLAVT 24 131 WEFLLRLLK 9 acids, and the end position for 48 RLIRCGYHV 23 2 SIVILDLSV 8 each peptide is the start 49 LIRCGYHVVW 23 7 DLSVEVLAS 8 position plus eight. 141 LIVKGFNVV 23 21 KCLGANILR 8 Pos 123456789 score 313 AMVHVAYSL 23 31 GLSEIVLPI 8 3 LTQEQKTKH 10 374 LAVTSIPSV 23 81 SSQIPVVGV 8 4 TQEQKTKHC 10 393 FIQSTLGYV 23 124 TNGVGPLWE 8 1 SKLTQEQKT 6 441 IVILDLLQL 23 132 EFLLRLLKS 8 8 KTKHCMFSL 6 106 HLLVGKILI 22 141 QAASGTLSL 8 9 TKHCMFSLI 5 180 ELARQLNF[ 22 162 SGTWMKLET 8 254 IVNKTLPIV 22 169 ETIILSKLT 8 TableXXII-V25-HLA- 258 TLPIVAITL 22 A1-9mers-98P4B6 262 VAITLLSLV 22 TableXXII-V8-HLA-Al- Each peptide is a portion of 265 TLLSLVYLA 22 9mers-98P4B6 SEQ ID NO: 51; each start 267 LSLVYLAGL 22 Each peptide is a portion of position is specified, the 268 SLVYLAGLL 22 SEQ ID NO: 17; each start length of peptide is 9 amino 333 FLNMAYQQV 22 position is specified, the acids, and the end position 378 SIPSVSNAL 22 length of peptide is 9 amino for each peptide is the start 404 LISTFHVLI 21 197 WO 03/087306 PCT/US03/10462 TableXXIII-V1l-HLA- TableXXIII-V 1-HLA- TableXXII-V2 HLA A0201-9mers-98P4B6 A0201-9mers-98P4B6 A0201-9mers-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NO: 5; each start position is specified, the length position is specified, the length position is specified, the of peptide is 9 amino acids, and of peptide is 9 amino acids, and length of peptide is 9 amino the end position for each the end position for each acids, and the end position peptide is the start position plus peptide is the start position plus for each peptide is the start eight. eight. position plus eight. Pos 123456789 score Pos 123456789 score Pos 123456789 score 435 ALVLPSIVI 21 50 IRCGYHVVI 15 10 SLSLSSGFT 16 107 LLVGKILID 20 111 KILIDVSNN 15 3 SPGLQALSL 15 108 LVGKILIDV 20 211 LWRGPVVVA 15 12 SLSSGFTPF 14 112 ILIDVSNNM 20 217 VVAISLATF 15 15 SGFTPFSCL 14 173 QARQQVIEL 20 221 SLATFFFLY 15 24 SLPSSWDYR 12 184 QLNFIPIDL 20 247 FYKIPIEIV 15 368 LGLLSLLAV 20 249 KIPIEIVNK 15 TableXXIII-V5A-HLA 65 FASEFFPHV 19 251 PIEIVNKTL 15 A0201-9mers-98P4B6 83 LTKTNIIFV 19 256 NKTLPIVAI 15 Each peptide is a portion of 133 LASLFPDSL 19 270 VYLAGLLAA 15 SEQ ID NO: 11; each start 177 QVIELARQL 19 299 LQCRKQLGL 15 position is specified, the length 257 KTLPIVAIT 19 324 PMRRSERYL 15 of peptide is 9 amino acids, 306 GLLSFFFAM 19 331 YLFLNMAYQ 15 and the end position for each 366 MSLGLLSLL 19 335 NMAYQQVHA 15 peptide is the start position 434 LALVLPSIV 19 385 ALNWREFSF 15 plus eight. 27 DARKVTVGV 18 400 YVALLISTF 15 Pos 123456789 score 196 SSAREIENL 18 437 VLPSIVILD 15 7 FTFWRGPVV 17 209 FTLWRGPVV 18 23 NGIKDARKV 14 1 NLPLRLFTF 16 259 LPIVAITLL 18 37 GSGDFAKSL 14 8 TFWRGPVVV 15 367 SLGLLSLLA 18 39 GDFAKSLTI 14 9 FWRGPVVVA 14 371 LSLLAVTSI 18 42 AKSLTIRLI 14 5 RLFTFWRGP 13 397 TLGYVALLI 18 164 QVYICSNNI 14 3 PLRLFTFWR 10 41 FAKSLTIRL 17 166 YICSNNIQA 14 6 LFTFWRGPV 10 81 DALTKTNII 17 220 ISLATFFFL 14 85 KTNIIFVAI 17 223 ATFFFLYSF 14 TableXXIII-V5B-HLA 103 DLRHLLVGK 17 266 LLSLVYLAG 14 A0201-9mers-98P4B6 104 LRHLLVGKI 17 275 LLAAAYQLY 14 Each peptide is a portion of 153 ALQLGPKDA 17 278 AAYQLYYGT 14 SEQ ID NO: 11; each start 155 QLGPKDASR 17 300 QCRKQLGLL 14 position is specified, the 212 WRGPVVVAI 17 309 SFFFAMVHV 14 length of peptide is 9 amino 250 IPIEIVNKT 17 362 SFGIMSLGL 14 acids, and the end position 253 EIVNKTLPI 17 373 LLAVTSIPS 14 for each peptide is the start 253 EIVNKTLPI 17 373 LLAVTSIPS 14 position plus eight. 363 FGIMSLGLL 17 395 QSTLGYVAL 14 Position 123456789 scoreit. 370 LLSLLAVTS 17 411 LIYGWKRAF 4 2 LELEFVFLL 21 410 VLIYGWKRA 17 427 YTPPNEVLA 14 22 LEFVFLLTL 21 428 TPPNFVLAL 17 443 ILDLLQLCR 14 24 FVFLLTLLL 20 438 LPSIVILDL 17 E 442 VILDLLQLC 17 TableXXIII-V2-HLA- 19 ELELEFVFL 18 25 IKDARKVTV 16 A0201-9mers-98P4B6 12 SFADTQTEL 17 68 EFFPHVVDV 16 Each peptide is a portion of - 17 QTELELEFV 17 88 IIFVAIHRE 16 SEQ ID NO: 5; each start 8 QIFCSFADT 15 93 IHREHYTSL 16 position is specified, the 6 FIQIFCSFA 14 99 TSLWDLRHL 16 length of peptide is 9 amino 14 ADTQTELEL 14 132 YLASLFPDS 16 acids, and the end position 23 EFVFLLTLL 11 148 VVSAWALQL 16 for each peptide is the start 21 ELEFVFLLT 10 171 NIQARQQVI 16 position plus eight. 190 IDLGSLSSA 16 Pos 123456789 score TableXXIII-V6-HLA 200 EIENLPLRL 16 5 GLQALSLSL 25 A0201-9mers-98P4B6 372 SLLAVTSIP 16 1 SGSPGLQAL 21 Each peptide is a portion of 12 SLSETCLPN 15 8 ALSLSLSSG 18 SEQ ID NO: 13; each start 44 SLTIRLIRC 15 17 FTPFSCLSL 17 position is specified, the 198 WO 03/087306 PCT/USO3/10462 length of peptide is 9 amino TableXXII-V7C-HLA- 8 GMGGTIPHV 26 adds, and the end position for A0201-9mers-98P4B6 4 FLEEGMGGT 19 each peptide is the start Each peptide is a portion of 5 LEEGMGGTI 13 position plus eight. SEQ ID NO: 15; each start Pos 123456789 score position is specified, the length TableXXIII-V13-HLA 7 ILGKIILFL 27 of peptide is 9 amino acids, A0201-9mers-98P4B6 38 GIGGTIPHV 26 and the end position for each Each peptide is a portion of 10 KIILFLPCI 25 peptide is the start position SEQ ID NO: 27; each start 14 FLPCISRKL 23 plus eight. position is specified, the 34 FLEEGIGGT 23 Pos 123456789 score length of peptide is 9 amino 5 IVILGKIIL 20 27 ILRGGLSEI 30 acids, and the end position 17 CISRKLKRI 20 4 VILDLSVEV 27 for each peptide is the start 45 HVSPERVTV 20 5 ILDLSVEVL 26 osition plus eight. 4 SIVILGKII 18 31 GLSEIVLPI 26 Pos 123456789 score 6 VILGKIILF 18 129 PLWEFLLRL 26 9 FLPNGINGI 27 12 ILFLPCISR 16 148 SLAFTSWSL 25 4 SLSETFLPN 15 1 VLPSIVILG 15 2 SIVILDLSV 24 27 KGWEKSQFL 15 141 QAASGTLSL 23 TableXXIll-V14-HLA 3 PSIVILGKI 13 155 SLGEFLGSG 21 A0201-9mers-98P4B6 35 LEEGIGGTI 13 163 GTWMKLETI 21 Each peptide is a portion of 41 GTIPHVSPE 13 81 SSQIPVVGV 20 SEQ ID NO: 29; each start 82 SQIPVVGVV 20 position is specified, the length TableXXIII-V7A-HLA- 119 PVLPHTNGV 19 of peptide is 9 amino acids, A0201-9mers-98P4B6 133 FLLRLLKSQ 19 and the end position for each Each peptide is a portion of 165 WMKLETIIL 19 peptide is the start position SEQ ID NO: 15; each start 24 GANILRGGL 18 plus eight. position is specified, the 57 AMWTEEAGA 18 Pos 123456789 score length of peptide is 9 amino 112 AANSWRNPV 18 7 FTFWRGPVV 17 acids, and the end position 126 GVGPLWEFL 18 1 NLPLRLFTF 16 for each peptide is the start 12 VLASPAAAW 17 8 TFWRGPVVV 15 osition plus eight.79 SSSSQIPVV 17 9 FWRGPVVVA 14 Pos 123456789 score134 LLRLLKSQA 17 5 RLFTFWRGP 13 9 FLPNGINGI 27 167 KLETIILSK 17 3 PLRLFTFWR 10 41SLSETFLPN 151 168 LETIILSKL 17 6 LFTFWRGPV 10 171 IILSKLTQE 17 172 ILSKLITQEQ 17 TableXXIII-V21-HLA TableXXIII-V7B-HLA- 42 QQDRKIPPL 16 A0201-9mers-98P4B6 A0201-9mers-98P4B6 142 AASGTLSLA 16 Each peptide is a portion of Each peptide is a portion of 160 LGSGTWMKL 16 SEQ ID NO: 43; each start SEQ ID NO: 15; each start 7 DLSVEVLAS 15 position is specified, the position is specified, the 17 AAAWKCLGA 15 length of peptide is 9 amino length of peptide is 9 amino 1 CLG 15 acids, and the end position acids, and the end position for 22 CLGANI LRGSE 15 for each peptide is the start each peptide is the start 2 LRGLSE position plus eight. position plus eight. 28 LRGGLSEV 15 Pos 123456789 score Pos 123456789 score 130 LWEFLLRLL 15 8 KTKHCMFSL 16 9 STLGYVALL 27 136 RLLKSQAAS 15 2 KLTQEQKTK 11 3 NMAYQQSTL 21 137 LLKSQAASG 15 1 SKLTQEQKT 10 6 YQQSTLGYV 16 159 FLGSGTWMK 15 3 LTQEQKTKH 10 8 QSTLGYVAL 14 185 CMFSLISGS 15 9 TKHCMFSLI 8 83 QIPVVGVVT 14 TableXXIII-V7C-HLA- TableXXIll-V25-HLA A0201-9mers-98P4B6 TableXXIII-V8-HLA- A0201-9mers-98P4B6 Each peptide is a portion of A0201-9mers-98P4B6 Each peptide is a portion of SEQ ID NO: 15; each start Each peptide is a portion of SEQ ID NO: 51; each start position is specified, the length SEQ ID NO: 17; each start position is specified, the of peptide is 9 amino acids, position is specified, the length of peptide is 9 amino and the end position for each length of peptide is 9 amino acids, and the end position peptide is the start position acids, and the end position for each peptide is the start plus eight for each peptide is the start position plus eight. Pos 123456789 score position plus eight. Pos 123456789 score Pos 123456789 score 3 FLPCISQKL 23 199 WO 03/087306 PCT/USO3/10462 I61CISQKLKRI 20 Pos 1234567891score TableXXV-VI-HLA-A3 1 ILFLPCISQ 16 NoResultsFound. 9mers-98P4B6 Each peptide is a portion of TabIeXXIV-V1-HLA- TableXXIV-V21- SEQ ID NO: 3; each start A0203-9mers-98P4B6 HLA-A0203-9mers- position is specified, the length Pos 1234567891score 98P4B6 of peptide is 9 amino acids, NoResultsFound. Pos 123456789 score and the end position for each [NoResultsFound. peptide is the start position TableXXIV-V2-HLA- plus eight. A0203-9mers-98P4B6 TableXXIV-V25- Pos 123456789 score Pos 123456789 score HLA-A0203-9mers- 411 LIYGWKRAF 19 NoResultsFound. 98P4B6 436 LVLPSIVIL 19 Pos 123456789 score 34 GVIGSGDFA 18 TableXXIV-V5A- NoResultsFound. 92 ATHREHYTS 18 HLA-A0203-9mers- 140 SLIVKGFNV 18 98P4B6 TableXXV-V1-HLA-A3- 191 DLGSLSSAR 18 Pos 123456789 score 9mers-98P4B6 221 SLATFFFLY 18 NoResultsFound. Each peptide is a portion of 435 ALVLPSIVI 18 SEQ ID NO: 3; each start 22 INGIKDARK 17 TableXXIV-V5B- position is specified, the length 49 LIRCGYHVV 17 HLA-A0203-9mers- of peptide is 9 amino acids, 82 ALTKTNIIF, 17 98P4B6 and the end position for each 111 KILIDVSNN 17 Pos 123456789 score peptide is the start position 112 ILIDVSNNM 17 NoResultsFound. plus eight. 135 SLFPDSLIV 17 Pos 123456789 score 153 ALQLGPKDA 17 TableXXIV-V6-HLA- 103 DLRHLLVGK 27 164 QVYICSNNI 17 A0203-9mers-98P4B6 56 VVIGSRNPK 26 203 NLPLRLFTL 17 Pos 123456789 score 249 KIPIEIVNK 26 271 YLAGLLAAA 17 NoResultsFound. 3 SISMMGSPK 25 304 QLGLLSFFF 17 155 QLGPKDASR 25 381 SVSNALNWR 17 TableXXIV-V7A- 263 AITLLSLVY 25 397 TLGYVALLI 17 HLA-A0203-9mers- 210 TLWRGPVVV 24 403 LLISTFHVL 17 98P4B6 4- 403 LLISTFHVL 17 B148 RLRCGYV 23 432 FVLALVLPS 17 Pos 123456789 score 142 IVKGFNVVS 23 32 TVGVIGSGD 16 NoResultsFound. 217 VVAISLATF 23 107 LLVGKILID 16 TableXXIV-V7B- 40 YVALLISTF 23 151 AWALQLGPK 16 HLalX-A0 VTBmr- 17'7 QVIELARQL 22 171 NI AR VI 16! HLA-A0203-9mers- 205 PLRLFTLWR 22 189 PIDLGSLSS 16 984136 281 QLYYGTKYR 22 216 VVVAISLAT 16 Pos 123456789 sco 370 LLSLLAVTS 22 216 VVVAISLATF 16 NoResultsFound. 441 IVILDLQL 22 234 D AISLATFFFRN 16 5 LQ 234 DVIHPYARN 16 TableXXIV-V7C- 35 VIGSGDFAK 21 266 LLSLVYLAG 16 HLA-A0203-9mers- 77 THHEDALTK 21 302 RKQLGLLSF 16 HL -02 39m r -148. WSAW ALQL 21 - 98P4B6 148 VVSAWALQL 21 402 ALLISTFHV 16 Pos 1234567891score 231 FVRDVIIIPY 21 12 SLSETCLPN 15 NoResultsFound. 269 LVYLAGLLA 21 21 GINGIKDAR 15 375 AVTSIPSVS 21 24 GIKDARKVT 15 TableXXIV-V8-HLA- 385 ALNWREFSF 21 30 KVTVGVIGS 15 A0203-9mers-98P4B6 274 GLLAAAYQL 20 121 RINQYPESN 15 Pos 123456789 score 322 CLPMRRSER 20 136 LFPDSLIVK 15 NoResultsFound. 409 HVLIYGWKR 20 179 IELARQLNF 15 443 ILDLLQLCR 20 268 SLVYLAGLL 15 TableXXIV-VI3- 46 TIRLIRCGY 19 356 RIEMYISFG 15 HLA-A0203-9mers- 87 NIIFVAIHR 19 367 SLGLLSLLA 15 98P4B6 90 FVAIHREHY 19 410 VLIYGWKRA 15 Pos 123456789 score 258, TLPIVAITL 19 433 VLALVLPSI 15 NoResultsFound. 261 1VAITLLSL 19 25 IKDARKVTV 14 275 LLAAAYQLY 19 44 SLTIRLIRC 14 TableXXIV-V14- 279 AYQLYYGTK 19 57 VIGSRNPKF 14 HLA-A0203-9mers- 369 GLLSLLAVT 19 61 RNPKFASEF 14 98P4B6 372 SLLAVTSIP 19 106 HLLVGKILI 14 200 WO 03/087306 PCT/USO3/10462 TableXXV-VI-HLA-A3- Pos 123456789 score acids, and the end position for 9mers-98P4B6 8 ALSLSLSSG 19 each peptide is the start Each peptide is a portion of 12 SLSSGFTPF 18 position plus eigh . SEQ ID NO: 3; each start 5 GLQALSLSL 17 Pos 123456789 score position is specifed, the length 22 CLSLPSSWD 15 45 HVSPERVTV 22 of peptide is 9 amino acids, 24 SLPSSWDYR 15 23 KRIKKGWEK 20 and the end position for each 10 SLSLSSGFT 13 12 ILFLPCISR 19 peptide is the start position 23 LSLPSSWDY 11 5 IVILGKIIL 18 plus eight. 33 CPPPCPADF 1 1 13 LFLPCISRK 18 Pos 123456789 score 3 SPGLQALSL 10 6 VILGKIILF 17 141 LIVKGFNVV 14 7 QALSLSLSS 9 21 KLKRIKKGW 17 180 ELARQLNFI 14 9 LSLSLSSGF 9 2 LPSIVILGK 15 207 RLFTLWRGP 14 11 LSLSSGFTP 9 7 ILGKIILFL 15 227 FLYSFVRDV 14 21 SCLSLPSSW 9 10 KIILFLPCI 15 235 VIHPYARNQ 14 37 CPADFFLYF 9 18 ISRKLKRIK 15 241 RNQQSDFYK 14 - 19 SRCLKRIKK 15 251 PIEIVNKTL 14 TableXXV-V5A-HLA-A3- 24 RIKKGWEKS 15 272 LAGLLAAAY 14 9mers-98P4B6 34 FLEEGIGGT 14 294 WLETWLQCR 14 Each peptide is a portion of 4 SIVILGKII 13 303 KQLGLLSFF 14 SEQ ID NO: 11; each start 11 IILFLPCIS 13 307 LLSFFFAMV 14 position is specified, the length 26 KKGWEKSQF 13 330 RYLFLNMAY 14 of peptide is 9 amino acids, 42 TIPHVSPER 13 331 YLFLNMAYQ 14 and the end position for each 15 LPCISRKLK 12 340 QVHANIENS 14 peptide is the start position 16 PCISRKLKR 12 353 EVWRIEMYI 14 plus eight. 17 CISRKLKRI 12 364 GIMSLGLLS 14 Pos 123456789 score 37 EGIGGTIPH 11 17 CLPNGINGI 13 1 NLPLRLFTF 21 1 VLPSILG 10 18 LPNGINGIK 13 3 PLRLFTFWR 19 14 FLPCISRKL 10 26 KDARKVTVG 13 5 RLFTFWRGP 14 35 LEEGIGGTI 10 43 KSLTIRLIR 13 8 TFWRGPVVV 14 38 GIGGTIPHV 10 55 HVVIGSRNP 13 9 FWRGPVVVA 13 70 FPHVVDVTH 13 TableXXV-V7A-HLA 100 SLWDLRHLL 13 TableXXV-V5B-HLA- A3-9mers-98P4B6 113 LIDVSNNMR 13 A3-9mers-98P4B6 Each peptide is a portion of 147 NVVSAWALQ 13 Each peptide is a portion of SEQ ID NO:15; each start 158 PKDASRQVY 13 SEQ ID NO: 11; each start position is specified, the 184 QLNFIPIDL 13 position is specified, the length of peptide is 9 amino 200 EIENLPLRL 13 length of peptide is 9 amino acids, and the end positon 211 LWRGPVVVA 13 acids, and the end position for each peptide is the start 215 PVVVAISLA 13 for each peptide is the start position plus eight. 253 EIVNKTLPI 13 osition plus eight. Pos 123456789 score 260 PIVAITLLS 13 Pos 123456789 score 4 SLSETFLPN 15 306 GLLSFFFAM 13 19 ELELEFVFL 15 9 FLPNGINGI 13 311 FFAMVHVAY 13 21 ELEFVFLLT 14 1 SPKSLSETF 10 314 MVHVAYSLC 13 24 FVFLLTLLL 14 8 TFLPNGING 8 333 FLNMAYQQV 13 8 QIFCSFADT 13 360 YISFGIMSL 13 6 FIQIFCSFA 12 392 SFIQSTLGY 13 18 TELELEFVF 11 TableXXV-V7B-HLA-A3 408 FHVLIYGWK 13 5 SFIQIFCSF 10 9mers-98P4B6 440 SILDLLQ 13 9 IFCSFADTQ 9 Each peptide is a portion of 2 REFSFIQIF 8 SEQ ID NO: 15; each start 16 TQTELELEF 8 position is specified, the TableXXV-V2-HLA-A3- 22 LEFVFLLTL 7 length of peptide is 9 amino 9mers-98P4B6 acids, and the end position for Each peptide is a portion of each peptide is the start SEQ ID NO: 5; each start TableXXV-V6-HLA-A3- position plus eight. position is specified, the 9mers-98P4B6 Pos 123456789 score length of peptide is 9 amino Each peptide is a portion of 1 FLNMAY QS 13 acids, and the end position SEQ ID NO: 13; each start 5 AYQQSTLGY 12 for each peptide is the start position is specified, the 8 QSTLGYVAL 10 position plus eight. length of peptide is 9 amino 7 QQSTLGYVA 9 201 WO 03/087306 PCT/USO3/10462 TableXXV-V7B-HLA-A3- TableXXV-V7C-HLA-A3- TableXXV-V1 4-HLA-A3 9mers-98P4B6 9mers-98P4B6 9mers-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 15; each start SEQ ID NO: 15; each start SEQ ID NO: 29; each start position is specified, the position is specified, the length position is specified, the length length of peptide is 9 amino of peptide is 9 amino acids, of peptide is 9 amino adds, acids, and the end position for and the end position for each and the end position for each each peptide is the start peptide is the start position peptide is the start position position plus eight. plus eight. plus eight. Pos 123456789 score Pos 123456789 score Pos 123456789 score 3 NMAYQQSTL 8 36 VLPIEWQQD 14 5 RLFTFWRGP 14 9 STLGYVALL 8 85 PVVGVVTED 14 8 TFWRGPVVV 14 4 MAYQQSTLG 129 PLWEFLLRL 14 9 FWRGPVVVA 13 146 TLSLAFTSW 14 TabIeXXV-V7C-HLA-A3- 148 SLAFTSWSL 14 TableXXV-V21-HLA-A3 9mers-98P4B6 25 ANILRGGLS 13 9mers-98P4B6 Each peptide is a portion of 82 SQIPVVGVV 13 Each peptide is a portion of SEQ ID NO: 15; each start 126 GVGPLWEFL 13 SEQ ID NO: 43; each start position is specified, the length position is specified, the of peptide is 9 amino acids, TabIeXXV-V8-HLA-A3- length of peptide is 9 amino and the end position for each 9mers-98P4B6 acids, and the end position peptide is the start position Each peptide is a portion of for each peptide is the start plus eight. SEQ ID NO: 17; each start position plus eight. Pos 123456789 score position is specified, the Pos 123456789 score 167 KLETHILSK 28 length of peptide is 9 amino 2 KLTQEQKTK 27 175 KLTQEQKSK 25 acids, and the end position for 109 ALKAANSWR 24 each peptide is the start TableXXV-V25-HLA 3 IVILDLSVE 23 position plus eight. A3-9mers-98P4B6 26 NILRGGLSE 23 Pos 123456789 score Each peptide is a portion of 159 FLGSGTWMK 23 4 FLEEGMGGT 14 SEQ ID NO: 51; each start 27 ILRGGLSEI 22 5 LEEGMGGTI 10 position is specified, the 83 QIPVVGWVVT 22 3 QFLEEGMGG 9 length of peptide is 9 amino 13 LASPAAAWK 20 7 EGMGGTIPH 8 acids, and the end position 35 IVLPIEWQQ 20 6 EEGMGGTIP 6 for each peptide is the start 134 LLRLLKSQA 20 position plus eight. 136 RLLKSQAAS 20 TableXXV-V13-HLA- Pos 123456789 score 11 EVLASPAAA 19 A3-9mers-98P4B6 2 LFLPCISQK 21 137 LLKSQAASG 19 Each peptide is a portion of 1 ILFLPCISQ 15 170 TILSKLTQ 19 SEQ ID NO: 27; each start 8 SQKLKRIKK 15 12 VLASPAAAW 18 position is specified, the 7 ISQKLKRIK 12 38 PIEWQQODRK 18 length of peptide is 9 amino 4 LPCISQKLK 11 73 GIRNKSSSS 18 acids, and the end position 3 FLPCISQKL 10 5 ILDLSVEVL 17 for each peptide is the start 5 PCISQKLKR 10 9 SVEVLASPA 17 position plus eight. 45 RKIPPLSTP 17 Pos 123456789 score TabIeXXVI-V1-HLA-A26 103 PESPDRALK 17 4 SLSETFLPN 15 9mers-98P4B6 133 FLLRLLKSQ 17 9 FLPNGINGI 13 Each peptide is a portion of 171 IILSKLTQE 17 1 SPKSLSETF 10 SEQ ID NO: 3; each start 2 SIVILDLSV 15 8 TFLPNGING 8 position is specified, the length 4 VILDLSVEV 15 of peptide is 9 amino acids, 22 CLGANILRG 15 TabIeXXV-V14-HLA-A3- and the end position for each 46 KIPPLSTPP 15 9mers-98P4B6 peptide is the start position 69 AQESGIRNK 15 Each peptide is a portion of plus eight 99 SIDPPESPD 15 SEQ ID NO: 29; each start Pos 123456789 score 119 PVLPHTNGV 15 position is specified, the length 352 EEVWRIEMY 29 120 VLPHTNGVG 15 of peptide is 9 amino acids, 75 DVTHHEDAL 28 120 VLPHTNGVG 15 and the end position for each 441 IVILDLLQL 28 131 WEFLLRLLK 15 peptide is the start position 177 QVIELARQL 26 155 SLGEFLGSG 15 plus eight. 223 ATFFFLYSF 25 173 LSKLTEQK 15 Pos 123456789 score 231 FVRDVIHPY 25 7 DLSVEVLAS 14 1 NLPLRLFTF 21 400 YVALLISTF 25 31 GLSEIVLPI 14 3 PLRLFTFWR 19 200 EIENLPLRL 24 202 WO 03/087306 PCT/US03/10462 TableXXVI-Vl-HLA-A26- TableXXVI-VIl-HLA-A26- Pos 123456789 score 9mers-98P4B6 9mers-98P4B6 1 NLPLRLFTF 13 Each peptide is a portion of Each peptide is a portion of 7 FTFWRGPV 13 SEQ ID NO: 3; each start SEQ ID NO: 3; each start position is specified, the length position is specified, the length TabIeXXVI-V5B-HLA of peptide is 9 amino acids, of peptide is 9 amino acids, A26-9mers-98P4B6 and the end position for each and the end position for each Each peptide is a portion of peptide is the start position peptide is the start position SEQ ID NO: 11; each start plus eight. plus eight. position is specified, the Pos 123456789 score Pos 123456789 score length of peptide is 9 amino 261 IVAITLLSL 24 57 VIGSRNPKF 14 acids, and the end position 217 VVAISLATF 23 83 LTKTNIIFV 14 for each peptide is the start 436 LVLPSIVIL 23 131 EYLASLFPD 14 position plus eight. 96 EHYTSLWDL 22 138 PDSLIVKGF 14 Pos 123456789 score 234 DVIHPYARN 22 180 ELARQLNFI 14 23 EFVFLLTLL 27 353 EVWRIEMYI 22 214 GPVVVAISL 14 24 FVFLLTLLL 24 390 EFSFIQSTL 22 218 VAISLATFF 14 15 DTQTELELE 20 396 STLGYVALL 21 254 IVNKTLPIV 14 19 ELELEFVFL 18 90 FVAIHREHY 20 302 RKQLGLLSF 14 22 LEFVFLLTL 18 148 VVSAWALQL 20 303 KQLGLLSFF 14 2 REFSFIQIF 17 253 EIVNKTLPI 20 316 HVAYSLCLP 14 5 SFIQIFCSF 16 264 ITLLSLVYL 20 365 IMSLGLLSL 14 16 TQTELELEF 14 15 ETCLPNGIN 19 366 MSLGLLSLL 14 20 LELEFVFLL 14 68 EFFPHVVDV 19 430 PNFVLALVL 14 3 EFSFIQIFC 13 115 DVSNNMRIN 19 444 LDLLQLCRY 14 215 PVVVAISLA 19 TableXXVI-V6-HLA 296 ETWLQCRKQ 19 TableXXVI-V2-HLA- A26-9mers-98P4B6 31 VTVGVIGSG 18 A26-9mers-98P4B6 Each peptide is a portion of 187 FIPIDLGSL 18 Each peptide is a portion of SEQ ID NO: 13; each start 216 VVVAISLAT 18 SEQ ID NO: 5; each start position is specified, the 406 STFHVLIYG 18 position is specified, the length of peptide is 9 amino 439 PSIVILDLL 18 length of peptide is 9 amino acids, and the end position for 2 ESISMMGSP 17 acids, and the end position each peptide is the start 45 LTIRLIRCG 17 for each peptide is the start position plus eight. 46 TIRLIRCGY' 17 position plus eight. Pos 123456789 score 108 LVGKILIDV 17 Pos 123456789 score 263 AITLLSLVY 17 17 FTPFSCLSL 18 5 IMLGKIIL 23 360 YISFGIMSL 1 7 1 SGSPGLQAL 15 6 VILGKIILF 18 363 FGIMSLGLL 17 15 SGFTPFSCL 14 41 GTIPHVSPE 18 30 KVTVGVIGS 16 3 SPGLQALSL 11 7 ILGKIILFL 15 117 SNNMRINQY 16 5 GLQALSLSL 11 37 EGIGGTIPH 15 128 SNAEYLASL 16 9 LSLSLSSGF it 30 EKSQFLEEG 141 259 LPIVAITLL 16 18 TPFSCLSLP 1110 KIILFLPCI 12 355 WREMYISF 16 23 LSLPSSWDY 11 10 _________ 12 392 SFIQSTLGY 16 12 SLSSGFTPF 10 45 HVSPERVTV 12 405 ISTFHVLIY 16 36 PCPADFFLY 10 4 SIVILGKII 11 432 FVLALVLPS 16 37 CPADFFLYF 10 14 FLPCISRKL 11L 32 TVGVIGSGD 13 33 CPPPCPADF 9 27 KGWEKSQFL II 34 GVIGSGDFA 15 35 PPCPADFFL 9 36 EEGIGGTIP 11 72 HVVDVTHHE 15 30 DYRCPPPCP 8 147 NVVSAWALQ 15 34 PPPCPADFF 8 A26-9mers-98P4B6V7A-HLA 257 KLPIVIT -A26-9mers-98P4B6 2S7 KTLPIVAIT 151 268 SLVYLAGLL TableXXVI-V5A-HLA- Each peptide is a portion of 329 ERYLFLNMA 15 A26-9mers-98P4B6 SEQ ID NO: 15; each start 340 QVHANIENSA 15 Each peptide is a portion of position is specified, the 340 QVHANENS 15 Ee a length of peptide is 9 amino 375 AVTSIPSVS 15 SEQ ID NO: 11; each start lenth e isain 378 SIPSVSNAL 15 position is specified, the racidsh peptide is the end positionart 381 SVSNALNWR 15 length of peptide is 9 amino position plus ei ht. 348 SPNVS AL 15 acids, and the end position os l sh 428 TPPNFVLAL 15 for each peptide is the start Pos 123456789 score 55 HVVIGSRNP 14 position plus eight. 7 ETFLPNGIN 23 56 VVIGSRNPK 14 1 SPKSLSETF 12 203 WO 03/087306 PCT/USO3/10462 TableXXVI-V7C-HLA- TableXXVI-V21-HLA TableXXVI-V7B-HLA- A26-9mers-98P4B6 A26-9mers-98P4B6 A26-9mers-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 15; each start SEQ ID NO: 43; each start SEQ ID NO: 15; each start position is specified, the length position is specified, the position is specified, the of peptide is 9 amino acids, length of peptide is 9 amino length of peptide is 9 amino and the end position for each acids, and the end position for acids, and the end position for peptide is the start position each peptide is the start each peptide is the start plus eight. position plus ei ht. position plus eight. Pos 123456789 score Pos 123456789 score Pos 123456789 score 65 ATAEAQESG 11 6 EQKTKHCMF 20 9 STLGYVALL 21 71 ESGIRNKSS 11 8 KTKHCMFSL 17 5 AYQQSTLGY 11 82 SQIPVVGVV 11 3 LTQEQKTKH 11 3 NMAYQQSTL 10 119 PVLPHTNGV 11 8 QSTLGYVAL 10 141 QAASGTLSL 11 TableXXVI-V25-HLA 143 ASGTLSLAF 11 A26-9mers-98P4B6 TableXXVI-V7C-HLA- 145 GTLSLAFTS 11 Each peptide is a portion of A26-9mers-98P4B6 158 EFLGSGTWM 11 SEQ ID NO: 51; each start Each peptide is a portion of 170 TIILSKLTQ 11 position is specified, the SEQ ID NO: 15; each start 171 IILSKLTQE 11 length of peptide is 9 amino position is specified, the length 185 CMFSLISGS 11 acids, and the end position of peptide is 9 amino acids, for each peptide is the start and the end position for each TabIeXXVI-V8-HLA- position plus eight. peptide is the start position A26-9mers-98P4B6 Pos 123456789 score plus eight. Each peptide is a portion of 3 FLPCISQKL 11 Pos 123456789 score SEQ ID NO: 17; each start 6 CISQKLKRI 9 169 ETIILSKLT 23 position is specified, the 2 LFLPCISQK 7 34 EIVLPIEWQ 22 length of peptide is 9 amino 5 PCISQKLKR 7 11 EVLASPAAA 21 acids, and the end position 1 ILFLPCISQ 6 151 FTSWSLGEF 21 for each peptide is the start 9 QKLKRIKKG 5 179 EQKSKHCMF 21 position plus eight t. 126 GVGPLWEFL 20 Pos 123456789 score TableXXVII-VI-HLA 3 IVILDLSVE 19 6 EEGMGGTIP 11 B0702-9mers-98P4B6 85 PVVGVVTED 18 7 EGMGGTIPH 11 Each peptide is a portion of 168 LETIILSKL 17 2 SQFLEEGMG 7 SEQ ID NO: 3; each start 125 NGVGPLWEF 16 position is specified, the length 132 EFLLRLLKS 16 TabIeXXVI-V13-HLA- of peptide is 9 amino acids, 95 EAQDSIDPP 15 A26-9mers-98P4B6 and the end position for each 129 PLWEFLLRL 15 Each peptide is a portion of peptide is the start position 7 DLSVEVLAS 14 SEQ ID NO: 27; each start plus eight. 35 IVLPIEWQQ 14 position is specified, the Pos 123456789 score 68 EAQESGIRN 14 length of peptide is 9 amino 428 TPPNFVLAL 24 88 GVVTEDDEA 14 acids, and the end position 438 LPSIVILDL 24 89 VVTEDDEAQ 14 for each peptide is the start 259 LPIVAITLL 21 98 DSIDPPESP 14 position plus eight. 291 FPPWLETWL 21 122 PHTNGVGPL 14 Pos 123456789 score 125 YPESNAEYL 20 163 GTWMKLETI 14 7 ETFLPNGIN 23 214 GPVVVAISL 20 9 SVEVLASPA 13 1 SPKSLSETF 12 250 IPIEIVNKT 18 42 QQDRKIPPL 13 62 NPKFASEFF 17 92 EDDEAQDSI 13 TabIeXXVI-V14-HLA- 211 LWRGPVVVA 17 104 ESPDRALKA 13 A26-9mers-98P4B6 429 PPNFVLALV 17 130 LWEFLLRLL 13 Each peptide is a portion of 157 GPKDASRQV 16 2 SIVILDLSV 12 SEQ ID NO: 29; each start 326 RRSERYLFL 16 5 ILDLSVEVL 12 position is specified, the 148 VVSAWALQL 15 59 WTEEAGATA 12 length of peptide is 9 amino 198 AREIENLPL 15 152 TSWSLGEFL 12 acids, and the end position 365 IMSLGLLSL 15 176 LTQEQKSKH 12 for each peptide is the start 426 FYTPPNFVL 15 81 LSVEVLASP 11 ~osition plus eight. 93 IHREHYTSL 14 8 LSVEVLASP 11 Pos 123456789 score 220 ISLATFFFL 14 45 RKISTPPLSTPAMW 1 1 NLPLRLFTF 13 261 IVAITLLSL 14 51 STPPPA!_lW 1 _"7FTW__V 13 27KRFPL 1 62 EAGATAEAQ 11 287 KYRRFPPWL 14 204 WO 03/087306 PCT/USO3/10462 TableXXVII-V1-HLA- TableXXVII-V1-HLA- Each peptide is a portion of B0702-9mers-98P4B6 B0702-9mers-98P4B6 SEQ ID NO: 11; each start Each peptide is a portion of Each peptide is a portion of position is specified, the SEQ 10D NO: 3; each start SEQ ID NO: 3; each start length of peptide is 9 amino position is specified, the length position is specified, the length acids, and the end position of peptide is 9 amino acids, of peptide is 9 amino acids, for each peptide is the start and the end position for each and the end position for each position plus eight. peptide is the start position peptide is the start position Pos 123456789 score plus eight. plus eight. 19 ELELEFVFL 15 Pos 123456789 score Pos 123456789 score 14 ADTQTELEL 14 379 IPSVSNALN 14 271 YLAGLLAAA 11 24 FVFLLTLLL 13 396 STLGYVALL 14 274 GLLAAAYQL 11 12 SFADTQTEL 12 5 SMMGSPKSL 13 292 PPWLETWLQ 11 22 LEFVFLLTL 12 10 PKSLSETCL 13 297 TWLQCRKQL 11 23 EFVFLLTLL 12 137 FPDSLIVKG 13 323 LPMRRSERY 11 20 LELEFVFLL 11 173 QARQQVIEL 13 328 SERYLFLNM 11 21 ELEFVFLLT 10 200 EIENLPLRL 13 378 SIPSVSNAL 11 10 FCSFADTQT 9 264 ITLLSLVYL 13 394 IQSTLGYVA 11 8 QIFCSFADT 8 289 RRFPPWLET 13 425 RFYTPPNFV 11 16 TQTELELEF 8 300 QCRKQLGLL 13 1 WREFSFIQI 7 315 VHVAYSLCL 13 TabIeXXVII-V2-HLA- 2 REFSFIQIF 7 362 SFGIMSLGL 13 B0702-9mers-98P4B6 5 SFIQIFCSF 7 390 EFSFIQSTL 13 Each peptide is a portion of 6 FIQIFCSFA 7 395 QSTLGYVAL 13 SEQ ID NO: 5; each start 17 QTELELEFV 7 430 PNFVLALVL 13 position is specified, the 18 TELELEFVF 7 436 LVLPSIVIL 13 length of peptide is 9 amino 441 IVILDLLQL 13 acids, and the end position 18 LPNGING1K 12 for each peptide is the start TableXXVTI-V6-HLA 27 DARKVTVGV 12 position plus eight. B0702-9mers-98P4B6 50 IRCGYHVVI 12 Pos 123456789 score Each peptide is a portion of 70 FPIHVVDVTH 12 3 SPGLQALSL 23 SEQ ID NO: 13; each start 105 RHLLVGKIL 12 35 PPCPADFFL 22 position is specified, the 128 SNAEYLASL 12 34 PPPCPADFF 20 length of peptide is 9 amino 133 LASLFPDSL 12 37 CPADFFLYF 20 acids, and the end position for 188 IPIDLGSLS 12 33 CPPPCPADF 18 each peptide is the start 202 ENLPLRLFT 12 1 SGSPGLQAL 14 position plus eight. 204 LPLRLFTLW 12 15 SGFTPFSCL 14 Pos 123456789 score 212 WRGPVVVAI 12 5 GLQALSLSL 13 43 IPHVSPERV 17 219 AISLATFFF 12 17 FTPFSCLSL 12 7 ILGKIILFL 16 256 NKTLPIVAI 12 25 LPSSWDYRC 12 2 LPSIVILGK 14 299 LQCRKQLGL 12 12 SLSSGFTPF 11 27 KGWEKSQFL 12 313 AMVHVAYSL 12 31 YRCPPPCPA 11 45 HVSPERVTV 12 324 PMRRSERYL 12 5 IMILGKIHL 11 360 YISFGIMSL 12 TabIeXXVII-VSA-HLA- 15 LPCISRKLK 11 366 MSLGLLSLL 12 BO0702-9mers-98P4B6 14 FLPCISRKL 10 403 LLISTFHVL 12 Each peptide is a portion of 38 GIGGTIPHV 10 435 ALVLPSIVI 12 SEQ ID NO: 11; each start 44 PHVSPERVT 10 25 IKDARKVTV 1 I position is specified, the length 35 LEEGIGGTI 9 37 GSGDFAKSL 11 of peptide is 9 amino acids, 46 VSPERVTVM 9 41 FAKSLTIRL 11 and the end position for each 6 VILGKIILF 8 68 EFFPHVVDV 11 peptide is the start position 10 KIILFLPCI 8 75 DVTHVEDAL 11 plus eight. 17 CISRKLKRI 8 75 DVTNIIHEDVAI 1 Pos 123456789 score 26 KKGWEKSQF 8 __KTN-_lVA 11 9 FWRGPVVVA 17 96 EHYTSLWDL 11 2LLLTW 1 9100 SLWDLRHLL 11 2 LPLRLFTFW 13 TableXXVII-V7A-HLA 10 SLWDLRHLL 1 7 FTFWRGPVV 9 B0702-9mers-98P4B6 134 ASLFPDSLI 11 8 TFWRGPVVV Each peptide is a portion of 146 FNVYSAWAL 11, 6 LFTFWRGPV 8 SEQ ID NO: 15; each start 196 SSAREIENL 11] 196 SARINL 11 position is specified, the 237 VPYARNQQS 11 TableXXVII-V5BHLA- length of peptide is 9 amino 253 EVNKTLPI 11 B0702-9mers-98P4B6 acids, and the end position 267 LSLVYLAGL 11 205 WO 03/087306 PCT/US03/10462 for each peptide is the start TabIcXXVII-V7C-HLA- peptide is the start position position plus eight. B0702-9mers-98P4B6 plus eight. Pos 123456789 score Each peptide is a portion of Pos 123456789 score SSPKSLSETF 16 SEQ ID NO: 15; each start 9 FWRGPVVVA 17 2 PKSLSETFL 14 position is specified, the length 2 LPLRLFTFW 13 of peptide is 9 amino acids, 7 FTFWRGPVV 9 TableXXVII-V7B-HLA- and the end position for each 8 TFWRGPVVV 9 B0702-9mers-98P4B6 peptide is the start position 6 LFTFWRGPV 8 Each peptide is a portion of plus eight SEQ ID NO: 15; each start Pos 123456789 score TableXXVII-V21-IILA position is specified, the 142 AASGTLSLA 12 B0702-9mers-98P4B6 length of peptide is 9 amino 143 ASGTLSLAF 12 Each peptide is a portion of acids, and the end position for 152 TSWSLGEFL 12 SEQ ID NO: 43; each start each peptide is the start 17 AAAWKCLGA 11 position is specified, the length position plus eight. 24 GANILRGGL 11 of peptide is 9 amino acids, Pos 123456789 score 27 ILRGGLSEI 11 and the end position for each 9 STLGYVALL 14 44 DRKIPPLST 11 peptide is the start position 8 QSTLGYVAL 13 53 PPPPAMWTE 11 plus eight. 3 NMAYQQSTL 11 125 NGVGPLWEF 11 Pos 123456789 score 7 QQSTLGYVA 10 148 SLAFTSWSL 11 8 KTKHCMFSL 11 2 LNMAYQQST 8 158 EFLGSGTWM 11 5 QEQKTKHCM . 7 6 YQQSTLGYV 6 165 WMKLETIIL 11 6 EQKTKHCMF 7 181 KSKHCMFSL I11 9 TKHCMFSLI 7 TabJeXXVII-V7C-HLA- 1 SKLTQEQKT 6 B0702-9mers-98P4B6 TableXXVII-V8-HLA Each peptide is a portion of B0702-9mers-98P4B6 TableXXVII-V25-HLA SEQ ID NO: 15; each start Each peptide is a portion of B0702-9mers-98P4B6 position is specified, the length SEQ ID NO: 17; each start Each peptide is a portion of of peptide is 9 amino adcids, position is specified, the SEQ ID NO: 51; each start and the end position for each length of peptide is 9 amino position is specified, the peptide is the start position acids, and the end position length of peptide is 9 amino plus eight. for each peptide is the start acids, and the end position Pos 123456789 score position plus eight. for each peptide is the start 102 PPESPDRAL 24 Pos 123456789 score positcn plus eight. 15 SPAAAWKCL 22 8 GMGGTIPHV 10 Pos 123456789 score 52 TPPPPAMWT 20 5 LEEGMGGTI 9 3 FLPCISQKL 10 55 PPAMWTEEA 18 1 KSQFLEEGM 7 4 LPCISQKLK 10 105 SPDRALKAA 18 4 FLEEGMGGT 6 6 CISQKLKRI 8 101 DPPESPDRA 16 7 EGMGGTIPH 6 1 ILFLPCISQ 4 113 ANSWRNPVL 16 6EEGMGGTIP 4 5 ILDLSVEVL 14 TableXXVIII-V1-HLA 47 IPPLSTPPP 14 B08-9mers-98P4B6 84 IPVVGVVTE 14 TableXXVII-V13-HLA- Each peptide is a portion of 118 NPVLPHTNG 14 B0702-9mers-98P4B6 SEQ ID NO: 3; each start 141 QAASGTLSL 14 Each peptide is a portion of position is specified, the length 160 LGSGTWMKL 14 SEQ ID NO: 27; each start of peptide is 9 amino acids, 29 RGGLSEIVL 13 position is specified, the and the end position for each 42 QQDRKIPPL 13 length of peptide is 9 amino peptide is the start position 49 PLSTPPPPA 13 acids, and the end position plus eight. 121 LPHTNGVGP 13 for each peptide is the start Pos 123456789 score 126 GVGPLWEFL 13 position plus eight. 41 FAKSLTIRL 25 128 GPLWEFLLR 13 Pos 123456789 score 203 NLPLRLFTL 25 31 GLSEIVLPI 12 1 SPKSLSETF 16 62 NPKFASEFF 22 48 PPLSTPPPP 12 2 PKSLSETFL 14 173 QARQQVIEL 22 50 LSTPPPPAM 12 253 EIVNKTLPI 22 54 PPPAMWTEE 12 TableXXVII-V14-HLA- 57 VIGSRNPKF 20 61 EEAGATAEA 12 B0702-9mers-98P4B6 81 DALTKTNII 20 81 SSQIPVVGV 12 Each peptide is a portion of 285 GTKYRRFPP 20 122 PHTNGVGPL 12 SEQ ID NO: 29; each start 299 LQCRKQLGL 20 129 PLWEFLLRL 12 position is specified, the length 326 RRSERYLFL 20 139 KSQAASGTL 12 of peptide is 9 amino acids, 385 ALNWREFSF 20 SKSQAASGTL 12 and the end position for each 206 WO 03/087306 PCT/USO3/10462 TableXXVIII-VI-HLA- TableXXVIII-V1-HLA- Each peptide is a portion of B08-9mers-98P4B6 B08-9mers-98P4B6 SEQ ID NO: 11; each start Each peptide is a portion of Each peptide is a portion of position is specified, the SEQ ID NO: 3; each start SEQ ID NO: 3; each start length of peptide is 9 amino position is specified, the length position is specified, the length acids, and the end position of peptide is 9 amino acids, of peptide is 9 amino acids, for each peptide is the start and the end position for each and the end position for each position pus eig ht. peptide is the start position peptide is the start position Pos 123456789 score plus eight. plus eight. 1 NLPLRLFTF 21 Pos 123456789 score Pos 123456789 score 3 PLRLFTFWR 13 93 [HREHYTSL 19 142 IVKGFNVVS 13 140 SLIVKGFNV 19 146 FNVVSAWAL 13 268 SLVYLAGLL 19 196 SSAREIENL 13 TableXXIX-V5B-HLA 9 SPKSLSETC 18 205 PLRLFTLWR 13 B08-9mers-98P4B6 28 ARKVTVGVI 18 264 ITLLSLVYL 13 Each peptide is a portion of 100 SLWDLRHLL 18 304 QLGLLSFFF 13 SEQ ID NO: 11; each start 171 NIQARQQVI 18 395 QSTLGYVAL 13 position is specified, the 214 GPVVVAISL 18 396 STLGYVALL 13 length of peptide is 9 amino 259 LPIVAITLL 18 397 TLGYVALLI 13 acids, and the end position 428 TPPNFVLAL 18 435 ALVLPSIVI 13 for each peptide is the start 39 GDFAKSLTI 17 37 GSGDFAKSL 12 position plus eight. 107 LLVGKILID 17 60 SRNPKFASE 12 Pos 123456789 score 157 GPKDASRQV 17 96 EHYTSLWDL 12 19 ELELEFVFL 20 274 GLLAAAYQL 17 105 RHLLVGKIL 12 12 SFADTQTEL 13 291 FPPWLETWL 17 109 VGKILIDVS 12 20 LELEFVFLL 13 378 SIPSVSNAL 17 177 QVIELARQL 12 23 EFVFLLTLL 12 438 LPSIVILDL 17 247 FYKIPIEIV 12 24 FVFLLTLLL 12 24 GIKDARKVT 16 325 MRRSERYLF 12 14 ADTQTELEL 11 44 SLTIRLIRC 16 362 SFGIMSLGL 12 22 LEFVFLLTL 11 125 YPESNAEYL 16 365 IMSLGLLSL 12 16 TQTELELEF 9 155 QLGPKDASR 16 390 EFSFIQSTL 12 184 QLNFIPIDL 16 414 GWKRAFEEE 12 200 EIENLPLRLI 16 426 FYTPPNFVL 12 237 HPYARNQQS 16 436 LVLPSIVIL 12 TableXXIX-V6-HLA 239 YARNQQSDF 16 441 IVILDLLQL 12B08-9mers-98P4B6 251 PIEIVNKTL 16 Each peptide is a portion of SEQ ID NO: 13; each start 258 TLPIVAITL 16 TableXXVIII-V2-HLA- si I ec t 283 YYGTKYRRF 16 B08-9mers-98P4B6 position is specified, the length of peptide is 9 amino 287 KYRRFPPWL 16 Each peptide is a portion of acids, and the end position for 300 QCRKQLGLL 16 SEQ ID NO: 5; each start each peptide is the start 324 PMRRSERYL 16 position is specified, the position plus eight 403 LLISTFHVL 16 length of peptide is 9 amino Position 123456789 score eight. 133 LASLFPDSL 15 acids, and the end position 19 S1RKLKRIKK 23 159 KDASRQVYI 15 for each peptide is the start 6 VILGKIILF 22 179 IELARQLNF 15 position plus eight. 27 KGWEKSQFL 22 187 FIPIDLGSL 15 Pos 123456789 score 17 CISRKLKRI 21 322 CLPMRRSER 15 3 SPGLQALSL 19 7 ISRKLKRI 21 360 YISFGIMSL 15 5 GLQALSLSL 17 7 ILGKILFL 18 106 HLLVGKILI 14 35 PPCPADFFL 16 14 FLPCISRKL 17 128 SNAEYLASL 14 12 SLSSGFTPF 14 21 LKRIKKGW 17 - 22 LK.RICKGWE 16 180 ELARQLNFI 14 1 SGSPGLQAL 13 24 RIKKGWEKS 14 197 SAREIENLP 14 15 SGFTPFSCL 12 4 SIILGKfI 13 245 SDFYKIPIE 14 33 CPPPCPADF 12 4 SIVILGKI 13 298 WLQCRKQLG 14 34 PPPCPADFF 12 5 IVILGKIL 12 323 LPMRRSERY 14 37 CPADFFLYF 12 25 IKKGWEKSQ 12 433 VLALVLPSI 14 17 FTPFSCLSL 11 46 VSPERVTVM 12 ____________10 KIILFLPCI 11t 5 SMMGSPKSL 13 28 SWDYRCPPP 11 3 KRIKKGWEK 11 17 CLPNGINGI 13 10 SLSLSSGFT 9 29 WEKSQFIKKGWEE 11 29A WE-KSQFLEE 11 82 ALTKTNIIF 13 91 VAIHREHYT 13 TableXXIX-V5A-HLA- TabeXXIX-V7A-HLA 13089mes-98413 TableXXIX-V7A-rLA 103 DLRHLLVGK 13 B08-9mers-98P4B6 207 WO 03/087306 PCT/USO3/10462 B08-9mers-98P4B6 TableXXIX-V8-HLA- for each peptide is the start Each peptide is a portion of B08-9mers-98P4B6 position plus eight. SEQ ID NO: 15; each start Each peptide is a portion of Pos 123456789 score position is specified, the SEQ ID NO: 17; each start 8 SQKLKRIKK 23 length of peptide is 9 amino position is specified, the 6 CISQKLKRI 21 acids, and the end position length of peptide is 9 amino 3 FLPCISQKL 17 for each peptide is the start acids, and the end position osition plus eight. for each peptide is the start TableXXIX-V 1-HLA Pos 123456789 score position plus eight. B1510-9mers-98P4B6 1 SPKSLSETF 24 Pos 123456789 score Each paptide is a portion of 9 FLPNGINGI 14 4 FLEEGMGGT 9 SEQ ID NO: 3; each start 2 PKSLSETFL 11 5 LEEGMGGTI 6 position is specified, the length of peptide is 9 amino acids, TabIeXXIX-V7B-HLA- and the end position for each B08-9mers-98P4B6 TableXXIX-V13-HLA- peptide is the start position Each peptide is a portion of B08-9mers-98P4B6 plus eight. SEQ ID NO: 15; each start Each peptide is a portion of Pos 123456789 score position is specified, the SEQ ID NO: 27; each start 93 IHREHYTSL 23 length of peptide is 9 amino position is specified, the 96 EHYTSLWDL 21 acids, and the end position for length of peptide is 9 amino 105 RHLLVGKIL 20 each peptide is the start acids, and the end position 315 VHVAYSLCL 20 position plus eight for each peptide is the start 200 EIENLPLRL 15 Pos 123456789 score position plus eight. 426 FYTPPNFVL 15 8 QSTLGYVAL 13 Pos 123456789 score 436 LVLPSIVIL 15 9 STLGYVALL 13 1 SPKSLSETF 24 54 YHVVIGSRN 14 3 NMAYQQSTL 11 9 FLPNGINGI 14 264 ITLLSLVYL 14 1 FLNMAYOQS 7 2 PKSLSETFL 11 360 YISFGIMSL 14 365 IMSIDLLSL 14 TabIeXXIX-V7C-HLA- TableXXIX-V14-HLA- 395 QSTLGYVAL 14 B08-9mers-98P4B6 B08-9mers-98P4B6 77 THHEDALTK 13 Each peptide is a portion of Each peptide is a portion of 99 TSLWDLRHL 13 SEQ ID NO: 15; each start SEQ ID NO: 29; each start 5 YPESNAEYL 13 position is specified, the length position is specified, the 1 EL 13 of peptide is 9 amino acids, length of peptide is 9 amino 173 QARQQVIEL 13 and the end position for each acids, and the end position 177 VIELARQL 13 peptide is the start position for each peptide is the start 236 IHPYARNQQ 13 plus eight. position plus eight. 261 IVAITLLSL 13 Pos 123456789 score Pos 123456789 score 297 TWLQCRKQL 13 179 EQKSKHCMF 28 1 NLPLRLFTF 21 390 EFSFIQSTL 13 42 QQDRKIPPL 21 3 PLRLFTFWR 13 428 TPPNFVLAL 13 73 GIRNKSSSS 21 430 PNFVLALVL 13 165 WMKLETIIL 21 TableXXIX-V21-HLA- 5 SMMGSPKSL 12 27 ILRGGLSEI 20 B08-9mers-98P4B6 37 GSGDFAKSL 12 181 KSKIHCMFSL 20 Each peptide is a portion of 41 FAKSLTIRL 12 5 ILDLSVEVL 19 SEQ ID NO: 43; each start 71 PHVVDVTHH 12 15 SPAAAWKCL 19 position is specified, the 78 HHEDALTKT 12 113 ANSWRNPVL 19 length of peptide is 9 amino 100 SLWDLRHLL 12 129 PLWEFLLRL 18 acids, and the end position for 128 SNAEYLASL 12 148 SLAFTSWSL 18 each peptide is the start 133 LASLFPDSL 12 102 PPESPDRAL 17 position plus eight. 146 FNVVSAWAL 12 109 ALKAANSWR 17 Pos 123456789 score 196 SSAREIENL 12 163 GTWMKLETI 17 6 EQKTKHCMF 28 214 GPVVVAISL 12 19 AWKCLGANI 16 8 KTKHCMFSL 20 220 ISLATFFFL 12 31 GLSEIVLPI 16 4 TQEQKTKHC 11 251 PIEIVNKTL 12 137 LLKSQAASG 16 258 TLPIVAITL 12 13724 GANL RGGLKSAASG 16 TableXXIX-V25-HLA- 259 LPIVAITLL 12 171 IILSKLTQE 15 B08-9mers-98P4B6 287 KYRRFPPWL 12 17 AAAWKCLGA 14 Each peptide is a portion of 324 PMRRSERYL 12 141 QAASGTLSL 14 SEQ ID NO: 51; each start 326 RRSERYLFL 12 134 LLRLLKSQA 13 position is specified, the 396 STLGYVALL 12 length of peptide is 9 amino 403 LLISTFHVL 12 acids, and the end position 438 LPSIVILDL 12 208 WO 03/087306 PCT/US03/10462 TableXXIX-V 1-HLA- TableXXIX-V5A-HLA- SEQ ID NO: 15; each start B1510-9mers-98P4B6 B 510-9mers-98P4B6 position is specified, the Each peptide is a portion of Each peptide is a portion of length of peptide is 9 amino SEQ ID NO: 3; each start SEQ ID NO: 11; each start acids, and the end position position is specified, the length position is specified, the length for each peptide is the start of peptide is 9 amino acids, of peptide is 9 amino acids, position plus eight. and the end position for each and the end position for each Pos 123456789 score peptide is the start position peptide is the start position 2 PKSLSETFL 11 plus eight. plus eight. 1 SPKSLSETF 7 Pos 123456789 score Pos 123456789 score 441 IVILDLLQL 12 1 NLPLRLFTF 7 TabIeXXIX-V7B-HLA 10 PKSLSETCL 11 8 TFWRGPVVV 7 B 1510-9mers-98P4B6 75 DVTHHEDAL 11 9 FWRGPVVVA 7 Each peptide is a portion of 148 VVSAWALQL I1 7 FTFWRGPVV 3 SEQ ID NO: 15; each start 184 QLNFIPIDL 11 position is specified, the 198 AREIENLPL 11 length of peptide is 9 amino 201 IENLPLRLF 11 TableXXIX-V5B-HLA- acids, and the end position for 203 NLPLRLFTL 11 B 1510-9mers-98P4B6 each peptide is the start '267 LSLVYLAGL 1I Each peptide is a portion of position plus eight. 274 GLLAAAYQL 11 SEQ ID NO: 11; each start Pos 123456789 score 283 YYGTKYRRF 11 position is specified, the 8 QSTLGYVAL 14 300 QCRKQLGLL 11 length of peptide is 9 amino 3 NMAYQQSTL 12 341 VHANIENSW 11 acids, and the end position 9 STLGYVALL 12 351 EEEVWRIEM i11 for each peptide is the start 366 MSLGLLSLL 11 position plus eight. 378 SIPSVSNAL 11 Pos 123456789 score TabIeXXIX-V7C-HLA 383 SNALNWREF 11 19 ELELEFVFL 14 B1510-9mers-98P4B6 411 LIYGWKRAF 11 12 SFADTQTEL 13 Each peptide is a portion of 439 PSIVILDLL 11 14 ADTQTELEL 12 SEQ ID NO: 15; each start 20 LELEFVFLL 12 position is specified, the length TabIeXXIX-V2-HLA- 22 LEFVFLLTL 12 of peptide is 9 amino acids, B 1510-9mers-98P4B6 23 EFVFLLTLL 11 and the end position for each Each peptide is a portion of 18 TELELEFVF 10 peptide is the start position SEQ ID NO: 5; each start 24 FVFLLTLLL 10 plus eight. position is specified, the 16 TQTELELEF 9 Pos 123456789 score length of peptide is 9 amino 2 REFSFIQIF 7 122 PHTNGVGPL 22 acids, and the end position 5 SFIQIFCSF 7 5 ILDLSVEVL 15 for each peptide is the start 102 PPESPDRAL 15 position plus eight . TableXXIX-V6-HLA- 113 ANSWRNPVL 14 Pos 123456789 score B 1510-9mers-98P4B6 126 GVGPLWEFL 13 1 SGSPGLQAL 15 Each peptide is a portion of 129 PLWEFLLRL 13 35 PPCPADFFL 12 SEQ ID NO: 13; each start 130 LWEFLLRLL 13 5 GLQALSLSL 11 , position is specified, the 24 GANILRGGL 12 15 SGFTPFSCL 11 length of peptide is 9 amino 29 RGGLSEIVL 12 3 SPGLQALSL 10 acids, and the end position for 42 QQDRKIPPL 12 17 FTPFSCLSL 10 each peptide is the start 50 LSTPPPPAM 12 33 CPPPCPADF 9 position plus eight. 141 QAASGTLSL 12 12 SLSSGFTPF 8 Pos 123456789 score 160 LGSGTWMKL 12 37 CPADFFLYF 8 44 PHVSPERVT 15 15 SPAAAWKCL 11 34 PPPCPADFF 7 5 IVILGKIIL 14 20 WKCLGANIL 11 7 ILGKIILFL 14 139 KSQAASGTL 11 TableXXIX-V5A-HLA- 14 FLPCISRKL 12 148 SLAFTSWSL 11 B1510-9mers-98P4B6 27 KGWEKSQFL 11 152 TSWSLGEFL 11 Each peptide is a portion of 46 VSPERVTVM 10 181 KSKHCMFSL 11 SEQ ID NO: 11; each start 6 VILGKIILF 8 127 VGPLWEFLL 10 position is specified, the length 26 KKGWEKSQF 7 165 WMKLETIIL 10 of peptide is 9 amino acids, 45 HVSPERVTV 7 168 LETIILSKL 10 and the end position for each 183 KHCMFSLIS 10 peptide is the start position TableXXIX-V7A-HLA plus eight. B 1510-9mers-98P4B6 TableXXIX-V8-HLA Pos 123456789 score Each peptide is a portion of B1510-9mers-98P4B6 209 WO 03/087306 PCT/USO3/10462 Each peptide is a portion of SEQ ID NO: 51; each start TableXXX-V1-HLA SEQ ID NO: 17; each star position is specified, the B2705-9mers-98P4B6 position is specified, the length of peptide is 9 amino Each peptide is a portion of length of peptide is 9 amino acids, and the end position SEQ ID NO: 3; each start acids, and the end position for each peptide is the start position is specified, the length for each peptide is the start position plus eight. of peptide is 9 amino acids, position plus eight. Pos 123456789 score and the end position for each Pos 123456789 score 3 FLPCISQKL 10 peptide is the start position 1 KSQFLEEGM 6 7 ISQKLKRIK 6 plus eight. 4 FLEEGMGGT 4 6 CISQKLKRI 4 Pos 123456789 score 8 GMGGTIPHV 4 22 INGIKDARK 16 5 LEEGMGGTI 3 TableXXX-VI-HLA- 39 GDFAKSLTI 16 7 EGMGGTIPH 3 B2705-9mers-98P4B6 40 DFAKSLTIR 16 9 MGGTIPHVS 3 Each peptide is a portion of 43 KSLTIRLIR 16 6 EEGMGGTIP 2 SEQ ID NO: 3; each start 56 VVIGSRNPK 16 position is specified, the length 112 ILIDVSNNM 16 TableXXIX-V13-HLA- of peptide is 9 amino acids, 175 RQQVIELAR 16 B 1510-9mers-98P4B6 and the end position for each 177 QVIELARQL 16 Each peptide is a portion of peptide is the start position 196 SSAREIENL 16 SEQ ID NO: 27; each start plus eight. 206 LRLFTLWRG 16 position is specified, the Pos 123456789 score 218 VAISLATFF 16 length of peptide is 9 amino 326 RRSERYLFL 26 225 FFFLYSFVR 16 acids, and the end position 424 YRFYTPPNF 26 233 RDVIHPYAR 16 for each peptide is the start 355 WRIEMYISF 25 313 AMVHVAYSL 16 position plus eight. 198 AREIENLPL 24 319 YSLCLPMRR 16 Pos 123456789 score 240 ARNQQSDFY 22 396 STLGYVALL 16 2 PKSLSETFL 11 325 , MRRSERYLF 22 418 AFEEEYYRF 16 1 SPKSLSETF 7 47 IRLIRCGYH 21 443 ILDLLQLCR 16 50 IRCGYHVVI 21 37 GSGDFAKSL 15 TableXXIX-V14-HLA- 104 LRHLLVGKI 21 82 ALTIKTNIIF 15 B1510-9mers-98P4B6 289 RRFPPWLET 21 87 NIIFVAIHR 15 Each peptide is a portion of 416 KRAFEEEYY 21 93 IHREHYTSL 15 SEQ ID NO: 29; each start 212 WRGPVVVAI 20 96 EIIYTSLWDL 15 position is specified, the length 302 RKQLGLLSF 20 155 QLGPKDASR 15 of peptide is 9 amino acids, 417 RAFEEEYYR 20 173 QARQQVIEL 15 and the end position for each 28 ARKVTVGVI 19 295 LETWLQCRK 15 peptide is the start position 61 RNPKFASEF 19 297 TWLQCRKQL 15 u 182 ARQLNFIPI 19 329 ERYLFLNMA 15 Pos 123456789 score 199 REIENLPLR 19 390 ERYFSF[QSTLLNMA 15 1 NLPLRLFTF 7 199 REINPL 19 390 EFSFIQSTL 15 1 NLPLRFTF 7 249 KIPIEIVNK 19 401 VALLISTFH 15 8 FWRGPVVVA 7 303 KQLGLLSFF 19 409 HVLIYGWKR 15 7 FFWRGPVV 3 53 GYHVVIGSR 18 411 LIYGWKRAF 15 S105 RHLLVGKIL 18 438 LPSIVILDL 15 179 IELARQLNF 18 5 SMMGSPKSL 14 TableXXIX-V21-HLA- 214 GPVVVAISL 18 0 PKSLSETCL 14 B1510-9mers-98P4B6 241 RNQQSDFYK 1810 PKSLSETCL 14 Each peptide is a portion of 2741 GLLAAAYQL 18 1833 VGVIGSGDFIK 14 SEQ ID NO: 43; each start 27482 GLLYYGTKYRRAAAYQL 18 33 VGVIGSGDF 14 position is specified, the length 282 LYYGTKYRR 18 41 FAKSLTIRL 14 of peptide is 9 amino acids, 436 LVLPSIVIL 18 57 VIGSRNPKF 14 and the end position for each 21 GINGIKDAR 17 60 SRNPKFASE 14 peptide is the start position 174 ARQQVIELA 17 77 THHEDALTK 14 plus eiht. 223 ATFFFLYSF 17 120 MRINQYPES 14 Pos 123456789 score 259 LPIVAITLL 17 128 SNAEYLASL 14 8 KTKHCMFSL 11 264 ITLLSLVYL 17 136 LFPDSLIVK 14 5QEQKTKHCM 8 330 RYLFLNMAY 17 146 FNVVSAWAL 14 6 EQKTKHCMF 7 360 YISFGIMSL 17 162 SRQVYICSN 14 4 TQEQKTKHC 365 IMSLGLLSL 17 167 ICSNNIQAR 14 366 MSLGLLSLL 17 193 GSLSSAREI 14 TableXXIX-V25-HLA- 400 YVALLISTF 17 200 EIENLPLRL 14 B1510-9mers-98P4B6 430 PNFVLALVL 17 201 IENLPL R L F 14 Each peptide is a portion of 441 IVILDLLQL 17 217 VVAISLATF 14 210 WO 03/087306 PCT/USO3/10462 TableXXX-V I-HLA- TableXXX-V I-HLA- TableXXX-V2-HLA B2705-9mers-98P4B6 B2705-9mers-98P4B6 B2705-9mers-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NO: 5; each start position is specified, the length position is specified, the length position is specified, the of peptide is 9 amino acids, of peptide is 9 amino acids, length of peptide is 9 amino and the end position for each and the end position for each acids, and the end position peptide is the start position peptide is the start position for each peptide is the start plus eight. plus eight. position plus eight. Pos 123456789 score Pos 123456789 score Pos 123456789 score 258 TLPIVAITL 14 17 CLPNGINGI 12 34 PPPCPADFF 12 261 IVAITLLSL 14 70 FPHVVDVTH 12 35 PPCPADFFL 12 263 AITLLSLVY 14 71 PHVVDVTHH 12 24 SLPSSWDYR 11 267 LSLVYLAGL 14 80 EDALTKTNI 12 37 CPADFFLYF 11 280 YQLYYGTKY 14 86 TNIIFVAIH 12 2 GSPGLQALS 9 281 QLYYGTKYR 14 89 IFVAIHREH 12 36 PCPADFFLY 8 299 LQCRKQLGL 14 106 HLLVGKILI 12 301 CRKQLGLLS 14 114 IDVSNNMRI 12 TableXXX-V5A-HLA 308 LSFFFAMVH 14 133 LASLFPDSL 12 B2705-9mers-98P4B6 318 AYSLCLPMR 14 134 ASLFPDSLI 12 Each peptide is a portion of 363 FGIMSLGLL 14 164 QVYICSNNI 12 SEQ ID NO: 11; each start 392 SFIQSTLGY 14 184 QLNFIPIDL 12 position is specified, the 395 QSTLGYVAL 14 187 FIPIDLGSL 12 length of peptide is 9 amino 426 FYTPPNFVL 14 205 PLRLFTLWR 12 acids, and the end position 439 PSIVILDLL 14 219 AISLATFFF 12 for each peptide is the start 444 LDLLQLCRY 14 231 FVRDVIIIPY 12 position plus eight. 35 VIGSGDFAK 13 232 VRDVIHPYA 12 Pos 123456789 score 98 YTSLWDLRH 13 256 NKTLPIVAI 12 4 LRLFTFWRG 15 99 TSLWDLRHL 13 272 LAGLLAAAY 12 1 NLPLRLFTF 13 103 DLRHLLVGK 13 288 YRRFPPWLE 12 3 PLRLFTFWR 11 113 LIDVSNNMR 13 317 VAYSLCLPM 12 5 RLFTFWRGP 7 117 SNNMRINQY 13 322 CLPMRRSER 12 124 QYPESNAEY 13 328 SERYLFLNM 12 TableXXX-V5B-HLA 129 NAEYLASLF 13 349 WNEEEVWRI 12 B2705-9mers-98P4B6 138 PDSLIVKGF 13 352 EEVWRIEMY 12 Each peptide is a portion of 148 VVSAWALQL 13 362 SFGIMSLGL 12 SEQ ID NO: 11; each start 151 AWALQLGPK 13 381 SVSNALNWR 12 position is specified, the 151 D AWALQLGPK 13 381 SVNALNWRF 12 length of peptide is 9 amino 20391 DLGSLSSAR 13 383 SALNWREFF 12 acids, and the end position 203 NLPLRLFTL _13 385. ALNWREFSF 1 2 for each peptide is the start 220 ISLATFFFL 13 428 TPPNFVLAL 12 position plus eight. 229 SFVRVU-1 131position Plus eight t. 229 YSFVRDVIH 13 Pos 123456789 score 239 YARNQQSDF 13 TableXXX-V2-HLA- 2 REFSFIQIF 20 246 DFYKIPIEI 13 B2705-9mers-98P4B6 REFSFIQI 1 WREFSFIQI 19 251 PIEIVNKTL 13 Each peptide is a portion of 5 SFIQIFCSF 16 268 SLVYLAGLL 13 SEQ ID NO: 5; each start 22 LEFVFLLTL 16 279 AYQLYYGTK 13 position is specified, the 24 FVFLLTLLL 16 283 YYGTKYRRF 13 length of peptide is 9 amino2 FLT L 1 287 KYRRFPPWL 13 acids, and the end position 12SFADTQTEL 15 291 FPPWLETWL 13 for each peptide is the start 14 ADTQTELEL 15 300 QCRKQLGLL 13 position plus eight t. 18 TELELEFVF 15 23 EFVFLLTLL 15 304 QLGLLSFFF 13 Pos 123456789 score 23 EFVFLLTLL 15 306 GLLSFFFAM 13 5 GLQALSLSL 17 16 TQTELELEF 14 315 VHVAYSLCL 13 9 LSLSLSSGF 15 20 LELEFVFLL 14 337 AYQQVHANI 13 15 SGFTPFSCL 15 19 ELELEFVFL 13 348 SWNEEEVWR 13 1 SGSPGLQAL 14eXXX 371 LSLLAVTSI 13 3 SPGLQALSL 14 TableXXX-V6-HLA 378 SIPSVSNAL 13 12 SLSSGFTPF 14 B2705-9mers-98P4B6 388 WREFSFIQS 13 23 LSLPSSWDY 14 Each peptide is a portion of 403 LLISTFHVL 13 17 FTPFSCLSL 13 SEQ ID NO: 13; each start 408 FHVLISTFHVYGWK 13 31 YRCPPPCPAL 13 position is specified, the 408 FHALVLYPSGVK 13 33 YCPPPCPAF 12 length of peptide is 9 amino 4 ALVLPS 13211 33 CPPPCPADF 12 211 WO 03/087306 PCT/US03/10462 acids, and the end position for plus eight. TableXXX-V7C-HLA each peptide is the start Pos 123456789 score B2705-9mers-98P4B6 position plus eight. 21 KCLGANILR 18 Each peptide is a portion of Pos 123456789 score 29 RGGLSEIVL 18 SEQ ID NO: 15; each start 23 KRIKKGWEK 29 69 AQESGIRNK 18 position is specified, the length 19 SRKLKRIKK 25 167 KLETIILSK 18 of peptide is 9 amino acids, 6 VILGKIILF 19 175 KLTQEQKSK 18 and the end position for each 13 LFLPCISRK 19 74 IRNKSSSSS 17 peptide is the start position 5 IVILGKIIL 18 125 NGVGPLWEF 17 plus eight. 7 ILGKIILFL 18 128 GPLWEFLLR 17 Pos 123456789 score 12 ILFLPCISR 18 107 DRALKAANS 16 164 TWMKLETII 11 16 PCISRKLKR 16 131 WEFLLRLLK 16 179 EQKSKHCMF 11 26 KKGWEKSQF 16 5 ILDLSVEVL 15 15 SPAAAWKCL 10 2 LPSIVILGK 15 20 WKCLGANIL 15 30 GGLSEIVLP 10 18 ISRKLKRIK 15 37 LPIEWQQDR 15 76 NKSSSSSQI 10 27 KGWEKSQFL 15 42 QQDRKIPPL 15 92 EDDEAQDSI 10 37 EGIGGTIPH 15 67 AEAQESGIR 15 75 RNKSSSSSQ 8 14 FLPCISRKL 14 100 IDPPESPDR 15 85 PVVGVVTED 8 42 TIPHVSPER 14 126 GVGPLWEFL 15 145 GTLSLAFTS 8 129 PLWEFLLRL 15 171 IILSKLTQE 8 TableXXX-V7A-HLA- 135 LRLLKSQAA 15 185 CMFSLISGS 8 B2705-9mers-98P4B6 158 EFLGSGTWM 15 Each peptide is a portion of 160 LGSGTWMKL 15 TableXXX-V8-HLA SEQ ID NO: 15; each start 168 LETHLSKL 15 B2705-9mers-98P4B6 position is specified, the 24 GANILRGGL 14 Each peptide is a portion of length of peptide is 9 amino 27 ILRGGLSEI 14 SEQ ID NO: 17; each start acids, and the end position 28 LRGGLSE1V 14 position is specified, the for each peptide is the start 38 PIEWQQDRK 14 length of peptide is 9 amino positionn plus eiht. 113 ANSWRNPVL 14 acids, and the end position Pos 123456789 score 116 WRNPVLPHT 14 for each peptide is the start 2 PKSLSETFL 14 139 position plus eight. 139 KSQAASGTL 14 1 SPKSLSETF 131 Pos 123456789 score 9 FLPNGINGI 12 141 QAASGTLSLF 14 7 EGMGGTIPH 13 143 ASGTLSLAF 14 6 SETFLPNGI 8 1 KSQFLEEGM 11 7 ETFLPNGIN .6 173 LSKLTQEQK 14 5 LEEGMGGTI 9 13 LASPAAAWK 13 8 TFLPNGING 6 13 8 GMGGTIPHV 9 31 GLSEIVLPI. 13 TableXXX-V7B-HLA- 44 DRKIPPLST 13 TableXXX-V13-HLA B2705-9mers-98P4B6 109 ALKAANSWR 13 B2705-9mers-98P4B6 Each peptide is a portion of 122 PHTNGVGPL 13 Each peptide is a portion of SEQ ID NO: 15; each start 148 SLAFTSWSL 13 SEQ ID NO: 27; each start position is specified, the 151 FTSWSLGEF 13 position is specified, the length of peptide is 9 amino 159 FLGSGTWMK 13 length of peptide is 9 amino acids, and the end position for 165 WMKLETI1L 13 acids, and the end position each peptide is the start 176 LTQEQKSKH 13 for each peptide is the start position plus eight. 181 KSKHCMFSL 13 position plus eight. Pos 123456789 score 39 IEWQQDRKI 12 Pos 123456789 score 9 STLGYVALL 16 102 PPESPDRAL 12 2 PKSLSETFL 14 3 NMAYQQSTL 14 103 PESPDRALK 12 1 SPKSLSETF 13 8 QSTLGYVAL 14 130 LWEFLLRLL 12 9 FLPNGINGI 12 5 AYQQSTLGY 13 136 RLLKSQAAS 12 6 SETFLPNGI 8 4 MAYQQSTLG 7 163 GTWMKLETI 12 7 ETFLPNGIN 6 178 QEQKSKIHICM 12 8 TFLPNGING 6 TableXXX-V7C-HLA- 19 AWKCLGANI 11 B2705-9mers-98P4B6 45 RKIPPLSTP 11 TableXXX-V14-HLA Each peptide is a portion of 50 LSTPPPPAM 11 B2705-9mers-98P4B6 SEQ ID NO: 15; each start 108 RALKAANSW 11 Each peptide is a portion of position is specified, the length 115 SWRNPVLPH 11 SEQ ID NO: 29; each start of peptide is 9 amino acids, 127 VGPLWEFLL 11 position is specified, the and the end position for each 152 TSWSLGEFL 11 length of peptide is 9 amino peptide is the start position 157 GEFLGSGTV 11 acids, and the end position for each peptide is the start 212 WO 03/087306 PCT/USO3/10462 position plus eight. TabIeXXXI-V1-HLA- TableXXXI-V1-HLA Pos 123456789 score B2709-9mers-98P4B6 B2709-9mers-98P4B6 4 LRLFTFWRG 15 Each peptide is a portion of Each peptide is a portion of 1 NLPLRLFTF 13 SEQ ID NO: 3; each start SEQ ID NO: 3; each start 3 PLRLFTFWR 11 position is specified, the length position is specified, the length 5 RLFT RGP 7 of peptide is 9 amino acids, of peptide is 9 amino acids, and the end position for each and the end position for each TableXXX-V21-HLA- peptide is the start position peptide is the start position TablXXX-V21-HLA- plus eight. plus eight B2705-9mers-98P4B6 u B2705-9mers-98P4B6 Pos 123456789 score Pos 123456789 score Each peptide is a portion of 182 ARQLNFIPI 19 365 IMSLGLLSL 12 SEQ ID NO: 43; each start 355 WRIEMYISF 19 366 MSLGLLSLL 12 position is specified, the length 2 L Y 1 3 SLG L 12 of peptide is 9 amino acids, 274 GLLAAAYQL 18 395 QSTLGYVAL 12 and the end position for each 289 RRFPPWLET 18 403 LLISTFHVL 12 peptide is the start position 105 RHLLVGKIL 16 416 KRAFEEEYY 12 plus eight. 193 GSLSSAREI 15 426 FYTPPNFVL 12 Pos 123456789 score 214 GPVVVAISL 15 428 TPPNFVLAL 12 2 KLTQEQKTK 18 441 IVILDLLQL 15 439 PSIVILDLL 12 3 LTQEQKTKH 14 37 GSGDFAKSI, 14 8 KTKHCMFSL 13 39 GDFAKSLTI 14 TableXXXI-V2-HLA 5 QEQKTKHCM 11 48 RLIRCGYHV 14 B2709-9mers-98P4B6 6 EQKTKHCMF 1 264 ITLLSLVYL 14 Each peptide is a portion of 306 GLLSFFFAM 14 SEQ ID NO: 5; each start TableXXX-V25-HLA- 313 AMVHVAYSL 14 position is specified, the B2705-9mers-98P4B6 425 RFYTPPNFV 14 length of peptide is 9 amino Each peptide is a portion of 430 PNFVLALVL 14 adcids, and the end position SEQ ID NO: 51; each start 436 LVLPSIVIL 14 for each peptide is the start position is specified, the 47 IRLIRCGYH 13 position plus eight. length of peptide is 9 amino 61 RNPKFASEF 13 Pos 123456789 score acids, and the end position 68 EFFPHVVDV 13 5 GLQALSLSL 14 for each peptide is the start 99 TSLWDLRHL 13 3 SPGLQALSL 12 position plus eight. 135 SLFPDSLIV 13 15 SGFTPFSCL 12 Pos 123456789 score 148 VVSAWALQL 13 1 SGSPGLQAL 11 2 LFLPCISQK 18 177 QVIELARQL 13 9 LSLSLSSGF 11 5 PCISQKLKR 16 179 IELARQLNF 13 17 FTPFSCLSL 11 7 ISQKLKRIK 15 206 LRLFTLWRG 13 31 YRCPPPCPA 11 8 SQKLKRIKK 15 220 ISLATFFFL 13 35 PPCPADFFL 11 3 FLPCISQKL 14 287 KYRRFPPWL 13 12 SLSSGFTPF 9 4 LPCISQKLK 13 297 TWLQCRKQL 13 33 CPPPCPADF 9 6 CISQKLKRI 12 302 RKQLGLLSF 13 34 PPPCPADFF 9 9 QKLKRIKKG 9 396 STLGYVALL 13 37 CPADFFLYF 9 1 ILFLPCISQ 8 41 FAKSLTIRL 12 32 RCPPPCPAD 6 85 KTNIIFVAI 12 TableXXXI-VI-HLA- 96 EHYTSLWDL 12 TableXXXI-V5A-HLA B2709-9mers-98P4B6 114 IDVSNNMRI 12 B2709-9mers-98P4B6 Each peptide is a portion of 120 MRINQYPES 12 Each peptide is a portion of SEQ ID NO: 3; each start 125 YPESNAEYL 12 SEQ ID NO: 11; each start position is specified, the length 146 FNVVSAWAL 12 position is specified, the of peptide is 9 amino acids, 157 GPKDASRQV 12 length of peptide is 9 amino and the end position for each 159 KDASRQVYI 12 acids, and the end position for peptide is the start position 200 EIENLPLRL 12 each peptide is the start plus eight. 223 ATFFFLYSF 12 position plus eight. Pos 123456789 score 227 FLYSFVRDV 12 Pos 123456789 score 326 RRSERYLFL 25 232 VRDVIHPYA 12 4 LRLFTFWRG 131 198 AREIENLPL 22 261 IVAITLLSL 12 7 FTFWRGPVV 11 424 YRFYTPPNF 22 267 LSLVYLAGL 12 6 LFTFWRGPVV 9 212 WRGPVVVAI 21 268 SLVYLAGLL 121 NLPRLFTF 89 28 ARKVTVGVI 20 303 KQLGLLSFF 12 1 NLPLRLFTFWRGP 6 50 IRCGYHVVI 20 315 VHVAYSLCL 12 5P 6 325 MRRSERYLF 20 317 VAYSLCLPM 12 TableXXXI-V5B-HLA 104 LRH-LLVGKI 19 329 ERYLFLNMA 12 213 WO 03/087306 PCT/USO3/10462 B2709-9mers-98P4B6 Position lus eight. TabIeXXXI-V7C-HLA Each peptide is a portion of Pos 123456789 score B2709-9mers-98P4B6 SEQ ID NO: 11; each start 2 PKSLSETFL 10 Each peptide is a portion of position is specified, the 1 SPKSLSETF 9 SEQ ID NO: 15; each start length of peptide is 9 amino 6 SETFLPNGI 9 position is specified, the length acids, and the end position 9 FLPNGINGI 8 of peptide is 9 amino acids, for each peptide is the start 3 KSLSETFLP 5 and the end position for each position plus eight. 8 TFLPNGING peptide is the start position Pos 123456789 score plus eight. 1 WREFSFIQI 19 Tab1eXXXI-V7B-HLA- Pos 123456789 score 2 REFSFIQIF 15 B2709-9mers-98P4B6 2 SIVILDLSV 10 14 ADTQTELEL 13 Each peptide is a portion of 15 SPAAAWKCL 10 20 LELEFVFLL 13 SEQ ID NO: 15; each start 19 AWKCLGANI 10 22 LEFVFLLTL 13 position is specified, the 76 NKSSSSSQI 10 24 FVFLLTLLL 13 length of peptide is 9 amino 79 SSSSQIPVV 10 19 ELELEFVFL 11 acids, and the end position for 81 SSQIPVVGV 10 23 EFVFLLTLL 11 each peptide is the start 112 AANSWRNPV 10 5 SFIQIFCSF 10 position pluseight. 127 VGPLWEFLL 10 12 SFADTQTEL 10 Pos 123456789 score 130 LWEFLLRLL 10 16 TQTELELEF 10 9 STLGYVALL 13 143 ASGTLSLAF 10 18 TELELEFVF 10 8 QSTLGYVAL 12 148 SLAFTSWSL 10 3 NMAYQQSTL 10 158 EFLGSGTWM 10 TableXXXI-V6-HLA- 6 YQQSTLGYV 9 160 LGSGTWMKL 10 B2709-9mers-98P4B6 165 WMKLETIIL 10 Each peptide is a portion of TabcleXXXI-V7C-HLA- 27 ILRGGLSEI 9 SEQ ID NO: 13; each start B2709-9mers-98P4B6 39 IEWQQDRKI 9 position is specified, the Each peptide is a portion of 78 SSSSSQIPV 9 length of peptide is 9 amino SEQ ID NO: 15; each start 125 NGVGPLWEF 9 acids, and the end position for position is specified, the length 179 EQKSKHCMF 9 each peptide is the start of peptide is 9 amino acids, 66 TAEAQESGI 8 position plus eight. and the end position for each 92 EDDEAQDSI 8 Pos 123456789 score peptide is the start position 151 FTSWSLGEF 8 7 ILGKIILFL 13 plus eight. 164 TWIMKLETII 8 23 KRIKKGWEK 13 Pos 123456789 score 5 IVILGKIIL 12 28 LRGGLSEIV 18 182 SKHCMFSLI 8 10 KIILFLPCI 12 29 RGGLSEIVL 14 27 KGWEKSQFL 12 31 GLSEIVLPI 14 TableXXXI-V8-HLA 38 GIGGTIPHV 12 126 GVGPLWEFL 14 B2709-9mers-98P4B6 14 FLPCISRKL 11 24 GANILRGGL 13 Each peptide is a portion of 26 KKGWEKSQF 11 5 ILDLSVEVL 12 SEQ ID NO: 17; each start S3 PSVILGKI 10 107 DRALKAANS 12 position is specified, the S6 VILGKIILF 10_ 113 ANSWRNPVL 12 length of peptide is 9 amino 19 SRKLKRIKK 10 116 WRNPVLPHT 12 acids, and the end position 31 KSQFLEEGI 10 122 PHTNGVGPL 12 for each peptide is the start 43 IPHVSPERV 10 129 PLWEFLLRL 12 position plus eight. 45 HVSPERVTV 10 135 LRLLKSQAA 12 Pos 123456789 score 4 SIVILGKII 9 139 KSQAASGTL 12 8 GMGGTIPHV 12 17 CISRKLKRI 9 141 QAASGTLSL 12 1 KSQFLEEGM 10 35 LEEGIGGTI 9 168 LETIILSKL 12 5 LEEGMGGTI 8 46 VSPERVTVM 9 181 KSKHCMFSL 12 20 RKLKRIKKG 6 4 VILDLSVEV 11 TableXXXI-V13-HLA 41 GTIPHVSPE 6 20 WKCLGANIL 11 B2709-9mers-98P4B6 42 QQDRKIPPL 11 Each peptide is a portion of TableXXXI-V7A-HLA- 44 DRKIPPLST 11 SEQ ID NO: 27; each start B2709-9mcrs-98P4B6 50 LSTPPPPAM 11 position is specified, the Each peptide is a portion of 74 IRNKSSSSS 11 length of peptide is 9 amino SEQ ID NO: 15; each start 82 SQIPVVGVV 11 acids, and the end position position is specified, the 102 PPESPDRAL 11 for each peptide is the start length of peptide is 9 amino 119 PVLPHTNGV 11 position plus ei ght. acids, and the end position 152 TSWSLGEFL 11 Pos 123456789 scor for each peptide is the start 163 GTWMKLETI 1 2 PKSLSETFL 10 214 WO 03/087306 PCT/US03/10462 1 SPKSLSETF 9 TableXXXII-V1-HLA- TablcXXXII-V1-HLA 6 SETFLPNGI 9 B4402-9mers-98P4B6 B4402-9mers-98P4B6 9 FLPNGINGI 8 Each peptide is a portion of Each peptide is a portion of 3 KSLSETFLP 5 SEQ ID NO: 3; each start SEQ ID NO: 3; each start 8 TFLPNGING 4 position is specified, the length position is specified, the length of peptide is 9 amino acids, of peptide is 9 amino acids, TableXXXI-VI4-HLA- and the end position for each and the end position for each B2709-9mers-98P4B6 peptide is the start position peptide is the start position Each peptide is a portion of plus eight. plus eight. SEQ ID NO: 29; each start Pos 123456789 score Pos 123456789 score position is specified, the 352 EEVWRIEMY 26 105 RHLLVGKIL 14 length of peptide is 9 amino 201 [ENLPLRLF 24 148 VVSAWALQL 14 acids, and the end position for 179 IELARQLNF 23 198 AREIENLPL 14 each peptide is the start 14 SETCLPNGI 21 204 LPLRLFTLW 14 position plus eight. 419 FEEEYYRFY 21 218 VAISLATFF 14 Pos 123456789 score 357 IEMYISFGI 20 221 SLATFFFLY 14 4 LRLFTFWRG 13 42 AKSLTIRLI 18 258 TLPIVAITL 14 7 FTFWRGPVV 11 436 LVLPSIVIL 18 264 ITLLSLVYL 14 6 LFTFWRGPV 9 117 SNNMRINQY 17 272 LAGLLAAAY 14 8 TFWRGPVVV 9 144 KGFNVVSAW 17 303 KQLGLLSFF 14 1 NLPLRLFTF 8 259 LPIVAITLL 17 313 AMVHVAYSL 14 5 RLFTFWRGP 6 441 IVILDLLQL 17 351 EEEVWRIEM 14 5 SMMGSPKSL 16 355 WRIEMYISF 14 TabIeXXXI-V21-HLA- 138 PDSLIVKGF 16 360 YISFGIIMSL 14 B2709-9mers-98P4B6 177 QVIELARQL 16 365 IMSLGLLSL 14 Each peptide is a portion of 199 REIENLPLR 16 366 MSLGLLSLL 14 SEQ ID NO: 43; each start 203 NLPLRLFTL 16 383 SNALNWREF 14 position is specified, the length 219 AISLATFFF 16 385 ALNWREFSF 14 of peptide is 9 amino acids, 223 ATFFFLYSF 16 395 QSTLGYVAL 14 and the end position for each 256 NKTLPIVAI 16 411 LIYGWKRAF 14 peptide is the start position 263 AITLLSLVY 16 426 FYTPPNFVL 14 plus eight. 290 RFPPWLETW 16 435 ALVLPSIVI 14 Pos 123456789 score 392 SFIQSTLGY 16 28 ARKVTVGVI 13 8 KTKHCMFSL 12 403 LLISTFHVL 16 46 TIRLIRCGY 13 5 QEQKTKHCM 8 428 TPPNFVLAL 16 99 TSLWDLRHL 13 6 EQKTKHChIF 8 439 PSIVILDLL 16 126 PESNAEYLA 13 9 TKHCMFSLI 8 9 TKHCMFSI 8 67 SEFFPHVVD 15 129 NAEYLASLF 13 79 HEDALTKTN 15 133 LASLFPDSL 13 TableXXXI-V25-HLA B2709-9mers-98P4B6 100 SLWDLRHLL 15 134 ASLFPDSLI 13 B2709-9mers-98P4B6 130 AEYLASLFP 15 146 FNVVSAWAL 13 Each peptide is a portion of SEQ ID NO: 51; each start 182 ARQLNFIPI 15 158 PKDASRQVY 13 position is specified, the 196 SSAREIENL 15 180 ELARQLNFI 13 length of peptide is 9 amino 200 EIENLPLRL 15 184 QLNFIPIDL 13 acids, and the end position 212 WRGPVVVAI 15 240 ARNQQSDFY 13 for each peptide is the start 231 FVRDVIHPY 15 251 PIEIVNKTL 13 position plus eight. 252 IEIVNKTLP 15 253 EIVNKTLPI 13 Pos 123456789 score 297 TWLQCRKQL 15 268 SLVYLAGLL 13 3 FLPCISQKL 11 363 FGIMSLGLL 15 274 GLLAAAYQL 13 6 CISQKLKRI 9 378 SIPSVSNAL 15 286 TKYRRFPPW 13 2 LFLPCISQK 4 389 REFSFIQST 15 287 KYRRFPPWL 13 390 EFSFIQSTL 15 302 RKQLGLLSF 13 TableXXXII-VI-HLA- 396 STLGYVALL 15 311 FFAMVHVAY 13 B4402-9mers-98P4B6 400 YVALLISTF 15 323 LPMRRSERY 13 Each peptide is a portion of 421 EEYYRFYTP 15 326 RRSERYLFL 13 SEQ ID NO: 3; each start 430 PNFVLALVL 15 328 SERYLFLNM 13 position is specified, the length 438 LPSIVILDL 15 330 RYLFLNMAY 13 of peptide is 9 amino acids, 17 CLPNGINGI 14 341 VHANIENSW 13 and the end position for each 37 GSGDFAKSL 14 347 NSWNEEEVW 13 peptide is the start position 82 ALTKTNIIF 14 380 PSVSNALNW 13 plus eight 85 KTNIFVAI 14 407 TFHVLIYGW 13 Posl 123456789 score 96 EHYTSLWDL 14 418 AFEEEYYRF 13 215 WO 03/087306 PCT/US03/10462 TableXXXII-VI-HLA- TableXXXII-V2-HLA- TableXXXII-V6-HLA B4402-9mers-98P4B6 B4402-9mers-98P4B6 B4402-9mers-98P4B6 Each peptide is a portion of Each peptide is a portion of Each peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 5; each start SEQ ID NO: 13; each start position is specified, the length position is specified, the position is specified, the of peptide is 9 amino acids, length of peptide is 9 amino length of peptide is 9 amino and the end position for each acids, and the end position acids, and the end position for peptide is the start position for each peptide is the start each peptide is the start plus eight, position plus eight. position plus eight. Pos 123456789 score Pos 123456789 score Pos 123456789 score 420 EEEYYRFYT 13 37 CPADFFLYF 13 6 VILGKIILF 17 424 YRFYTPPNF 13 17 FTPFSCLSL 12 5 IVILGKIIL 15 444 LDLLQLCRY 13 34 PPPCPADFF 12 7 ILGKIILFL 15 10 PKSLSETCL 12 5 GLQALSLSL 11 21 KLKRIKKGW 15 39 GDFAKSLTI 12 9 LSLSLSSGF 11 3 PSIVILGKI 14 41 FAKSLTIRL 12 10 KIILFLPCI 14 57 VIGSRNPKF 12 TabIeXXXII-V5A-HLA- 14 FLPCISRKL 14 61 RNPKFASEF 12 B4402-9mers-98P4B6 17 CISRKLKRI 13 75 DVTHHEDAL 12 Each peptide is a portion of 26 KKGWEKSQF 12 81 DALTKTNII 12 SEQ ID NO: 11; each start 29 WEKSQFLEE 12 94 HREHYTSLW 12 position is specified, the 36 EEGIGGTIP 12 125 YPESNAEYL 12 length of peptide is 9 amino 4 SIVILGKII 11 128 SNAEYLASL 12 acids, and the end position 27 KGWEKSQFL 11 173 QARQQVIEL 12 for each peptide is the start 187 FIPIDLGSL 12 position plus eight TableXXXII-V7A-HLA 214 GPVVVAISL 12 Pos 123456789 score B4402-9mers-98P4B6 217 VVAISLATF 12 1 NLPLRLFTF 16 Each peptide is a portion of 220 ISLATFFFL 12 2 LPLRLFTFW 13 SEQ ID NO: 15; each start 261 IVAITLLSL 12 position is specified, the 267 LSLVYLAGL 12 length of peptide is 9 amino 280 YQLYYGTKY 12 TableXXXII-V5B-HLA- acids, and the end position 283 YYGTKYRRF 12 B4402-9mcrs-98P4B6 for each peptide is the start 299 LQCRKQLGL 12 Each peptide is a portion of position plus eight. 300 QCRKQLGLL 12 SEQ ID NO: 11; each start Pos 123456789 score 324 PMRRSERYL 12 position is specified, the 6 SETFLPNGI 21 325 MRRSERYLF 12 length of peptide is 9 amino 9 FLPNGINGI 14 350 NEEEVR 12 acids, and the end position 1 SPKSLSETF 12 350 NEEEVV TRIE 12 for each peptide is the start 2 PKSLSETFL 12 353 EVWRIEMYI 12 position plus eig ht.2 PKSLSETFL 12 362 SFGIMSLGL 12 Pos 123456789 score TabeXXXII-VB-HLA 404, LISTFHVLI 12 2 REFSFIQIF 251 TableXXXIl-V7B-HLA 404 LISTFHVLI 12 22 LEFSFIQFLLTL 25 B4402-9mers-98P4B6 405 ISTFHVLIY 12 22 LEFVFLLTL 25 Each peptide is a portion of TableXXXII-V2-HLA- LELEFVFLL 23 SEQ ID NO: 15; each start B4402-9mers-98P4B6 18 TELELEFF 22 position is specified, the Each peptide is a portion of 5 SFIQIFCSF 16 length of peptide is 9 amino E ach eptide is a posartion of 24 FVFLLTLLL 16 acids, and the end position for positionO ec t 19 ELELEFVFL 15 each peptide is the start length of peptide is 9 amino 14 ADTQTELEL 14 position plus eight. acids, and the end position 23 EFVFLLTLL 14 Pos 123456789 score for each peptide is the start 12 SFADTQTEL 12 5 AYQQSTLGY 15 position plus eight. 9 STLGYVALL 15 Pos 123456789 score TabeXXXII-V6-HLA- 8 QSTLGYVAL 14 1 SGSPGLQAL 18 B4402-9mers-98P4B6 3 NMAYQQSTL 12 15 SGFTPFSCL 15 Each peptide is a portion of 33 CPPPCPADF 15 SEQ ID NO: 13; each start TableXXXII-V7C-HLA 3 SPGLQALSL 14 position is specified, the B4402-9mers-98P4B6 23 LSLPSSWDY 14 length of peptide is 9 amino Each peptide is a portion of 2SLSS 1 acids, and the end position for SEQ ID NO: 15; each start 12 SLSSGFTPF 13 each peptide is the start position is specified, the length 21 SCLSLPSSW 13 position plus eight. of peptide is9 amino acids, 35 PPCPADFFL 13 Pos 123456789 score and the end position for each 36 PCPADFFLY 13 35 LEEGIGGTI 21 peptide is the start position 216 WO 03/087306 PCT/US03/10462 plus eight, for each peptide is the start TabIeXXXIIII-VI-HLA Pos 123456789 score )osition plus eight. B5101-9mers-98P4B6 33 SEIVLPIEW 26 Pos 123456789 score Each peptde is a portion of 157 GEFLGSGTW 24 6 SETFLPNGI 21 SEQ ID NO: 3; each start 168 LETIILSKL 23 9 FLPNGINGI 14 position is specified, the length 39 IEWQQDRKI 20 1 SPKSLSETF 12 of peptide is 9 amino acids, and 143 ASGTLSLAF 17 2 PKSLSETFL 12 the end position for each 51 STPPPPAMW 16 peptide is the start position plus 70 QESGIRNKS 16 TableXXXII-V14-HLA- eight. 103 PESPDRALK 16 B4402-9mers-98P4B6 Pos 123456789 score 113 ANSWRNPVL 16 Each peptide is a portion of 27 DARKVTVGV _26 131 WEFLLRLLK 16 SEQ ID NO: 29; each start 65 FASEFFPHV 23 42 QQDRKIPPL 15 position is specified, the 374 LAVTSIPSV 23 5 ILDLSVEVL 14 length of peptide is 9 amino 434 LALVLPSIV 23 61 EEAGATAEA 14 acids, and the end position 438 LPSIVILDL 22 10 VEVLASPAA 13 for each peptide is the start 246 DFYKIPIEI 21 12 VLASPAAAW 13 position plus eight. 262 VAITLLSLV 21 15 SPAAAWKCL 13 Pos 123456789 score 368 LGLLSLLAV 21 20 WKCLGANIL 13 1 NLPLRLFTF 16 428 TPPNFVLAL 21 29 RGGLSE1VL 13 2 LPLRLFTFW 13 429 PPNFVLALV 21 60 TEEAGATAE 13 23 NGIKDARKV 20 67 AEAQESGIR 13 TableXXXII-V21-HLA- 157 GPKDASRQV 20 91 TEDDEAQDS 13 B4402-9mers-98P4B6 214 GPVVVAISL 20 102 PPESPDRAL 13 Each peptide is a portion of 259 LPIVAITLL 20 108 RALKAANSW 1 SEQ ID NO: 43; each start 41 FAKSLTIRL 19 125 NGVGPLWEF 13 position is specified, the length 125 YPESNAEYL 19 126 GVGPLWEFL 13 of peptide is 9 amino acids, 133 LASLFPDSL 19 127 VGPLWEFLL 13 and the end position for each 173 QARQQVIEL 19 13 VGPLWEFRLL 13 peptide is the start position 2503 IPIEIVNKT 19 130 LWEFLLRLL 13 pluseiqht. 291 FPPWLETWL 19 146 TLSLAFTSW 13 Pos 123456789 score 291 IFPPWCGYLETWVVLETL 18 160 LGSGTWMKL 13 6 EQKTKHCMF 13 50 IRCGYHVVI 18 16 LSGW KL 13~228 LYSFVR.DVI 17 165 WMKLETIIL 13 5 QEQKTKHCM 11 228 LYSFVRDVIHAN 17 31 GLSEIVLPI 12 8 KTKHCMFSL 11 336 MAYQQVHAN 17 122 PHTNGVGPL 12 9 TKHCMFSLI 10 371 LSLLAVTSI 17 123 HTNGVGPLW 12 28 ARKVTVGVI 16 129 PLWEFLLRL 12 TableXXXII-V25-HLA- 39 GDFAKSLTI 16 139 KSQAASGTL 12 B4402-9mers-98P4B6 70 FPHVVDVTH 16 141 QAASGTLSL 12 Each peptide is a portion of 104 LRHLLVGKI 16 151 FTSWSLGEF 12 SEQ ID NO: 51; each start 141 LIVKGFNVV 16 179 EQKSKHCMF 12 position is specified, the 160 DASRQVYIC 16 length of peptide is 9 amino 204 LPLRLFTLW 16 TabIeXXXII-V8-HLA- acids, and the end position 227 FLYSFVRDV 16 B4402-9mers-98P4B6 for each peptide is the start 237 HIPYARNQQS 16 Each peptide is a portion of position plus eight. 317 VAYSLCLPM 16 SEQ ID NO: 17; each start Pos 123456789 score 52 CGYHVVIGS 15 position is specified, the 3 FLPCISQKL 13 137 FPDSLIVKG 15 length of peptide is 9 amino 6 CISQKLKRI 12 164 QVYICSNNI 15 acids, and the end position 2 LFLPCISQK 8 171 NIQARQQVI 15 for each peptide is the start 9 QKLKRIKKG 8 193 GSLSSAREI 15 position plus eight 210 TLWRGPVVV 15 Pos 123456789 score TableXXXIIII-V1-HLA. 212 WRGPVVVAI 15 5 LEEGMGGTI 20 B5101-9mers-98P4B6 276 LAAAYQLYY 15 6 EEGMGGTIP 12 Each peptide is a portion of 349 WNEEEVWRI 15 SEQ ID NO: 3; each start 363 FGIMSLGLL 15 TableXXXII-V13-HLA- position is specified, the length 397 TLGYVALLI 15 B4402-9mers-98P4B6 of peptide is 9 amino acids, and 425 RFYTPPNFV 15 Each peptide is a portion of the end position for each 18 LPNGINGIK 14 SEQ ID NO: 27; each start peptide is the start position plus 25 IKDARKVTV 14 position is specified, the eight. 114 IDVSNNMRI 14 length of peptide is 9 amino Pos 123456789 score 152 WALQLGPKD 14 acids, and the end position 81 DALTKTNII 29 209 FTLWRGPVV 14 217 WO 03/087306 PCT/USO3/10462 TableXXXIIII-V1-HLA- TableXXXIIII-V5A-HLA- TabIeXXXIIII-V7A B5101-9mers-98P4B6 B5101-9mers-98P4B6 HLA-B5101-9mers Each peptide is a portion of Each peptide is a portion of 98P4B6 SEQ ID NO: 3; each start SEQ ID NO: 11; each start Each peptide is a portion of position is specified, the length position is specified, the length SEQ ID NO: 15; each start of peptide is 9 amino acids, and of peptide is 9 amino acids, position is specified, the the end position for each and the end position for each length of peptide is 9 amino peptide is the start position plus peptide is the start position acids, and the end position eight. plus eight. for each peptide is the start Pos 123456789 score Pos 123456789 score position plus eight. 222 LATFFFLYS 14 4 LRLFTFWRG 7 Pos 123456789 score 242 NQQSDFYKI 14 9 FLPNGINGI 14 258 TLPIVAITL 14 TableXXXIIII-V5B- 1 SPKSLSETF 12 278 AAYQLYYGT 14 HLA-B5101-9mers- 6 SETFLPNGI 12 379 IPSVSNALN 14 98P4B6 2 PKSLSETFL 386 LNWREFSFI 14 Each peptide is a portion of 398 LGYVALLIS 14 SEQ ID NO: 11; each start TableXXXIII-V7B-HLA 401 VALLISTFH 14 position is specified, the B510 1-9mers-98P4B6 404 LISTFHVLI 14 length of peptide is 9 amino Each peptide is a portion of 433 VLALVLPSI 14 acids, and the end position SEQ ID NO: 15; each start 435 ALVLPSIVI 14 for each peptide is the start position is specified, the position plus eight. length of peptide is 9 amino TableXXXIIII-V2-HLA- Pos 123456789 score acids, and the end position for B5101-9mers-98P4B6 20 LELEFVFLL 14 each peptide is the start Each peptide is a portion of 1 WREFSFIQI 13 position plus eight. SEQ ID NO: 5; each start 22 LEFVFLLTL 13 Pos 123456789 score position is specified, the 13 FADTQTELE 12 4 MAYQQSTLG 16 length of peptide is 9 amino 12 SFADTQTEL 9 6 YQQSTLGYV 12 acids, and the end position 17 QTELELEFV 9 9 STLGYVALL 12 for each peptide is the start 24 FVFLLTLLL 9 3 NMAYQQSTL 9 position plus eight. 14 ADTQTELEL 8 8 QSTLGYVAL 7 Pos 123456789 score 18 TELELEFVF 8 3 SPGLQALSL 18 19 ELELEFVFL 8 TableXXXII-V7C-HLA 35 PPCPADFFL 16 23 EFVFLLTLL 8 B5101-9mers-98P4B6 15 SGFTPFSCL 15 15 DTQTELELE 6 Each peptide is a portion of 1 SGSPGLQAL 13 SEQ ID NO: 15; each start 7 QALSLSLSS 13 TableXXXII-V6-HLA- position is specified, the length 18 TPFSCLSLP 13 B5101-9mers-98P4B6 of peptide is 9 amino acids, 25 LPSSWDYRC 13 Each peptide is a portion of and the end position for each 37 CPADFFLYF 13 SEQ ID NO: 13; each start peptide is the start position 33 CPPPCPADF 12 position is specified, the plus eight. 34 PPPCPADFF 12 length of peptide is 9 amino Pos 123456789 score 17 FTPFSCLSL 10 acids, and the end position for 66 TAEAQESGI 22 4 PGLQALSLS 9 each peptide is the start 101 DPPESPDRA 20 5 GLQALSLSL 8 position plus eight. 112 AANSWRNPV 19 Pos 123456789 score 15 SPAAAWKCL 18 TableXXXIIII-VSA-HLA- 43 IPHVSPERV 23 160 LGSGTWMKL 18 B5101-9mers-98P4B6 2 LPSIMLGK 16 29 RGGLSEIVL 17 Each peptide is a portion of 27 KGWEKSQFL 16 84 IPVVGVVTE 17 SEQ ID NO: 11; each start 35 LEEGIGGTI 15 102 PPESPDRAL 17 position is specified, the length 15 LPCISRKLK 14 141 QAASGTLSL 17 of peptide is 9 amino acids, 17 CISRKLKRI 14 24 GANILRGGL 16 and the end position for each 3 PSIVILGKI 13 39 IEWQQDRKI 16 peptide is the start position 39 IGGTIPHVS 13 31 GLSEIVLPI 15 plus eight. 38 GIGGTIPHV 12 68 EAQESGIRN 15 Pos 123456789 score 4 SIVILGKII 11 82 SQIPVVGVV 15 2 LPLRLFTFW 16 7 ILGKIILFL 11 108 RALKAANSW 15 8 TFWRGPVVV 15 10 KIILFLPCI 11 149 LAFTSWSLG 15 7 FTFWRGPVVW 13 14 FLPCISRKL 11 163 GTWMKLETI 15 6 LFTFWRGPV 10 45 HVSPERVTV 11 5 ILDLSVEVL 14 9 FWRGPVVVA 8 27 ILRGGLSEI 14 218 WO 03/087306 PCT/USO3/10462 TableXXXIIII-V7C-HLA- 8 GMGGTIPHV 12 6 CISQKLKRI 14 B5101-9mers-98P4B6 9 MGGTIPHVS 12 3 FLPCISQKL 10 Each peptide is a portion of 7 EGMGGTIPH 8 9 QKLKRIKKG 7 SEQ ID NO: 15; each start position is specified, the length TableXXXIIII-V13- TabIeXXIV-V1-HLA-A1 of peptide is 9 amino acids, IILA-B5101-9mers- 10mers-98P4B6 and the end position for each 98P4B6 Each peptide is a portion of SEQ peptide is the start position Each peptide is a portion of ID NO: 3; each start position is plus eight. SEQ ID NO: 27; each start specified, the length of peptide Pos 123456789 score position is specified, the is 10 amino acids, and the end 37 LPIEWQQDR 14 length of peptide is 9 amino position for each peptide is the 47 IPPLSTPPP 14 acids, and the end position start position plus nine. 48 PPLSTPPPP 14 for each peptide is the start Pos 1234567890 score 54 PPPAMWTEE 14 position plus eight. 351 EEEVWRIEMY 26 121 LPHTNGVGP 14 Pos 123456789 score 391 FSFIQSTLGY 26 127 VGPLWEFLL 14 9 FLPNGINGI 14 418 AFEEEYYRFY 26 128 GPLWEFLLR 14 1 SPKSLSETF 12 443 ILDLLQLCRY 26 4 VILDLSVEV 13 6 SETFLPNGI 12 220 ISLATFFFLY 24 13 LASPAAAWK 13 2 PKSLSETFL 8 262 VAITLLSLVY 23 18 AAWKCLGAN 13 327 RSERYLFLNM 23 52 TPPPPAMWT 13 TableXXXIIII-V14-HLA- 45 LTIRLIRCGY 22 53 PPPPAMWTE 13 B5101-9mers-98P4B6 275 LLAAAYQLYY 22 62 EAGATAEAQ 13 Each peptide is a portion of 404 LISTFHVLIY 22 95 EAQDSIDPP 13 SEQ ID NO: 29; each start 116 VSNNM R QY 20 142 AASGTLSLA 13 position is specified, the length 123 NQYPESNAEY 20 164 TWMKLETII 13 of peptide is 9 amino acids, 271 YLAGLLAAAY 19 17 AAAWKCLGA 12 and the end position for each 279 AYQLYYGTKY 19 64 GATAEAQES 12 peptide is the start position 427 YTPPNFVLAL 19 76 NKSSSSSQI 12 plus eight. 38 SGDFAKSLTI 18 79 SSSSQIPVV 12 Pos 123456789 score 274 GLLAAAYQLY 18 92 EDDEAQDSI 12 2 LPLRLFTFW 16 101 LWDLRHLLVG 17 105 SPDRALKAA 12 8 TFWRGPVVV 15 157 GPKDASRQVY 17 111 KAANSWRNP 12 7 FTFWRGPVV 13 178 VIELARQLNF 17 118 NPVLPHTNG 12 6 LFTFWRGPV 10 230 SFVRDVIHPY 17 129 PLWEFLLRL 12 9FWRGPVVVA 8 239 YARNQQDVFHPY 17 42239 YARNQSDFY 17 182 SKHCMFSLI 12 396 STLGYVALLI 17 16 PAAAWKCLG 11 66 ASEFFPHVVD 16 28 LRGGLSEIV 11 TableXXXIIII-V21-HLA- 89 IFVAIHREHY 16 56 PAMWTEEAG 11 B5101-9mers-98P4B6 94 FHREHYTSLWD 16 81 SSQIPWEGV 11 Each peptide is a portion of 9 EY SL 16 81 SSQIPVVGV 11 SEQ ID NO: 43; each start 129 NAEYLASLFP 16 119 PVLPHTNGV 11 position is specified, the 310 FFFAMVHVAY 16 168 LETIILSKL 11 length of peptide is 9 amino 322 CLPMRRSERY 16 19 AWKCLGANI 10 acids, and the end position 329 ERYLFLNMAY 16 23 LGANILRGG 10 for each peptide is the start 350 NEEEVWRIEM 15 30 GGLSEIVLP 10 position plus eight. 41 GWKRAFEEEY 15 55 PPAMWTEEA 10 Pos 123456789 score 415 WKRGAFEEEYY 15 78 SSSSSQIPV 10 9 TKHCMFSLI 13 13 LSETCLPNGI 14 113 ANSWRNPVL 10 3 LTQEQKTKH 7 125 YPESNAEYLA 14 130 LWEFLLRLL 10 KKHCMFSL 6 244 QSDFYKIPIE 14 257 KTLPIVAITL 14 TableXXXIIII-V8-HLA- TableXXXIIH-V25-HLA- 76 VTHHEDALTK 13 B5101-9mers-98P4B6 B5101-9mers-98P4B6. 198 AREIENLPLR 13 Each peptide is a portion of Each peptide is a portion of 366 MSLGLLSLLA 13 SEQ ID NO: 17; each start SEQ ID NO: 51; each start 420 EEEYYRFYTP 13 position is specified, the position is specified, the 25 IKDARKVTVG 12 length of peptide is 9 amino length of peptide is 9 amino 135 SLFPDSLIVK 12 acids, and the end position acids, and the end position 137 FPDSLIVKGF 12 for each peptide is the start for each peptide is the start 200 EIENLPLRLF 12 position plus eight. osition plus eight. 221 SLATFFFLYS 12 Pos 123456789 score Pos 123456789 score 251 PIEIVNKTLP 12 5 LEEGMGGTI 16 4 LPCISQKLK 14 268 SLVYLAGLLA 12 219 WO 03/087306 PCT/US03/10462 TableXXXIV-V1-HLA-Al1- TabIeXXXIV-V7C-HLA 10mers-98P4B6 TabIeXXXIV-V6-HLA-A1- Al-10mers-98P4B6 Each peptide is a portion of SEQ 10mers-98P4B6 Each peptide is a portion of SEQ ID NO: 3; each start position is Each peptide is a portion of ID NO: 15; each start position is specified, the length of peptide SEQ ID NO: 13; each start specified, the length of peptide is 10 amino acids, and the end position is specified, the length is 10 amino acids, and the end position for each peptide is the of peptide is 10 amino acids, position for each peptide is the start position plus nine. and the end position for each start position plus nin e. Pos 1234567890 score peptide is the start position plus Pos 1234567890 score 419 FEEEYYRFYT 12 nine. 6 ILDLSVEVLA 13 439 PSIVILDLLQ 12 Pos 1234567890 score 103 PPESPDRALK 13 29 GWEKSQFLEE 19 124 HTNGVGPLWE 13 TableXXXIV-V2-HLA-A1- 35 FLEEGIGGTI 13 168 KLETIILSKL 13 10mers-98P4B6 36 LEEGIGGTIP 12 10 SVEVLASPAA 12 Each peptide is a portion of 1 LVLPS1VILG 11 39 PIEWQQDRKI 12 SEQ ID NO: 5; each start 19 ISRKLKRIKK 11 43 QQDRKIPPLS 12 position is specified, the length 42 GITIPHVSPER 10 52 STPPPPAMWT 12 of peptide is 10 amino adcids, 9 LGKIILFLPC 9 104 PESPDRALKA 12 and the end position for each 106 SPDRALKAAN 12 peptide is the start position TableXXXIV-V7A-HLA- 128 VGPLWEFLLR 12 plus nine. Al-10mers-98P4B6 170 ETIILSKLTQ 12 Pos 1234567890 score Each peptide is a portion of 97 AQDSIDPPES 1I 35 PPCPADFFLY 24 SEQ ID NO: 15; each start 115 NSWRNPVLPH 11 22 CLSLPSSWDY 16 position is specified, the 154 SWSLGEFLGS 11 28 SWDYRCPPPC 12 length of peptide is 10 amino 2 PSIVILDLSV 10 2 GSPGLQALSL 11 acids, and the end position for 61 TEEAGATAEA 10 ____ ___ ~ each peptide is the start 6 T S 10 TableXXXIV-V5A-HLA- position plus nine. 67 TAEAQESGIR 10 Al-10mers-98P4B6 Pos 1234567890 score 92 TEDDEAQDSI 10 Each peptide is a portion of 6 LSETFLPNGI 14 9357 LGEFLGSGTWD 10 SEQ ID NO: 11; each start 4 KSLSETFLPN 13 15762 GSEFLGSGTW 10 position is specified, the length 8 ETFLPNGING 11 162 GSGTW KLET 10 of peptide is 10 amino acids, 178 TQEQKSKHCM 10 and the end position for each TableXXXIV-V7B-HLA- 51 LSTPPPPAMW 9 peptide is the start position plus Al-10mers-98P4B6 146 GTLSLAFTSW 9 nine. Each peptide is a portion of 182 KSKHCMFSLI 9 Pos 1234567890 score SEQ ID NO: 15; each start 8 FTFWRGPVVV 8 position is specified, the length TableXXXIV-V8-HLA 1 ENLPLRLFTF 4 of peptide is 10 amino acids, Al-10mers-98P4B6 2 NLPLRLFTFW 4 and the end position for each Each peptide is a portion of 4 PLRLFTFWRG 4 peptide is the start position plus SEQ ID NO: 17; each start 10 FWRGPVVVAI 3 nine. position is specified, the length Pos 1234567890 score of peptide is 10 amino acids, TableXXXIV-V5B-HLA- 5 MAYQQSTLGY 21 and the end position for each Al-10mers-98P4B6 10 STLGYVALLI 17 peptide is the start position Each peptide is a portion of plus nine. SEQ ID NO: 11; each start TableXXXIV-V7C-HLA- Pos 1234567890 score position is specified, the length Al-10mers-98P4B6 5 FLEEGMGGTI 13 of peptide is 10 amino acids, Each peptide is a portion of SEQ 6 LEEGMGGTIP 12 and the end position for each ID NO: 15; each start position is peptide is the start position specified, the length of peptide TableXXXIV-V13-HLA plus nine. is 10 amino acids, and the end Al-10mers-98P4B6 Pos 1234567890 score position for each peptide is the Each peptide is a portion of -14 FADTQTELEL 17 start position plus nine. SEQ ID NO: 27; each start 18 QTELELEFVF 17 Pos 1234567890 score position is specified, the 22 ELEFVFLLTL 17 131 LWEFLLRLLK 19 length of peptide is 10 amino 20 ELELEFVFLL 14 33 LSEIVLPIEW 18 acids, and the end position for 16 DTQTELELEF 12 91 VTEDDEAQDS 17 each peptide is the start 21 LELEFVFLLT 11 60 WTEEAGATAE 16 position plus nine. 2 W E FHQIF 10 100 SIDPPESPDR 16 Ps13579 cr 2APos 1234567890 score 2 FSFQ 1 1 SDPPESPDR 16 LSETFLPNGI 14 5 FSFIQIFCSF 8 70 AQESGIRNKS 14 4 KLSETFLPNI 13 24_ EFFLT___SGg S 1 4 KSLSETFLPN 1 24 EFVFLLTLLL 8 94 DDEAQDSIDP 14 220 WO 03/087306 PCT/US03/10462 8 ETFLPNGING 11 TableXXXV-V1 -HLA- TableXXXV-V1-HLA A0201-10mers-98P4B6 A0201-10mers-98P4B6 TableXXXIV-V14-HLA- Each peptide is a portion of SEQ Each peptide is a portion of SEQ Al-10mers-98P4B6 ID NO; 3; each start position is ID NO: 3; each start position is Each peptide is a portion of specified, the length of peptide is specified, the length of peptide is SEQ ID NO: 29; each start 10 amino acids, and the end 10 amino acids, and the end position is specified, the length position for each peptide is the position for each peptide is the of peptide is 10 amino acids, start position plus nine. start position plus nine. and the end position for each Pos 1234567890 score Pos 1234567890 score peptide is the start position plus 364 GLMSLGLLSL 27 179 1ELARQLNFI 17 nine. 132 YLASLFPDSL 26 202 ENLPLRLFTL 17 Pos 1234567890 score 370 LLSLLAVTSI 26 250 IPIEIVNKTL 17 8 FTFWRGPVVV 8 437 VLPSIVILDL 26 264 ITLLSLVYLA 17 1 ENLPLRLFTF 4 82 ALTKTNIIFV 25 269 LVYLAGLLAA 17 2 NLPLRLFTFW 4 100 SLWDLRHLLV 25 348 SWNEEEVWRI 17 4 PLRLFTFWRG 4 140 SLIVKGFNVV 25 361 ISFGIMSLGL 17 10 FWRGPVVVAI 3 263 AITLLSLVYL 25 369 GLLSLLAVTS 17 306 GLLSFFFAMV 25 401 VALLISTFHV 17 TableXXXIV-V21-HLA-Al- 402 ALLISTFHVL 25 26 KDARKVTVGV 16 10mers-98P4B6 440 SIVILDLLQL 25 41 FAKSLTIRLI 16 Each peptide is a portion of 258 TLPIVAITLL 24 111 KILIDVSNNM 16 SEQ ID NO: 43; each start 365 IMSLGLLSLL 24 112 ILIDVSNNMR 16 position is specified, the length 403 LLISTFHVLI 24 127 ESNAEYLASL 16 of peptide is 10 amino acids, 427 YTPPNFVLAL 24 195 LSSAREIENL 16 and the end position for each 24 GIKDARKVTV 23 223 ATFFFLYSFV 16 peptide is the start position plus 48 RLIRCGYHVV 23 226 FFLYSFVRDV 16 nine. -- _ S1234567890 103 DLRHILLVGKI 23 268 SLVYLAGLLA 16 Pos 1234567890 score 433 VLALVLPSIV 23 299 LQCRKQLGLL 16 9 KTKHCMfSLI 11 QGL 1 5 TQEQKTKHCM i10 92 AIHREHYTSL 22 356 RIEMYISFGI 16 1 LSKLTQEQKT 6 260 PIVAITLLSL 22 362 SFGIMSLGLL 16 4 LTEKTKHC 6 261 IVAITLLSLV 22 377 TSIPSVSNAL 16 0 LTQEQKFKHC 6 298 WLQCRKQLGL 22 428 TPPNFVLALV 16 101 TKHCMFSLIS 6' 432 FVLALVLPSI 22 434 LALVLPSIVI 16 TableXXXIV-V25-HLA- 207 RLFTLWRGPV 21 438 LPSIVILDLL 16 Al-10meXXIV-V25-HLA- 210 TLWRGPVVVA 21 443 ILDLLQLCRY 16 A1l0mers-98P4B6___ Each peptide is a portion of 257 KTLPIVAITL 21 27 DARKVTVGVI 15 SEQ ID NO: 51; each start 385 ALNWREFSFI 21 36 IGSGDFAKSL 15 SEQ ID NO: 51; each start position is specified, the 49 LIRCGYHVVI 20 44 SLTIRLIRCG 15 length of peptide is 10 amino 98 YTSLWDLRHL 20 47 IRLIRCGYHV 15 acids, and the end position for 172 IQARQQVIEL 20 147 NVVSAWALQL 15 each peptide is the start 186 NFIPIDLGSL 20 166 YICSNIAQAR 15 position plus nine. 219 AISLATFFFL 20 189 PIDLGSLSSA 15 Pos 1234567890 score 227 FLYSFVRDVI 20 199 REIENLPLRL 15 8 ISQKLKluIKK 11 249 KIPIEIVNKT 20 221 SLATFFFLYS 15 5 LPCISQ KLKR 8 253 EIVNKTLPIV 20 255 VNKTLPIVAI 15 3 LFLPCISQKL 6 12 SLSETCLPNG 19 273 AGLLAAAYQL 15 135 SLFPDSLIVK 19 275 LLAAAYQLYY 15 TableXXXV-V1-HLA- 142 1VKGFNVVSA 19 314 MVHVAYSLCL 15 A0201-10mers-98P4B6 197 SAREIENLPL 19 335 NMAYQQVHAN 15 Each peptide is a portion of SEQ 209 FTLWRGPVVV 19 336 MAYQQVHANI 15 ID NO: 3; each start position is 211 LWRGPVVVAI 19 345 IENSWNEEEV 15 specified, the length of peptide is 271 YLAGLLAAAY 19 394 IQSTLGYVAL 15 10 amino acids, and the end 312 FAMVHVAYSL 19 395 QSTLGYVALL 15 position for each peptide is the 396 STLGYYALLI 19 404 LISTFHVLIY 15 start position plus nine. 16 TCLPNGINGI 18 411 LIYGWKRAFE 15 Pos 1234567890 score 65 FASEFFPHVV 18 373 LLAVTSIPSV 31 67 SEFFPHVVDV 18 TableXXXV-V2-HLA 266 LLSLVYLAGL 29 113 LIDVSNNMRI 18 A0201-10mers-98P4B6 107 LLVGKILIDV 28 359 MYISFGIMSL 18 Each peptide is a portion of 367 SLGLLSLLAV 28 392 SFIQSTLGYV 18 SEQ ID NO: 5; each start 435 ALVLPSIVIL 28 106 HLLVGKILID 17 position is specified, the length 221 WO 03/087306 PCT/US03/10462 of peptide is 10 amino adcids, A0201 -1 O10mers-98P4B6 Each peptide is a portion of SEQ and the end position for each Each peptide is a portion of ID NO: 15; each start position is peptide is the start position SEQ ID NO: 13; each start specified, the length of peptide is plus nine. position is specified, the length 10 amino acids, and the end Pos 1234567890 score of peptide is 10 amino acids, position for each peptide is the 2 GSPGLQALSL 16 and the end position for each start position plus nine. 5 GLQALSLSLS 15 peptide is the start position plus Pos 1234567890 score 16 GFTPFSCLSL 15 nine. 5 VILDLSVEVL 26 10 SLSLSSGFTP 14 Pos 1234567890 score 168 KLETIILSKL 26 8 ALSLSLSSGF 13 7 VILGKIILFL 28 27 NILRGGLSEF 24 12 SLSSGFTPFS 13 35 FLEEGIGGTI 22 28 ILRGGLSEIV 24 24 SLPSSWDYRC 13 5 SIVILGKIIL 20 130 PLWEFLLRLL 24 4 PGLQALSLSL 12 14 LFLPCISRKL 18 160 FLGSGTWMKL 23 7 QALSLSLSSG 12 43 TIPHVSPERV 18 4 IVLDLSVEV 22 14 SSGFTPFSCL 11 2 VLPSIVILGK 17 66 ATAEAQESGI 19 22 1CLSLPSSWDY 10 13 ILFLPCISRK 17 81 SSSQIPVVGV 19 9 LSLSLSSGFT 8 3 LPSIVILGKI 16 156 SLGEFLGSGT 19 17 FTPFSCLSLP 8 8 ILGKIILFLP 16 6 ILDLSVEVLA 18 6 LQALSLSLSS 7 10 GKIILFLPCI 16 32 GLSEIVLPIE 18 34 PPPCPADFFL 7 38 EGIGGTIPHV 16 112 KAANSWRNPV 18 1 LVLPSIVILG 14 113 AANSWRNPVL 18 TableXXXV-V5A-HLA- 46 HVSPERVTVM 14 129 GPLWEFLLRL 18 A0201-10mers-98P4B6 12 IILFLPCISR 13 8 DLSVEVLASP 17 Each peptide is a portion of 34 QFLEEGIGGT 13 19 AAWKCLGANI 17 SEQ ID NO: 11; each start 79 SSSSSQIPVV 17 position is specified, the length TableXXXV-V7A-HLA- 127 GVGPLWEFLL 17 of peptide is 10 amino acids, A0201-10mers-98P4B6 134 FLLRLLKSQA 17 and the end position for each Each peptide is a portion of 135 LLRLLKSQAA 17 peptide is the start position plus SEQ ID NO: 15; each start 141 SQAASGTLSL 17 nine. position is specified, the 31 GGLSEIVLPI 16 Pos 1234567890 score length of peptide is 10 amino 42 WQQDRKIPPL 16 6 RLFTFWRGPV 21 acids, and the end position for 58 AVMWTEEAGAT 16 8 FTFWRGPVVV 18 each peptide is the start 82 SSQPVVGVV 16 10 FWRGPVVVAI 18 position plus nine. 84 QIPVVGVVTE 16 7 LFTFWRGPVV 11 Pos 1234567890 score 122 LPHTNGVGPL 16 9 TFWRGPVVVA 11 5 SLSETFLPNG 19 137 RLLKSQAASG 16 137 RLLKSQAASG 16 2 NLPLRLFTFW 10 9 TFLPNGINGI 18 138 LLKSQAASGT 16 _2 SPKSLSETFL 11 148 LSLAFTSWSL 16 TableXXXV-V5B-HLA- 6 LSETFLPNGI 11 13 VLASPAAAWK 15 A0201-10mers-98P4B6 10 FLPNGINGIK 1123 CLGANLRGG 15 Each peptide is a portion of 24 LGANLRGG 15 SEQ ID NO: 11; each start TabIeXXXV-V7B-HLA- 24 LGANILRGGL 15 position is specified, the length A0201-10mers-98P4B6 152 FTSWSLGEFL 15 of peptide is 10 amino acids, Each peptide is a portion of 163 SGTWMKLETI 15 and the end position for each SEQ ID NO: 15; each start 3 SIVILDLSVE 14 peptide is the start position position is specified, the length 29 LRGGLSEIVL 14 plus nine. of peptide is 10 amino acids, 39 PIEWQQDRKI 14 Pos 1234567890 score and the end position for each 121 VLPHTNGVGP 14 22 ELEFVFLLTL 22 peptide is the start position plus 139 LKSQAASGTL 14 20 ELELEFVFLL 2( nine. 142 QAASGTLSLA 14 14 FADTQTELEL 18 Pos 1234567890 score 164 GTWMKLETII 14 23 LEFVFLLTLL 17 10 STLGYVALLI 19 171 TIILSKLTQE 14 19 TELELEFVFL 16 2 FLNMAYQQST 18 172 IILSKLTQEQ 14 17 TQTELELEFV 15 6 AYQQSTLGYV 16 18 AAAWKCLGAN 13 12 CSFADTQTEL 13 3 LNMAYQQSTL 15 50 PLSTPPPPAM 13 9 QIFCSFADTQ 119 QSTLGYVALL 15 100 SIDPPESPDR 13 21 LELEFVFLLT 11 8 QQSTLGYVAL 13 149 SLAFTSWSLG 13 I NWREFSFIQI 10 4 NMAYQQSTLG 9 2 PSIVILDLSV 12 7 FIQIFCSFAD 10 20 AWKCLGANIL 12 TableXXXV-V7C-HLA- 47 KIPPLSTPPP 12 TableXXXV-V6-HLA- A0201-10mers-98P4B6 52 STPPPPAMWT 12 222 WO 03/087306 PCT/US03/10462 TableXXXV-V7C-HLA- 7 LFTFWRGPW I 1 TableXXXVI-V2-HLA A020 1-10mers-98P4B6 9 TFWRGPVVVA 11 A0203-10mers-98P4B6 Each peptide is a portion of SEQ 2 NLPLRLFTFW 1 Each peptide is a portion of ID NO: 15; each start position is SEQ ID NO: 5; each start specified, the length of peptide is TabIeXXXV-V2 1-HLA- position is specified, the length 10 amino acids, and the end A0201-10mers-98P4B6 of peptide is 10 amino acids, position for each peptide is the Each peptide is a portion of and the end position for each start position plus nine. SEQ ID NO: 43; each start peptide is the start position Pos 1234567890 score position is specified, the length plus nine. 83 SQIPVYGVVT 12 of peptide is 10 amino acids, Pos 1234567890 score 102 DPPESPDRAL 12 and the end position for each 30 DYRCPPPCPA 10 119 NPVLPHTNGV 12 peptide is the start position plus 31 YRCPPPCPAD 9 126 NGVGPLWEFL 12 nine. 1 SGSPGLQALS 8 144 ASGTLSLAFT 12 Pos 1234567890 score 32 RCPPPCPADF 8 173 ILSKLTQEQK 12 3 KLTQEQKTKH 12 176 KLTQEQKSKH 12 9 KTKHCMFSLI 12 TableXXXVI-V5A-HLA 181 QKSKHCMFSL 12 8 QKTKHCMFSL 11 A0203-10mers-98P4B6 1 LSKLTQEQKT 7 Each peptide is a portion of 4 LTQEQKTKHC 7 SEQ ID NO: 11; each start TableXXXV-V8-HLA- 2 SKLTQEQKTK 5 position is specified, the length A0201-10mers-98P4B6 of peptide is 10 amino acids, Each peptide is a portion of TableXXXV-V25-HLA- and the end position for each SEQ ID NO: 17; each start A0201-10mers-98P4B6 peptide is the start position plus position is specified, the length Each peptide is a portion of nine. of peptide is 10 amino acids, SEQ ID NO: 51; each start Pos 1234567890 score and the end position for each position is specified, the 9 TFWRGPVVVA 10 peptide is the start position length of peptide is 10 amino 10 FWRGPVVVAI 9 S plus nine acids, and the end position Pos 1234567890 score for each peptide is the start TableXXXVI-V5B-HLA 5 FLEEGMGGTI 22 position plus nine. A0203-10mers-98P4B6 8 EGMGGTIIPHV 15 Pos 1234567890 score Each peptide is a portion of 9 GMGGTIPHVS 12 3 LFLPCISQKL 18 SEQ ID NO: 11; each start 2 ILFLPCISQK 17 position is specified, the TabIeXXXV-V13-HLA- 1 IILFLPCISQ 13 length of peptide is 10 amino A0201-10mers-98P4B6 4 FLPCISQKLK 10 acids, and the end position Each peptide is a portion of 6 PCISQKLKRI 10 for each peptide is the start SEQ ID NO: 27; each start 7 CISQKLKRIK 8 position plus nine. position is specified, the Pos 1234567890 score length of peptide is 10 amino TableXXXVI-V1-HLA- 6 SEIQIFCSFA 10 acids, and the end position for A0203-10mers-98P4B6 7 FIQIFCSFAD 9 each peptide is the start Each peptide is a portion of SEQ 8 IQIFCSFADT 8 . position plus nine. ID NO: 3; each start position is Pos 123,4567890 score specified, the length of peptide is TabIeXXXVI-V6-HLA 5 SLSETFLPNG 19 10 amino acids, and the end A0203-10mers-98P4B6 9 TFLPNGINGI 18 position for each peptide is the Pos 1234567890 score 2 SPKSLSETFL 11 start position plus nine. NoResultsFound. 6 LSETFLPNGI 11 Pos 1234567890 score 10 FLPNGINGIK 11 270 VYLAGLLAAA 27 TabIeXXXVI-V7A 269 LVYLAGLLAA 19 HLA-A0203-10mers TabIeXXXV-V14-HLA- 144 KGFNVVSAWA 18 98P4B6 A0201-10mers-98P4B6 271 YLAGLLAAAY 17 Pos 1234567890 score Each peptide is a portion of NoResultsFound. SEQ ID NO: 29; each start TabIeXXXV[-V2-HLA position is specified, the length A0203-10mers-98P4B6 of peptide is 10 amino acids, Each peptide is a portion of TableXXXVI-V7B-HLA and the end position for each SEQ ID NO: 5; each start A0203-10mers-98P4B6 peptide is the start position plus position is specified, the length Each peptide is a portion of nine. of peptide is 10 amino acids, SEQ ID NO: 15; each start Pos 1234567890 score and the end position for each position is specified, the length 6 RLFTFWRGPV 21 peptide is the start position of peptide is 10 amino acids, 8 FTFWRGPVVV 18 plus nine. and the end position for each 10 FWRGPVVVAI 18 Posl 1234567890 Iscore peptide is the start position plus 223 WO 03/087306 PCT/US03/10462 nine. 10 amino acids, and the end TableXXXVII-Vl-HLA-A3 Pos 1234567890 score position for each peptide is the 10mers-98P4B6 7 YQQSTLGYVA 10 start position plus nine. Each peptide is a portion of SEQ 8 QQSTLGYVAL 9 Pos 1234567890 score ID NO: 3; each start position is 9 QSTLGYVALL 8 135 SLFPDSLIVK 28 specified, the length of peptide is 34 GVIGSGDFAK 26 10 amino acids, and the end TableXXXVI-V7C-HLA- 271 YLAGLLAAAY 26 position for each peptide is the A0203-10mers-98P4B6 48 RLIRCGYHVV 24 start position plus nin e. Each peptide is a portion of SEQ 21 GINGIKDARK 23 Pos 1234567890 score ID NO: 15; each start position is 216 VVVAISLATF 23 262 VAITLLSLVY 16 specified, the length of peptide is 369 GLLSLLAVTS 23 263 AITLLSLVYL 16 10 amino acids, and the end 17 CLPNGINGIK 22 265 TLLSLVYLAG 16 position for each peptide is the 55 HVVIGSRNPK 22 306 GLLSFFFAMV 16 start position plus nine. 275 LLAAAYQLYY 22 322 CLPMRRSERY 16 Pos 1234567890 score 278 AAYQLYYGTK 22 340 QVHANIENSW 16 11 VEVLASPAAA 27 307 LLSFFFAMVH 22 367 SLGLLSLLAV 16 10 SVEVLASPAA 19 112 ILIDVSNNMR 21 385 ALNWREFSFI 16 105 ESPDRALKAA 19 142 IVKGFNVVSA 21 432 FVLALVLPSI 16 135 LLRLLKSQAA 19 155 QLGPKDASRQ 21 433 VLALVLPSIV 16 57 PAMWTEEAGA 18 210 TLWRGPVVVA 21 440 SIVILDLLQL 16 59 MWTEEAGATA 18 76 VTI-IHHEDALTK 20 441 IVILDLLQLC 16 61 TEEAGATAEA 18 217 VVAISLATFF 20 32 TVGVIGSGDF 15 12 EVLASPAAAW 17 248 YKIPIEIVNK 20 100 SLWDLRHLLV 15 106 SPDRALKAAN 17 274 GLLAAAYQLY 20 106 HLLVGKILID 15 136 LRLLKSQAAS 17 281 QLYYGTKYRR 20 121 RIjNQYPEESNA 15 294 WLETWLQCRK 20 153 ALQLGPKDAS 15 TableXXXVI-V8-HLA- 402 ALLISTFHVL 20 187 FIPIDLGSLS 15 A0203-10mers-98P4B6 2 ESISMMQSPK 19 221 SLATFFFLYS 15 Pos 1234567890 score 49 LIRCGYHVVI 19 235 VIHPYARNQQ 15 NoResultsFound. 56 VVIGSRNPKF 19 257 KTLPIVAITL 15 TableXXXVI-V13- 102 WDLRHLLVGK 19 260 PIVAITLLSL 15 HLA-A0203-10mers- 147 NVVSAWALQL 19 320 SLCLPMRRSE 15 98P4BHLA-A6203mers- 227 FLYSFVRDVI 19 372 SLLAVTSIPS 15 Ps 123456780 scre 269 LVYLAGLLAA 19 393 FIQSTLGYVA 15 NoResultsFound. 375 AVTSIPSVSN 19 436 LVLPSIVILD 15 443 ILDLLQLCRY 19 60 SRNPKFASEF 14 TableXXXVI-V14-HLA- 24 GIKDARKVTV 18 8 8 IIFVAIHREH 14 A0203-10mers-98P4B6 140 SLIVKGFNVV 18 103 DLRHLLVGKI 14 333 FLNMAYQQVH 18 108 LVGKILIDVS 14 Pos 1234567890 score 410 VLIYGWKRAF 18 111 KILIDVSNNM 14 9 TFWRGPVVVA 10 411 LIYGWKRAFE 18 132 YLASLFPDSL 14 10 FWRGPVVVAI 9 435 ALVLPSIVIL 18 150 SAWALQLGPK 14 442 VILDLLQLCR 18 171 NIQARQQVIE 14 TableXXXVI-V21- 46 TIRLIRCGYH 17 180 ELARQLNFIP 14 HLA-A0203-10mers- 92 AIHREHYTSL 17 189 PIDLGSLSSA 14 98P4B6 164 QVYICSNNIQ 17 190 IDLGSLSSAR 14 Pos 1234567890 score 177 QVIELARQLN 17 205 PLRLFTLWRG 14 NoResultsFound... 254 IVNKTLPIVA 17 215 PVVVAISLAT 14 261 IVAITLLSLV 17 231 FVRDVIIPYA 14 TableXXXVI-V25- 268 SLVYLAGLLA 17 266 LLSLVYLAGL 14 HLA-A0203-10mers- 331 YLFLNMAYQQ 17 279 AYQLYYGTKY 14 98P4B6 400 YVALLISTFH 17 316 HVAYSLCLPM 14 Pos 1234567890 score 403 LLISTFHVLI 17 370 LLSLLAVTSI 14 NoResultsFound. 404 LISTFHVLIY 17 45 LTIRLIRCGY 13 30 KVTVGVIGSG 16 75 DVTHHEDALT 13 TabIeXXXVII-V1-HLA-A3- 123 NQYPESNAEY 16 82 ALTKTNIIFV 13 10mers-98P4B6 141 LVKGFNVVS 16 128 SNAEYLASLF 13 Each peptide is a portion of SEQ 178 VIELARQLNF 16 154 LQLGPKDASR 13 ID NO: 3; each start position is 207 RLFTLWRGPV 16 157 GPKDASRQVY 13 specified, the length of peptide is 234 DVIIPYARNQ 16 166 YICSNNIQAR 13 191 DLGSLSSARE 13 224 WO 03/087306 PCT/US03/10462 TableXXXVII-Vi1-HLA-A3- TableXXXVII-V5A-HLA 10mers-98P4B6 A3-10mers-98P4B6 TableXXXVII-V7A-HLA Each peptide is a portion of SEQ Each peptide is a portion of A3-10mers-98P4B6 ID NO: 3; each start position is SEQ ID NO: 11; each start Each peptide is a portion of specified, the length of peptide is position is specified, the length SEQ ID NO: 15; each start 10 amino acids, and the end of peptide is 10 amino acids, position is specified, the position for each peptide is the and the end position for each length of peptide is 10 amino start position plus nine. peptide is the start position plus acids, and the end position for Pos 1234567890 score nine. each peptide is the start 200 EIENLPLRLF 13 Pos 1234567890 score position plus nine. 204 LPLRLFTLWR 13 9 TFWRGPVVVA 11 Pos 1234567890 score 240 ARNQQSDFYK 13 3 LPLRLFTFWR 10 10 FLPNGINGIK 22 298 WLQCRKQLGL 13 10 FWRGPVVVAI 10 5 SLSETFLPNG 12 304 QLGLLSFFFA 13 8 FTFWRGPVVV 9 310 FFFAMVHVAY 13 7 LFTFWRGPVV 7 TabIeXXXVII-V7B-HLA 314 MVHVAYSLCL 13 A3-10mers-98P4B6 321 LCLPMRRSER 13 TableXXXVII-V5B-HLA- Each peptide is a portion of 329 ERYLFLNMAY 13 A3-10mers-98P4B6 SEQ ID NO: 15; each start 353 EVWRIEMYIS 13 Each peptide is a portion of position is specified, the length 364 GIMSLGLLSL 13 SEQ ID NO: 11; each start of peptide is 10 amino acids, 373 LLAVTSIPSV 13 position is specified, the and the end position for each 397 TLGYVALLIS 13 length of peptide is 10 amino peptide is the start position plus 399 GYVALLISTF 13 acids, and the end position for nine. 409 HIIVLIYGWKRA 13 each peptide is the start Pos 1234567890 score 437 VLPSIVILDL 13 position plus nine. 5 MAYQQSTLGY 13 445 DLLQLCRYPD 13 Pos 1234567890 score 2 FLNMAYQQST 12 _ QIFCSFADTQ 17 10 STLGYVALLI 11 TabIeXXXVII-V2-HLA- 22 ELEFVFLLTL 17 3 LNMAYQQSTL 9 A3-10mers-98P4B6 18 QTELELEFVF 11 7 YQQSTLQGYVA 7 Each peptide is a portion of 20 ELELEFVFLL 11 8 QQSTLGYVAL 7 SEQ ID NO: 5; each start 7 FIQIFCSFAD 10 1 LFLNMAYQQS 6 position is specified, the length 8 IQIFCSFADT 8 9 QSTLGYVALL 6 of peptide is 10 amino acids, and the end position for each TableXXXVII-V6-HLA- TableXXXVII-V7C-HLA peptide is the start position A3-10mers-98P4B6 A3-10mers-98P4B6 plus nine. Each peptide is a portion of Each peptide is a portion of SEQ Pos 1234567890 score SEQ ID NO: 13; each start ID NO: 15; each start position is 8 ALSLSLSSGF 21 position is specified, the length specified, the length of peptide is 10 SLSLSSGFTP 19 of peptide is 10 amino acids, 10 amino acids, and the end 22 CLSLPSSWDY 17 and the end position for each position for each peptide is the 5 GLQALSLSLS 15 peptide is the start position plus start position plus nine. 32 RCPPPCPADF 15 nine. Pos 1234567890 score 12 SLSSGFTPFS 11 Pos 1234567890 score 13 VLASPAAAWK 28 24 SLPSSWDYRC 11 13 ILFLPCISRK 26 173 ILSKLTEQK 25 2 GSPGLQALSL 10 2 VLPSIVILGK 23 137 RLLKSQAASG 24 33 CPPPCPADFF 10 15 FLPCISRKLK 21 12 EVLASPAAAW 21 18 CISRKLKRIK 21 134 FLLRLLKSQA 21 TableXXXVII-V5A-HLA- 6 IVILGKIILF 20 4 IVILDLSVEV 20 A3-10mers-98P4B6 22 KLKRIKKGWE 19 36 IVLPIEWQQD 20 Each peptide is a portion of 35 FLEEGIGGTI 19 120 PVLPHTNGVG 20 SEQ ID NO: 11; each start 12 IILFLECISR 18 176 KLTQEQKSKH 20 position is specified, the length 46 HVSPERVTVM 18 83 SQIPVVGVVT 18 of peptide is 10 amino acids, 23 LKRIKKGWEK 17 84 QIPVVGVVTE 18 and the end position for each 11 KIILFLPCIS 16 156 SLGEFLGSGT 18 peptide is the start position plus 19 ISRKLKRIKK 16 167 MKLETIILSK 18 nine. 1 LVLPSMVILG 15 3 SIVILDLSVE 17 Pos 1234567890 score 7 VILGKIILFL 15 6 ILDLSVEVLA 17 6 RLFTFWRGPV 16 25 RIKKGWEKSQ 15 28 ILRGGLSEIV 17 4 PLRLFTFWRG 14 26 IKKGWEKSQF 15 74 GIRNKSSSSS 17 1 ENLPLRLFTF 13 39 GIGGTIPHVS 15 90 VVTEDDEAQD 17 2 NLPLRLFTFW 12 8 ILGKIILFLP 12 121 VLPHTNGVGP 17 225 WO 03/087306 PCT/USO3/10462 TableXXXVII-V7C-HLA- SEQ ID NO: 29; each start TabIeXXXVII-VI-HLA A3-10mers-98P4B6 position is specified, the length A26-1l0mers-98P4B6 Each peptide is a portion of SEQ of peptide is 10 amino acids, Each peptide is a portion of SEQ ID NO: 15; each start position is and the end position for each ID NO: 3; each start position is specified, the length of peptide is peptide is the start position plus specified, the length of peptide is 10 amino acids, and the end nine. 10 amino acids, and the end position for each peptide is the Pos 1234567890 score position for each peptide is the start position plus nine. 6 RLFTFWRGPV 16 start position plus nine. Pos 1234567890 score 4 PLRLFTFWRG 14 Pos 1234567890 score 138 LLKSQAASGT 17 1 ENLPLRLFTF 13 127 ESNAEYLASL 23 27 NILRGGLSEI 16 2 NLPLRLFTFW 12 427 YTPPNFVLAL 23 100 SIDPPESPDR 16 9 TFWRGPVVVA 11 440 SIVILDLLQL 23 110 ALKAANSWRN 16 3 LPLRLFTFWR 10 45 LTIRLIRCGY 22 168 KLETILLSKL 16 10 FWRGPVVVAI 10 234 DVIHPYARNQ 22 171 TIILSKLTQE 16 8 FTFWRGPVVV 9 253 EIVNKTLPIV 22 5 VILDLSVEVL 15 7 LFTFWRGPVV 7 260 PIVAITLLSL 22 8 DLSVEVLASP 15 329 ERYLFLNMAY 21 26 ANILRGGLSE 15 TableXXXVII-V21-HLA- 15 ETCLPNGING 20 37 VLPIEWQQDR 15 A3-10mers-98P4B6 32 TVGVIGSGDF 20 135 LLRLLKSQAA 15 Each peptide is a portion of 98 YTSLWDLRHL 20 147 TLSLAFTSWS 15 SEQ ID NO: 43; each start 353 EVWRIEMYIS 20 149 SLAFTSWSLG 15 position is specified, the length 68 EFFPHVVDVT 19 159 EFLGSGTWMK 15 of peptide is 10 amino acids, 75 DVTHHEDALT 19 175 SKLTQEQKSK 15 and the end position for each 115 DVSNNMRINQ 19 38 LPIEWQQDRK 14 peptide is the start position plus 186 NFIPIDLGSL 19 47 KIPPLSTPPP 14 nine. 230 SFVRDVIHPY 19 103 PPESPDRALK 14 Pos 1234567890 score 257 KTLPIVAITL 19 109 RALKAANSWR 14 3 KLITQEKTKH 18 314 MVHVAYSLCL 19 131 LWEFLLRLLK 14 2 SKLTQEQKTK 17 364 GIMSLGLLSL 19 127 GVGPLWEFLL 13 404 LISTFHVLIY 19 143 AASGTLSLAF 13 TableXXXVII-V25-HLA- 217 VVAISLATFF 18 A3-10mers-98P4B6 A3-0mers-98P4B6359 MYISFGIMSL 18 TableXXXVII-V8-HLA- Each peptide is a portion of 399 GYVALLISTF 18 A3-10mers-98P4B6 SEQ ID NO: 51; each start 441 IVILDLLQLC 18 Each peptide is a portion of position is specified, the 2 ESISMMGSPK 17 SEQ ID NO: 17; each star length of peptide is 10 amino 30 KVTVGVIGSG 17 position is specified, the length acids, and the end position 30 KVTVGVIGSG 17 of peptide is 10 amino acids, for each peptide is the start 40 DFAKSLTIRL 17 and the end position for each position plus nine. 8 DALTKTNIF 17 peptide is the start position Pos 1234567890 score 263 AITLLSLVYL 17 plus nine. 2 ILFLPCISQK 29 406 STFHVLIYGW 17 Pos 1234567890 score 4 FLPCISQKLK 20 177 QVIELARQLN 16 S5IFLEEGMGGTI 19 7 CISQKLKR1K 18 215 PVVVAISLAT 16 1 IILFLPCISQ 14 269 LVYLAGLLAA 16 TableXXXVII-VI3-HLA- 435 ALVLPSML 16 A3-10mers-98P4B6 TableXXXVII-V Il-HLA- 436 LVLPSIVILD 16 Each peptide is a portion of A26-10mers-98P4B6 34 GVIGSGDFAK 15 SEQ ID NO: 27; each start Each peptide is a portion of SEQ 72 HVVDVTHHED 15 position is specified, the ID NO: 3; each start position is 116 VSNNMRINQY 15 length of peptide is 10 amino specified, the length of peptide is 142 IVKGFNVVSA 15 acids, and the end position for 10 amino acids, and the end 199 REIENLPLRL 15 each peptide is the start position for each peptide is the 250 IPIEIVNKTL 15 position plus nine. start position plus nine. 261 IVAITLLSLV 15 Pos 1234567890 score Pos 1234567890 score 262 VAITLLSLVY 15 10 FLPNGINGIK 22 216 VVVAISLATF 27 310 FFFAMVHVAY 15 5 SLSETFLPNG 12 296 ETWLQCRKQL 27 377 TSIPSVSNAL 15 200 EIENLPLRLF 26 389 REFSFIQSTL 15 147 NVVSAWALQL 25 391 FSFIQSTLGY 15 TableXXXVII-V 14-HLA- 351 EEEVWRIEMY 25 432 FVLALVLPSI 15 A3-10mers-98P4B6 202 ENLPLRLFTL 24 31 VTVGVIGSGD 14 Each peptide is a portion of 56 VVIGSRNPKF 23 55 HVVIGSRNPK 14 89 IFVAIHREHY 14 226 WO 03/087306 PCT/US03/10462 TableXXXVII-V1 -HLA- TableXXXVmI-V2-HLA- 38 EGIGGTIPHV 18 A26-10mers-98P4B6 A26-10mers-98P4B6 7 VILGKIILFL 17 Each peptide is a portion of SEQ Each peptide is a portion of 1 LVLPSIVILG 16 ID NO: 3; each start position is SEQ ID NO: 3; each start 46 HVSPERVTVM 15 specified, the length of peptide is position is specified, the length 42 GTIPHVSPER 13 10 amino acids, and the end of peptide is 10 amino acids, position for each peptide is the and the end position for each TableXXXVIII-V7A Sstart position plus nine. peptide is the start position HLA-A26-10mers-98P4B6 Pos 1234567890 score plus nine. Each peptide is a portion of 103 DLRHLLVGKI 14 Pos 1234567890 score SEQ ID NO: 15; each start 108 LVGKILIDVS 14 30 DYRCPPPCPA 8 position is specified, the 148 VVSAWALQLG 14 34 PPPCPADFFL 8 length of peptide is 10 amino 222 LATFFFLYSF 14 7 QALSLSLSSG 7 acids, and the end position for 301 CRKQLGLLSF 14 18 TPFSCLSLPS 7 each peptide is the start 352 EEVWRIEMYI 14 3 SPGLQALSLS 6 position plus nine. 362 SFGIMSLGLL 14 Pos 1234567890 score 417 RAFEEEYYRF 14 TableXXXVIII-VSA-HLA- I8 ETFLPNGING I 24 437 VLPSIVILDL 14 A26-10mers-98P4B6 443 ILDLLQLCRY 14 Each peptide is a portion of TableXXXVIII-V7B-HLA 27 DARKVTVGVI 13 SEQ ID NO: 11; each start A26-10mers-98P4B6 74 VDVTHHEDAL 13 position is specified, the length Each peptide is a portion of 92 AIHREHYTSL 13 of peptide is 10 amino acids, SEQ ID NO: 15; each start 137 FPDSLIVKGF 13 and the end position for each position is specified, the length 172 IQARQQVIEL 13 peptide is the start position plus of peptide is 10 amino acids, 176 QQVIELARQL 13 nine. and the end position for each 178 VIELARQLNF 13 Pos 1234567890 score peptide is the start position plus 218 VAISLATFFF 13 1 ENLPLRLFTF 24 nine. 223 ATFFFLYSFV 13 8 FTFWRGPVVV 12 Pos 1234567890 score 258 TLPIVAITLL 13 9, QSTLGYVALL 13 299 LQCRKQLGLL 13 TableXXXVIII-V5B-HLA- 5 MAYQQSTLGY 11 302 RKQLGLLSFF 13 A26-10mers-98P4B6 3 LNMAYQQSTL 10 358 EMYISFGIMS 13 Each peptide is a portion of 10 STLGYVALLI 10 361 ISFGIMSLGL 13 SEQ ID NO: 11; each start 8 QQSTLGYVAL 9 365 IMSLGLLSLL 13 position is specified, the length 365 IMSLGLLSLL 13 375 AVTSIPSVSN 13 of peptide is 10 amino acids, TableXXXVIII-V7C-HLA 376 AVTSIPSVSN 13 and the end position for each A26-10mers-98P4B6 395 QSTLGYVALL 13 peptide is the start position Each peptide is a portion of 410 VLIYGWKRAF 13 plus nine. SEQ ID NO: 15; each start 410 VLIYGW A 13 Pos 1234567890 score position is specified, the length TabeXXXVIII-V2-HLA- 16 DTQTELELEF 25 of peptide is 10 amino acids, A26-10mers-9V2-4B6A- 22 ELEFVFLLTL 24 and the end position for each Each peptide is a portion of 24 EFVFLLTLLL 23 peptide is the start position plus Each peptide is a portion ef 2 LLFFL 2 ie 20 ELELEFVFLL 22 nine. SEQ ID NO: 3; each start 18 QTELELEFVF 16 Pos 1234567890 score position is specified, the length 2 TELELEFVF 16 Pos 1234567890 score of peptide is 10 amino acids, 23 LEFVFLLTLL 16 170 ETHLSKLTQ 24 and the end position for each 4 EFSFIQIFCS 14 12 EVLASPAAAW 21 peptide is the start position 5 FSFIQIFCSF 13 35 EIVLPIEWQQ 19 plus nine. 2 WREFSFIQIF 12 102 DPPESPDRAL 19 Pos 1234567890 score 12 CSFADTQTEL 12 127 GVGPLWEFLL 19 17 FTPFSCLSLP 13 5 VILDLSVEVL 17 16 GFTPFSCLSL 12 TableXXXVIII-V6-HLA- 152 FTSWSLGEFL 17 35 PPCPADFFLY 11 A26-10mers-98P4B6 69 EAQESGIRNK 16 2 GSPGLQALSL 10 Each peptide is a portion of 105 ESPDRALKAA 16 4 PGLQALSLSL 10 SEQ ID NO: 13; each start 89 GVVTEDDEAQ 15 14 SSGFTPFSCL 10 position is specified, the length 133 EFLLRLLKSQ 15 22 CLSLPSSWDYGFTPFSCL 10 of peptide is 10 amino acids, 151 AFTSWSLGEF 15 8 ALSLSLSSGF 91 and the end position for each 3 SIVILDLSVE 14 118 ALSLSSSGFTPF 9 peptide is the start position plus 4 IVILDLSVEV 14 11 RCPLSLSSGFTPPCPADF 9 nine. 45 DRKIPPLSTP 14 32 RCPPPCPADF 9 Pos 1234567890 score 86 PVVGVVTEDD 14 33 CPPPCPADFFLYF 9 6 IVILGKIILF 27 90o VVTEDDEAQD 14 36 PCPADFFLYF 9 5 SIVILGKIIL 18 227 WO 03/087306 PCT/US03/10462 TableXXXVIII-V7C-HLA- 8JETFLPNGING 24 TableXXXIXV1-HLA A26- 10mers-98P4B6 B0702-10mers-98P4B6 Each peptide is a portion of TableXXXVIII-V14-HLA- Each peptide is a portion of SEQ SEQ ID NO: 15; each start A26-10mers-98P4B6 ID NO: 3; each start position is position is specified, the length Each peptide is a portion of specified, the length of peptide is of peptide is 10 amino acids, SEQ ID NO: 29; each start 10 amino acids, and the end and the end position for each position is specified, the length position for each peptide is the peptide is the start position plus of peptide is 10 amino acids, start position plus nine. nine. and the end position for each Pos 1234567890 score Pos 1234567890 score peptide is the start position plus 323 LPMRRSERYL 21 99 DSIDPPESPD 14 nine. 137 FPDSLIVKGF 18 130 PLWEFLLRLL 14 Pos 1234567890 score 428 TPPNFVLALV 17 168 KLETIILSKL 14 1 ENLPLRLFTF 24 125 YPESNAEYLA 16 171 TIILSKLTQE 14 8 FTFWRGPVVV 12 214 GPVVVAISLA 16 8 DLSVEVLASP 13 219 AISLATFFFL 16 42 WQQDRKIPPL 13 TableXXXVHI-V21-HLA- 394 IQSTLGYVAL 16 93 EDDEAQDSID 13 A26-10mers-98P4B6 36 IGSGDFAKSL 15 122 LPHTNGVGPL 13 Each peptide is a portion of 197 SAREIENLPL 15 125 TNGVGPLWEF 13 SEQ ID NO: 43; each start 325 MRRSERYLFL 15 129 GPLWEFLLRL 13 position is specified, the length 361 ISFGIMSLGL 15 10 SVEVLASPAA 12 of peptide is 10 amino acids, 379 IPSVSNALNW 15 36 IVLPIEWQQD 12 and the end position for each 427 YTPPNFVLAL 15 72 ESGIRNKSSS 12 peptide is the start position plus 211 LWRGPVVVAI 14 95 DEAQDSIDPP 12 nine. 263 AITLLSLVYL 14 120 PVLPHTNGVG 12 Pos 1234567890 score 402 ALLISTFHVL 14 126 NGVGPLWEFL 12 4 LTQEQKTKHC ' 10 435 ALVLPSIVIL 14 41 EWQQDRKIPP 11 7 EQKTKHCMFS 10 40 DFAKSLTIRL 13 60 WTEEAGATAE 11 8 QKTKHCMFSL 10 92 AIHREHYTSL 13 62 EEAGATAEAQ 11 6 QEQKTKHCMF 9 127 ESNAEYLASL 13 63 EAGATAEAQE 11 91 KTKHCMFSLI 9 172 IQARQQVIEL 13 66 ATAEAQESGI 11 188 IPIDLGSLSS 13 96 EAQDSIDPPE 11 TableXXXVIII-V25-HLA- 195 LSSAREIENL 13 141 SQAASGTLSL 11 A26-10mers-98P4B6 199 RETENLPLRL 13 159 EFLGSGTVWMvK 11 Each peptide is a portion of 204 LPLRLFTLWR 13 180 EQKSKHCMFS 1SEQ ID NO: 51; each start 259 LPIVAITLLS 13 position is specified, the length 260 PIVAITLLS 13 of peptide is 10 amino acids, 260 PVAITLLSL 13 TableXXXVII-V8-HLA- and the end position for each 266 LLSLVYLAGL 13 A26-10mers-98P4B6 peptide is the start position 290 RFPPWLETWL 13 Each peptide is a portion of plus nine. 364 GIMSLGLLSL 13 SEQ ID NO: 17; each start Pos 1234567890 score 365 IMSLGLLSLL 13 position is specified, the length 2 ILFLPCISQK 10 4 ISMMGSPKSL 12 of peptide is 10 amino acids, 3 LFLPCISQKL 10 18 LPNGINGIKD 12 and the end position for each 6 PCISQKLKRI 70 FPHVVDVTHH 12 peptide is the start position plus 6 PCISQKLKRI 9 70 FPHVVDVTHH 12 nine. I IILFLPCISQ 6 98 YTSLWDLRHL 12 Pos 1234567890 score 9 SQKLKRIKKG 6 142 IVKGFNVVSA 12 8 EGMGGTIPHV 14 7 CISQKLKRIK 4 147 NVVSAWALQL 12 7 EEGMGGTIPH 11 157 GPKDASRQVY 12 1 SEEGMT 202 ENLPLRLFTL 12 1 EKSQFLEEGM 10 SSQFLEEGM G 61 TableXXXIXVI-HLA- 257 KTLPIVAITL 12 B0702-10mers-98P4B6 273 AGLLAAAYQL 12 TableXXXVIII-V13-HLA- Each peptide is a portion of SEQ 292 PPWLETWLQC 12 A26-10mers-98P4B6 ID NO: 3; each start position is 296 ETWLQCRKQL 12 Each peptide is a portion of specified, the length of peptide is 298 WLQCRKQLGL 12 SEQ ID NO 27; each start 10 amino acids, and the end 314 MVHVAYSLCL 12 poSEQ ID NO: 27; each started position for each peptide is the 377 TSIPSVSNAL 12 length of peptide is 10 amino start position plus nine. 395 QSTLGYVALL 12 acids, and the end position for Pos 1234567890 score 425 RFYTPPNFVL 12 each peptide is the start 429 PPNFVLALVL 23 437 VLPSIVILDL 12 each peptide is the start__ __________ position plus nine. 438 LPSIVILDLL 22 440 SIVILDLLQL 12 Ps 1234567890 score 9 SPKSLSETCL 21 26 KDARKVTVGV 11 250 IPIEIVNKTL 21 27 DARKVTVGVI 11 228 WO 03/087306 PCT/US03/10462 TabIcXXXIX VI-HLA- TableXXXIX-V5A-HLA- TabIeXXXIX-V6-HLA B0702-10mers-98P4B6 B0702-10mers-98P4B6 B0702-10mers-98P4B6 Each peptide is a portion of SEQ nine. Each peptide is a portion of ID NO: 3; each start position is Pos 1234567890 score SEQ ID NO: 13; each start specified, the length of peptide is 10 FWRGPVVVAI 14 position is specified, the length 10 amino acids, and the end 3 LPLRLFTFWVR 11 of peptide is 10 amino acids, position for each peptide is the 9 TFWRGPVVVA 10 and the end position for each Start position plus nine. 6 RLFTFWRGPV 9 peptide is the start position plus Pos 1234567890 score 8 FTFWRGPVVV 9 nine. 49 LIRCGYHVVI 11 1 ENLPLRLFTF 8 Pos 1234567890 score 62 NPKFASEFFP 11 7 LFTFWRGPVV 8 45 PHVSPERVTV 9 74 VDVTHHEDAL 11 95 REHYTSLWDL 11 TableXXXIX-V5B-HLA- TableXXXIX-V7A-HLA 99 TSLWDLRHLL 11 B0702-10mers-98P4B6 B0702-10mers-98P4B6 132 YLASLFPDSL 11 Each peptide is a portion of Each peptide is a portion of 145 GFNVVSAWAL 11 SEQ ID NO: 11; each start SEQ ID NO: 15; each start 183 RQLNFIPIDL 11 position is specified, the length position is specified, the 186 NFIPIDLGSL 1I of peptide is 10 amino acids, length of peptide is 10 amino 201 IENLPLRLFT 11 and the end position for each acids, and the end position 213 RGPVVVAISL 11 peptide is the start position for each peptide is the start 237 HPYARNQQSD 11 plus nine. position plus nine. 252 IEIVNKTLPI 11 Pos 1234567890 score Pos 1234567890 score 258 TLPIVAITLL 11 19 TELELEFVFL 14 2 SPKSLSETFL 22 286 TKYRRFPPWL 11 24 EFVFLLTLLL 14 291 FPPWLETWLQ 11 14 FADTQTELEL 13 TableXXXIX-V7B-HLA 312 FAMVHVAYSL 11 22 ELEFVFLLTL 13 B0702-10mers-98P4B6 362 SFGIMSLGLL 11 12 CSFADTQTEL 12 Each peptide is a portion of 389 REFSFIQSTL 11 20 ELELEFVFLL 12 SEQ ID NO: 15; each start 23 LEFVFLLTLL 11 position is specified, the length TableXXXIX-V2-HLA- 1 NWREFSFIQI 9 of peptide is 10 amino acids, B0702-10mers-98P4B6 8 IQIFCSFADT 9 and the end position for each Each peptide is a portion of 21 LELEFVFLLT 9 peptide is the start position plus SEQ ID NO: 5; each start 10 IFCSFADTQT 8 Pnine, 1234567890 score position is specified, the length 16 DTQTELELEF 8 Po8 QQSTLGYVAL 15score of peptide is 10 amino acids, 5 FSFIQIFCSF 7 8 QSTLGYVAL 15 and the end position for each 6 SFIQIFCSFA 7 3 LNMAYQQSTL 12 peptide is the start position 17 TQTELELEFV 7 10 STLGYVALL 10 plus nine. 18 QTELELEFVF 7 6 AYQSTLGYVALLI 10 Pos 1234567890 score 2 WREFSFIQIF 6 6 AYQQSTLGYV 8 34 PPPCPADFFL 21 7 YQQSTLGYVA 1 7 33 CPPPCPADFF 18 TableXXXIX-V6-HLA 2 GSPGLQALSL 14 B0702-10mers-98P4B6 TableXXXIX-V7C-HLA 16 GFTPFSCLSL 13 Each peptide is a portion of B702-10mEach p eptide is a portion of SE4B6 18 TPFSCLSLPS 13 SEQ ID NO: 13; each start Each peptide is a portion of SEQ 4 PGLQALSLSL 12 position is specified, the length specified, the lengtach ofstart poseptionde is .14 SSGFTPFSCL 12 of peptide is 10 amino acids, spec10 amino acids, and the of peptide is 25 LPSSWDYRCP 12 and the end position for each 10 amposition for ach peptide is the end 35 PPCPADFFLY 12 peptide is the start position plus start position plus nine. 3 SPGLQALSLS 11 nine. . start position plus nine. 8 ALSLSLSSGF 10 Pos 1234567890 score Po122 LPHTNGVGPL 22score 36 PCPADFFLYF 10 3 LPSIVILGKI 18 129 GPLWEFLLRL 22 44 IPHVSPERVT 18 2 PE RL 2 102 DPPESPDRAL 21 7 VILGKIILFL 15 TableXXXIX-V5A-HLA- 27 KKGWEKSQFL 13 49 PPLSTPPPPA 18 B0702-10mers-98P4B6 16 LPCISRKLKR 12 55 PPPAMWTEEA 18 Each peptide is a portion of 46 HVSPERVTVM 12 119 NPVLPHTNGV 17 SEQ ID NO: 11; each start 14 LFLPCISRKL 11 141 SQAASGTLSL 15 position is specified, the length 5 SIVILGKIIL 10 143 AASGTLSLAF 15 of peptide is 10 amino acids, 38 EGIGGTIPHV 10 29 LRGGLSEIVL 14 and the end position for each 26 IKKGWEKSQF 9 13 5AANSWRNPVKCL 13 peptide is the start position plus 31 EKSQFLEEGI 9 15 48 IPPLSTPPPPAAA KCL 13 22948 IPPLSTPPPP 1 229 WO 03/087306 PCT/US03/10462 TableXXXIX-V7C-HLA- B08-10mers-98P4B6 B0702-10mers-98P4B6 TabIeXXXIX-Vl 3-HILA- Pos 1234567890 score Each peptide is a portion of SEQ B0702-10mers-98P4B6 NoResultsFound. ID NO: 15; each start position is Each peptide is a portion of specified, the length of peptide is SEQ ID NO: 27; each start TableXL-V2-HLA 10 amino acids, and the end position is specified, the BO8-10mers-98P4B6 position for each peptide is the length of peptide is 10 amino Pos 1234567890 score start position plus nine, acids, and the end position NoResultsFound. Pos 1234567890 score for each peptide is the start 85 IPVVGVVTED 13 position plus nine. TableXL-V5A-HLA 106 SPDRALKAAN 13 Pos 1234567890 score B08-10mers-98P4B6 126 NGVGPLWEFL 13 2 SPKSLSETFL 22 Pos 1234567890 score 152 FTSWSLGEFL 13 NoResultsFound. 165 TWMKLETIIL 13 TableXXXIX-V14-HLA 181 QKSKHCMFSL 13 BO702-10mers-98P4B6 TableXL-V5B-HLA 1 LPSIVILDLS 12 Each peptide is a portion of B08-10mers-98P4B6 5 VILDLSVEVL 12 SEQ ID NO: 29; each start Pos 1234567890 score 16 SPAAAWKCLG 12 position is specified, the length NoResultsFound. 20 AWKCLGANIL 12 of peptide is 10 amino acids, 24 LGANILRGGL 12 and the end position for each TableXL-V6-HLA 42 WQQDRKIPPL 12 peptide is the start position plus B08-10mers-98P4B6 54 PPPPAMWTEE 12 nine. Pos 1234567890 score 56 PPAMWTEEAG 12 Pos 1234567890 score NoResultsFound. 103 PPESPDRALK 12, 10 FWRGPVVVAI 14 127 GVGPLWEFLL 12 3 LPLRLFTFWR 11 TableXL-V7A-HLA 139 LKSQAASGTL 12 _9 TFWRGPVVVA 10 B08-10mers-98P4B6 28 ILRGGLSEIV 11 6 RLFTFWRGPV 9 Pos 12345678901score 44 DRKIPPLST 11 8 FTFWRGPVVV 9 NoResultsFound. 53 TPPPPAMWTE 11 1 ENLPLRLFTF 8 81 SSSQIPVVGV 11 7 LFTFWRGPVV 8 TableXL-V7B-HLA 104 PESPDRALKA 11 BO8-10mers-98P4B6 144 ASGTLSLAFT 11 TabIeXXXIX-V21-HLA- Pos 1234567890 score 148 LSLAFTSWSL 11 B0702-10mers-98P4B6 NoResultsFound. 160 FLGSGTWMKL 11 Each peptide is a portion of 168 KLETIILSKL 11 SEQ ID NO: 43; each start TableXL-V7C-HLA 6 ILDLSVEVLA 101 position is specified, the length B08-10mers-98P4B6 176 ILDLSVIKCVLA 10 of peptide is 10 amino acids, Pos 1234567890 score 17 PAAAWKCLGANI 10 and the end position for each NoResultsFound. 19 AAWKCLGALNI 10 peptide is the start position plus 31 GGLSEIVLPI 10 nine. TableXL-V8-HLA 38 LPIEWQQDRK 1 Pos 1234567890 score B08-10mers-98P4B6 50 PLSTPPPPAIV 10 _ 8 QKTKHCMFSL 11 Pos 1234567890 score 8 KTSSSSSQIPV 10 9 KTKHICMFSLI 8 NoResultsFound. 79 SSSSSQIPVVA 10 6 QEQKTKHCMF 7 83 SQIPVVGVVT 10 1 LSKLTQEQKT 6 TableXL-V13-HLA 112 KAANSWRNPV 10 5 TQEQKTKHCM 6 B08-10mers-98P4B6 130 PLWEFLLRLL 10 Pos 1234567890 score TableXXXIX-V25-HLA- NoResultsFound. TabBeXXXIX-V8-HLA. B0702-10mers-98P4B6 B0702-10mers-98P4B6 Each peptide is a portion of TableXL-V14-HLA Each peptide is a portion of SEQ ID NO: 51; each start B08-10mcrs-98P4B6 SEQ D N: 1; eah sartB08-10mers-98P4B6 SEQ I NO: 17; each start position is specified, the Pos 1234567890 score position is specified, the length length of peptide is 10 amino NoResultsFound. of peptide is 10 amino acids, acids, and the end position for and the end position for each each peptide is the start TableXL-V21-HLA peptide is the start position plus position plus nine. I B08-l0mers-98P4B6 nine. Pos 1234567890 score [Pos 1234567890score 1234567890 score 5 LPCISQKLKR 12 [ NoResultsFotnd. 8 EGMGGTIPHV 11 3 LFLPCISQKL 11 4 EQLEEGM 9 6 PCISQKLKRI 6 f TableXL-V25-HLA B08-10mers-98P4B6 5 FLEEGMGGTI 6 TableXL-VI-HLA- ]Pos 1234567890 score 230 WO 03/087306 PCT/USO3/10462 TableXL-V25-HLA- Pos 1234567890 score B08-10mers-98P4B6 NoResultsFound. TableXLI-V21-HLA Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V25-HLA- Pos 1234567890 score B 1510-10mers-98P4B6 NoResultsFound. TableXLI-V1-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V25-HLA Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-VI-HLA- Pos 1234567890 score _____________ B2705-10mers-98P4B6 NoResultsFound. TableXLI-V2-HLA- Pos 1234567890 score B 1510-10mers-98P4B6 NoResultsFound. TableXLI-V I -HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V2-HLA- Pos 12345678901 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V5A-HLA- Pos 1234567890 score B 1510-10mers-98P4B6 NoResultsFound. TableXLI-V2-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V5A-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V5B-HLA- Pos 1234567890 score B 1510-10mers-98P4B6 NoResultsFound. TableXLI-V5A-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXIJ-V5B-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V6-HLA- Pos 1234567890 Iscore B 1510-10mers-98P4B6 NoResultsFound. TableXLI-V5B-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V6-HLA- Pos 1234567890 score __________ B2705-10mers-98P4B6 NoResultsFound. STableXLI-V7A-HLA- Pos 1234567890 score B 1510-10mers-98P4B6 NoResultsFound. TableXLI-V6-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V7A-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V7B-HLA- Pos 1234567890 score B 1510-10mers-98P4B6 NoResultsFound. TableXLI-V7A-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V7B-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V7C-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V7B-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V7C-HLA- Pos 1234567890 score 1B2705-10mers-98P4B6 NoResultsFound. TableXLI-V8-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V7C-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-V8-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V13-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V8-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-VI3-HLA- Pos I 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V14-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V13-HLA Pos 1234567890 score B2709-10mers-98P4B6 NoResultsFound. TableXLI-VI4-HLA- Pos 1234567890 score B2705-10mers-98P4B6 NoResultsFound. TableXLI-V21-HLA- Pos 1234567890 score B1510-10mers-98P4B6 NoResultsFound. TableXLI-V14-HLA 231 WO 03/087306 PCT/USO3/10462 B2709-10 Omers-98P4B6 TableXLIV-V I -HLA-B4402- TableXLIV-V1-HLA-B4402 Pos 1234567890 score 10mers-98P4B6 10mers-98P4B6 NoResultsFound. Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position is ID NO: 3; each start position is TableXLI-V21-HLA- specified, the length of peptide is specified, the length of peptide is B2709-10mers-98P4B6 10 amino acids, and the end 10 amino acids, and the end Pos 1234567890 score position for each peptide is the position for each peptide is the NoResultsFound. start position plus nine. start position plus nine. Pos 1234567890 score Pos 1234567890 score TableXLI-V25-HLA- 255 VNKTLPIVAI 15 323 LPMRRSERYL 13 B2709-10mers-98P4B6 258 TLPIVAITLL 15 324 PMRRSERYLF 13 Pos 1234567890 score 279 AYQLYYGTKY 15 328 SERYLFLNMA 13 NoResultsFound. 310 FFFAMVHVAY 15 350 NEEEVWRIEM 13 329 ERYLFLNMAY 15 362 SFGIMSLGLL 13 394 IQSTLGYVAL 15 364 GIMSLGLLSL 13 TableXLIV-VlI-HLA-B4402- 437 VLPSIVILDL 15 379 IPSVSNALNW 13 10mers-98P4B6 4 ISMMGSPKSL 14 384 NALNWREFSF 13 Each peptide is a portion of SEQ 92 AIHREHYTSL 14 395 QSTLGYVALL 13 ID NO: 3; each start position is 98 YTSLWDLRHL 14 403 LLISTFHVLI 13 specified, the length of peptide is 99 TSLWDLRHLL 14 429 PPNFVLALVL 13 10 amino acids, and the end 123 NQYPESNAEY 14 438 LPSIVILDLL 13 position for each peptide is the 137 FPDSLIVKGF 14 443 ILDLLQLCRY 13 start position plus nine. 147 NVVSAWALQL 14 38 SGDFAKSLTI 12 Pos 1234567890 score 183 RQLNFIPIDL 14 40 DFAKSLTIRL 12 199 REIENLPLRL 25 195 LSSAREIENL 14 93 IHREHYTSLW 12 351 EEEVWRIEMY 25 218 VAISLATFFF 14 105 RHLLVGKILI 12 252 IEIVNKTLPI 23 271 YLAGLLAAAY 14 124 QYPESNAEYL 12 389 REFSFIQSTL 23 290 RFPPWLETWL 14 178 VIELARQLNF 12 95 REHYTSLWDL 21 346 ENSWNEEEVW 14 192 LGSLSSAREI 12 179 IELARQLNFI 21 361 ISFGIMSLGL 14 197 SAREIENLPL 12 352 EEVWRIEMYI 20 365 IMSLGLLSLL 14 216 VVVAISLATF 12 79 HEDALTKTNI 19 391 FSFIQSTLGY 14 260 PIVAITLLSL 12 377 TSIPSVSNAL 19 396 STLGYVALLI 14 274 GLLAAAYQLY 12 186 NFIPIDLGSL 18 399 GYVALLISTF 14 282 LYYGTKYRRF 12 202 ENLPLRLFTL 18 404 LISTFHVLIY 14 286 TKYRRFPPWL 12 257 KTLPIVAITL 18 418 AFEEEYYRFY 14 295 LETWLQCRKQ 12 427 YTPPNFVLAL 18 420 EEEYYRFYTP 14 301 CRKQLGLLSF 12 435 ALVLPSIVIL 18 435 ALVLPSIVIL 18 440 SIVILDLLQL 14 302 RKQLGLLSFF 12 273 AGLLAAAYQL 17 41 FAKSLTIRLI 13 312 FAMVHVAYSL 12 289 RRFPPWLETW 17 74 VDVTHHEDAL 13 357 IEMYISFGIM 12 296 ETWLQCRKQL 17 80 EDALTKTNII 13 385 ALNWREFSFI 12 402 ALLISTFHVL 17 81 DALTKTNIIF 13 417 RAFEEEYYRF 12 16 TCLPNGINGI 16 84 TKTNIIFVAI 13 421 EEYYRFYTPP 12 116 VSNNMRINQY 16 104 LRHLLVGKIL 13 425 RFYTPPNFVL 12 200 EIENLPLRLF 16 127 ESNAEYLASL 13 219 AISLATFFFL 16 128 SNAEYLASLF 13 TableXLIV-V2-HLA 230 SFVRDVIHPY 16 143 VKGFNVVSAW 13 B4402-10mers-98P4B6 250 IPIEIVNKTL 16 145 GFNVVSAWAL 13 Each peptide is a portion of 262 VAITLLSLVY 16 157 GPKDASRQVY 13 SEQ ID NO: 5; each start 263 AITLLSLVYL 16 170 NNIQARQQVI 13 position is specified, the length 359 MYISFGIMSL 16 172 IQARQQVIEL 13 of peptide is 10 amino acids, 406 STFHVLIYGWRAF 16 176 QQVIELARQL 13 and the end position for each 410 VLIYGWKRAF 16 201 IENLPLRLFT 13 peptide is the start position 36 IGSGDFAKSL 15 211 LWRGPVVVAI 13 plus nine. 45 LTIRLIRCGY 15 213 RGPVVVAISL 13 Pos 1234567890 score 56 VVIGSRNPKF 15 220 ISLATFFFLY 13 8 ALSLSLSSGF 15 60 SRNPKFASEF 15 245 SDFYKIPIEI 13 32 RCPPPCPADF 15 67 SEFFPHVVDV 15 266 LLSLVYLAGL 13 33 CPPPCPADFF 15 126 PESNAEYLAS 15267 LSLVYLAGLL 13 35 PPCPADFFLY 15 130 AEYLASLFPD 15 299 LQCRKQLGLL 13 2 GSPGLQALSL 14 203 NLPLRLFTLW 15 303 KQLGLLSFFF 13 16 GFTPFSCLSL 14 232 WO 03/087306 PCT/USO3/10462 TableXLIV-V2-HLA- SEQ ID NO: 13; each start specified, the length of peptide is B4402-10mers-98P4B6 position is specified, the length 10 amino acids, and the end Each peptide is a portion of of peptide is 10 amino acids, position for each peptide is the SEQ ID NO: 5; each start and the end position for each start position plus nine. position is specified, the length peptide is the start position plus Pos 1234567890 score of peptide is 10 amino acids, nine. 92 TEDDEAQDSI 20 and the end position for each Pos 1234567890 score 179 QEQKSKHCMF 2( peptide is the start position 6 IVILGKIILF 19 143 AASGTLSLAF 18 plus nine. 7 VILGKIILFL 16 34 SEIVLPIEWQ 17 Pos 1234567890 score 14 LFLPCISRKL 16 104 PESPDRALKA 17 36 PCPADFFLYF 13 17 PCISRKLKRI 14 12 EVLASPAAAW 16 4 PGLQALSLSL 12 37 EEGIGGTIPH 14 15 ASPAAAWKCL 16 11 LSLSSGFTPF 12 4 PSIVILGKII 13 62 EEAGATAEAQ 16 14 SSGFTPFSCL 12 21 RKLKRIKKGW 13 132 WEFLLRLLKS 16 20 FSCLSLPSSW 12 5 SIVILGKIIL 12 20 AWKCLGANIL 15 22 CLSLPSSWDY 12 10 GKIILFLPCI 12 5 VILDLSVEVL 14 34 PPPCPADFFL 11 26 IKKGWEKSQF 12 11 VEVLASPAAA 14 3 LPSIVILGKI 11 42 WQQDRKIPPL 141 27 KKGWEKSQFL 1 51 LSTPPPPAMW 14 Tab1eXLIV-V5A-HLA- 30 WEKSQFLEEG 11 68 AEAQESGIRN 14 B4402-0mers-98P4B6 31 EKSQFLEEGI 11 71 QESGIRNKSS 14 Each peptide is a portion of 36 LEEGIGGTIP 11 102 DPPESPDRAL 14 SEQ ID NO: 11; each start 35 FLEEGIGGTI 9 113 AANSWRINPVL 14 position is specified, the length 38 EGIGGTIPHV 9 127 GVGPLWEFLL 14 of peptide is 10 amino acids, 1527 AFTSWSLGPL EFL 14 and the end position for each TableXLIV-V7A-HLA- 15168 KLETIILSKWSLGEF 14 peptide is the start position plus B4402-l0mers-98P4B6 KLETLSKL 14 nine. B4402-10mers-98P4B6 29 LRGGLSEIVL 13 Pos 1234567890 score Each peptide is a portion of 40 IEWQQDRKIP 13 1 ENLPLRLFTF 18 SEQ ID NO: 15; each start 95 DEAQDSIDPP 13 2 NLPLRLFTFW 14 position is specified, the 108 DRALKAANSW 13 1 F PVV 1 length of peptide is 10 amino 129 GPLWEFLLRL 13 10 FWRGPVVVAI 13 acids, and the end position 130 PLWEFLLRLL 13 for each peptide is the start 141 SQAASGTLSL 13 TableXLIV-V5B-HLA- position plus nine. 141 SQAASGTLSL 13 B4402-10mers-98P4B6 Pos 1234567890 score 158 GEFLGSGTWM 13 Each peptide is a portion of 9 TFLPNGINGI 16 165 TWMKLETIIL 13 SEQ ID NO: 11; each start 1 GSPKSLSETF 12 169 LETIILSKLT 13 position is specified, the length 2 SPKSLSETFL 11 24 LGANILRGGL 12 of peptide is 10 amino acids, 6 LSETFLPNGI 11 27 NILRGGLSEI 12 and the end position for each 7 SETFLPNGIN 11 33 LSEIVLPIEW 12 peptide is the start position 122 LPHTNGVGPL 12 plus nine. TabeXLVV7BHLA123 PHTNGVGPLW 12 Pos 1234567890 score TableXLIV-V7B-HLA-126 NGVGPLWEFL 12 23 LEFVFLLTLL 24 B4402-10mers-98P4B6 13926 NGVGPLWEFLKSQAASGTL 12 23 LEFVFLLTLL 2 Each peptide is a portion of 139 LKSQAASGTL 12 19 TELELEFVFL 23 SEQ ID NO: 15; each start 146 GTLSLAFTSW 12 20 ELELEFVFLL 15 position is specified, the length 19 AAWKCLGANI 11 22 ELEFVFLLTL 15 of peptide is 10 amino acids, 31 GGLSEIVLPI 11 24 EFVFLLTLLL 15 and the end position for each 61 TEEAGATAEA 11 21 LELEFVFLLT 14 peptide is the start position plus 66 ATAEAQESGI 11 2 WREFSFIQIF 13 nine. 125 TNGVGPLWEF 11 3 REFSFIQIFC 13 Pos 1234567890 score 148 LSLAFTSWSL 11 5 FSFIQIFCSF 13 8 QQSTLGYVAL 15 152 FTSWSLGEFL 11 14 FADTQTELEL 13 10 STLGYVALLI 14 157 LGEFLGSGTW 11 1 NWREFSFIQI 12 9 QSTLGYVALL 13 160 FLGSGTWMKL 11 12 CSFADTQTEL 12 3 LNMAYQQSTL 12 163 SGTWMKLETI 11 16 DTQTELELEF 12 5 MAYQQSTLGY 12 181 QKSKHCMFSL 11 18 QTELELEFVF 12 182 KSKHCMFSLI 11 TableXLIV-V7C-HLA- 39 PIEWQQDRKI 10 TableXLIV-V6-HLA- B4402-10mers-98P4B6 76 RNKSSSSSQI 9 B4402-10mers-98P4B6 Each peptide is a portion of SEQ 83 SQIPVVGVVT 9 Each peptide is a portion of ID NO: 15; each start position is 105 ESPDRALKAA 9 233 WO 03/087306 PCT/US03/10462 B4402-10mers-98P4B6 Pos 11234567890 score TableXLIV-V8-HLA- Each peptide is a portion of NoResultsFound.] B4402-10mers-98P4B6 SEQ ID NO: 51; each start Each peptide is a portion of position is specified, the length TableXLV-V 4-HLA SEQ ID NO: 17; each start of peptide is 10 amino acids, B5101-10mers-98P4B6 position is specified, the length and the end position for each Pos 11234567890 score of peptide is 10 amino acids, peptide is the start position plus [NoResultsFound. and the end position for each nine. peptde is the start position Pos 1234567890 score TableXLV-V21-HLA plus nine. 3 LFLPCISQKL 15 B5101-10mers-98P4B6 Pos 1234567890 score 6 PCISQKLKRI 14. Pos 1234567890 score 7 EEGMGGTIPH 14 10 QKLKRIKKGW 13 NoResultsFound. 6 LEEGMGGTIP 11 9 SQKLKRIKKG 8 5 FLEEGMGGTI 9 2 ILFLPCISQK 7 TableXLV-V25-HLA 8 EGMGGTIPHV 7 B5101-10mers-98P4B6 TableXLV-V1-HLA- Pos 1234567890 score TableXLIV-V13-HLA- B5101-10mers-98P4B6 NoResultsFound.| B4402-10mers-98P4B6 Pos 1234567890 score Each peptide is a portion of NoResultsFound. TableXLVI-V1-HLA-DRBI-0101 SEQ ID NO: 27; each start 15mers-98P4B6 position is specified, the TableXLV-V2-HLA- Each peptide is a portion of SEQ ID NO: length of peptide is 10 amino B5101-10mers-98P4B6 3; each start position is specified, the acids, and the end position Pos 11 234567890 s core length of peptide is 15 amino acids, and for each peptide is the start NoResultsFound. the end position for each peptide is the position plus nine. start position plus fourteen. Pos1 1234567890 score TableXLV-V5A-HLA- Pos 123456789012345 score 91 TFLPNGINGI 16 B5101-10mers-98P4B6 143 VKGFNVVSAWALQLG 33 1 GSPKSLSETF 12 Pos 1234567890 score 266 LLSLVYLAGLLAAAY 33 2 SPKSLSETFL 11 NoResultsFound. 367 SLGLLSLLAVTSIPS 32 1 6 LSETFLPNGI 11 1 MESISMMGSPKSLSE 31 7 SETFLPNGIN 11 TableXLV-V5B-HLA- 130 AEYLASLFPDSLIVK 30 B5101-10mers-98P4B6 30 KVTVGVIGSGDFAKS 29 TableXLIV-V14-HLA- Pos 1234567890 score 431 NFVLALVLPSIVILD 29 B4402-10mers-98P4B6 NoResultsFound. 206 LRLFTLWRGPVVVAI 28 Each peptide is a portion of 215 PVVVAISLATFFFLY 28 SEQ ID NO: 29; each start TableXLV-V6-HLA- 370 LLSLLAVTSIPSVSN 28 position is specified, the length B5101-10mers-98P4B6 438 LPSIVILDLLQLCRY 28 of peptide is 10 amino acids, Pos 1234567890 score 101 LWDLRHLLVGKILID 27 and the end position for each NoResultsFound. 5 LNFIPIDLGSLSSAR 27 peptide is the start position plus 185 LNFIPIDLGSLSSAR 27 nine. TableXLV-V7A-HLA- 356 RIEMYISFGIMSLGL 27 Pos 1234567890 score B5101-10mers-98P4B6 360 YISFGIMSLGLLSLL 27 1 ENLPLRLFTF 18 Pos 1234567890 397 TLGYVALLISTFHVL 27 SNLPLRLFTFW 1 Pos u2s34567890 score 421 EEYYRFYTPPNFVLA 27 10 FWNLPRLFTFWGPVVVA 14 NoResulsFound. 38 SGDFAKSLTIRLIRC 26 STableXLV-V7B-HLA- 102 WDLRHLLVGKILIDV 26 B101-10mers-98P4B6 122 INQYPESNAEYLASL 26 B5 101-10mers-98P4B6 19VAAQGKAR 2 TableXLIV-V21 -HLA- Pos 1234567890 score 149 VSAWALQLGPKDASR 26 B4402-10mers-98P4B6 NoResultsFound. 244 QSDFYKIPIEIVNKT 26 Each peptide is a portion of 249 KIPIEIVNKTLPIVA 26 SEQ ID NO: 43; each start TableXLV-V7C-HLA- 256 NKTLPIVAITLLSLV 26 position is specified, the length B5101-10mers-98P4B6 261 IVAITLLSLVYLAGL 26 of peptide is 10 amino acids, Pos 1 1 234567890 score 298 WLQCRKQLGLLSFFF 26 and the end position for each NoResultsFound. 368 LGLLSLLAVTSIPSV 26 peptide is the start position plus 109 VGKILIDVSNNMRIN 25 nine. TableXLV-V8-HLA- 137 FPDSLIVKGFNVVSA 25 Pos 1234567890 score B5101-10mers-98P4B6 145 GFNVVSAWALQLGPK 25 6 QEQKTKHCMF 20 Pos 234567890 score 198 AREIENLPLRLFTLW 25 9 KTKHCMFSLI 11 NoResultsFound.1234567890 score 222 LATFFFLYSFVRDVI 25 8 QKTKHCMFSL 10 252 IEIVNKTLPIVAITL 25 ___________ _ ~ TableXLV-V13-HLA- 264 ITLLSLVYLAGLLAA 25 TabIeXLIV-V25-HLA- B5101-10mers-98P4B6 302 RKQLGLLSFFFAMVH 25 234 WO 03/087306 PCT/USO3/10462 TableXLVI-VI-HLA-DRB 1-0101- TableXLVI-VI-HLA-DRB 1-0101- TableXLVI-VI-HLA-DRB -0101 15mers-98P4B6 l15mers-98P4B6 S15mers-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: 3; each start position is specified, the 3; each start position is specified, the 3; each start position is specified, the length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and the end position for each peptide is the the end position for each peptide is the the end position for each peptide is the start position plus fourteen, start position plus fourteen, start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 3091 SFFFAMVHVAYSLCL 25 429 PPNFVLALVLPSIVI 20 90 FVAIHREHYTSLWDL 17 354 VWRIEMYISFGIMSL 25 45 LTIRLIRCGYHVVIG 19 105 RHLLVGKILIDVSNN 17 362 SFGIMSLGLLSLLAV 25 80 EDALTKTNIIFVAIH 19 119 NMRINQYPESNAEYL 17 365 IMSLGLLSLLAVTSI 25 95 REHYTSLWDLRHLLV 19 138 PDSLIVKGFNVVSAW 17 51 RCGYHVVIGSRNPKF 24 135 SLFPDSLIVKGFNVV 19 140 SLIVKGFNVVSAWAL 17 98 YTSLWDLRHLLVGKI 24 139 DSLIVKGFNVVSAWA 19 151 AWALQLGPKDASRQV 17 106 HLLVGKILIDVSNNM 24 224 TFFFLYSFVRDVIHP 19 154 LQLGPKDASRQVYIC 17 150 SAWALQLGPKDASRQ 24 259 LPIVAITLLSLVYLA 19 176 QQVIELARQLNFIPI 17 184 QLNFIPIDLGSLSSA 24 280 YQLYYGTKYRRFPPW 19 187 FIPIDLGSLSSAREI 17 205 PLRLFTLWRGPVVVA 24 281 QLYYGTKYRRFPPWL 19 195 LSSAREIENLPLRLF 17 229 YSFVRDVIHPYARNQ 24 288 YRRFPPWLETWLQCR 19 217 VVAISLATFFFLYSF 17 269 LVYLAGLLAAAYQLY 24 307 LLSFFFAMVHVAYSL 19 226 FFLYSFVRDVIHPYA 17 330 RYLFLNMAYQQVHAN 24 322 CLPMRRSERYLFLNM 19 232 VRDVIHPYARNQQSD 17 335 NMAYQQVHANIENSW 24 328 SERYLFLNMAYQQVH 19 251 PIEIVNKTLPIVAIT 17 388 WREFSFIQSTLGYVA 24 357 IEMYISFGIMSLGLL 19 253 EIVNKTLPIVAITLL 17 391 FSFIQSTLGYVALLI 24 400 YVALLISTFHVLIYG 19 270 VYLAGLLAAAYQLYY 17 398 LGYVALLISTFHVLI 24 424 YRFYTPPNFVLALVL 19 271 YLAGLLAAAYQLYYG 17 427 YTPPNFVLALVLPSI 24 7 MGSPKSLSETCLPNG 18 305 LGLLSFFFAMVHVAY 17 430 PNFVLALVLPSIVIL 24 25 IKDARKVTVGVIGSG 18 316 HVAYSLCLPMRRSER 17 52 CGYHVVIGSRNPKFA 23 27 DARKVTVGVIGSGDF 18 317 VAYSLCLPMRRSERY 17 55 HVVIGSRNPKFASEF 23 39 GDFAKSLTIRLIRCG 18 329 ERYLFLNMAYQQVHA 17 186 NFIPIDLGSLSSARE 23 47 IRLIRCGYHVVIGSR 18 361 ISFGIMSLGLLSLLA 17 214 GPVVVAISLATFFFL 23 62 NPKFASEFFPI-VVDV 18 363 FGIMSLGLLSLLAVT 17 258 TLPIVAITLLSLVYL 23 129 NAEYLASLFPDSLIV 18 389 REFSFIQSTLGYVAL 17 351 EEEVWRIEMYISFGI 23 163 RQVYICSNNIQARQQ 18 392 SFIQSTLGYVALLIS 17 352 EEVWRIEMYISFGIM 23 167 ICSNNIQARQQVIEL 18 406 STFHVLIYGWKRAFE 17 127 ESNAEYLASLFPDSL 22 179 IELARQLNFIPIDLG 18 408 FHVLIYGWKRAFEEE 17 178 VIELARQLNFIPIDL 22 190 IDLGSLSSAREIENL 18 436 LVLPSIVILDLLQLC 17 189 PIDLGSLSSAREIEN 22 236 IHPYARNQQSDFYKI 18 2 ESISMMGSPKSLSET 16 211 LWRGPVVVAISLATF 22 267 LSLVYLAGLLAAAYQ 18 3 SISMMGSPKSLSETC 16 216 VVVAISLATFFFLYS 22 268 SLVYLAGLLAAAYQL 18 8 GSPKSLSETCLPNGI 16 255 VNKTLPIVAITLLSL 22 285 GTKYRRFPPWLETWL 18 11 KSLSETCLPNGINGI 16 301 CRKQLGLLSFFFAMV 22 296 ETWLQCRKQLGLLSF 18 16 TCLPNGINGIKDARK 16 312 FAMVHVAYSLCLPMR 22 299 LQCRKQLGLLSFFFA 18 24 GIKDARKVTVGVIGS 16 359 MYISFGIMSLGLLSL 22 326 RRSERYLFLNMAYQQ 18 59 GSRNPKFASEFFPHV 16 364 GIMSLGLLSLLAVTS 22 380 PSVSNALNWREFSFI 18 67 SEFFPHVVDVTHiHED 16 395 QSTLGYVALLISTFH 22 383 SNALNWREFSFIQST 18 71 PHVVDVTHHEDALTK 16 432 FVLALVLPSIVILDL 22 390 EFSFIQSTLGYVALL 18 103 DLRHLLVGKILIDVS 16 435 ALVLPSIVILDLLQL 22 405 ISTFHVLIYGWKRAF 18 111 KILIDVSNNMRINQY 16 20 NGINGIKDARKVTVG 21 410 VLIYGWKRAFEEEYY 18 126 PESNAEYLASLFPDS 16 117 SNNMRINQYPESNAE 21 423 YYRFYTPPNFVLALV 18 153 ALQLGPKDASRQVYI 16 161 ASRQVYICSNNIQAR 21 433 VLALVLPSIVILDLL 18 166 YICSNNIQARQQVIE 16 174 ARQQVIELARQLNFI 21 22 INGIKDARKVTVGVI 17 171 NIQARQQVIELARQL 16 277 AAAYQLYYGTKYRRF 21 29 RKVTVGVIGSGDFAK 17 175 RQQVIELARQLNFIP 16 373 LLAVTSIPSVSNALN 21 33 VGVIGSGDFAKSLTI 17 182 ARQLNFIPIDLGSLS 16 399 GYVALLISTFHVLIY 21 34 GVIGSGDFAKSLTIR 17 200 EIENLPLRLFTLWRG 16 407 TFHVLIYGWKRAFEE 21 44 SLTIRLIRCGYHVVI 17 208 LFTLWRGPVVVAISL 16 31 VTVGVIGSGDFAKSL 20 46 TIRLIRCGYIHVVIGS 17 219 AISLATFFFLYSFVR 16 142 IVKGFNVVSAWALQL 20 54 YHVVIGSRNPKFASE 17 225 FFFLYSFVRDVIHPY 16 209 FTLWRGPVVVAISLA 20 58 IGSRNPKFASEFFPH 17 263 AITLLSLVYLAGLLA 16 346 ENSWNEEEVWRIEMY 20 77 THHEDALTKTNIIFV 17 265 TLLSLVYLAGLLAAA 16 385 ALNWREFSFIQSTLG 20 87 NIIFVAIHREHYTSL 17 294 WLETWLQCRKQLGLL 16 235 WO 03/087306 PCT/USO3/10462 TableXLVI-V -HLA-DRB -0101- TabIcXLVI-V5A-HLA-DRB1- TableXLVI-V6-HLA-DRB -0101 15mers-98P4B6 0101-15mers-98P4B6 15mers-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: 3; each start position is specified, the 11; each start position is specified, the 13; each start position is specified, the length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and the end position for each peptide is the the end position for each peptide is the the end position for each peptide is the start position plus fourteen. start position plus fourteen, start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 304 QLGLLSFFFAMVHVA 16 10 PLRLFTFWRGPVVVA 16 18 ILFLPCISRKLKRIK 15 308 LSFFFAMVHVAYSLC 16 12 RLFTFWRGPVVVAIS 15 25 SRKLKRIKKGWEKSQ 15 310 FFFAMVHVAYSLCLP 16 2 SAREIENLPLRLFTF 14 30 RIKKGWEKSQFLEEG 14 314 MVHVAYSLCLPMRRS 16 7 ENLPLRLFTFWRGPV 14 43 EGIGGTIPHVSPERV 14 371 LSLLAVTSIPSVSNA 16 15 TFWRGPVVVAISLAT 14. 394 IQSTLGYVALLISTF 16 TableXLVI-V7A-HLA-DRB1 401 VALLISTFHVLIYGW 16 TableXLVI-V5B-HLA-DRB I- 0101-15mers-98P4B6 420 EEEYYRFYTPPNFVL 16 0101-15mers-98P4B6 Each peptide is a portion of SEQ ID 428 TPPNFVLALVLPSIV 16 Each peptide is a portion of SEQ ID NO: 15; each start position is specified, 440 SIVILDLLQLCRYPD 16 NO: 11; each start position is specified, the length of peptide is 15 amino acids, the length of peptide is 15 amino acids, and the end position for each peptide is TableXLVI-V2-HLA-DRBI-0101- and the end position for each peptide is the start position plus fourteen. 15mers-98P4B6 the start position plus fourteen. Pos 123456789012345 score Each peptide is a portion of SEQ ID Pos 123456789012345 score 12 SETFLPNGINGIKDA 21 NO: 5; each start position is specified, 7 WREFSFIQIFCSFAD 25 5 MGSPKSLSETFLPNG 18 the length of peptide is 15 amino acids, 9 EFSFIQIFCSFADTQ 24 1 SISMMGSPKSLSETF 16 and the end position for each peptide is 4 ALNWREFSFIQIFCS 20 4 MMGSPKSLSETFLPN 16 the start position plus fourteen. 2 SNALNWREFSFIQIF 18 6 GSPKSLSETFLPNGI 16 Pos 123456789012345 score 20 ADTQTELELEFVFLL 18 9 KSLSETFLPNGINGI 16 17 FTPFSCLSLPSSWDY 26 8 REFSFIQIFCSFADT 17 14 TFLPNGINGIKDARK 16 28 SWDYRCPPPCPADFF 26 10 FSFIQIFCSFADTQT 17 2 ISMMGSPKSLSETFL 14 6 LQALSLSLSSGFTPF 25 22 TQTELELEFVFLLTL 17 15 FLPNGINGIKDARKV 13 8 ALSLSLSSGFTPFSC 25 23 QTELELEFVFLLTLL 17 10 SLSETFLPNGINGIK 10 3 SPGLQALSLSLSSGF 24 12 FIQIFCSFADTQTEL 16 10 SLSLSSGFTPFSCLS 22 16 FCSFADTQTELELEF 16 TableXLVI-V7B-HLA-DRB1-0101 14 SSGFTPFSCLSLPSS 19 17 CSFADTQTELELEFV 14 15mers-98P4B6 26 PSSWDYRCPPPCPAD 16 Each peptide is a portion of SEQ ID NO: 31 YRCPPPCPADFFLYF 16 TabIeXLVI-V6-HLA-DRB-0101- 15; each start position is specified, the 1 SGSPGLQALSLSLSS 15 15mers-98P4B6 length of peptide is 15 amino acids, and 4 PGLQALSLSLSSGFT 15 Each peptide is a portion of SEQ ID NO: the end position for each peptide is the 20 FSCLSLPSSWDYRCP 15 13; each start position is specified, the start position plus fourteen. 2 GSPGLQALSLSLSSG 14 length of peptide is 15 amino acids, and Pos 123456789012345 score 7 QALSLSLSSGFTPFS 14 the end position for each peptide is the 4 RYLFLNMAYQQSTLG 24 13 LSSGFTPFSCLSLPS 14 start position plus fourteen. 14 QSTLGYVALLISTFH 22 16 GFTPFSCLSLPSSWD 14 Pos 123456789012345 score 7 FLNMAYQQSTLGYVA 21 19 PFSCLSLPSSWDYRC 14 1 NFVLALVLPSIVILG 29 2 SERYLFLNMAYQQST 19 27 SSWDYRCPPPCPADF 14 8 LPSIVILGKIILFLP 29 9 NMAYQQSTLGYVALL 18 30 DYRCPPPCPADFFLY 14 46 GGTIPHVSPERVTVM 28 3 ERYLFLNMAYQQSTL 17 17 IILFLPCISRKLKRI 26 11 AYQQSTLGYVALLIS 17 TableXLVI-V5A-HLA-DRB1- 11 IVILGKIILFLPCIS 24 10 MAYQQSTLGYVALLI 16 0101-15mers-98P4B6 38 SQFLEEGIGGTIPHV 24 13 QQSTLGYVALLISTF 16 Each peptide is a portion of SEQ ID NO: 39 QFLEEG[GGTIPHVS 24 8 LNMAYQQSTLGYVAL 14 11; each start position is specified, the 7 VLPSIVILGKIILFL 23 length of peptide is 15 amino acids, and 14 LGKIILFLPCISRKL 23 TabIeXLVI-V7C-HLA-DRB1-0101 the end position for each peptide is the 2 FVLALVLPSIVILGK 22 15mers-98P4B6 start position plus fourteen. 42 EEGIGGTIPHVSPER 22 Each peptide is a portion of SEQ ID NO: Pos 123456789012345 score 13 ILGKIILFLPCISRK 19 15; each start position is specified, the 11 LRLFTFWRGPVVVAI 28 3 VLALVLPSIVILGKI 18 length of peptide is 15 amino adds, and 3 AREIENLPLRLFTFW 25 6 LVLPSIVILGKIILF 18 the end position for each peptide is the 16 FWRGPVVVAISLATF 22 9 PSIVILGKIILFLPC 17 start position plus fourteen. 14 FTFWRGPVVVAISLA 20 15 GKILFLPCISRKLK 17 Pos 123456789012345 score 13 LFTFWRGPVVVAISL 18 5 ALVLPSIVILGKIIL 16 23 AAAWKCLGANILRGG 36 5 EIENLPLRLFTFWRG 16 10 SIVILGKHILFLPCI 16 168 SGTWMKLETIILSKL 35 236 WO 03/087306 PCT/USO3/10462 TableXLVI-V7C-HLA-DRBl-0101- TableXLVI-V8-HLA-DRBl-0101- length of peptide is 15 amino acids, and 15mers-98P4B6 15mers-98P4B6 the end position for each peptide is the Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: start position plus fourteen. 15; each start position is specified, the 17; each start position is specified, the Pos 123456789012345 score length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and 3 TIILSKLTQEQKTKH 18 the end position for each peptide is the the end position for each peptide is the 2 ETIILSKLTQEQKTK 14 start position plus fourteen, start position plus fourteen. 7 SKLTQEQKTKHCMFS 13 Pos 123456789012345 score Pos 123456789012345 score 6 LSKLTQEQKTKHCMF 11 138 EFLLRLLKSQAASGT 33 8 SQFLEEGMGGTIPHV 24 1 lQEQKTKHCMFSLISG 11 13 DLSVEVLASPAAAWK 30 9 QFLEEGMGGTIPHVS 24 1 LETIILSKLTQEQKT . 10 50 DRKIPPLSTPPPPAM 30 12 EEGMGGTIPHVSPER 22 9 LTQEQKTKHCMFSLI 10 28 CLGANILRGGLSEIV 28 13 EGMGGTIPHVSPERV 14 10 TQEQKTKHCMFSLIS 9 62 PAMWTEEAGATAEAQ 27 7 KSQFLEEGMGGTIPH 13 12 EQKTKHCMFSLISGS 9 110 ESPDRALKAANSWRN 26 2 KKGWEKSQFLEEGMG 12 5 ILSKLTQEQKTKHCM 8 124 NPVLPHTNGVGPLWE 26 6 EKSQFLEEGMGGTIP 12 8 KLTQEQKTKHCMFSL 8 141 LRLLKSQAASGTLSL 25 8 SIVILDLSVEVLASP 24 TableXLVI-V13-HLA-DRB1 31 ANILRGGLSEIVLPI 24 0101-15mers-98P4B6 TableXLVI-V25-HLA-DRB1-0101 42 VLPIEWQQDRKIPPL 24 Each peptide is a portion of SEQ ID 15mers-98P4B6 77 ESGIRNKSSSSSQIP 24 NO: 27; each start position is specified, Each peptide is a portion of SEQ ID NO: 130 TNGVGPLWEFLLRLL 24 the length of peptide is 15 amino adcids, 51; each start position is specified, the 137 WEFLLRLLKSQAASG 24 and the end position for each peptide is length of peptide is 15 amino acids, and 7 PSIVILDLSVEVLAS 23 the start position plus fourteen. the end position for each peptide is the 12 LDLSVEVLASPAAAW 23 Pos 123456789012345 score start position plus fourteen. 150 SGTLSLAFTSWSLGE 23 12 SETFLPNGINGIKDA 21 Pos 123456789012345 score 171 WMKLETIILSKLTQE 23 5 MGSPKSLSETFLPNG 18 6 IILFLPCISQKLKRI 25 3 ALVLPSIVILDLSVE 22 1 SISMMGSPKSLSETF 16 3 LGKIILFLPCISQKL 23 53 IPPLSTPPPPAMWTE 22 4 MMGSPKSLSETFLPN 16 2 ILGKIILFLPCISQK 19 157 FTSWSLGEFLGSGTW 22 6 GSPKSLSETFLPNGI 16 4 GKIILFLPCISQKLK 17 89 QLPVVGVVTEDDEAQ 21 9 KSLSETFLPNGINGI 16 7 ILFLPCISQKLKRIK 15 6 LPSIVILDLSVEVLA 20 14 TFLPNGINGIKDARK 16 9 FLPCISQKLKRIKKG 15 58 TPPPPAMWTEEAGAT 20 2 ISMMGSPKSLSETFL 14 14 SQKLKRIKKGWEKSQ 15 97 TEDDEAQDSIDPPES 20 15 FLPNGINGIKDARKV 13 15 QKLKRIKKGWEKSQF 13 100 DEAQDSIDPPESPDR 20 10 SLSETFLPNGINGIK 10 134 GPLWEFLLRLLKSQA 19 TableXLVII-V1-HLA-DRB 1-0301 154 SLAFTSWSLGEFLGS 19 TableXLVI-V14-HLA-DRBI-0101- 15mers-98P4B6 1 VLALVLPSIVILDLS 18 15mers-98P4B6 Each peptide is a portion of SEQ ID NO: 22 PAAAWKCLGANILRG 18 Each peptide is a portion of SEQ ID NO: 3; each start position is specified, the 44 PIEWQQDRKIPPLST 18 29; each start position is specified, the length of peptide is 15 amino acids, and 122 WRNPVLPHTNGVGPL 18 length of peptide is 15 amino acids, and the end position for each peptide is the 135 PLWEFLLRLLKSQAA 18 the end position for each peptide is the start position plus fourteen. 140 LLRLLKSQAASGTLS 18 start position plus fourteen. Pos 123456789012345 score 148 AASGTLSLAFTSWSL 18 Pos 123456789012345 score 97 HYTSLWDLRHLLVGK 28 159 SWSLGEFLGSGTWMK 18 10 LRLFTFWRGPVVVAI 28 176 QQVIELARQLNFIPI 27 161 SLGEFLGSGTWMKLE 18 2 AREIENLPLRLFTFW 25 228 LYSFVRDVIHPYARN 27 169 GTWMKLETIILSKLT 18 15 FWRGPVVVAISLATF 22 322 CLPMRRSERYLFLNM 27 176 TIILSKLTQEQKSKH 18 13 FTFWRGPVVVAISLA 20 54 YHVVIGSRNPKFASE 26 4 LVLPSIVILDLSVEV 17 12 LFTFWRGPVVVAISL 18 296 ETWLQCRKQLGLLSF 26 9 IVILDLSVEVLASPA 17 4 EIENLPLRLFTFWRG 16 408 FHVLIYGWKRAFEEE 26 30 GANILRGGLSEIVLP 17 9 PLRLFTFWRGPVVVA 16 273 AGLLAAAYQLYYGTK 25 61 PPAMWTEEAGATAEA 17 11 RLFTFWRGPVVVAIS 15 439 PSIVILDLLQLCRYP 25 67 EEAGATAEAQESGIR 17 1 SAREIENLPLRLFTF 14 109 VGKILIDVSNNMRIN 24 94 GVVTEDDEAQDSIDP 17 6 ENLPLRLFTFWRGPV 14 288 YRRFPPWLETWLQCR 24 101 EAQDSIDPPESPDRA 17 14 TFWRGPVVVAISLAT 14 87 NIIFVAlHREHYTSL 23 107 DPPESPDRALKAANS 17 8 LPLRLFTFWRGPVVV 12 423 YYRFYTPPNFVLALV 23 133 VGPLWEFLLRLLKSQ 17 133 LASLFPDSLIVKGFN 22 143 LLKSQAASGTLSLAF 17 185 LNFIPIDLGSLSSAR 22 162 LGEFLGSGTWMKLET 17 TableXLVI-V21-HLA-DRB1-0101- 261 IVAITLLSLVYLAGL 22 163 GEFLGSGTWMKLETI 17 15mers-98P4B6 272 LAGLLAAAYQLYYGT 22 172 MKLETILSKLTQEQ 17 Each peptide is a portion of SEQ ID NO: 433 VLALVLPSIVILDLL 22 143; each start position is specified, the 145 GFNVVSAWALQLGPK 21 237 WO 03/087306 PCT/US03/10462 TableXLVII-V 1-HLA-DRB 1-0301- TableXLVII-V1-HLA-DRB 1-0301- TableXLVII-V2-HLA-DR 1-0301 15mers-98P4B6 15mers-98P4B6 15mers-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: Each peptide is a porton of SEQ ID 3; each start position is specified, the 3; each start position is specified, the NO: 5; each start position is specified, length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and the length of peptide is 15 amino acids, the end position for each peptide is the the end position for each peptide is the and the end position for each peptide is start position plus fourteen. start position plus fourteen, the start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 214 GPVVVAISLATFFFL 21 327 RSERYLFLNMAYQQV 17 14 SSGFTPFSCLSLPSS 20 269 LVYLAGLLAAAYQLY 21 338 YQQVHANIENSWNEE 17 20 FSCLSLPSSWDYRCP 20 362 SFGIMSLGLLSLLAV 21 379 IPSVSNALNWREFSF 17 24 SLPSSWDYRCPPPCP 16 363 FGIMSLGLLSLLAVT 21 416 KRAFEEYYRFYTPP 17 2 GSPGLQALSLSLSSG 12 175 RQQVIELARQLNFIP 20 15 ETCLPNGINGIKDAR 16 3 SPGLQALSLSLSSGF 12 198 AREIENLPLRLFTLW 20 72 HVVDVTHHEDALTKT 16 8 ALSLSLSSGFTPFSC 12 258 TLPIVAITLLSLVYL 20 79 HEDALTKTNIIFVAI 16 9 LSLSLSSGFTPFSCL 12 264 ITLLSLVYLAGLLAA 20 88 IIFVAIHREHYTSLW 16 10 SLSLSSGFTPFSCLS 11 376 VTSIPSVSNALNWRE 20 111 KILIDVSNNMRINQY 16 22 CLSLPSSWDYRCPPP 11 400 YVALLISTFHVLIYG 20 205 PLRLFTLWRGPVVVA 16 30 DYRCPPPCPADFFLY 10 435 ALVLPSMILDLLQL 20 248 YKIPIEIVNKTLPIV 16 31 YRCPPPCPADFFLYF 10 438 LPSIVILDLLQLCRY 20 279 AYQLYYGTKYRRFPP 16 12 SLSSGFTPFSCLSLP 9 440 SIVILDLLQLCRYPD 20 342 HANIENSWNEEEVWR 16 17 FTPFSCLSLPSSWDY 9 30 KVTVGVIGSGDFAKS 19 382 VSNALNWREFSFIQS 16 53 GYHYVIGSRNPKFAS 19 413 YGWKRAFEEEYYRFY 16 110 GKILIDVSNNMRINQ 19 43 KSLTIRLIRCGYHVV 15 TableXLVII-V5A-HLA-DR1-0301 130 AEYLASLFPDSLIVK 19 263 AITLLSLVYLAGLLA 15 15mers-98P4B6 151 AWALQLGPKDASRQV 19 294 WLETWLQCRKQLGLL 15 Each peptide is a portion of SEQ ID NO: 215 PVVVAISLATFFFLY 19 321 LCLPMRRSERYLFLN 15 11; each start position is specified, the 217 VVAISLATFFFLYSF 19 367 SLGLLSLLAVTSIPS 15 length of peptide is 15 amino acids, and 256 NKTLPIVAITLLSLV 19 387 NWREFSFIQSTLGYV 15 the end position for each peptide is the 312 FAMVHVAYSLCLPMR 19 412 IYGWKRAFEEEYYRF 15 - start position plus fourteen. 320 SLCLPMRRSERYLFL 19 73 VVDVTHHEDALTKTN 14 Pos 123456789012345 score 402 ALLISTFHVLIYGWK 19 104 LRHLLVGKILIDVSN 14 3 AREIENLPLRLFTFW 20 3 SISMMGSPKSLSETC 18 236 IHPYARNQQSDFYKI 14 10 PLRLFTFWRGPVVVA 16 22 INGIKDARKVTVGVI 18 267 LSLVYLAGLLAAAYQ 14 2 SAREIENLPLRLFTF 12 34 GVIGSGDFAKSLTIR 18 304 QLGLLSFFFAMVHVA 14 6 IENLPLRLFTFWRGP 12 90 FVAIHREHYTSLWDL 18 365 IMSLGLLSLLAVTSI 14 8 NLPLRLFTFWRGPVV 12 119 NMRINQYPESNAEYL 18 373 LLAVTSIPSVSNALN 14 5 EIENLPLRLFTFWRG 11 139 DSLIVKGFNVVSAWA 18 401 VALLISTFHVLIYGW 14 13 LFTFWRGPVVVAISL 10 143 VKGFNVVSAWALQLG 18 434 LALVLPSIVILDLLQ 14 4 REIENLPLRLFTFWR 9 162 SRQVYICSNNIQARQ 18 1 MESISMMGSPKSLSE 1 11 LRLFTFWRGPVVVAI 9 184 QLNFIPIDLGSLSSA 18 4 ISMMGSPKSLSETCL 13 195 LSSAREIENLPLRLF 18 32 TVGVIGSGDFAKSLT 13 TabIeXLVII-VSB-HLA-DRI 233 RDVIHPYARNQQSDF 18 33 VGVIGSGDFAKSLTI 13 0301-15mers-98P4B6 308 LSFFFAMVHVAYSLC 18 101 LWDLRHLLVGKILID 13, Each peptide is a portion of SEQ ID 331 YLFLNMAYQQVHANI 18 138 PDSLIVKGFNVVSAW 13 NO: 11; each start position is specified, 360 YISFGIMSLGLLSLL 18 164 QVYICSNNIQARQQV 13 the length of peptide is 15 amino acids, 3 6 0 _ _ _ _ _ _ _ _ _ _ _ _ _ _ __ _ a n d th e e n d p o s itio n f o r e a c h p e p t id e is 409 HVLIYGWKRAFEEEY 18 189 PIDLGSLSSAREIEN 13 and the staendrt position plus for each peptide in. 7 MGSPKSLSETCLPNG 17 201 IENLPLRLFTLWRGP 13 the start position plus fourteen. 21 GINGIKDARKVTVGV 17 213 RGPVVVAISLATFFF 13' s I2357 4 38 SGDFAKSLTIRLIRC 17 266 LLSLVYLAGLLAAAY 13 15 ICSFADTTELELE 24 113 LIDVSNNMRINQYPE 17 407 TFHVLIYGWKRAFEE 1 3 QTELELEFVFLLTLL 20 121 RINQYPESNAEYLAS 17 1 VSNALNWREFSFIQI 161 155 QLGPKDASRQVYICS 17 TableXLVII-V2-HLA-DRI-0301- 19 FADTQTELELEFVFL 16 169 SNNIQARQQVIELAR 17 15mers-98P4B6 21 DTQTELELEFVFLLT 16 178 VIELARQLNFIPIDL 17 Each peptide is a portion of SEQ ID 17 CSFADTQTELELEFV 15 192 LGSLSSAREIENLPL 17 NO: 5; each start position is specified, 22 TQTELELEFVFLLTL 13 225 FFFLYSFVRDVIHPY 17 the length of peptide is 15 amino acids, 2 SNALNWREFSFIQIF 11 249 KIPIEIVNKTLPIVA 17 and the end position for each peptide is 10 FSFIQIFCSFADTQT 11 292 PPWLETWLQCRKQLG 17 the start position plus fourteen. 318 AYSLCLPMRRSERYL 17 Pos 123456789012345 score TableXLVII-V6-HLA-DRI-0301 SLQALSLSLSSGFTPF 20 15mers-98P4B6 238 WO 03/087306 PCT/USO3/10462 Each peptide is a portion of SEQ ID NO: 15mers-98P4B6 TableXLVII-V13-HLA-DR1-0301 13; each start position is specified, the Each peptide is a portion of SEQ ID NO: 15mers-98P4B6 length of peptide is 15 amino acids, and 15; each start position is specified, the Each peptide is a portion of SEQ ID the end position for each peptide is the length of peptide is 15 amino acids, and NO: 27; each start position is specified, start position plus fourteen. the end position for each peptide is the the length of peptide is 15 amino acids, Pos 123456789012345 score start position plus fourteen, and the end position for each peptide is 8 LPSIVILGKIILFLP 26 Pos 123456789012345 score the start position plus fourteen. 3 VLALVLPSIVILGKI 22 93 VGVVTEDDEAQDSID 29 Pos 123456789012345 score 9 PS1VILGKIILFLPC 22 130 TNGVGPLWEFLLRLL 26 13 ETFLPNGINGIKDAR 16 10 SIVILGKITLFLPCI 21 7 PSIVILDLSVEVLAS 24 2 ISMMGSPKSLSETFL 13 17 IILFLPCISRKLKRI 20 1 VLALVLPSIVILDLS 22 12 SETFLPNGINGIKDA 13 18 ILFLPCISRKLKRIK 18 8 SIVILDLSVEVLASP 21 8 PKSLSETFLPNGING 12 25 SRKLKRIKKGWEKSQ 18 133 VGPLWEFLLRLLKSQ 21 4 MMGSPKSLSETFLPN 9 21 LPCISRKLKRIKKGW 17 3 ALVLPSIVILDLSVE 20 10 SLSETFLPNGINGIK 8 28 LKRIKKGWEKSQFLE 17 163 GEFLGSGTWMKLETI 20 29 KRIKKGWEKSQFLEE 16 9 IVILDLSVEVLASPA 19 TableXLVII-V14-HLA-DR1-0301 4 LALVLPSIVILGKII 14 123 RNPVLPHTNGVGPLW 19 15mers-98P4B6 14 LGKIILFLPCISRKL 13 137 WEFLLRLLKSQAASG 19 Each peptide is a portion of SEQ ID NO: 15 GKILFLPCISRKLK 13 154 SLAFTSWSLGEFLGS 19 29; each start position is specified, the 1 NFVLALVLPSIVILG 12 171 WMKLETIILSKLTQE 19 length of peptide is 15 amino acids, and 5 ALVLPSIVILGKIIL 12 38 LSEIVLPIEWQQDRK 18 the end position for each peptide is the 37 KSQFLEEGIGGTIPH 12 179 LSKLTQEQKSKHCMF 18 start position plus fourteen. 40 EIVLPIEWQQDRKIP 17 Pos 123456789012345 score TableXLVII-V7A-HLA-DR1-0301 44 PIEWOOQQDRKIPPLST 16 2 AREIENLPLRLFTFW 20 15mcrs-98P4B6 90 IPVVGVVTEDDEAQD 16 9 PLRLFTFWRGPVVVA 16 Each peptide is a portion of SEQ ID 176 TIILSKLTQEQKSKH 16 1 SAREIENLPLRLFTF 12 NO: 15; each start position is specified, 15 SVEVLASPAAAWKCL 15 5 IENLPLRLFTFWRGP 12 the length of peptide is 15 amino acids, 27 KCLGANILRGGLSEI 15 7 NLPLRLFTFWRGPVV 12 and the end position for each peptide is 32 NILRGGLSEIVLPIE 15 4 EIENLPLRLFTFWRG 1 the start position plus fourteen. 39 SEIVLPIEWQQDRKI 15 12 LFTFWRGPVVVAISL 10 Pos 123456789012345 score 116 LKAANSWRNPVLPHT 15 3 REIENLPLRLFTFWR 9 I SISMMGSPKSLSETF 18 138 EFLLRLLKSQAASGT 15 10 LRLFTFWRGPVVVAI 9 5 MGSPKSLSETFLPNG 17 175 ETIILSKLTQEQKSK 15 13 ETFLPNGINGIKDAR 16 2 LALVLPS1VILDLSV 14 TableXLVII-V21-HLA-DR1-0301 2 ISMMGSPKSLSETFL 13 15mers-98P4B6 12 SETFLPNGNGIKDA 13 TableXLVII-V8-HLA-DR1-0301- Each peptide is a portion of SEQ ID NO: 8 PKSLSETFLPNGING 12 15mers-98P4B6 43; each start position is specified, the 4 MMGSPKSLSETFLPN 9 Each peptide is a portion of SEQ ID NO: length of peptide is 15 amino acids, and 10 SLSETFLPNGINGIK 8 17; each start position is specified, the the end position for each peptide is the length of peptide is 15 amino acids, and start position plus fourteen. TableXLVII-V7B-HLA-DR1-0301- the end position for each peptide is the Pos 123456789012345 score 15mers-98P4B6 start position plus fourteen. 6 LSKLTQEQKTKHCMF 18 Each peptide is a portion of SEQ ID NO: Pos 123456789012345 score 3 TIILSKLTQEQKTKH 16 15; each start position is specified, the 7 KSQFLEEGMGGTIPH 12 2 ETIILSKLTQEQKTK 15 length of peptide is 15 amino acids, and 8 SQFLEEGMGGTIPHV 11 1 LETILSKLTQEQKT 13 the end position for each peptide is the 12 EEGMGGTIPHVSPER 10 _ 4 IILSKLTQEQKTKHC 10 start position plus fourteen. 1 IKKGWEKSQFLEEGM 9 5 ILSKLTQEQKTKHCM 9 Pos 123456789012345 score 4 GWEKSQFLEEGMGGT 7 9 LTQEQKTKHCMFSLI 9 YLFLNMAYQQSTLGY 19 5 YLFLNMAYQQSTLGY 18 5 WEKSQFLEEGMGGTI 7 11 QEQKTKHCMFSLISG 9 1 RSERYLFLNMAYQQS 17 6 LFLNMAYQQSTLGYV 14 TableXLVII-V25-HLA-DRI -0301 12 YQQSTLGYVALLIST 12 TableXLVII-V 13-HLA-DR1-0301- 15mers-98P4B6 3 ERYLFLNMAYQQSTL 11 15mers-98P4B6 Each peptide is a portion of SEQ ID NO: 4 RYLFLNMAYQQSTLG 11 Each peptide is a portion of SEQ ID 51; each start position is specified, the 7 FLNMAYQQSTLGYVA 1 1 NO: 27; each start position is specified, length of peptide is 15 amino acids, and 11 AYQQSTLGYVALLIS 11 the length of peptide is 15 amino acids, the end position for each peptide is the 14 QSTLGYVALLISTFII 11 and the end position for each peptide is start position plus fourteen. 8 LNMAYQQSTLGYVAL 10 the start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score 6 IILFLPCISQKLKRI 21 1 SISMMGSPKSLSETF 18 7 ILFLPCISQKLKRIK 18 TableXLVII-V7C-HLA-DR1-0301- 5 MGSPKSLSETFLPNG 17 14 SQKLKRIKKGWEKSQ 18 239 WO 03/087306 PCT/USO3/10462 TableXLVII-V25-HLA-DR1-0301- TableXLVIII-V 1-HLA-DR1-0401- TableXLVIII-V1-HLA-DR1-0401 15mers-98P4B6 15mers-98P4B6 15mers-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: 51; each start position is specified, the 3; each start position is specified, the 3; each start position is specified, the length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and the end position for each peptide is the the end position for each peptide is the the end position for each peptide is the start position plus fourteen. start position plus fourteen, start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 10 LPCISQKLKRIKKGW 17 86 TNIIFVAIHREHYTS 20 142 IVKGFNVVSAWALQL 18 3 LGKIILFLPCISQKL 13 90 FVAIHREHYTSLWDL 20 154 LQLGPKDASRQVYIC 18 4 GKIILFLPCISQKLK 13 101 LWDLRHLLVGKILID 20 161 ASRQVYICSNNIQAR 18 5 KIILFLPCISQKLKR 11 106 HLLVGKILIDVSNNM 20 168 CSNNIQARQQVIELA 18 110 GKILIDVSNNMRINQ 20 186 NFIPIDLGSLSSARE 18 TableXLVIII-V1-HLA-DRl-0401- 111 KILIDVSNNMRINQY 20 195 LSSAREIENLPLRLF 18 15mers-98P4B6 113 LIDVSNNMRINQYPE 20 234 DVIHPYARNQQSDFY 18 Each peptide is a portion of SEQ ID NO: 130 AEYLASLFPDSLIVK 20 248 YKIPIEIVNKTLPLV 18 3; each start position is specified, the 133 LASLFPDSLIVKGFN 20 257 KTLPIVAITLLSLVY 18 length of peptide is 15 amino acids, and 139 DSLIVKGFNVVSAWA 20 289 RRFPPWLETWLQCRK 18 the end position for each peptide is the 140 SLIVKGFNVVSAWAL 20 339 QQVHANIENSWNEEE 18 start position plus fourteen. 145 GFNVVSAWALQLGPK 20 3481 SWNEEEVWRIEMYIS 18 Pos 123456789012345 score 162 SRQVYICSNNIQARQ 20 359 MYISFGIMSLGLLSL 18 420 EEEYYRFYTPPNFVL 28 176 QQVIELARQLNFIP1 20 364 GIMSLGLLSLLAVTS 18 98 YTSLWDLRHLLVGKI 26 185 LNFIPIDLGSLSSAR 20 384 NALNWREFSFIQSTL 18 109 VGKILIDVSNNMRIN 26 189 PIDLGSLSSAREIEN 20 387 NWREFSFIQSTLGYV 18 175 RQQVIELARQLNFIP 26 192 LGSLSSAREIENLPL 20 399 GYVALLISTFHVLIY 18 205 PLRLFTLWRGPVVVA 26 217 VVAISLATFFFLYSF 20 432 FVLALVLPSIVILDL 18 213 RGPVVVAISLATFFF 26 219 AISLATFFFLYSFVR 20 66 ASEFFPHVVDVTHHE 16 225 FFFLYSFVRDVlHPY 26 233 RDVIHPYARNQQSDF 20 67 SEFFPHVVDVTHHED 16 229 YSFVRDVIHPYARNQ 26 247 FYKIPIEIVNKTLPI 20 95 REHYTSLWDLRHLLV 16 312 FAMVHVAYSLCLPMR 26 256 NKTLPIVAITLLSLV 20 122 INQYPESNAEYLASL 16 370 LLSLLAVTSIPSVSN 26 258 TLPIVAITLLSLVYL 20 129 NAEYLASLFPDSLIV 16 373 LLAVTSIPSVSNALN 26 261 IVAITLLSLVYLAGL 20 206 LRLFTLWRGPVVVAI 16 376 VTSIPSVSNALNWRE 26 264 ITLLSLVYLAGLLAA 20 209 FTLWRGPVVVAISLA 16 38 SGDFAKSLTIRLIRC 22 266 LLSLVYLAGLLAAAY 20 224 TFFFLYSFVRDVIHP 16 51 RCGYHVVIGSRNPKF 22 267 LSLVYLAGLLAAAYQ 20 226 FFLYSFVRDVIHPYA 16 62 NPKFASEFFPHVVDV 22 273 AGLLAAAYQLYYGTK 20 228 LYSFVRDVIHPYARN 16 87 NIIFVAIHREHYTSL 22 292 PPWLETWLQCRKQLG 20 236 IHPYARNQQSDFYKI 16 143 VKGFNVVSAWALQLG 22 302 RKQLGLLSFFFAMVH 20 245 SDFYKIPIEIVNKTL 16 163 RQVYICSNNIQARQQ 22 304 QLGLLSFFFAMVHVA 20 268 SLVYLAGLLAAAYQL 16 184 QLNFIPIDLGSLSSA 22 331 YLFLNMAYQQVHANI 20 285 GTKYRRFPPWLETWL 16 222 LATFFFLYSFVRDVI 22 351 EEEVWRIEMYISFGI 20 288 YRRFPPWLETWLQCR 16 244 QSDFYKIPIEIVNKT 22 354 VWRIEMYISFGIMSL 20 308 LSFFFAMVHjVAYSLC 16 307 LLSFFFAMVHVAYSL 22 362 SFGIMSLGLLSLLAV 20 330 RYLFLNMAYQQVHAN 16 309 SFFFAMVHVAYSLCL 22 365 IMSLGLLSLLAVTSI 20 335 NMAYQQVHANIENSW 16 328 SERYLFLNMAYQQVH 22 367 SLGLLSLLAVTSIPS 20 352- EEVWRIEMYISFGIM 16 346 ENSWNEEEVWRIEMY 22 368 LGLLSLLAVTSIPSV 20 360 YISFGIMSLGLLSLL 16 357 IEMYISFGIMSLGLL 22 379 IPSVSNALNWREFSF 20 390 EFSFIQSTLGYVALL 16 385 ALNWREFSFIQSTLG 221 395 QSTLGYVALLISTFH 20 397 TLGYVALLISTFHVL 16 388 WREFSFIQSTLGYVA 22 398 LGYVALLISTFHVLI 20 412 IYGWKRAFEEEYYRF 16 405 ISTFHVLIYGWKRAF 22 401 VALLISTFHVLIYGW 20 416 KRAFEEEYYRFYTPP 16 423 YYRFYTPPNFVLALV 22 430 PNFVLALVLPS1VIL 20 424 YRFYTPPNFVLALVL 16 429 PPNFVLALVLPSIVI 22 431 NFVLALVLPSIVILD 20 296 ETWLQCRKQLGLLSF 15 I MESISMMGSPKSLSE 20 435 ALVLPSIVILDLLQL 20 3 SISMMGSPKSLSETC 14 15 ETCLPNGINGIKDAR 20 438 LPSIVILDLLQLCRY 20 4 ISMMGSPKSLSETCL 14 19 PNGINGIKDARKVTV 20 440 SIVILDLLQLCRYPD 20 32 TVGVIGSGDFAKSLT 14 22 INGIKDARKVTVGVI 20 12 SLSETCLPNGINGIK 18 33 VGVIGSGDFAKSLTI 14 30 KVTVGVIGSGDFAKS 20 21 GINGIKDARKVTVGV 18 44 SLTIRLIRCGYHVVI 14 47 IRLIRCGYHVVIGSR 20 36 IGSGDFAKSLTIRLI 18 46 TIRLIRCGYHVVIGS 14 53 GYHVVIGSRNPKFAS 20 176 VTHHEDALTKTNIIF 18 54 YHVVIGSRNPKFASE 14 70 FPHVVDVTHHEDALT 20 7 HYTSLWDLRHLLVGK ' 18 73 VVDVTHHEDALTKTN 14 71 PHVVDVTHHEDALTK 20 240 WO 03/087306 PCT/USO3/10462 TableXLVIII-V1-HLA-DRI -0401- TableXLVIII-VSA-HLA-DRB 1- TableXLVIII-V6-HLA-DRB1 15mers-98P4B6 0401-15mers-98P4B6 0401-15mers-98P4B6 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID NO: 3; each start position is specified, the NO: 11; each start position is specified, 13; each start position is specified, the length of peptide is 15 amino acids, and the length of peptide is 15 amino acids, length of peptide is 15 amino acids, and the end position for each peptide is the and the end position for each peptide is the end position for each peptide is the start position plus fourteen, the start position plus fourteen, start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 80 EDALTKTNIIFVAIH 14 28 SWDYRCPPPCPADFF 16 11 IVILGKIILFLPCIS 14 85 KTNIIFVAIHREHYT 14 6 LQALSLSLSSGFTPF 14 15 GKIILFLPCISRKLK 14 88 IIFVAIHREHYTSLWV 14 20 FSCLSLPSSWDYRCP 14 16 KIILFLPCISRKLKR 14 117 SNNMRINQYPESNAE 14 4 PGLQALSLSLSSGFT 12 25 SRKLKRIKKGWEKSQ 14 119 NMRINQYPESNAEYL 14 13 LSSGFTPFSCLSLPS 12 28 LKRIKKGWEKSQFLE 14 151 AWALQLGPKDASRQV 14 16 GFTPFSCLSLPSSWD 12 38 SQFLEEGIGGTIPHV 14 178 VIELARQLNFIPIDL 14 19 PFSCLSLPSSWDyRC 12 42 EEGIGGTIPHVSPER 14 182 ARQLNFIPIDLGSLS 14 24 SLPSSWDYRCPPPCP 12 6 LVLPSIVILGKIILF 12 187 FIPIDLGSLSSAREI 14 7 VLPSIVILGKIILFL 12 198 AREIENLPLRLFTLW 14 TableXLVIII-V5B-HLA-DRBl- 13 ILGKIILFLPCISRK 12 203 NLPLRLFTLWRGPVV 14 0401-15mers-98P4B6 34 GWEKSQFLEEGIGGT 12 208 LF.TLWRGPVVVAISL 14 Each peptide is a portion of SEQ ID 43 EGIGGTIPHVSPERV 12 214 GPVVVAISLATFFFL 14 NO: 11; each start position is specified, 232 VRDVIHPYARNQQSD 14 the length of peptide is 15 amino acids, 249 KIPIEIVNKTLPIVA 14 and the end position for each peptide is TableXLVIl-V7A-HLA-DRBl 252 IEIVNKTLPIVAITL 14 the start position plus fourteen. 0401-15mers-98P4B6 259 LPIVAITLLSLVYLA 14 Pos 123456789012345 score Each peptide is a portion of SEQ ID 263 AITLLSLVYLAGLLA 14 4 ALNWREFSFIQIFCS 22 NO: 15; each start position is specified, 269 LVYLAGLLAAAYQLY 14 7 WREFSFIQIFCSFAD 22 the length of peptide is 15 amino acids, 272 LAGLLAAAYQLYYGT 14 9 EFSFIQIFCSFADTQ 22 and the end position for each peptide is 305 LGLLSFFFAMVHVAY 14 13 IQIFCSFADTQT'ELE 22 the start position plus fourteen. 311 FFAMVHVAYSLCLPM 14 10 FSFIQIFCSFADTQT 20 Pos 123456789012345 score 314 MVHVAYSLCLPMRRS 14 23 QTELELEFVFLLTLL 20 13 ETFLPNGINGIKDAR 20 318 AYSLCLPvMRRSERYL 14 3 NALNWREFSFIQIFC 18 10 SLSETFLPNGINGIK 18 322 CLPMRRSERYLFLNM 14 15 IFCSFADTQTELELE 18 12 SETFLPNGINGIKDA 16 329 ERYLFLNMAYQQVHA 14 16 FCSFADTQTELELEF 16 1 SISMMGSPKSLSETF 14 333 FLNMAYQQVHANIEN 14 12 FIQIFCSFADTQTEL 14 2 ISMMGSPKSLSETFL 14 342 HANIENSWNEEEVWR 14 6 NWREFSFIQIFCSFA 12 5 MGSPKSLSETFLPNG 12 356 RIEMYISFGIMSLGL 14 14 QIFCSFADTQTELEL 12 7 SPKSLSETFLPNGIN 12 363 FGLMSLGLLSLLAVT 14 20 ADTQTELELEFVFLL 12 9 KSLSETFLPNGINGI 12 371 LSLLAVTSIPSVSNA 14 22 TQTELELEFVFLLTL 12 391 FSFIQSTLGYVALLI 14 24 TELELEFVFLLTLLL 12 TableXLVIII-V7B-HLA-DRB1 400 YVALLISTFHVLIYG 14 0401-15mers-98P4B6 402 ALLISTFHVLIYGWK 14 TableXLVIII-V6-HLA-DRB1- Each peptide is a portion of SEQ ID NO: 407 TFHVLIYGWKRAFEE 14 .0401-15mers-98P4B6 15; each start position is specified, the 409 HVLIYGWKRAFEEEY 14 Each peptide is a portion of SEQ ID NO: length of peptide is 15 amino acids, and 433 VLALVLPSIVILDLL 14 13; each start position is specified, the the end position for each peptide is the 439 PSIVILDLLQLCRYP 14 length of peptide is 15 amino acids, and start position plus fourteen. M I A the end position for each peptide is the Pos 123456789012345 score TableXLVIII-V5A-HLA-DRB 1- start position plus fourteen. 5 YLFLNMAYQQSTLGY 26 0401-15mers-98P4B6 Pos 123456789012345 score 2 SERYLFLNMAYQQST 22 Each peptide is a portion of SEQ ID 18 ILFLPCISRKLKRIK 26 14 QSTLGYVALLISTFH 20 NO: 11; each start position is specified, 17 IILFLPCISRKLKRI 22 4 RYLFLNMAYQQSTLG 16 the length of peptide is 15 amino acids, 37 KSQFLEEGIGGTIPH 22 9 NMAYQQSTLGYVALL 16 and the end position for each peptide is 1 NFVLALVLPSIVILG 20 3 ERYLFLNMAYQQSTL 14 the start position plus fourteen. 5 ALVLPSIVILGKIIL 20 7 FLNMAYQQSTLGYVA 14 Pos 123456789012345 score 8 LPSIVILGKIILFLP 20 1 RSERYLFLNMAYQQS 12 14 SSGFTPFSCLSLPSS 22 14 LGKIILFLPCISRKL 20 6 LFLNMAYQQSTLGYV 12 17 FTPFSCLSLPSSWDY 22 46 GGTIPHVSPERVTVM 20 11 AYQQSTLGYVALLIS 12 3 SPGLQALSLSLSSGF 20 2 FVLALVLPSIVILGK 18 15 STLGYVALLISTFHV 12 10 SLSLSSGFTPFSCLS 20 22 PCISRKLKRIKKGWE 18 2 GSPGLQALSLSLSSG 18 30 RIKKGWEKSQFLEEG 18 TableXLVIII-V7C-HLA-DRBl 7 QALSLSLSSGFTPFS 18 3. VLALVLPSMILGKI 14 0401-15mers-98P4B6 241 WO 03/087306 PCT/USO3/10462 Each peptide is a portion of SEQ ID NO: TableXLVIII-V7C-HLA-DRBl1- TableXLVIII-V21-HLA-DRBl 15; each start position is specified, the 04 0 1-15mers-98P4B6 0401-15mers-98P4B6 length of peptide is 15 amino acids, and Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: the end position for each peptide is the 15; each start position is specified, the 43; each start position is specified, the start position plus fourteen. length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and Pos 123456789012345 score the end position for each peptide is the the end position for each peptide is the 134 GPLWEFLLRLLKSQA 28 start position plus fourteen, start position plus fourteen. 168 SGTWMKLETIILSKL 28 Pos 123456789012345 score Pos 123456789012345 score 7 PSIVILDLSVEVLAS 26 179 LSKLTQEQKSKHCMF 14 3 TIILSKLTQEQKTKH 26 13 DLSVEVLASPAAAWK 26 2 ETIILSKLTQEQKTK 15 113 DRALKAANSWRNPVL 26 TableXLVIII-V8-HLA-DRBI-0401- 6 LSKLTQEQKTKHCMF 14 138 EFLLRLLKSQAASGT 26 15mers-98P4B6 5 1LSKLTQEQKTKHCM 12 150 SGTLSLAFTSWSLGE 26 Each peptide is a portion of SEQ ID NO: 176 TIILSKLTQEQKSKH 26 17; each start position is specified, the TableXLVIII-V25-HLA-DRB1 23 AAAWKCLGANILRGG 22 length of peptide is 15 amino acids, and 0401-15mers-98P4B6 62 PAMWTEEAGATAEAQ 22 the end position for each peptide is the Each peptide is a portion of SEQ ID NO: 162 LGEFLGSGTWVMKLET 22 start position plus fourteen. 51; each start position is specified, the 3 ALVLPSMVILDLSVE 20 Pos 123456789012345 score length of peptide is 15 amino acids, and 8 SIVILDLSVEVLASP 20 7 KSQFLEEGMGGTIPH 22 the end position for each peptide is the 31 ANILRGGLSEIVLPI 20 8 SQFLEEGMGGTIPHV 14 start position plus fourteen. 40 EIVLPIEWQQDRKIP 20 12 EEGMGGTIPHVSPER 14 Pos 123456789012345 score 50 DRKIPPLSTPPPPAM 20 4 GWEKSQFLEEGMGGT 12 7 ILFLPCISQKLKRIK 26 61 PPAMWTEEAGATAEA 20 13 EGMGGTIPHVSPERV , 12 6 IILFLPCISQKLKRI 22 89 QPVVGVVTEDDEAQ 20 2 KKGWEKSQFLEEGMG 10 3 LGKIILFLPCISQKL 20 92 VVGVVTEDDEAQDSI 20 4 GKIILFLPCISQKLK 20 130 TNGVGPLWEFLLRLL 20 TabIeXLVIII-V13-HLA-DRB1- 11 PCISQKLKRIKKGWE 18 133 VGPLWEFLLRLLKSQ 20 0401-15mers-98P4B6 5 KIILFLPCISQKLKR 14 137 WEFLLRLLKSQAASG 20 Each peptide is a portion of SEQ ID 14 SQKLKRIKKGWEKSQ 14 159 SWSLGEFLGSGTWMK 20 NO: 27; each start position is specified, 2 ILGKIILFLPCISQK 12 169 GTWMKLETIILSKLT 20 the length of peptide is 15 amino acids, 171 WMKLETIILSKLTQE 20 and the end position for each peptide is 27 KCLGANILRGGLSE 18 the start position plus fourteen. TableXLIX-VI-HLA-DRBI-1101 74 EAQESGINKSSSSS 18 Pos 123456789012345 score 15mers-98P4B6 95 VTEDDEAQDSIDPP 18 13 ETFLPNGINGIKDAR 20 Each peptide is a portion of SEQ ID NO: 95 VVTEDDEAQDSIDPP 18 142 RLLKSQAASGTLSLA 18 10 SLSETFLPNGINGIK 18 3; each start position is specified, the 151 GTLSLAFTSWSLGEF 18 12 SETFLPNGINGIKDA 16 length of peptide is 15 amino acids, and 172 MKLETIILSKLTQEQ 18 1 SISMMGSPKSLSETF 14 the end position for each peptide is the 44 PIEWQQDRKIPPLST 16 2 ISMMGSPKSLSETFL 14 start position plus fourteen. 119 ANSWRNPVLPHTNGV 16 5 MGSPKSLSETFLPNG 12 Pos 123456789012345 score 157 FTSWSLGEFLGSGTW 16 7 SPKSLSETFLPNGIN 12 249 KIPIEIVNKTLPIVA 27 77 ESGIRNKSSSSSQIP 15 9 KSLSETFLPNGINGI 12 308 LSFFFAMVHVAYSLC 27 175 E LSKLTQEQKSK 15 229 YSFVRDVIHPYARNQ 26 1 VLALVLPSIVILDLS 14 TableXLVIII-V14-HLA-DRB1- 281 QLYYGTKYRRFPPWL 25 6 VLALVLPSIVI LDLSVEVLA 14 0401-15mers-98P4B6 295 LETWLQCRKQLGLLS 25 6 LSIVILDLSVEVLSPA 14 Each peptide is a portion of SEQ ID NO: 87 NIIFVAIHREHYTSL 24 9 IVILDLSVEVLASPA 14 29; each start position is specified, the 388 WREFSFIQSTLGYVA 23 11 ILDLSVEVLASPAAA 14 length of peptide is 15 amino acids, and 309 SFFFAMVHVAYSLCL 22 161 VEVLASPAAAWKCLG 14 the end position for each peptide is the 3 SISMMGSPKSLSETC 21 30 GANILRGGLSEIVLP 14 start position plus fourteen 71 PHVVDVTHHEDALTK 21 35 RGGLSIVLPIEWQQ 14 Pos 123456789012345 score 98 YTSLWDLRHLLVG 21 38 LSEIVLPIEWQQDRK 14 9 PLRLFTFWRGPVVVA 26 175 RQQVIELARQLNFIP 21 39 SEIVLPIEWQQDRKI 14 10 LRLFTFWRGPVVVAI 16 205 PLRLFTLWRGPVVVA 21 42 VLPIEWQQDRKIPPL 14 12 LFTFWRGPVVVAISL 16 70 FPHVVDVTHHEDALT 20 53 IPPLSTPPPPAMWTE 14 13 F1TWRGPVVVAISLA 16 95 REHYTSLWDLRHLLV 20 87 SSQIPVVGVVTEDDE 14 2 AREIENLPLRLFTFW 14 151 AWALQLGPKDASRQV 20 90 IPWVVGVVTEDDEAQD 14 7 NLPLRLFTFWRGPVV 14 263 AITLLSLVYLAGLLA 20 93 VGVVIEDDEAQDSID 14 3 REIENLPLRLFTFWR 12 1 MESISMMGSPKSLSE 19 103 QDSIDPPESPDRALK 14 6 ENLPLRLFTFWRGPV 12 51 RCGYVVIGSRNPKF 19 123 RNPVLPHTNGVGPLW 14 14 TFWRGPVVVAISLAT 12 106 HLLVGKILIDVSNNM 19 141 LRLLKSQAASGTLSL 14 15 FWRGPVVVAISLATF 12 182 ARQLNFIPIDLGSLS 19 163 GEFLGSGTWMKL 14 266 LLSLVYLAGLLAAAY 19 242 WO 03/087306 PCT/US03/10462 TableXLIX-VI-HLA-DRB 1-1101- TabIcXLIX-V1-HLA-DRBI -1101 15mers-98P4B6 15mers-98P4B6 TablIeXLIX-V5A-HLA-DRB 1 Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: 1101-15mers-98P4B6 3; each start position is specified, the 3; each start position is specified, the Each peptide is a portion of SEQ ID NO: length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and 11; each start position is specified, the the end position for each peptide is the the end position for each peptide is the length of peptide is 15 amino acids, and start position plus fourteen, start position plus fourteen, the end position for each peptide is the Pos 123456789012345 score Pos 123456789012345 score start position plus fourteen. 351 EEEVWRIEMYISFGI 19 89 IFVAIHREHYTSLWD 14 Pos 123456789012345 score 395 QSTLGYVALLISTFH 19 113 LIDVSNNMRINQYPE 14 13 LFTFWRGPVVVAISL 17 424 YRFYTPPNFVLALVL 19 189 PIDLGSLSSAREIEN 14 10 PLRLFTFWRGPVVVA 15 67 SEFFPHVVDVTHHED 18 198 AREIENLPLRLFTLW 14 15 TFWRGPVVVAISLAT 15 222 LATFFFLYSFVRDVI 18 203 NLPLRLFTLWRGPVV 14 3 AREIENLPLRLFTFW 14 302 RKQLGLLSFFFAMVH 18 212 WRGPVVVAISLATFF 14 8 NLPLRLFTFWRGPVV 14 307 LLSFFFAMVHVAYSL 18 233 RDVIHPYARNQQSDF 14 11 LRLFTFWRGPVVVAI 13 367 SLGLLSLLAVTSIPS 18 261 IVAITLLSLVYLAGL 14 14 FTFWRGPVVVAISLA 12 370 LLSLLAVTSIPSVSN 18 319 YSLCLPMRRSERYLF 14 16 FWRGPVVVAISLATF 9 28 ARKVTVGVIGSGDFA 17 348 SWNEEEVWRIEMYIS 14 4 REIENLPLRLFTFWR 8 86 TNIIFVAIHREHYTS 17 373 LLAVTSIPSVSNALN 14 99 TSLWDLRHLLVGKIL 17 381 SVSNALNWREFSFIQ 14 134 ASLFPDSLIVKGFNV 17 407 TFHVLIYGWKRAFEE 14 TableXLIX-V5B-HLA-DRB1 143 VKGFNVVSAWALQLG 17 409 HVL1YGWKRAFEEEY 14 1101-15mers-98P4B6 225 FFFLYSFVRDVIHPY 17 430 PNFVLALVLPSIVIL 14 Each peptide is a portion of SEQ ID 226 FFLYSFVRDVIHPYA 17 435 ALVLPSIVILDLLQL 14 NO: 11; each start position is 244 QSDFYKIPIEIVNKT 17 30 KVTVGVIGSGDFAKS 13 specified, the length of peptide is 15 335 NMAYQQVHANIENSW 1'7 33 VGVIGSGDFAKSLTI 13 amino acids, and the end position for 360 YISFGIMSLGLLSLL 17 101 LWDLRHLLVGKILID 13 each peptide is the start position plus 405 ISTFHVLIYGWKRAF 17 139 DSLIVKGFNVVSAWA 13 fourteen. 129 NAEYLASLFPDSLIV 16 146 FNVVSAWALQLGPKD 13 Pos 123456789012345 score 136 LFPDSLIVKGFNVVS 16 178 VIELARQLNFIPIDL 13 7 WREFSFIQIFCSFAD 22 163 RQVYICSNNIQARQQ 16 185 LNFIPIDLGSLSSAR 13 9 EFSFIQIFCSFADTQ 22 184 QLNFIPIDLGSLSSA 16 206 LRLFTLWRGPVVVAI 13 16 FCSFADTQTELELEF 11 268 SLVYLAGLLAAAYQL 16 208 LFTLWRGPVVVAISL 13 4 ALNWREFSFIQIFCS 10 279 AYQLYYGTKYRRFPP 16 223 ATFFFLYSFVRDVIH 13 13 IQIFCSFADTQTELE 10 282 LYYGTKYRRFPPWLE 16 252 IEIVNKTLPIVAITL 13 328 SERYLFLNMAYQQVH 16 256 NKTLPIVAITLLSLV 13 TableXLIX-V6-HLA-DRBI-1101 330 RYLFLNMAYQQVHAN 16 280 YQLYYGTKYRRFPPW 13 15mers-98P4B6 385 ALNWREFSFIQSTLG 16 311 FFAMVHVAYSLCLPM '13 Each peptide is a portion of SEQ ID NO: 397 TLGYVALLISTFHVL 16 358 EMYISFGIMSLGLLS 13 13; each start position is specified, the 429 PPNFVLGYVALLSTFHIVI 16 36458 EMYISFGIMSLGLLS 13 length of peptide is 15 amino acids, and 42 AKSLTIRLIRCGYHV 15 364 GVTMSLGLSLLAVTSLNWRE 13 the end position for each peptide is the 42 AKSLTIRLIRCGY 1 376 VTSIPSVSNALNWRE 13 start position plus fourteen. 47 IRLIRCGYHVVIGSR 15 391 FSFIQSTLGYVALLI 13 Pos 123456789012345 score 103 DLRHLLVGKILIDVS 15 431 NFVLALVLPSIVILD 13 8 LPSIVILGKIILFLP 21 142 IVKGFNVVSAWALQL 15 18 ILFLPCISRKLKRIK 21 210 TLWRGPVVVAISLAT 15 TableXLIX-V2-HLA-DRB1-1101- 25 SRKLKRIKKGWEKSQ 20 317 VAYSLCLPMRRSERY 15 15mers-98P4B6 43 EGIGGTIPHVSPERV 20 318 AYSLCLPMRRSERYL 15 Each peptide is a portion of SEQ ID 11 IVILGKIILFLPCIS 19 322 CLPMRRSERYLFLNM 15 NO: 5; each start position is specified, 21 LPCISRKLKRIKKGW 16 401 VALLISTFHVLIYGW 15 the length of peptide is 15 amino acids, 22 PCISRKLKRKKGWE 15 408 FHVLIYGWKRAFEEE 15 and the end position for each peptide is 22 PCISRKLKRIKKGWE 15 428 TPPNFVLALVLPSIV 1 5 the start position plus fourteen. 45 GGTALVLPHVSPERVTVMLGKIIL 14 19 PNGINGIKDARKVTV 14 Pos 123456789012345 score 46 GGTIPHVSPERVTVM 14 22 INGIKDARKVTVGVI 14 17 FTPFSCLSLPSSWDY 22 1 NFVLALVLPSIVILG 13 43 KSLTIRLIRCGYHVV 14 3 SPGLQALSLSLSSGF 19 4 LALVLPSIVILGKII 13 52 CGYHVVIGSRNPKFA 14 28 SWDYRCPPPCPADFF 16 14 LGKIILFLPCISRKL 13 53 GYHVVIGSRNPKFAS 14 24 SLPSSWDYRCPPPCP 14 35 WEKSQFLEEGIGGTI 13 56 VVIGSRNPKFASEFF 14 5 GLQALSLSLSSGFTP 12 39 QFLEEGIGGTIPHVS 13 66 ASEFFPHVVDVTHHE 14 8 ALSLSLSSGFTPFSC 12 42 EEGIGGTIPHVSPER 13 77 THHEDALTKTNIIFV 14 10 SLSLSSGFTPFSCLS 12 15 GKIILFLPCISRKLK 12 85 KTNIIFVAIHREHYT 14 14 SSGFTPFSCLSLPSS 12 17 I1LFLPCISRKLKRI 12 85 KT32I!FVAIHREHEETI14, 26 PSSWDYRCPPPCPAD 10 32 KKGWEKSQFLEEGIG 10 243 WO 03/087306 PCT/US03/10462 TablcXLIX-V6-HLA-DRBI-1 101- TabIeXLIX-V7C-HLA-DRBl-1101- Each peptide is a portion of SEQ ID 15mers-98P4B6 15mers-98P4B6 NO: 27; each start position is Each peptide is a portion of SEQ ID NO: Each peptide is a portion of SEQ ID NO: specified, the length of peptide is 15 13; each start position is specified, the 15; each start position is specified, the amino acids, and the end position for length of peptide is 15 amino acids, and length of peptide is 15 amino acids, and each peptide is the start position plus the end position for each peptide is the the end position for each peptide is the fourteen. start position plus fourteen, start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score Pos 123456789012345 score 1 SISMMGSPKSLSETF 21 37 KSQFLEEGIGGTIPH 10 43 LPIEWQQDRKIPPLS 15 8 PKSLSETFLPNGING 12 73 AEAQESGIRNKSSSS 15 12 SETFLPNGINGIKDA 10 TableXLIX-V7A-HLA-DRB1- 3 ALVLPSIVILDLSVE 14 1101-15mers-98P4B6 27 KCLGANILRGGLSEI 14 TableXLIX-VI 4-HLA-DRB l-1101 Each peptide is a portion of SEQ ID 75 AQESGIRNKSSSSSQ 14 15mers-98P4B6 NO: 15; each start position is 89 QIPVVGVVTEDDEAQ 14 Each peptide is a portion of SEQ ID NO: specified, the length of peptide is 15 135 PLWEFLLRLLKSQAA 14 29; each start position is specified, the amino acids, and the end position for 173 KLETIILSKLTQEQK 14 length of peptide is 15 amino acids, and each peptide is the start position plus 4 LVLPSIVILDLSVEV 13 the end position for each peptide is the fourteen. 6 LPSIVILDLSVEVLA 13 start position plus fourteen. Pos 123456789012345 score 8 SIVILDLSVEVLASP 13 Pos 123456789012345 score 1 SISMMGSPKSLSETF 21 26 WKCLGANILRGGLSE 13 12 LFTFWRGPVVVAISL 17 8 PKSLSETFLPNGING 12 28 CLGANILRGGLSEIV 13 9 PLRLFTFWRGPVVVA 15 12 SETFLPNGINGIKDA 10 87 SSQIPVVGVVTEDDE 13 14 TFWRGPVVVAISLAT 15 90 IPVVGVVTEDDEAQD 13 2 AREIENLPLRLFTFW 14 TableXLIX-V7B-HLA-DRBI-1 101- 123 RNPVLPHTNGVGPLW 13 7 NLPLRLFTFWRGPVV 14 15mers-98P4B6 130 TNGVGPLWEFLLRLL 13 10 LRLFTFWRGPVVVAI 13 Each peptide is a portion of SEQ ID NO: 152 TLSLAFTSWSLGEFL 13 13 FTFWRGPVVVAISLA 12 15; each start position is specified, the 156 AFTSWSLGEFLGSGT 13 15 FWRGPVVVAISLATF 9 length of peptide is 15 amino acids, and 169 GTWMKLETIILSKLT 13 3 REIENLPLRLFTFWR 8 the end position for each peptide is the 171 WMKLETIILSKLTQE 13 strtpoitonpls outen. 171 WMKLETHILSKLTQE 13 start position plus fourteen. 10 VILDLSVEVLASPAA 12 TableXLIX-V21-HLA-DRB 1-1101 Pos 123456789012345 score 12 LDLSVEVLASPAAAW 12 15mers-98P4B6 4 RYLFLNMAYQQSTLG 2 12 LDLSVEVLASPAAAW 12 14 QSTLGYVALLISTFH 39 SEIVLPIEWQQDRKI 12 Each peptide is a portion of SEQ ID NO: SS YLL ST 16 58 TPPPPAWvAWTEEAGAT 12 43; each start position is specified, the 7 FLNMAYQQSTLGYVA 13 74 EAQESGIR-KSSSSS 12 length of peptide is 15 amino acids, and 7 FLNMAYQQSTLGYVAL 10 77 ESGIRNKSSSSSSQIP 12 the end position for each peptide is the 9 AYQQSTLGYVALL 10 start position plus fourteen 100 DEAQDSIDPPESPDR 12 Pos 123456789012345 score TableXLIX-V7C-HLA-DRB I-1101- 110 ESPDRALKAANSWRN 12 6 LSKLTEKTKHCMF 17 15mers-98P4B6 119 ANSWRNPVLPHTNGV 12 3 TIILSKLTQEQKTKH 12 Each peptide is a portion of SEQ ID NO: 124 NPVLPHTNGVGPLWE 12 8 KLTQEQKTKHCMFSL 8 15; each start position is specified, the 140 LLRLLKSQAASGTLS 12 9 LTQEQKTKHCMFSLI 8 length of peptide is 15 amino acids, and 150 SGTLSLAFTSWSLGE 12 8 the end position for each peptide is the 154 SLAFTSWSLGEFLGS 12 TableXLIX-V25-HLA-DRBl-1101 start position plus fourteen. 176 TIILSKLTQEQKSKH 12 15mers-98P4B6 Pos 123456789012345 score Each peptide is a portion of SEQ ID NO: 137 WEFLLRLLKSQAASG 26 TableXLIX-V8-HLA-DRBI-1101- 51; each start position is specified, the 134 GPLWEFLLRLLKSQA 25 15mers-98P4B6 length of peptide is 15 amino acids, and 44 PIEWQQDRKIPPLST 24 Each peptide is a portion of SEQ ID NO: the end position for each peptide is the 121 SWRNPVLPHTNGVGP 21 17; each start position is specified, the start position plus fourteen. 13 DLSVEVLASPAAAWK 19 length of peptide is 15 amino acids, and Pos 123456789012345 score 50 DRKIPPLSTPPPPAM 18 the end position for each peptide is the 14 SQKLKRIKKGWEKSQ 20 62 PAMWTEEAGATAEAQ 18 start position plus fourteen. 10 LPCISQKLKRIKKGW 16 138 EFLLRLLKSQAASGT 18 Pos 123456789012345 score PCISQKLKRIKKGWE 15 23 AAAWKCLGANILRGG 17 13 EGMGGTIPHVSPERV 20 3 LGKIILFLPCISQKL 13 168 SGTWMKLETIILSKL 17 9 QFLEEGMGGTIPHVS 13 ILFLPCISQKLKRIK 13 179 LSKLTQEQKSKHCMF 17 12 EEGMGGTIPHVSPER 13 GKIILFLPCISQKLK 12 157 FTSWSLGEFLGSGTW 16 5 WEKSQFLEEGMGGTI 12 6 IILFLPCISQKLKRI 11 9 IVILDLSVEVLASPA 15 2 KKGWEKSQFLEEGMG 10 LFLPCSQKLKRIKK 19 11 ILDLSVEVLASPAAA 15 7 KSQFLEEGMGGTIPH -10 8 LFLPCSQKLKRKK 9 19 LASPAAAWKCLGANI 15eXLIX-V3-HLA-DRB TableXLIX-V13-HLA-DRBl1 35 RGGLSEIVLPIEWQQ 15 1101-5mers-98P4B6 241101-15mers-98P4B6 244 WO 03/087306 PCT/USO3/10462 Table L: Properties of 98P4B6 V.1 Bioinformatic URL Outcome Program ORF ORF finder Protein length 454 aa Transmembrane region TM Pred http://www.ch.embnet.org/ 6TM, aa 214-232, 261 286, 304-325, 359-379, 393-415, 426-447, N term inside HMMTop http://www.enzim.hu/hmmtop/ 6TM, aa 215-232 261 279 306-325 360-379 396-415 428-447 N term out Sosui http://www.genome.ad.jp/SOSui/ 6TM, aa 206-228, 255 277, 304-325, 359-381, 393-415, 428-450 TMHMM http://www.cbs.dtu.dk/servicesffMHMM 6TM, aa 210-232, 262 284, 304-323, 360-382, 392-414, 427-449 Signal Peptide Signal P http://www.cbs.dtu.dk/services/SignalP/ none PI p1/MW tool http://www.expasy.ch/tools/ pl 8.74 Molecular weight pI/MW tool http://www.expasy.ch/tools/ 52.0 kD Localization PSORT http://psort.nibb.ac.jp/ Plasma membrane 60%, golgi 40% PSORT 11 http://psort.nibb.ac.jp/ Endoplasmic reticulum 39%, plasma membrane 34% Motifs Pfam http://www.sanger.ac.uk/Pfam/ no known motifs Prints http://www.biochem.ucl.ac.uk/ pyridine nucleotide reductase ProDom http://prodes.toulouse.inra.f Dudulin, oxidoreductase Blocks http://www.blocks.fhcrc.org/ adenosyl-L homocysteine hydrolase V.2 Bioinformatic URL Outcome Program ORF ORF finder Protein length 45 aa Transmembrane region TM Pred http://www.ch.embnet.org/ I TM, aa 5-23, N-term inside HMMTop http://www.enzim.hu/hmmtop/ no TM Sosui http://www.genome.ad.jp/SOSui/ souble protein TMHMM http://www.cbs.dtu.dk/servicesfrMHMM no TM Signal Peptide Signal P http://www.cbs.dtu.dk/services/SignalP/ none pl pl/MW tool http://www.expasy.ch/tools/ pI 4.2 Molecular weight pl/MW tool http://www.expasy.ch/tools/ 4.84 kD Localization PSORT http://psort.nibb.ac.jp/ Ouside 37%, microbody 32% PSORT II http://psort.nibb.ac.jp/ Extracellular 33%, nuclear 33% Motifs Pfam http://www.sanger.ac.uk/Pfam/ no known motifs Prints http://www.biochem.ucl.ac.uk/ no known motifs Blocks http://www.blocks.thcrc.org/ no known motifs V.5 Bioinformatic URL Outcome Program ORF ORF finder 245 WO 03/087306 PCT/USO3/10462 Protein length 419 aa Transmembrane region TM Pred http://www.ch.embnet.org/ 4TM, as 214-232, 261 286, 304-325, 359-379 N-term inside HMMTop http://www.enzim.hu/hmmtop/ 4TM, aa 215-232,259 278, 305-324, 360-379 N-term outside Sosui http://www.genome.ad.jp/SOSui/ 4TM, aa 209-231, 255 277, 304-325, 356-379 TMHMM http://www.cbs.dtu.dk/servicesTMHMM 4TM, as 210-232, 262 284, 304-323, 360-382 Signal Peptide Signal P http://www.cbs.dtu.dk/services/SignalP/ none pl pl/MW tool http://www.expasy.ch/tools/ pI 8.1 Molecular weight pl/MW tool http://www.expasy.ch/tools/ 47.9 kD Localization PSORT http://psort.nibb.ac.jp/ Plasma membrane 60%, golgi 40% PSORT II http://psort.nibb.ac.jp/ Endoplasmic reticulum 44%, plasma membrane 22% Motifs Pfam http://www.sanger.ac.uk/Pfam/ no known motifs Prints http://www.biochem.ucl.ac.uk/ no known motifs ProDom http://prodes.toulouse.inra.f Dudulin, oxidoreductase Blocks http://www.blocks.fhcre.org/ no known motifs V.6 Bioinformatic URL Outcome Program ORF ORF finder Protein length 490 aa Transmembrane region TM Pred http://www.ch.embnet.org/ 6TM, aa 214-232, 261 286, 304-325, 359-379, 393-415, 432-455 HMMTop http://www.enzim.hu/hmmtop/ 7TM, aa 140-158, 214 232, 259-280, 305-323, 361-383, 396-413, 432 455, N -term out Sosui http://www.genome.ad.jp/SOSui/ 6TM, aa 206-228, 255 277, 304-325, 359-381, 393-415, 428-450 TMHIMM http://www.cbs.dtu.dk/services/TMHMM 6TM, aa 210-232, 262 284, 304-323, 360-382, 392-414, 427-449 Signal Peptide Signal P http://www.cbs.dtu.dk/services/SignalP/ none pl pI/MW tool http://www.expasy.ch/tools/ pI 9.2 Molecular weight pI/MW tool http://www.expasy.ch/tools/ 55.9 kD Localization PSORT http://psort.nibb.ae.jp/ Plasma membrane 60%, golgi 40% PSORT II http://psort.nibb.ac.jp/ Endoplasmie reticulum 39%, plasma membrane 34% Motifs Pfam http://www.sanger.ac.uk/Pfaim/ no known motifs Prints http://www.biochem.ucl.ac.uk/ pyridine nucleotide reductase ProDom http://prodes.toulouse.inra.f Dudulin, oxidoreductase Blocks http://www.blocks.thcrc.org/ adenosyl-L homocysteine hydrolase 246 WO 03/087306 PCT/USO3/10462 V.7 Bioinformatic URL Outcome Program ORF ORF finder Protein length 576 as Transmembrane region TM Pred http://www.ch.embnet.org/ 6TM, aa 214-232, 262 280, 306-322, 331-360, 371-393, 525-544. N term out HMMTop http://www.enzim.huihmmtop/ 5TM, aa 215-232, 261 279, 306-325, 342-359, 378-397 N -term out Sosui http://www.genome.ad.jp/SOSui/ 5 TM, aa 206-228, 255 277, 304-325, 339-360, 380-402 TMI-IMM http://www.cbs.dtu.dk/services/TMHMM 4TM, aa 210-232, 262-284, 304-323, 343-360 Signal Peptide Signal P http://www.cbs.dtu.dk/services/SignalPI none pl pI/MW tool http://www.expasy.ch/tools/ pI 8.5 Molecular weight pl/MW tool http://www.expasy.ch/tools/ 64.5 kD Localization PSORT http://psort.nibb.ac.jp/ Plasma membrane 60%, golgi 40% PSORT II http://psort.nibb.ac.jp/ Endoplasmic reticulum 44%, plasma membrane 22% Motifs Pfam http://www.sanger.ac.uk/Pfam/ no known motifs Prints http://www.biochem.ucl.ac.uk/ pyridine nucleotide reductase ProDom http://prodes.toulouse.inra.f Dudulin, oxidoreductase Blocks http://www.blocks.thcrc.org/ Ets domain, adenosyl L-homoeysteine hydrolase Table LI. Exon boundaries of transcript98P4B6 v.1 Exon Number Start End Length 1 23 321 299 2 322 846 525 3 847 1374 528 4 1375 1539 165 5 1540 1687 148 6 1688 2453 766 Table LII(a). Nucleotide sequence (partial, 5' open) of transcript variant 98P4B6 v.2 (SEQ ID NO: 153) agtggatccc ccgggctgca ggctctctct ctctctctct cttccgggtt cacgccattc 60 tcctgcctca gcctcccgag tagctgggac tacaggtgcc cgccaccatg cccggctgat 120 ttctttttgt atttttagta cagacggagt ttcaccgtgt tagccaggat ggtctcgatc 180 tcctgacctc gtgatccgcc cgccttggcc tccaaagtgc tgggattaca ggtgtgagct 240 accgcgcccg gcctattatc ttgtactttc taactgagcc ctctattttc tttattttaa 300 taatatttct ccccacttga gaatcacttg ttagttcttg gtaggaattc agttgggcaa 360 tgataacttt tatgggcaaa aacattctat tatagtgaac aaatgaaaat aacagcgtat 420 tttcaatatt ttcttattcc ttaaattcca ctcttttaac actatgctta accacttaat 480 gtgatgaaat attcctaaaa gttaaatgac tattaaagca tatattgttg catgtatata 540 ttaagtagcc gatactctaa ataaaaatac cactgttaca gataaatggg gcctttaaaa 600 atatgaaaaa caaacttgtg aaaatgtata aaagatgcat ctgttgtttc aaatggcact 660 atcttctttt cagtactaca aaaacaqaat aattttgaag ttttagaata aatgtaatat 720 atttactata attctaaatg tttaaatgct tttctaaaaa tgcaaaacta tgatgtttag 780 ttgctttatt ttacctctat gtgattattt ttcttaattg ttatttttta taatcattat 840 247 WO 03/087306 PCT/USO3/10462 ttttctgaac cattcttctg gcctcagaag taggactgaa ttctactatt gctaggtgtg 900 agaaagtggt ggtgagaacc ttagagcagt ,ggagatttgc tacctggtct gtgttttgag 960 aagtgcccct tagaaagtta aaagaatgta gaaaagatac tcagtcttaa tcctatgcaa 1020 aaaaaaaatc aagtaattgt tttcctatga ggaaaataac catgagctgt atcatgctac 1080 ttagctttta tgtaaatatt tcttatgtct cctctattaa gagtatttaa aatcatattt 1140 aaatatgaat ctattcatgc taacattatt tttcaaaaca tacatggaaa tttagcccag 1200 attgtctaca tataaggttt ttatttgaat tgtaaaatat ttaaaagtat gaataaaata 1260 tatttatagg tatttatcag agatgattat tttgtgctac atacaggttg gctaatgagc 1320 tctagtgtta aactacctga ttaatttctt ataaagcagc ataaccttgg cttgattaag 1380 gaattctact ttcaaaaatt aatctgataa tagtaacaag gtatattata ctttcattac 1440 aatcaaatta tagaaattac ttgtgtaaaa gggcttcaag aatatatcca atttttaaat 1500 attttaatat atctcctatc tgataactta attcttctaa attaccactt gccattaagc 1560 tatttcataa taaattctgt acagtttccc ccaaaaaaag agatttattt atgaaatatt 1620 taaagtttct aatgtggtat tttaaataaa gtatcataaa tgtaataagt aaatatttat 1680 ttaggaatac tgtgaacact gaactaatta ttcctgtgtc agtctatgaa atccctgttt 1740 tgaaataagt aaacagccta aaatgtgttg aaattatttt gtaaatccat gacttaaaac 1800 aagatacata catagtataa cacacctcac agtgttaaga tttatattgt gaaatgagac 1860 accctacctt caattgttca tcagtgggta aaacaaattc tgatgtacat tcaggacaaa 1920 tgattagccc taaatgaaac tgtaataatt tcagtggaaa ctcaatctgt ttttaccttt 1980 aaacagtgaa ttttacatga atgaatgggt tcttcacttt ttttttagta tgagaaaatt 2040 atacagtgct taattttcag agattctttc catatgttac taaaaaatgt tttgttcagc 2100 ctaacatact gagttttttt taactttcta aattattgaa tttccatcat gcattcatcc 2160 aaaattaagg cagactgttt ggattcttcc agtggccaga tgagctaaat taaatcacaa 2220 aagcagatgc ttttgtatga tctccaaatt gccaacttta aggaaatatt ctcttgaaat 2280 tgtctttaaa gatcttttgc agctttgcag atacccagac tgagctggaa ctggaatttg 2340 tcttcctatt gactctactt ctttaaaagc ggctgcccat tacattcctc agctgtcctt 2400 gcagttaggt gtacatgtga ctgagtgttg gccagtgaga tgaagtctcc tcaaaggaag 2460 gcagcatgtg tcctttttca tcccttcatc ttgctgctgg gattgtggat ataacaggag 2520 ccctggcagc tgtctccaga ggatcaaagc cacacccaaa gagtaaggca gattagagac 2580 cagaaagacc ttgactactt ccctacttcc actgcttttt cctgcattta agccattgta 2640 aatctgggtg tgttacatga agtgaaaatt aattctttct gcccttcagt tctttatcct 2700 gataccattt aacactgtct gaattaacta gactgcaata attctttctt ttgaaagctt 2760 ttaaaggata atgtgcaatt cacattaaaa ttgattttcc attgtcaatt agttatactc 2820 attttcctgc cttgatcttt cattagatat tttgtatctg cttggaatat attatcttct 2880 ttttaactgt gtaattggta attactaaaa ctctgtaatc tccaaaatat tgctatcaaa 2940 ttacacacca tgttttctat cattctcata gatctgcctt ataaacattt aaataaaaag 3000 tactatttaa tgatttaaaa aaaaaaaaaa aaaaaaaaaa a 3041 Table LIIl(a). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 154) and 98P4B6 v.2 (SEQ ID NO: 155) Score = 1429 bits (743), Expect = 0.01dentities = 750f751 (99%), Gaps = 1/751 (0%) Strand = Plus / Plus V.1: 1687 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 1746 111 1 iii l 11111111 11111||lii ll ll l lli lll lil ll11 11111111 V.2: 2291 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 2350 V.1: 1747 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 1806 I I I i l l l l ll l i I l l i ll I i l i I I I l l l l I Il l l l l l l l l l 1 i1 l l l lI V.2: 2351 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 2410 V.1: 1807 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 1866 iliIlilillIillllllllIlllll11111111111111111111111111111l V.2: 2411 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 2470 V.1: 1867 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 1926 1fil 1111111111111 11111111111111111l 111111111 11111111111111 V.2: 2471 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 2530 V.1: 1927 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 1986 11111111111 11f111111111111111111fflll lll llll l l 11111111111 V.2: 2531 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 2590 V.1; 1987 ttgactacttccctacttccactgctttt-cctgcatttaagccattgtaaatctgggtg 2045 248 WO 03/087306 PCT/US03/10462 l i l l l 1 l l l l l l l l l l l l i I I I l l l Il lll l l l l i l l l l l l l1 l l1 l l V.2: 2591 ttgactacttccctacttccactgctttttcctgcatttaagccattgtaaatctgggtg 2650 V.1: 2046 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2105 I l l 1l l l lIll l l l l l i l l l l |1 | l l l l l l l l l l I llI I l l l Il l l l l l I V.2: 2651 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2710 V.1: 2106 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2165 V.2: 2711 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2770 V.1: 2166 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2225 I * I 111 11111 111111 11111 1111 11111 IiII V.2: 2771 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2830 V.1: 2226 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2285 1111 ii 1111111111i11I 11111111111 11111 II V.2: 2831 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2890 V.1: 2286 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2345 I l l | I IIll II l l l l l l l l I l l i l l l l I l l l l l l l l l i l l i V.2: 2891 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2950 V.1: 2346 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 2405 V.2: 2951 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 3010 V.1: 2406 tgatttaaaaaaaaaaaaaaaaaaaaaaaaa 2436 V.2: 3011 tgatttaaaaaaaaaaaaaaaaaaaaaaaaa 3041 NOTE: THERE WAS A SINGLE NUCLEOTIDE INSERTION OF A SINGLE BASE AT 2620 OF V.2. Table LIV(a). Peptide sequences (partial) of protein coded by 98P4B6 v.2 (SEQ ID NO: 156) SGSPGLQALS LSLSSGFTPF SCLSLPSSWD YRCPPPCPAD FFLYF 45 Table LV(a). Amino acid sequence alignment of 98P4B6 v.1 and 98P4B6 v.2 -NO SIGNIFICANT HOMOLOGY Table LII(b). Nucleotide sequence of transcript variant 98P4B6 v.3 (SEQ ID NO: 157) ttctgctata gagatggaac agtatatgga aagctcccaa gaaagtgaag agaggaaatt 60 ggaaaattgt gagtggacct tctgatactg ctcctccttg cgtggaaaag gggaaagaac 120 tgcatgcata ttattcagcg tcctatattc aaaggatatt cttggtgatc ttggaagtgt 180 ccgtatcatg gaatcaatct ctatgatggg aagccctaag agccttagtg aaacttgttt 240 acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg tgattggaag 300 tggagatttt gccaaatcct tgaccattcg acttattaga tgcggctatc atgtggtcat 360 aggaagtaga aatcctaagt ttgcttctga attttttcct catgtggtag atgtcactca 420 tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca gagaacatta 480 tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg atgtgagcaa 540 taacatgagg ataaaccagt acccagaatc caatgctgaa tatttggctt cattattccc 600 agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc agttaggacc 660 taaggatgcc agccggcagg tttatatatg cagcaacaat attcaagcgc gacaacaggt 720 tattgaactt gcccgccagt tgaatttcat tcccattgac ttgggatcct tatcatcagc 780 249 WO 03/087306 PCT/USO3/10462 cagagagatt gaaaatttac ccctacgact ctttactctc tggagagggc cagtggtggt 840 agctataagc ttggccacat tttttttcct ttattccttt gtcagagatg tgattcatcc 900 atatgctaga aaccaacaga gtgactttta caaaattcct atagagattg tgaataaaac 960 cttacctata gttgccatta ctttgctctc cctagtatac cttgcaggtc ttctggcagc 1020 tgcttatcaa ctttattacg gcaccaagta taggagattt ccaccttggt tggaaacctg 1080 gttacagtgt agaaaacagc ttggattact aagttttttc ttcgctatgg tccatgttgc 1140 ctacagcctc tgcttaccga tgagaaggtc agagagatat ttgtttctca acatggctta 1200 tcagcaggtt catgcaaata ttgaaaactc ttggaatgag gaagaagttt ggagaattga 1260 aatgtatatc tcctttggca taatgagcct tggcttactt tccctcctgg cagtcacttc 1320 tatcccttca gtgagcaatg ctttaaactg gagagaattc agttttattc agtctacact 1380 tggatatgtc gctctgctca taagtacttt ccatgtttta atttatggat ggaaacgagc 1440 ttttgaggaa gagtactaca gattttatac accaccaaac tttgttcttg ctcttgtttt 1500 gccctcaatt gtaattctgg atcttttgca gctttgcaga tacccagact gagctggaac 1560 tggaatttgt cttcctattg actctacttc tttaaaagcg gctgcccatt acattcctca 1620 gctgtccttg cagttaggtg tacatgtgac tgagtgttgg ccagtgagat gaagtctcct 1680 caaaggaagg cagcatgtgt cctttttcat cccttcatct tgctgctggg attgtggata 1740 taacaggagc cctggcagct gtctccagag gatcaaagcc acacccaaag agtaaggcag 1800 attagagacc agaaagacct tgactacttc cctacttcca ctgctttttc ctgcatttaa 1860 gccattgtaa atctgggtgt gttacatgaa gtgaaaatta attctttctg cccttcagtt 1920 ctttatcctg ataccattta acactgtctg aattaactag actgcaataa ttctttcttt 1980 tgaaagcttt taaaggataa tgtgcaattc acattaaaat tgattttcca ttgtcaatta 2040 gttatactca ttttcctgcc ttgatctttc attagatatt ttgtatctgc ttggaatata 2100 ttatcttctt tttaactgtg taattggtaa ttactaaaac tctgtaatct ccaaaatatt 2160 gctatcaaat tacacaccat gttttctatc attctcatag atctgcctta taaacattta 2220 aataaaaagt actatttaat gatttaactt ctgttttgaa aaaaaaaaaa aaaaaaaaaa 2280 Table Lill(b). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 158) and 98P4B6 v.3 (SEQ ID NO: 159) Score = 4013 bits (2087), Expect = 0.01dentities = 2116/2128 (99%), Gaps = 1/2128 (0%) Strand = Plus / Plus V.1: 320 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 379 I i l l l l i l l I l l l l l l lill l l l l l l l l l l l l I l Ili l l l l lI l l l l l l l V.3: 153 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 212 V.1: 380 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 439 Il lI II l l l l l l l l l l l l l l l l l l l l l l l l i l l 1 V.3: 213 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 272 V.1: 440 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 499 I l l l l lllil lI l l l l l ll1l l l l l li l l l l l I llII l I l II l l l I l V.3: 273 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 332 V.1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 559 l l l l l l l l l Il I l I l l l l lI l l l l l l ll I l V.3: 333 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 392 V.1: 560 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 619 Ili l l l11 I l Il l f ill I I l ll li l l l l l l l l l i l lll Il l l ll l l ll1 V.3: 393 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 452 V.1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 I li i I l lll l l l I l i l ll l lll l l ll l l l l l l llll i il l l l i l l l l l l l l l l l V.3: 453 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 512 V.1: 680 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 739 I Il l l l l l I I l l l lI l l l I I l l l l l l l l ll l l Il l I 250 WO 03/087306 PCT/USO3/10462 V.3: 513 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 572 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 I 1 l l 1 l l l l l l l l l l I l l ll I I il l1 1 l l l l l I l l l l l l l l l l l l l l l l l l l l I V.3: 573 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 632 V.1: 800 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 I l l I l ~ l l I I I I l I l l l l i l l li l l l l l l l i l l I V.3: 633 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 692 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 111111111111111111111 li 111II 111111111 V.3: 693 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 752 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 V.3: 753 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 812 V.1: 980 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1039 V.3: 813 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 872 V.1: 1040 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1099 V.3: 873 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 932 V.1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 1111111 111111 11111 1111 Ii 1 V.3: 933 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgcttctcc 992 V.1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 lii 1111111111111 lii 11111111111 111 V.3: 993 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1052 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 I llllllllillll llli lli lllll11 1111111 I 111111111111111111 V.3: 1053 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1112 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1339 Il i i I I l l l l I l l l l l l l l l l l l l l i l l l l l l l l Il l l l l l l i l l l l l I V.3: 1113 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1172 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 I I l l l l i l l l l I I I i ll1l lI l l l l l l l l l l l l l l l l l l l l l l l l l l l i l V.3: 1173 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1232 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 1 l l l l l l l l l l l i I I l l l I I Il lI l l l l l i l l l l l lI I I l l V.3: 1233 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1292 251 WO 03/087306 PCT/USO3/10462 V.1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1519 l ili i l l l l l l I l (I l l f I l l l i l i l i llil l i l l l l lI ill l il l l l l V.3: 1293 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1352 V.1: 1520 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1579 111111 1 1 111111111 11111111111111111 11 1 IIlll illll 1 11 V.3: 1353 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1412 V.1: 1580 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1639 V.3: 1413 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1472 V.1: 1640 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1699 111f f1 ff1 11 f1 11 1 f( 11111 11| l fll i illlll il l fil l ill V.3: 1473 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1532 V.1: 1700 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1759 V.3: 1533 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1592 V.1: 1760 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1819 lIlllifi 1flill1lilfII il f1l1l llll 1lli ll i llI l l l V.3: 1593 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1652 V.1: 1820 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1879 1li 11 1 f ff11l1f 1 11l1 1 11 11fillf11 f111 illil i l l i l l l l l l l i l l l l l l l l l V.3: 1653 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1712 V.1: 1880 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1939 11l 1ll 1lllil 11llilllilllll 11lfllll 11ll 1 flllllll f llll 1lflll lll V.3: 1713 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1772 V.1: 1940 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1999 l I l l l l i l l li l i l l l l l 1 1 1 1 1 1 1 1 1 i1' 1 1 1 1 1 V.3: 1773 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1832 V.1: 2000 tacttccactgctttt-cctgcatttaagccattgtaaatctggtgtgttacatgaagt 2058 I l l l l1 l l l 1 l l l l l i I li1 1l l l l l l l l l l l i l l l l llf l l1 l lil l l Il l V.3: 1833 tacttccactgctttttcctgcatttaagccattgtaaatctgggtgtgttacatgaagt 1892 V.1: 2059 gaaaattaattctttctgcccttcagttctttatcctgataccatttaacactgtctgaa 2118 11111ff11111111111111111 f111111 f 1111 1 1111 1 11111111 I1 V.3: 1893 gaaaattaattctttctgcccttcagttctttatcctgataccatttaacactgtctgaa 1952 V.1: 2119 ttaactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcac 2178 I l l 1 l l 1 l l l l l l lIIl l Il l I l l l l l l i l l il l l i l l l l l l lI l l l l I V.3: 1953 ttaactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcac 2012 V.1: 2179 attaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcat 2238 II lllllI lll l I li lll llll I I 11111 1111111111111111111 1111i V.3: 2013 attaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcat 2072 252 WO 03/087306 PCT/US03/10462 V.1: 2239 tagatattttgtatctgcttggaatatattatcttctttttaactgtgtaattggtaatt 2298 ll11l iii l lilliJJl lii I Iliii lj l 11111 111111 I 111111l V.3: 2073 tagatattttgtatctgcttggaatatattatcttctttttaactgtgtaattggtaatt 2132 V.1: 2299 actaaaactctgtaatctccaaaatattgctatcaaattacacaccatgttttctatcat 2358 iii JJJliilll i l~lJill lJJJllilIII IllJill Ijia V.3: 2133 actaaaactctgtaatctccaaaatattgctatcaaattacacaccatgttttctatcat 2192 V.1: 2359 tctcatagatctgccttataaacatttaaataaaaagtactatttaatgatttaaaaaaa 2418 V.3: 2193 tctcatagatctgccttataaacatttaaataaaaagtactatttaatgatttaacttct 2252 V.1: 2419 aaaaaaaaaaaaaaaaaaaaaaaaaaaa 2446 V.3: 2253 gttttgaaaaaaaaaaaaaaaaaaaaaa 2280 NOTE: AN INSERTION OF A SINGLE BASE AT 1845 OF V.3 Table LV(b). Peptide sequences of protein coded by 98P4B6 v.3 (SEQ ID NO: 160) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ.VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILDLLQLC RYPD 454 Table LV(b). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 161) and 98P4B6 v.3 (SEQ ID NO: 162) Score= 910 bits (2351), Expect= 0.01Identities = 4541454(100%), Positives= 454/454 (100%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.3: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.3: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.3: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.3: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.3: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY V.3: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 253 WO 03/087306 PCT/USO3/10462 V.3: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V.1: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD V.3: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 Table LII(c). Nucleotide sequence of transcript variant 98P4B6 v.4 (SEQ ID NO: 163) cccacgcgtc cgcggacgcg tgggcggacg cgtgggttcc tcgggccctc ggcgccacaa 60 gctgtccggg cacgcagccc ctagcggcgc gtcgctgcca agccggcctc cgcgcgcctc 120 cctccttcct tctcccctgg ctgttcgcga tccagcttgg gtaggcgggg aagcagctgg 180 agtgcgaccg ccacggcagc caccctgcaa ccgccagtcg gagagctaag ggcaagtcct 240 gaggttgggc ccaggagaaa gaaggcaagg agacattgtc ccaggatatt cttggtgatc 300 ttggaagtgt ccgtatcatg gaatcaatct ctatgatggg aagccctaag agccttagtg 360 aaacttgttt acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg 420 tgattggaag tggagatttt gccaaatcct tgaccattcg acttattaga tgcggctatc 480 atgtggtcat aggaagtaga aatcctaagt ttgcttctga attttttcct catgtggtag 540 atgtcactca tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca 600 gagaacatta tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg 660 atgtgagcaa taacatgagg ataaaccagt acccagaatc caatgctgaa tatttggctt 720 cattattccc agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc 780 agttaggacc taaggatgcc agccggcagg tttatatatg cagcaacaat attcaagcgc 840 gacaacaggt tattgaactt gcccgccagt tgaatttcat tcccattgac ttgggatcct 900 tatcatcagc cagagagatt gaaaatttac ccctacgact ctttactctc tggagagggc 960 cagtggtggt agctataagc ttggccacat tttttttcct ttattccttt gtcagagatg 1020 tgattcatcc atatgctaga aaccaacaga gtgactttta caaaattcct atagagattg 1080 tgaataaaac cttacctata gttgccatta ctttgctctc cctagtatac cttgcaggtc 1140 ttctggcagc tgcttatcaa ctttattacg gcaccaagta taggagattt ccaccttggt 1200 tggaaacctg gttacagtgt agaaaacagc ttggattact aagttttttc ttcgctatgg 1260 tccatgttgc ctacagcctc tgcttaccga tgagaaggtc agagagatat ttgtttctca 1320 acatggctta tcagcaggtt catgcaaata ttgaaaactc ttggaatgag gaagaagttt 1380 ggagaattga aatggatatc tcctttggca taatgagcct tggcttactt tccctcctgg 1440 cagtcacttc tatcccttca gtgagcaatg ctttaaactg gagagaattc agttttattc 1500 agtctacact tggatatgtc gctctgctca taagtacttt ccatgtttta atttatggat 1560 ggaaacgagc ttttgaggaa gagtactaca gattttatac accaccaaac tttgttcttg 1620 ctcttgtttt gccctcaatt gtaattctgg atcttttgca gctttgcaga tacccagact 1680 gagctggaac tggaatttgt cttcctattg actctacttc tttaaaagcg gctgcccatt 1740 acattcctca gctgtccttg cagttaggtg tacatgtgac tgagtgttgg ccagtgagat 1800 gaagtctcct caaaggaagg cagcatgtgt cctttttcat cccttcatct tgctgctggg 1860 attgtggata taacaggagc cctggcagct gtctccagag gatcaaagcc acacccaaag 1920 agtaaggcag attagagacc agaaagacct tgactacttc cctacttcca ctgcttttcc 1980 tgcatttaag ccattgtaaa tctgggtgtg ttacatgaag tgaaaattaa ttctttctgc 2040 ccttcagttc tttatcctga taccatttaa cactgtctga attaactaga ctgcaataat 2100 tctttctttt gaaagctttt aaaggataat gtgcaattca cattaaaatt gattttccat 2160 tgtcaattag ttatactcat tttcctgcct tgatctttca ttagatattt tgtatctgct 2220 tggaatatat-tatcttcttt ttaactgtgt aattggtaat tactaaaact ctgtaatctc 2280 caaaatattg ctatcaaatt acacaccatg ttttctatca ttctcataga tctgccttat 2340 aaacatttaa ataaaaagta ctatttaatg attt 2374 Table Lill(c). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 164) and 98P4B6 v.4 (SEQ ID NO: 165) Score = 404 bits (210), Expect= e-1091dentities = 210/210 (100%) Strand = Plus/ Plus V.1: 1 ggacgcgtgggcggacgcgtgggttcctcgggccctcgqcgccacaagctgtccgggcac 60 11111111111111111111i111111 1111111111 1 1111111111111111111 V.4: 14 ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccgggcac 73 V.1: 61 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctccttccttct 120 Il l l l l l l l l l l i l l l l l l l l llll l l l l l l l l l i lli i I 1 1 1 1 1 1 1 1 l l l i l l V.4: 74 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctccttccttct 133 254 WO 03/087306 PCT/US03/10462 V.1: 121 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 180 1111111111111 1111111111 1 11 1 1i l l ll llllilll I I l l ll V.4: 134 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 193 V.1: 181 cggcagccaccctgcaaccgccagtcggag 210 V.4: 194 cggcagccaccctgcaaccgccagtcggag 223 Score = 4022 bits (2092), Expect = 0.Oldentities = 2092/2092(100%) Strand = Plus / Plus V.1: 320 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 379 I I I l l l l l lI I Ill l l l l l ill ll l lil l l l l lill ll l l l l l l l i Il l V.4: 283 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 342 V.I1: 380 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 439 I l lI ffll l l I 1 I l l l l l l l l l l l l l l l l l l l i l l l l l l I V.4: 343 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 402 V.1: 440 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 499 I l l lI l l I I I l l ~ i l l ~ l l l l l I l l l l l lI l l li V.4: 403 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 462 V.1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 559 V.4: 463 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 522 V.1: 560 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 619 I l l l 1l l l l l fl I I I I l l i l l ll1 l l l l l l l l l l ll1 l l l l l l l l ll1 l l l l ll1 lI V.4: 523 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 582 V.1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 V.4: 583 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 642 V.1: 680 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 739 V.4: 643 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 702 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 l l l l l l I l l l l l l l llIl l l l i i l l l l l II I ~ V.4: 703 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 762 V.1: 800 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 i l l l l l l l l l l l l l l l il l l l I l l l l l l l l lI V.4: 763 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 822 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 I l 1l l l I I I l il l l i l l l llfl l l l l l l l l I I l l l l l l1 I l l l l l l l l l l l V.4: 823 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 882 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 l 1 l l l l l 1 il l l l l l I I l i l l l l l l l l I I Il l l i l I l l i ll 255 WO 03/087306 PCT/USO3/10462 V.4: 883 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 942 V.1: 980 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1039 I l l l l l l l l l l l l lllli l l l l l l l l l l l l l l l l l l l l l l l l l l V.4: 943 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1002 V.1: 1040 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1099 I l l l l l l l l l l li l l l l l i l l l l l l l l l l i l i l I l l li l l l l i V.4: 1003 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1062 V.1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 11lil1 l l l lI i l iili l l l l 1 iI l l i l l l Ill1 I l l li l l l V.4: 1063 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1122 V.1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 i i1111i11i111 1111 i11111111 1i 1 V.4: 1123 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1182 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 V.4: 1183 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1242 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggfcag 1339 I 111 11111111111111111i 111111i1 I V.4: 1243 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1302 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 V.4: 1303 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1362 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 II 11 11i l iii I ll l ll 1l i ll ll ll l l l l i ii ll ll l l1 ll l1 lll l I V.4: 1363 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1422 V.1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1519 I I 1 1 l l l l l l i lllii i l I l l l i l I l l l l l I l l l llli I l V.4: 1423 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1482 V.1: 1520 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1579 11111| ii 111111111111111111111111 1 I1ill lll illll ll l ill V.4: 1483 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1542 V.1: 1580 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1639 l i l i ll l i l l l l l l l l l l l l l l il i l l l ll lli l l l il V.4: 1543 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1602 V.1: 1640 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1699 I 1 l l i l l l l l l l 1l l l l l l l l 1 l l l l l l lll ll l I l l l l i l l iI I I l l Il l V.4: 1603 caccaaactttgttcttgctcttgttttgccctcaattgtaattctggatcttttgcagc 1662 256 WO 03/087306 PCT/US03/10462 V.1: 1700 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1759 I I l l i f i l l l I [ ii i l i l i l i l lif l l l l l il i i l i i l lf l l l i l l V.4: 1663 tttgcagatacccagactgagctggaactggaatttgtcttcctattgactctacttctt 1722 V.1: 1760 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1819 V.4: 1723 taaaagcggctgcccattacattcctcagctgtccttgcagttaggtgtacatgtgactg 1782 V.1: 1820 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1879 I f I f l fl i f i l l i l f I f i i l l l l l i l l l il l l i l l l l l l i l l l lI V.4: 17,83 agtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtgtcctttttcatcc 1842 V.1: 1880 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1939 111111111 111111f 11111 11111 1 flillll1 ill Ill lll lll fill V.4: 1843 cttcatcttgctgctgggattgtggatataacaggagccctggcagctgtctccagagga 1902 V.1: 1940 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1999 l ill l I i l l i l l l I I l l l l l i l i l l l l l l l l l l l l l l l l l l I i V.4: 1903 tcaaagccacacccaaagagtaaggcagattagagaccagaaagaccttgactacttccc 1962 V.1: 2000 tacttccactgcttttcctgcatttaagccattgtaaatctgggtgtgttacatgaagtg 2059 lilll1 lli 11fflilll lllilll I II l llIllllllll111 11 f 11 Illll V.4: 1963 tacttccactgcttttcctgcatttaagccattgtaaatctgggtgtgttacatgaagtg 2022 V.1: 2060 aaaattaattctttctgcccttcagttctttatcctgataccatttaacactgtctgaat 2119 i l l l i l i f i l i f i l i l l l l l i l l l i l l l l l l l l l l i l l l l l l l 1 l l l l l llf l lf|1 | l1 1 V.4: 2023 aaaattaattctttctgcccttcagttctttatcctgataccatttaacactgtctgaat 2082 V.1: 2120 taactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcaca 2179 Ill 1l i l l 1l fl l l l 1ll l l l lI l l l l l l l l i l l l l l l l l l l l l I ll l l l l i V.4: 2083 taactagactgcaataattctttcttttgaaagcttttaaaggataatgtgcaattcaca 2142 V.1: 2180 ttaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcatt 2239 V.4: 2143 ttaaaattgattttccattgtcaattagttatactcattttcctgccttgatctttcatt 2202 V.1: 2240 agatattttgtatctgcttggaatatattatcttctttttaactgtgtaattggtaatta 2299 111111|111111 1111111 1 i | 1 111111| ll fllllllllll lllll lll llI V.4: 2203 agatattttgtatctgcttggaatatattatcttctttttaactgtgtaattggtaatta 2262 V.I1: 2300 ctaaaactctgtaatctccaaaatattgctatcaaattacacaccatgttttctatcatt 2359 I l l i l l 1l i l l l l l l l l l I l l l l l l l l l l l l l l l l l l1 fl l i l l I l i l l ll V.4: 2263 ctaaaactctgtaatctccaaaatattgctatcaaattacacaccatgttttctatcatt 2322 V.1: 2360 ctcatagatctgccttataaacatttaaataaaaagtactatttaatgattt 2411 I l l l l l l i l l i l l lll l l l l l l i l i l l l V.4: 2323 ctcatagatctgccttataaacatttaaataaaaagtactatttaatgattt 2374 Table LIV(c). Peptide sequences of protein coded by 98P4B6 v.4 (SEQ ID NO: 166) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 257 WO 03/087306 PCT/USO3/10462 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILDLLQLC RYPD 454 Table LV(c). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 167) and 98P4B6 v.4 (SEQ ID NO: 168) Score = 910 bits (2351), Expect = 0.01dentiies = 454/454 (100%), Positives = 454/454 (100%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.4: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.4: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.4: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.4: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.4: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY V.4: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE V.4: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V. 1: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD V.4: 421 EEYYRFYTPPNFVLALVLPSIVILDLLQLCRYPD 454 Table LIl(d). Nucleotide sequence of transcript variant 98P4B6 v.5 (SEQ ID NO: 169) cccacgcgtc cgcggacgcg tgggcggacg cgtgggttcc tcgggccctc ggcgccacaa 60 gctgtccggg cacgcagccc ctagcggcgc gtcgctgcca agccggcctc cgcgcgcctc 120 cctccttcct tctcccctgg ctgttcqcga tccagcttgg gtaggcgggg aagcagctgg 180 agtgcgaccg ctacggcagc caccctgcaa ccgccagtcg gagagctaag ggcaagtcct 240 gaggttgggc ccaggagaaa gaaggcaagg agacattgtc ccaggatatt cttggtgatc 300 ttggaagtgt ccgtatcatg gaatcaatct ctatgatggg aagccctaag agccttagtg 360 aaacttgttt acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg 420 tgattggaag tggagatttt gccaaatcct tgaccattcg acttattaga tgcggctatc 480 atgtggtcat aggaagtaga aatcctaagt ttgcttctga attttttcct catgtggtag 540 atgtcactca tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca 600 gagaacatta tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg 660 atgtgagcaa taacatgagg ataaaccagt acccagaatc caatgctgaa tatttggctt 720 cattattccc agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc 780 agttaggacc taaggatgcc agccggcagg tttatatatg cagcaacaat attcaagcgc 840 gacaacaggt tattgaagtt gcccgccagt tgaatttcat tcccattgac ttgggatcct 900 tatcatcagc cagagagatt gaaaatttac ccctacgact ctttactttc tggagagggc 960 cagtggtggt agctataagc ttggccacat tttttttcct ttattccttt gtcagagatg 1020 tgattcatcc atatgctaga aaccaacaga gtgactttta caaaattcct atagagattg 1080 tgaataaaac cttacctata gttgccatta ctttgctctc cctagtatac cttgcaggtc 1140 258 WO 03/087306 PCT/USO3/10462 ttctggcagc tgcttatcaa ctttattacg gcaccaagta taggagattt ccaccttggt 1200 tggaaacctg gttacagtgt agaaaacagc ttggattact aagttttttc ttcgctatgg 1260 tccatgttgc ctacagcctc tgcttaccga tgagaaggtc agagagatat ttgtttctca 1320 acatggctta tcagcaggtt catgcaaata ttgaaaactc ttggaatgag gaagaagttt 1380 ggagaattga aatgtatatc tcctttggca taatgagcct tggcttactt tccctcctgg 1440 cagtcacttc tatcccttcg gtgagcaatg ctttaaactg gagagaattc agttttattc 1500 agatcttttg cagctttgca gatacccaga ctgagctgga actggaattt gtcttcctat 1560 tgactctact tctttaaaag cggctgccca ttacattcct cagctgtcct tgcagttagg 1620 tgtacatgtg actgagtgtt ggccagtgag atgaagtctc ctcaaaggaa ggcagcatgt 1680 gtcctttttc atcccttcat cttgctgctg ggattgtgga tataacagga gccctggcag 1740 ctgctccaga ggatcaaagc cacacccaaa gagtaaggca gattagagac cagaaagacc 1800 ttgactactt ccctacttcc actgcttttt cctgcattta agccattgta aatctgggtg 1860 tgttacatga agtgaaaatt aattctttct gcccttcagt tctttatcct gataccattt 1920 aacactgtct gaattaacta gactgcaata attctttctt ttgaaagctt ttaaaggata 1980 atgtgcaatt cacattaaaa ttgattttcc attgtcaatt agttatactc attttcctgc 2040 cttgatcttt cattagatat tttgtatctg cttggaatat attatcttct ttttaactgt 2100 gtaattggta attactaaaa ctctgtaatc tccaaaatat tgctatcaaa ttacacacca 2160 tgttttctat cattctcata gatctgcctt ataaacattt aaataaaaag tactatttac 2220 caaaaaaaaa aaaaaaaaaa aaaaaaaaa 2249 Table Lill(d). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 170) and 98P4B6v.5 (SEQ ID NO: 171) Score= 398 bits (207), Expect = e-1071dentities = 209/210 (99%) Strand = Plus / Plus V.1: 1 ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccgggcac 60 Illlilllllllllllllllllllllilllllllllllllllllllllllillllil V.5: 14 ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccgggcac 73 V.1; 61 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctccttccttct 120 Illlllllillllllllllllllllllllllllllllllllllilllllllllilllllll V.5: 74 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctccttccttct 133 V.1: 121 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 180 Illllllllllllllllllllllllllllillllllllllllllllllllllill| | V.5: 134 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcta 193 V.1: 181 cggcagccaccctgcaaccgccagtcggag 210 ]lllilllllillllllilllllllllll V.5: 194 cggcagccaccctgcaaccgccagtcggag 223 Score = 2334 bits (1214), Expect = 0.01dentities = 1218/1220 (99%) Strand = Plus / Plus V.1: 320 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 379 Il l l l l l l l l l l l l l l l l l l 1 1 1 1 1 1 l l l l l l l l l l l l l l l l I Il l l l l l l l l V.5: 283 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 342 V.1: 380 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 439 Illlllllllllllllllllllllllllllllilllllllllllllllllllllllll V.5: 343 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 402 V.1: 440 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 499 ll l l l li l l l I l I l l ll l l l l l l l ll l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l V.5: 403 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 462 V.1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 559 Illllllll lllllllllll lillllll |111 ll 11111111111111111111111 V.5: 463 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 522 259 WO 03/087306 PCT/US03/10462 V.1: 560 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 619 I l l l lIll l lI1l l 1 1 1 l l l l l l l l IIl I l l I l l l l l l I I1 l l l l l l l l l V.5: 523 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 582 V.1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 IIl l l Il l l l I l l l l l l i l l l l l l I l l ll I l l l l i V.5: 583 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 642 V.1: 680 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 739 Il l l I l l l l l lI l l l l l l i I III l l l l l i l l i l V.5: 643 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 702 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 Illll llllll1lllllllllll1ll1lllll1l1llllllllllllllllllll1lll V.5: 703 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 762 V.1: 800 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 V.5: 763 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 822 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 V.5: 823 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 882 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 V.5: 883 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 942 V.1: 980 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1039 I I I I I l l I l lll l l l l l l l I l l l l l I l l I l I I V.5: 943 ttactttctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1002 V.1: 1040 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1099 I l l I l l I l l l l lI I I I l l l l i l l l l l l l I l I l l l V.5: 1003 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1062 V.l1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 II l l I I I i l lIIl l 1 l l l I I l l I l l l l l l I l l l V.5: 1063 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1122 V.1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 I I II II II1I1I I I I V.5: 1123 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1182 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 I l li l I l l l l l l l l l l l l l l l l l l l l l I I l l l l l l l l I I l l I V.5: 1183 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1242 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1339 l I l i l l I lII lI260lI 260 WO 03/087306 PCT/USO3/10462 V.5: 1243 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1302 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 I l l l il l l l ll l ll l i l l i l l i l l li ll l l l l li l l l il il l l l l l l l i l i l V.5: 1303 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1362 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 Illillllllllilllllllllllilllllllllllllllllllllllll V.5: 1363 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1422 V.I1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1519 I i l l l l l l l l l l l i l l l l l II Il l i l l l l l i l l l i i i l l l l l l l l l l l ll l l l l V.5: 1423 gcttactttccctcctggcagtcacttctatcccttcggtgagcaatgctttaaactgga 1482 V.1: 1520 gagaattcagttttattcag 1539 1111111111111111111 V.5: 1483 gagaattcagttttattcag 1502 Score =1375 bits (715), Expect = 0.01dentities= 741/749(98%), Gaps = 2/749 (0%) Strand = Plus / Plus V.1: 1687 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 1746 I l l l l li l l l i i l l l l liI il i i l l I I l l l l l lll ll l l l l l iii V.5: 1502 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 1561 V.1: 1747 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 1806 II I I I l l l l l l l1ll l l l 1l l i l l l l l l l I i l l l i I I I I Il V.5: 1562 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 1621 V.1: 1807 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 1866 11111 1111 111111 II 111 11111111111lllI l 1Il llllll l l i V.5: 1622 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 1681 V.1: 1867 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 1926 I l l l I I l l l l ~ l l l l I~ll Il I I i l l l I l l l l l V.5: 1682 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 1741 V.1: 1927 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 1986 S11 l l l l l i l l I IIl i l l i l I I1iI l l l l i l l l llIl l l l l l l l l l l l l V.5: 1742 tg-ctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 1800 V.1: 1987 ttgactacttccctacttccactgctttt-cctgcatttaagccattgtaaatctgggtg 2045 i l l l l l l i l l l I I l l 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 V.5: 1801 ttgactacttccctacttccactgctttttcctgcatttaagccattgtaaatctgggtg 1860 V.1: 2046 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2105 I I I I I I i Ii l i i I I V.5: 1861 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 1920 V.1: 2106 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2165 li ii l Iii! lIiil IIil IlJillill V.5: 1921 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 1980 261 WO 03/087306 PCT/USO3/10462 V.1: 2166 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2225 illllilllillllllflllllllllllllllllllillllllillllillllliillli V.5: 1981 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2040 V.1: 2226 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2285 IIllllllillllli111illlllilllilllllllIIIIlililllllilllli V.5: 2041 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2100 V.1: 2286 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2345 IllllllllllllllilillllililllliltlllIllliIIllllilllillllllllI V.5: 2101 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2160 V.1: 2346 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 2405 l1i111|1|111111 111111111111llllllllllll|llIlllilllil V.5: 2161 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttac 2220 V.1; 2406 tgatttaaaaaaaaaaaaaaaaaaaaaaa 2434 I 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 V.5: 2221 caaaaaaaaaaaaaaaaaaaaaaaaaaaa 2249 NOTE: A SNP AT 192 AND AT 1510, A DELETION AT 1742-1743, AND AN INSERTION OF SINGLE BASE AT 1830 OF V.5. Table LIV(d). Peptide sequences of protein coded by 98P4B6 v.5 (SEQ ID NO: 172) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT EFWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQIFCSF ADTQTELELE FVFLLTLLL 419 Table LV(d). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 173) and 98P4B6 v.5 (SEQ ID NO: 174) Score = 788 bits (2036), Expect = 0.01dentities = 394/395 (99%), Positives = 394/395 (99%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.5: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHWVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.5: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.5: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFT WRGPVVVAISLATFFFLYSFVRDVIHPYA V.5: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTFWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.5: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 262 WO 03/087306 PCT/USO3/10462 V.5: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQ 395 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQ V.5: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQ 395 NOTE: A SNP CAUSED A SINGEL AMINO ACID DIFFERENCE AT 211. Table LII(e). Nucleotide sequence of transcript variant 98P4B6 v.6 (SEQ ID NO: 175) cccacgcgtc cgcggacgcg tgggcggacg cgtgggttcc tcgggccctc ggcgccacaa 60 gctgtccggg cacgcagccc ctagcggcgc gtcgctgcca agccggcctc cgcgqcgcctc 120 cctccttcct tctcccctgg ctgttcgcga tccagcttgg gtaggcgggg aagcagctgg 180 agtgcgaccg ccacggcagc caccctgcaa ccgccagtcg gagagctaag ggcaagtcct 240 gaggttgggc ccaggagaaa gaaggcaagg agacattgtc ccaggatatt cttggtgatc 300 ttggaagtgt ccgtatcatg gaatcaatct ctatgatggg aagccctaag agccttagtg 360 aaacttgttt acctaatggc ataaatggta tcaaagatgc aaggaaggtc actgtaggtg 420 tgattggaag tggagatttt gccaaatcct tgaccattcg acttattaga tgcggctatc 480 atgtggtcat aggaagtaga aatcctaagt ttgcttctga attttttcct catgtggtag 540 atgtcactca tcatgaagat gctctcacaa aaacaaatat aatatttgtt gctatacaca 600 gagaacatta tacctccctg tgggacctga gacatctgct tgtgggtaaa atcctgattg 660 atgtgagcaa taacatgagg ataaaccagt acccagaatc caatgctgaa tatttggctt 720 cattattccc agattctttg attgtcaaag gatttaatgt tgtctcagct tgggcacttc 780 agttaggacc taaggatgcc agccggcagg tttatatatg cagcaacaat attcaagcgc 840 gacaacaggt tattgaactt gcccgccagt tgaatttcat tcccattgac ttgggatcct 900 tatcatcagc cagagagatt gaaaatttac ccctacgact ctttactctc tggagagggc 960 cagtggtggt agctataagc ttggccacat tttttttcct ttattccttt gtcagagatg 1020 tgattcatcc atatgctaga aaccaacaga gtgactttta caaaattcct atagagattg 1080 tgaataaaac cttacctata gttgccatta ctttgctctc cctagtatac cttgcaggtc 1140 ttctggcagc tgcttatcaa ctttattacg gcaccaagta taggagattt ccaccttggt 1200 tggaaacctg gttacagtgt agaaaacagc ttggattact aagttttttc ttcgctatgg 1260 tccatgttgc ctacagcctc tgcttaccga tgagaaggtc agagagatat ttgtttctca 1320 acatggctta tcagcaggtt catgcaaata ttgaaaactc ttggaatgag gaagaagttt 1380 ggagaattga aatgtatatc tcctttggca taatgagcct tggcttactt tbcctcctgg 1440 cagtcacttc tatcccttca gtgagcaatg ctttaaactg gagagaattc agttttattc 1500 agtctacact tggatatgtc gctctgctca taagtacttt ccatgtttta atttatggat 1560 ggaaacgagc ttttgaggaa gagtactaca gattttatac accaccaaac tttgttcttg 1620 ctcttgtttt gccctcaatt gtaattctgg gtaagattat tttattcctt ccatgtataa 1680 gccgaaagct aaaacgaatt aaaaaaggct gggaaaagag ccaatttctg gaagaaggta 1740 ttggaggaac aattcctcat gtctccccgg agagggtcac agtaatgtga tgataaatgg 1800 tgttcacagc tgccatataa agttctactc atgccattat ttttatgact tctacgttca 1860 gttacaagta tgctgtcaaa ttatcgtgg ttgaaacttg ttaaatgaga tttcaactga 1920 cttagtgata gagttttctt caagttaatt ttcacaaatg tcatgtttgc caatatgaat 1980 ttttctagtc aacatattat tgtaatttag gtatgttttg ttttgttttg cacaactgta 2040 accctgttgt tactttatat ttcataatca gacaaaaata cttacagtta ataatataga 2100 tataatgtta aaaacaattt gcaaaccagc agaattttaa gcttttaaaa taattcaatg 2160 gatatacatt tttttctgaa gattaagatt ttaattattc aacttaaaaa gtagaaatgc 2220 attattatac atttttttaa gaaaggacac gttatgttag catctaggta aggctgcatg 2280 atagcattcc tatatttctc tcataaaata ggatttgaag gatgaaatta attgtatgaa 2340 gcaatgtgat tatatgaaga gacacaaatt aaaaagacaa attaaacctg aaattatatt 2400 taaaatatat ttgagacatg aaatacatac tgataataca tacctcatga aagattttat 2460 tctttattgt gttacagagc agtttcattt tcatattaat atactgatca ggaagaggat 2520 tcagtaacat ttggcttcca aaactgctat ctctaatacg gtaccaatcc taggaactgt 2580 atactagttc ctacttagaa caaaagtatc aagtttgcac acaagtaatc tgccagctga 2640 cctttgtcgc accttaacca gtcaccactt gctatggtat aggattatac tgatgttctt 2700 tgagggattc tgatgtgcta ggcatggttc taagtacttt acttgtatta tcccatttaa 2760 tacttagaac aaccccgtga gataagtagt tattatcctc attttacaca tgagggaccg 2820 aaggatagaa aagttatttt tcaaaggtct tgcagttaat aaatggcaga gtgagcattc 2880 aagtccaggt agtcatattc cagaggccac ggttttaacc actaggctct agagctcccg 2940 ccgcgcccct atgcattatg ttcacaatgc caatctagat gcttcctctt ttgtataaag 3000 tcactgacat tctttagagt gggttgggtg catccaaaaa tgtataaaaa tattattata 3060 ataaacttat tactgcttgt agggtaattc acagttactt accctattct tgcttggaac 3120 atgagcctgg agacccatgg cagtccatat gcctccctat gcagtgaagg gccctagcag 3180 263 WO 03/087306 PCT/USO3/10462 tgttaacaaa ttgctgagat cccacggagt ctttcaaaaa tctctgtaga gttagtcttc 3240 tccttttctc ttcctgagaa gttctcctgc ctgcataacc attcattagg gagtacttta 3300 caagcatgaa ggatattagg gtaagtggct aattataaat ctactctaga gacatataat 3360 catacagatt attcataaaa tttttcagtg otgtccttcc acatttaatt gcattttgct 3420 caaactgtag aatgccctac attcccccca coccaatttg ctatttcctt attaaaatag 3480 aaaattatag gcaagataca attatatgcg ttcctcttcc tgaaattata acatttctaa 3540 acttacccac gtagggacta ctgaatccaa ctgccaacaa taaaaagact tttatttagt 3600 agaggctacc tttcccccca gtgactcttt ttctacaact gccttgtcag tttggtaatt 3660 cacttatgat tttctaatgt tctcttggtg aattttatta tcttggaccc tctttttttt 3720 tttttttaaa gacagagtct tgctctgtca ccca 3754 Table LIII(e). Nucleotide sequence alignment of 98P486 v.1 (SEQ ID NO: 176) and 98P4B6 v.6 (SEQ ID NO: 177) Score= 404 bits (210), Expect= e-1091dentities = 210/210(100%) Strand= Plus/ Plus V.1: 1 ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccgggcac 60 ff11 11I II lIt f fll I flI I ll I ff11 11I 111f ff I lfl Ill II V.6: 14 ggacgcgtgggcggacgcgtgggttcctcgggccctcggcgccacaagctgtccgggcac 73 V.1: 61 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctccttccttct 120 11111 iIii ff11111 f f ff1111 ff111111III I lff1111ilIl 11ff 1f V.6: 74 gcagcccctagcggcgcgtcgctgccaagccggcctccgcgcgcctccctccttccttct 133 V.1: 121 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 180 111111 fiIIIIIiIIlII 111ff 111111 ff1111111111111111 V.6: 134 cccctggctgttcgcgatccagcttgggtaggcggggaagcagctggagtgcgaccgcca 193 V.1: 181 cggcagccaccctgcaaccgccagtcggag 210 IIl il l l i f l l l li i l l I i il i li l l l i V.6: 194 cggcagccaccctgcaaccgccagtcggag 223 Score= 2630 bits (1368), Expect= 0.01Odentities = 1368/1368 (100%) Strand= Plus/ Plus V.1: 320 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 379 111111ff111111111ff 111111f fll] ~l~l 11111111111ff 1111111ff V.6: 283 aggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaa 342 V.1: 380 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 439 V.6: 343 gccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaa 402 V.1: 440 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 499 V.6: 403 ggaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgac 462 V.1: 500 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 559 V.6: 463 ttattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaat 522 V.1: 560 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 619 V.6: 523 tttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataa 582 V.1: 620 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 679 264 WO 03/087306 PCT/USO3/10462 I l l l l l l l I l l I l l l l I l l ll i l l I l l l l l l l l I l l V.6: 583 tatttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttg 642 V.1: 680 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 739 I lI l l l ll1 l l l l l l l l l l l l l 1 l l l1 l 1l l l l l l l l ll i l l lI l l ill l Ill V.6: 643 tgggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatcca 702 V.1: 740 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 799 V.6: 703 atgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttg 762 V.1: 800 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 859 IIilllill l llI IIIIlli I llll Il l l 11 llI V.6: 763 tctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgca 822 V.1: 860 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 919 V.6: 823 gcaacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattc 882 V.1: 920 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 979 l l ll l ll l l ll I I ll lIi l i l l ll l l l l ll l ll l l 1l l i l l l l ll l l l il V.6: 883 ccattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactct 942 V.1: 980 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1039 V.6: 943 ttactctctggagagggccagtggtggtagctataagcttggccacattttttttccttt 1002 V.1: 1040 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1099 V.6: 1003 attcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttaca 1062 V.1: 1100 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1159 1 11 11 1111111111111111111111111l ll lllli ll lI i l lI V.6: 1063 aaattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccc 1122 V~1: 1160 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1219 I lilllIllI lllllll Il illl lIi IIlIllIIII li llllll V.6: 1123 tagtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtata 1182 V.1: 1220 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1279 I I li l ll l l I l l l 1 1 1 1 1 1i V.6: 1183 ggagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaa 1242 V.1: 1280 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1339 I i i III ii ll Jll ii V.6: 1243 gttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcag 1302 V.1: 1340 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1399 1 1 1III 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1111 1 1 i 1 I V.6: 1303 agagatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactctt 1362 265 WO 03/087306 PCT/USO3/10462 V.1: 1400 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1459 IlllllillllllillllllllllllllllllilllllllllllIIlllllllllllllllIl V.6: 1363 ggaatgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttg 1422 V.1: 1460 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1519 Ill1lllllllllllllllllllllllllllllllIllllllllllllllllllll V.6: 1423 gcttactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactgga 1482 V.I: 1520 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1579 11 11111 111111111111 111111111111111lil ll t|l ll ll 1ll llll V.6: 1483 gagaattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttcc 1542 V.1: 1580 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1639 IllllllllllllllllillllllllllllllllllllllllllllillllllllllIl V.6: 1543 atgttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacac 1602 V.1: 1640 caccaaactttgttcttgctcttgttttgccctcaattgtaattctgg 1687 l i l l ll l li l l l l l l l l l l li l l l l l l l ll l l l l l l l l l l l l l l l V.6: 1603 caccaaactttgttcttgctcttgttttgccctcaattgtaattctgg 1650 Table LIV(e). Peptide sequences of protein coded by 98P4B6 v.6 (SEQ ID NO: 178) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILGKIILF LPCISRKLKR IKKGWEKSQF LEEGIGGTIP 480 HVSPERVTVM 490 Table LV(e). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 179) and 98P4B6 v.6 (SEQ ID NO: 180) Score = 888 bits (2294), Expect = 0.01dentities = 444/444 (100%), Positives = 444/444 (100%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.6: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYRVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.6: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.6: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.6: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.6: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 266 WO 03/087306 PCT/USO3/10462 V.6: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE V.6: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V.1: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 EEYYRFYTPPNFVLALVLPSIVIL V.6: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 Table LII(f). Nucleotide sequence of transcript variant 98P4B6 v.7 (SEQ ID NO: 181) ggagaaaatt tacagaaacc cagagccaaa ggtgctctca ggggatcccc tgaaacattc 60 aaagccattg cggccccaga agcttgggta ggcggggaag cagctggagt gcgaccgccg 120 cggcagccac cctgcaaccg ccagtcggag gtgcagtccg taggccctgg cccccgggtg 180 ggcccttggg gagtcggcgc cgctcccggg gagctgcaag gctcgcccct gcccggcgtg 240 gagggcgcgg ggggcgcgga ggatattctt ggtgatcttg gaagtgtccg tatcatggaa 300 tcaatctcta tgatgggaag ccctaagagc cttagtgaaa cttttttacc taatggcata 360 aatggtatca aagatgcaag gaaggtcact gtaggtgtga ttggaagtgg agattttgcc 420 aaatccttga ccattcgact tattagatgc ggctatcatg tggtcatagg aagtagaaat 480 cctaagtttg cttctgaatt ttttcctcat gtggtagatg tcactcatca tgaagatgct 540 ctcacaaaaa caaatataat atttgttgct atacacagag aacattatac ctccctgtgg 600 gacctgagac atctgcttgt gggtaaaatc ctgattgatg tgagcaataa catgaggata 660 aaccagtacc cagaatccaa tgctgaatat ttggcttcat tattcccaga ttctttgatt 720 gtcaaaggat ttaatgttgt ctcagcttgg gcacttcagt taggacctaa ggatgccaqc 780 cggcaggttt atatatgcag caacaatatt caagcgcgac aacaggttat tgaacttgcc 840 cgccagttga atttcattcc cattgacttg ggatccttat catcagccag agagattgaa 900 aatttacccc tacgactctt tactctctgg agagggccag tggtggtagc tataagcttg 960 gccacatttt ttttccttta ttcctttgtc agagatgtga ttcatccata tgctagaaac 1020 caacagagtg acttttacaa aattcctata gagattgtga ataaaacctt acctatagtt 1080 gccattactt tgctctccct agtatacctc gcaggtcttc tggcagctgc ttatcaactt 1140 tattacggca ccaagtatag gagatttcca ccttggttgg aaacctggtt acagtgtaga 1200 aaacagcttg gattactaag ttttttcttc gctatggtcc atgttgccta cagcctctgc 1260 ttaccgatga gaaggtcaga gagatatttg tttctcaaca tggcttatca qcagtctaca 1320 cttggatatg tcgctctgct cataagtact ttccatgttt taatttatgg atggaaacga 1380 gcttttgagg aagagtacta cagattttat acaccaccaa actttgttct tgctcttgtt 1440 ttgccctcaa ttgtaattct ggatctgtct gtggaggttc tggcttcccc agctgctgcc 1500 tggaaatgct taggtgctaa tatcctgaga ggaggattgt cagagatagt actccccata 1560 gagtggcagc aggacaggaa gatcccccca ctctccaccc cgccgccacc ggccatgtgg 1620 acagaggaag ccggggcgac cgccgaggcc caggaatccg gcatcaggaa caagtctagc 1680 agttccagtc aaatcccggt ggttggggtg gtgacggagg acgatgaggc gcaggattcc 1740 attgatcccc cagagagccc tgatcgtgcc ttaaaagccg cgaattcctg gaggaaccct 1800 gtcctgcctc acactaatgg tgtggggcca ctgtgggaat tcctgttgag gcttctcaaa 1860 tctcaggctg cgtcaggaac cctgtctctt gcgttcacat cctggagcct tggagagttc 1920 cttgggagtg ggacatggat gaagctggaa accataattc tcagcaaact aacacaggaa 1980 cagaaatcca aacactgcat gttctcactg ataagtggga gttgaacaat gagaacacat 2040 ggacacaggg aggggaacgt cacacaccag ggcctgtcgg gggtgggagg cctagcaatt 2100 cattagaatt acctgtgaag cttttaaaat gtaaggtttg gatggaatgc tcagacccta 2160 ccttagaccc aattaagccc aca'gctttga gg 2192 Table LIIl(f). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 182) and 98P4B6 v.7 (SEQ ID NO: 183) Score = 2350 bits (1222), Expect = 0.01dentities = 1230/1234 (99%) Strand = Plus / Plus V.1: 141 agcttgggtaggcggggaagcagctggagtgcgaccgccacggcagccaccctgcaaccg 200 Ill lill l l lll lllll lllllll1 1 111111 1 l 11111 1i1i 11 111 11i 11 V.7: 81 agcttgggtaggcggggaagcagctggagtgcgaccgccgcggcagccaccctgcaaccg 140 V.1: 201 ccagtcggaggtgcagtccgtaggccctggcccccgggtgggcccttggggagtcggcgc 260 I l 1 11Ill l l l l l l I l ll il ll l i l l l J1 1 1ilill1 1 1 1 1 1 1 1 1 1 1 V.7: 141 ccagtcggaggtgcagtccgtaggccctggcccccgggtgggcccttggggagtcggcgc 200 267 WO 03/087306 PCT/US03/10462 V.1: 261 cgctcccgaggagctgcaaggctcgcccctgcccggcgtggagggcgcggggggcgcgga 320 Ii11 1 I II 1 111 illll11ll 1ll ll 1lll lll111 l1 lllli lljj ll lll V.7: 201 cgctcccggggagctgcaaggctcgcccctgcccggcgtggagggcgcgggggcgcgga 260 V.1: 321 ggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaag 380 l i l l 1 l l l i l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l i l V.7: 261 ggatattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaag 320 V.1: 381 ccctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaag 440 V.7: 321 ccctaagagccttagtgaaacttttttacctaatggcataaatggtatcaaagatgcaag 380 V.1: 441 gaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgact 500 I I l l l l l l l l l I l l l l1 1 1 i l l l l l l l l l l l i li l l l l i l l l l V.7: 381 gaaggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgact 440 V.1: 501 tattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaatt 560 V.7: 441 tattagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaatt 500 V.1: 561 ttttactcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataat 620 I l l l l l l l l l l l l l l l l l l l l l l i l 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 V.7: 501 ttttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataat 560 V.1: 621 atttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttgt 680 Illi lll 1llll 1lll llllli l l llll il llll11 llililll11 lillll|1 V.7: 561 atttgttgctatacacagagaacattatacctccatgtgggacctgagacatctgcttgt 620 V.1: 681 gggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaa 740 V.7: 621 gggtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaa 680 V.1: 741 tgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttgt 800 V.7: 681 tgctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttgt 740 V.1: 801 ctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcag 860 V.7: 741 ctcagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcag 800 V.1: 861 caacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattcc 920 V.7: 801 caacaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattcc 860 V.1: 921 cattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactatt 980 V.7: 861 cattgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactctt 920 V.1: 981 tactctctggagagggccagtggtggtagctataagcttggccacattttttttacttta 1040 268 WO 03/087306 PCT/USO3/10462 V.7: 921 tactctctggagagggccagtggtggtagctataagcttggccacattttttttccttta 980 V.1: 1041 ttcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttacaa 1100 II l l l l l l i l l i l l I l l I l ll lll l l l l l l l l l l l i l llll1l 1ll i l l l l l l V.7: 981 ttcctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttacaa 1040 V.1: 1101 aattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccct 1160 I l ll IIl IIIIIlI l l l IlIII I l llllllllI l lll l ll illllllll V.7: 1041 aattcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccct 1100 V.1: 1161 agtataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtatag 1220 I I l l l lI l l I 1 l l l l l i l I l l l l i l l l l l l l l l l l I I I l l l l l1 1 II I II l V.7: 1101 agtatacctcgcaggtcttctggcagctgcttatcaactttattacggcaccaagtatag 1160 V.1: 1221 gagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaag 1280 V.7: 1161 gagatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaag 1220 V.1: 1281 ttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcaga 1340 l l l l l l l l l l I l ll ll l l i l l l l l l l I ll l l l l l l l l l l l l I V.7: 1221 ttttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcaga 1280 V.1: 1341 gagatatttgtttctcaacatggcttatcagcag 1374 V.7: 1281 gagatatttgtttctcaacatggcttatcagcag 1314 Score = 298 bits (155), Expect = 2e-771dentities = 155/155 (100%) Strand Plus / Plus V.1: 1537 cagtctacacttggatatgtcgctctgctcataagtactttccatgttttaatttatgga 1596 Il l l l l l l l l l l l I I l l l l l l l l l l l l l l l l l l 1 1 1 l l l l l l l l l l l l l l l l1 V.7: 1312 cagtctacacttggatatgtcgctctgctcataagtactttccatgttttaatttatgga 1371 V.1: 1597 tggaaacgagcttttgaggaagagtactacagattttatacaccaccaaactttgttctt 1656 IlilllllilllllllllllllllllllilllIlllllllIIllllllllli V.7: 1372 tggaaacgagcttttgaggaagagtactacagattttatacaccaccaaactttgttctt 1431 V.1: 1657 gctcttgttttgccctcaattgtaattctggatct 1691 IllllllllllllllllllllllllIlllllII V.7: 1432 gctcttgttttgccctcaattgtaattctggatct 1466 Table LIV(f). Peptide sequences of protein coded by 98P4B6 v.7 (SEQ ID NO: 184) MESISMMGSP KSLSETFLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ STLGYVALLI STFHVLIYGW 360 KRAFEEEYYR FYTPPNFVLA LVLPSIVILD LSVEVLASPA AAWKCLGANI LRGGLSEIVL 420 PIEWQQDRKI PPLSTPPPPA MWTEEAGATA EAQESGIRNK SSSSSQIPVV GVVTEDDEAQ 480 DSIDPPESPD RALKAANSWR NPVLPHTNGV GPLWEFLLRL LKSQAASGTL SLAFTSWSLG 540 EFLGSGTWMK LETITLSKLT QEQKSKHCMF SLISGS 576 269 WO 03/087306 PCT/US03/10462 Table LV(f). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 185) and 98P4B6 v.7 (SEQ ID NO: 186) Score = 753 bits (1944), Expect = 0.01dentities = 390/446 (87%), Positives = 390/446 (87%), Gaps = 55/446 (12%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSET LPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.7: 1 MESISMMGSPKSLSETFLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.7: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.I1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.7: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.7: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.I1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.7: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQ V.7: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQ-- ------------------ 340 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 STLGYVALLISTFHVLIYGWKRAFE V.7: 341 ------------------------------------ STLGYVALLISTFHVLIYGWKRAFE 365 V.1: 421 EEYYRFYTPPNFVLALVLPSIVILDL 446 EEYYRFYTPPNFVLALVLPSIVILDL V.7: 366 EEYYRFYTPPNFVLALVLPSIVILDL 391 Table Ll1(g). Nucleotide sequence of transcript variant 98P4B6 v.8 (SEQ ID NO: 187) gccccctccg agctccccga ctcctccccg cgctccacgg ctcttcccga ctccagtcag 60 cgttcctcgg gccctcggcg ccacaagctg tccgggcacg cagcccctag cggcgcgtcg 120 ctgccaagcc ggcctccgcg cgcctccctc cttccttctc ccctggctgt tcgcgatcca 180 gcttgggtag gcggggaagc agctggagtg cgaccgccac ggcagccacc ctgcaaccgc 240 cagtcggagg tgcagtccgt aggccctggc ccccgggtgg gcccttgggg agtcggcgcc 300 gctcccgagg agctgcaagg ctcgcccctg cccggcgtgg agggcgcggg gggcgcggag 360 gatattcttg gtgatcttgg aagtgtccgt atcatggaat caatctctat gatgggaagc 420 cctaagagcc ttagtgaaac ttgtttacct aatggcataa atggtatcaa agatgcaagg 480 aaggtcactg taggtgtgat tggaagtgga gattttgcca aatccttgac cattcgactt 540 attagatgcg gctatcatgt ggtcatagga agtagaaatc ctaagtttgc ttctgaattt 600 tttcctcatg tggtagatgt cactcatcat gaagatgctc tcacaaaaac aaatataata 660 tttgttgcta tacacagaga acattatacc tccctgtggg acctgagaca tctgcttgtg 720 ggtaaaatcc tgattgatgt gagcaataac atgaggataa accagtaccc agaatccaat 780 gctgaatatt tggcttcatt attcccagat tctttgattg tcaaaggatt taatgttgtc 840 tcagcttggg cacttcagtt aggacctaag gatgccagcc ggcaggttta tatatgcagc 900 aacaatattc aagcgcgaca acaggttatt gaacttgccc gccagttgaa tttcattccc 960 attgacttgg gatccttatc atcagccaga gagattgaaa atttacccct acgactcttt 1020 actctctgga gagggccagt ggtggtagct ataagcttgg ccacattttt tttcctttat 1080 tcctttgtca gagatgtgat tcatccatat gctagaaacc aacagagtga cttttacaaa 1140 attcctatag agattgtgaa taaaacctta cctatagttg ccattacttt gctctcccta 1200 gtataccttg caggtcttct ggcagctgct tatcaacttt attacggcac caagtatagg 1260 agatttccac cttggttgga aacctggtta cagtgtagaa aacagcttgg attactaagt 1320 tttttcttcg ctatggtcca tgttgcctac agcctctgct taccgatgag aaggtcagag 1380 agatatttgt ttctcaacat ggcttatcag caggttcatg caaatattga aaactcttgg 1440 aatgaggaag aagtttggag aattgaaatg tatatctcct ttggcataat gagccttggc 1500 ttactttccc tcctggcagt cacttctatc ccttcagtga gcaatgcttt aaactggaga 1560 270 WO 03/087306 PCT/US03/10462 gaattcagtt ttattcagtc tacacttgga tatgtcgctc tgctcataag tactttccat 1620 gttttaattt atggatggaa acgagctttt gaggaagagt actacagatt ttatacacca 1680 ccaaactttg ttcttgctct tgttttgccc tcaattgtaa ttctgggtaa gattatttta 1740 ttccttccat gtataagccg aaagctaaaa cgaattaaaa aaggctggga aaagagccaa 1800 tttctggaag aaggtatggg aggaacaatt cctcatgtct ccccggagag ggtcacagta 1860 atgtgatgac aaatggtgtt cacagctgcc atataaagtt ctactcatgc cattattttt 1920 atgacttcta cgttcagtta caagtatgct gtcaaattat cgtgggttga aacttgttaa 1980 atgagatttc aactgactta gtgatagagt tttcttcaag ttaattttca caaatgtcat 2040 gtttgccaat atgaattttt ctagtcaaca tattattgta atttaggtat gttttgtttt 2100 gttttgcaca actgtaaccc tgttgttact ttatatttca taatcaggca aaaatactta 2160 cagttaataa tatagatata atgttaaaaa caatttgcaa accagcagaa ttttaagctt 2220 ttaaaataat tcaatggata tacatttttt tctgaagatt aagattttaa ttattcaact 2280 taaaaagtag aaatgcatta ttatacattt ttttaagaaa ggacacgtta tgttagcatc 2340 taggtaaggc tgcatgatag cattcctata tttctctcat aaaataggat ttgaaggatg 2400 aaattaattg tatgaagcaa tgtgattata tgaagagaca caaattaaaa agacaaatta 2460 aacctgaaat tatatttaaa atatatttga gacatgaaat acatactgat aatacatacc 2520 tcatgaaaga ttttattctt tattgtgtta cagagcagtt tcattttcat attaatatac 2580 tgatcaggaa gaggattcag taacatttgg cttccaaaac tgctatctct aatacggtac 2640 caatcctagg aactgtatac tagttcctac ttagaacaaa agtatcaagt ttgcacacaa 2700 gtaatctgcc agctgacctt tgtcgcacct taaccagtca ccacttgcta tggtatagga 2760 ttatactgat gttctttgag ggattctgat gtgctaggca tggttctaag tactttactt 2820 gtattatccc atttaatact tagaacaacc ccgtgagata agtagttatt atcctcattt 2880 tacacatgag ggaccgaagg atagaaaagt tatttttcaa aggtcttgca gttaataaat 2940 ggcagagtga gcattcaagt ccaggtagtc atattccaga ggccacggtt ttaaccacta 3000 ggctctagag ctcccgccgc gcccctatgc attatgttca caatgccaat ctagatgctt 3060 cctcttttgt ataaagtcac tgacattctt tagagtgggt tgggtgcatc caaaaatgta 3120 taaaaatatt attataataa acttattact gcttgtaggg taattcacag ttacttaccc 3180 tattcttgct tggaacatga gcctggagac ccatggcagt ccatatgcct ccctatgcag 3240 tgaagggccc tagcagtgtt aacaaattgc tgagatccca cggagtcttt caaaaatctc 3300 tgtagagtta gtcttctcct tttctcttcc tgagaagttc tcctgcctgc ataaccattc 3360 attagggagt actttacaag catgaaggat attagggtaa gtggctaatt ataaatctac 3420 tctagagaca tataatcata cagattattc ataaaatttt tcagtgctgt ccttccacat 3480 ttaattgcat tttgctcaaa ctgtagaatg ccctacattc cccccacccc aatttgctat 3540 ttccttatta aaatagaaaa ttataggcaa gatacaatta tatgcgttcc tcttcctgaa 3600 attataacat ttctaaactt acccacgtag gtactactga atccaactgc caacaataaa 3660 aagactttta tttagtagag gctacctttc ccaccagtga ctctttttct acaactgcct 3720 tgtcagtttg gtaattcact tatgattttc taatgttctc ttggtgaatt ttattatctt 3780 gtaccctctt tttttttttt ttttttttta aagacagagt cttgctctgt cacccaggct 3840 ggagtgcagt ggcacgatct cggctcactg caagctctgc ctcccgggtt cacgccattc 3900 tcctgcctca gcctcccgag tagctgggac tacaggtgcc cgccaccatg cccggctgat 3960 ttctttttgt atttttagta gagacggagt ttcaccgtgt tagccaggat ggtctcgatc 4020 tcctgacctc gtgatccgcc cgccttggcc tccaaagtgc tgggattaca ggtgtgagct 4080 accgcgcccg gcctattatc ttgtactttc taactgagcc ctctattttc tttattttaa 4140 taatatttct ccccacttga gaatcacttg ttagttcttg gtaggaattc agttgggcaa 4200 tgataacttt tatgggcaaa aacattctat tatagtgaac taatgaaaat aacagcgtat 4260 tttcaatatt ttcttattcc ttaaattcca ctcttttaac actatgctta accacttaat 4320 gtgatgaaat attcctaaaa gttaaatgac tattaaagca tatattgttg catgtatata 4380 ttaagtagcc gatactctaa ataaaaatac cactgttaca gataaatggg gcctttaaaa 4440 atatgaaaaa caaacttgtg aaaatgtata aaagatgcat ctgttgtttc aaatggcact 4500 atcttctttt cagtactaca aaaacagaat aattttgaag ttttagaata aatgtaatat 4560 atttactata attctaaatg tttaaatgct tttctaaaaa tgcaaaacta tgatgtttag 4620 ttgctttatt ttacctctat gtgattattt ttcttaattg ttatttttta taatcattat 4680 ttttctgaac cattcttctg gcctcagaag taggactgaa ttctactatt gctaggtgtg 4740 agaaagtggt ggtgagaacc ttagagcagt ggagatttgc tacctggtct gtgttttgag 4800 aagtgcccct tagaaagtta aaagaatgta gaaaagatac tcagtcttaa tcctatgcaa 4860 aaaaaaaaat caagtaattg ttttcctatg aggaaaataa ccatgagctg tatcatgcta 4920 cttagctttt atgtaaatat ttcttatgtc tcctctatta agagtattta aaatcatatt 4980 taaatatgaa tctattcatg ctaacattat ttttcaaaac atacatggaa atttagccca 5040 gattgtctac atataaggtt tttatttgaa ttgtaaaata tttaaaagta tgaataaaat 5100 atatttatag gtatttatca gagatgatta ttttgtgcta catacaggtt ggctaatgag 5160 ctctagtgtt aaactacctg attaatttct tataaagcag cataaccttg gcttgattaa 5220 ggaattctac tttcaaaaat taatctgata atagtaacaa ggtatattat actttcatta 5280 caatcaaatt atagaaatta cttgtgtaaa agggcttcaa gaatatatcc aatttttaaa 5340 271 WO 03/087306 PCT/USO3/10462 tattttaata tatctcctat ctgataactt aattcttcta aattaccact tgccattaag 5400 ctatttcata ataaattctg tacagtttcc ccccaaaaaa gagatttatt tatgaaatat 5460 ttaaagtttc taatgtggta ttttaaataa agtatcataa atgtaataag taaatattta 5520 tttaggaata ctgtgaacac tgaactaatt attcctgtgt cagtctatga aatccctgtt 5580 ttgaaatacg taaacagcct aaaatgtgtt gaaattattt tgtaaatcca tgacttaaaa 5640 caagatacat acatagtata acacacctca cagtgttaag atttatattg tgaaatgaga 5700 caccctacct tcaattgttc atcagtgggt aaaacaaatt ctgatgtaca ttcaggacaa 5760 atgattagcc ctaaatgaaa ctgtaataat ttcagtggaa actcaatctg tttttacctt 5820 taaacagtga attttacatg aatgaatggg ttcttcactt tttttttagt atgagaaaat 5880 tatacagtgc ttaattttca gagattcttt ccatatgtta ctaaaaaatg ttttgttcag 5940 cctaacatac tgagtttttt ttaactttct aaattattga atttccatca tgcattcatc 6000 caaaattaag gcagactgtt tggattcttc cagtggccag atgagctaaa ttaaatcaca 6060 aaagcagatg cttttgtatg atctccaaat tgccaacttt aaggaaatat tctcttgaaa 6120 ttgtctttaa agatcttttg cagctttgca gatacccaga ctgagctgga actggaattt 6180 gtcttcctat tgactctact tctttaaaag cggctgccca ttacattcct cagctgtcct 6240 tgcagttagg tgtacatgtg actgagtgtt ggccagtgag atgaagtctc ctcaaaggaa 6300 ggcagcatgt gtcctttttc atcccttcat cttgctgctg ggattgtgga tataacagga 6360 gccctggcag ctgtctccag aggatcaaag ccacacccaa agagtaaggc agattagaga 6420 ccagaaagac cttgactact tccctacttc cactgctttt tcctgcattt aagccattgt 6480 aaatctgggt gtgttacatg aagtgaaaat taattctttc tgcccttcag ttctttatcc 6540 tgataccatt taacactgtc tgaattaact agactgcaat aattctttct tttgaaagct 6600 tttaaaggat aatgtgcaat tcacattaaa attgattttc cattgtcaat tagttatact 6660 cattttcctg ccttgatctt tcattagata ttttgtatct gcttggaata tattatcttc 6720 tttttaactg tgtaattggt aattactaaa actctgtaat ctccaaaata ttgctatcaa 6780 attacacacc atgttttcta tcattctcat agatctgcct tataaacatt taaataaaaa 6840 gtactattta atgattt 6857 Table LIIl(g). Nucleotide sequence alignment of 98P4B6 v.1 (SEQ ID NO: 188) and 98P4B6 v.8 (SEQ ID NO: 189) Score = 3201 bits (1665), Expect = 0.01dentities = 1665/1665 (100%) Strand = Plus / Plus V.1: 23 gttcctcgggecctcggcgccacaagctgtccgggcacgcagcccctagcggcgcgtcgc 82 l I l l l l l l l l l l l l l l l l l l l i l l l l l l l l llllI l l I l l l l l l l l I l l l I l V.8: 62 gttcctcgggccctcggcgccacaagctgtccgggcacgcagcccctagcggcgtcqc 121 V.1: 83 tgccaagccggcctccgcgcgcctccctccttccttctcccctggctgttcgcgatccag 142 I I l ~ l l l I l l l l l i l l l l l I l l l l l lI l lI l l l l I I l l V.8: 122 tgccaagccggcctccgcgcgcctccctccttccttctcccctggctgttcgcgatccag 181 V.1: 143 cttgggtaggcggggaagcagctggagtgcgaccgccacggcagccaccctgcaaccgcc 202 I I I 1 l l l i l l l l 1l i l l l l l l l i l l l l l l l l l l l I I I I I l l l l l l l l lll l l I l l l l V.8: 182 cttgggtaggcggggaagcagctggagtgcgaccgccacggcagccaccctgcaaccgcc 241 V.1: 203 agtcggaggtgcagtccgtaggccctggcccccgggtgggcccttggggagtcggcgccg 262 I l l l l i l l l l lllll l l l l l I l II l l l l l l l l l I I I l l V.8: 242 agtcggaggtgcagtccgtaggccctggcccccgggtgggcccttggggagtcggcgccg 301 V.1: 263 ctcccgaggagctgcaaggctcgcccctgcccggcgtggagggcgcggggggcgcggagg 322 I l l l l l I l lI I I l I I l l l l Il l l l l l l l l l l l l i l l V.8: 302 ctcccgaggagctgcaaggctcqcccctgcccggcgtggagggcgcggggggcgcggagg 361 V.1: 323 atattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaagcc 382 IIl l I ll l l l l 1 1 1 1 1 1 1 1 | I I I1 V.8: 362 atattcttggtgatcttggaagtgtccgtatcatggaatcaatctctatgatgggaagcc 421 V.1: 383 ctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaagga 442 IIi l l l l l l l l l l l l l l l l lI Il l l l l l ll7l l I l l l l i l l I I 272 WO 03/087306 PCT/USO3/10462 V.8: 422 ctaagagccttagtgaaacttgtttacctaatggcataaatggtatcaaagatgcaagga 481 V.1: 443 aggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgactta 502 V.8: 482 aggtcactgtaggtgtgattggaagtggagattttgccaaatccttgaccattcgactta 541 V.1: 503 ttagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgettctgaatttt 562 IllilllllllIl11llll1II1llllllll1|11111111111111111111111111 V.8: 542 ttagatgcggctatcatgtggtcataggaagtagaaatcctaagtttgcttctgaatttt 601 V.1: 563 ttcctcatgtggtagatgtcactcatcatgaagatgctctcacaaaaacaaatataatat 622 111111111||1111111111111|11111|lllllllllllllllllllllll1lllil V.8: 602 ttcctcatgtggtagatgtcactcatcatgaagatgetctcacaaaaacaaatataatat 661 V.1: 623 ttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttgtgg 682 V.8: 662 ttgttgctatacacagagaacattatacctccctgtgggacctgagacatctgcttgtgg 721 V.1: 683 gtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaatg 742 I l 1 1l l l l l l l l l l 1 1l l i l I l l l l l l l l l l l l l l l l l l l l l l l l i l l l l l l l l l l l V.8: 722 gtaaaatcctgattgatgtgagcaataacatgaggataaaccagtacccagaatccaatg 781 V.1: 743 ctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttgtot 802 V.8: 782 ctgaatatttggcttcattattcccagattctttgattgtcaaaggatttaatgttgtot 841 V.1: 803 cagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcagca 862 IIlllIlilll11lil111I1ll11ll111l1llllllllllllllllllllll11l V.8: 842 cagcttgggcacttcagttaggacctaaggatgccagccggcaggtttatatatgcagca 901 V.1: 863 acaatattcaagcgcgacaacaggttattgaacttgcccgccagttgaatttcattacca 922 I l l l l l l l l l 11l 1l l l l l l 1 1I 1l l l l l l l l l l l i l l l l l l l l l 1l l l l l l il l l l l l V.8: 902 acaatattcaagcgcgacaacaggttattgaacttgcccgacagttgaatttcattccca 961 V.1: 923 ttgacttgggatccttatcatcagccagagagattgaaaatttacccctacgactattta 982 Il i l l l l l l l I l l l l l l l l l l l l l l l l l l l 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 1 | 1 1 1 1 1 1 1 V.8: 962 ttgacttgggatccttatcatcagccagagagattgaaaatttacecctacgactcttta 1021 V.1: 983 ctctctggagagggccagtggtggtagctataagcttggccacattttttttcctttatt 1042 V.8: 1022 ctctctggagagggccagtggtggtagctataagcttggccacattttttttactttatt 1081 V.1: 1043 cctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttacaaaa 1102 V.8: 1082 cctttgtcagagatgtgattcatccatatgctagaaaccaacagagtgacttttacaaaa 1141 V.1: 1103 ttactatagagattgtgaataaaaccttacctatagttgccattactttgctctccctag 1162 V.8: 1142 ttcctatagagattgtgaataaaaccttacctatagttgccattactttgctctccctag 1201 273 WO 03/087306 PCT/USO3/10462 V.1: 1163 tataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtatagga 1222 11 f1 11 l11 11 ill f1 1111111111 11 11 Ill fil(I l ill I I I V.8: 1202 tataccttgcaggtcttctggcagctgcttatcaactttattacggcaccaagtatagga 1261 V.1: 1223 gatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaagtt 1282 ff11 11111f II f I[ I I I11111 I I liffIf fil V.8: 1262 gatttccaccttggttggaaacctggttacagtgtagaaaacagcttggattactaagtt 1321 V.1: 1283 ttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcagaga 1342 LIIff11 1111f 1111f f ff111 Il 1111f 11 I l Ill V.8: 1322 ttttcttcgctatggtccatgttgcctacagcctctgcttaccgatgagaaggtcagaga 1381 V.1: 1343 gatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactcttgga 1402 ff11111il 11 II I ff1t 1111f 1f ff1 f il il l V.8: 1382 gatatttgtttctcaacatggcttatcagcaggttcatgcaaatattgaaaactcttgga 1441 V.1: 1403 atgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttggct 1462 fi l l ~ ~ l i i i i I I l f ff f I i i I i i i f i l f i I I I I I V.8: 1442 atgaggaagaagtttggagaattgaaatgtatatctcctttggcataatgagccttggct 1501 V.1: 1463 tactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactggagag 1522 1111111111111111 f1111111 1111ff 1 I 1111111 l I ill I II Ill V.8: 1502 tactttccctcctggcagtcacttctatcccttcagtgagcaatgctttaaactggagag 1561 V.1: 1523 aattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttccatg 1582 l i l l lf I i il li l l i l l f Il il lill l i f I l l l l l l l l I I V.8: 1562 aattcagttttattcagtctacacttggatatgtcgctctgctcataagtactttccatg 1621 V.1: 1583 ttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacaccac 1642 l1 l l l lI i f il ii l l ll i f 1 f i l l l i l l l l l I l l l l l l Il i V.8: 1622 ttttaatttatggatggaaacgagcttttgaggaagagtactacagattttatacaccac 1681 V.1: 1643 caaactttgttcttgctcttgttttgccctcaattgtaattctgg 1687 l i l l if l l i i f i ll l i l l i l lll ill I l l l l l l l l V.8: 1682 caaactttgttcttgctcttgttttgccctcaattgtaattctgg 1726 Score = 1381 bits (718), Expect = 0.01dentities = 725/726 (99%), Gaps = 1/726 (0%) Strand = Plus / Plus V.1: 1687 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 1746 l i l l l l l ll l l l l l l l l l l l l l l l l 1 1 1 1 il l l li l l l l l lI l lf ll ll l l l li l lI V.8: 6132 gatcttttgcagctttgcagatacccagactgagctggaactggaatttgtcttcctatt 6191 V.1: 1747 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 1806 l l l l l l l ll l l l l l ll l f l l|l l l l l l l l l l l l l l I l l l l l l i l1 1 1 1 1 1 1 1l V.8: 6192 gactctacttctttaaaagcggctgcccattacattcctcagctgtccttgcagttaggt 6251 V.1: 1807 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 1866 Illlllll1 flllllllll ll1 i111l i i lli111 1111 f lllll l11111 V.8: 6252 gtacatgtgactgagtgttggccagtgagatgaagtctcctcaaaggaaggcagcatgtg 6311 V.1: 1867 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 1926 Ill l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l l1 ll l il l l li l l l If lll l l il 274 WO 03/087306 PCT/USO3/10462 V.8: 6312 tcctttttcatcccttcatcttgctgctgggattgtggatataacaggagccctggcagc 6371 V.1: 1927 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 1986 I l1l l l i l i I I l ll l l l l l iI l l l ll l i l l l il l l l l l l l l l l l l l i V.8: 6372 tgtctccagaggatcaaagccacacccaaagagtaaggcagattagagaccagaaagacc 6431 V.1: 1987 ttgactacttccctacttccactgctttt-cctgcatttaagccattgtaaatctgggtg 2045 i i l l l l l l l l ll l l i l l l i [ II I l l l l l l il l l l l Il l I l l V.8: 6432 ttgactacttccctacttccactgctttttcctgcatttaagccattgtaaatctgggtg 6491 V.1: 2046 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 2105 l l1 l1 l l11 i lilllI l I iill ll1 llIII1ll1 l l! l lI ll ll lI l l V.8: 6492 tgttacatgaagtgaaaattaattctttctgcccttcagttctttatcctgataccattt 6551 V.1: 2106 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 2165 i l lI l l i i l l l l l l l l l I l i l I I I I l l l ll l l l l i l l l l l l l l l I V.8: 6552 aacactgtctgaattaactagactgcaataattctttcttttgaaagcttttaaaggata 6611 V.1: 2166 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 2225 il l l l l l l il l l l l l i l l l ll1 l l l l lll ll l i l l l l l lI l l l l l l l l l l l l l V.8: 6612 atgtgcaattcacattaaaattgattttccattgtcaattagttatactcattttcctgc 6671 V.1: 2226 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 2285 I 1 l l i l l l l l l lI i l l l l l l l l l l l l l l l l l l l l l l l l l l l ll1l l l l l l l l l l i V.8: 6672 cttgatctttcattagatattttgtatctgcttggaatatattatcttctttttaactgt 6731 V.1: 2286 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 2345 I I l l l i l I i l l l i l l l l l l i l l lllI l l l I I l I V.8: 6732 gtaattggtaattactaaaactctgtaatctccaaaatattgctatcaaattacacacca 6791 V.1: 2346 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 2405 Il l I l l I l I l l l l l l l l l i l l l il I l l l l i l I l l l l l l l l l l l l l l l I V.8: 6792 tgttttctatcattctcatagatctgccttataaacatttaaataaaaagtactatttaa 6851, V.1: 2406 tgattt 2411 IilMI V.8: 6852 tgattt 6857 Table LIV(g). Peptide sequences of protein coded by 98P4B6 v.8 (SEQ ID NO: 190) MESISMMGSP KSLSETCLPN GINGIKDARK VTVGVIGSGD FAKSLTIRLI RCGYHVVIGS 60 RNPKFASEFF PHVVDVTHHE DALTKTNIIF VAIHREHYTS LWDLRHLLVG KILIDVSNNM 120 RINQYPESNA EYLASLFPDS LIVKGFNVVS AWALQLGPKD ASRQVYICSN NIQARQQVIE 180 LARQLNFIPI DLGSLSSARE IENLPLRLFT LWRGPVVVAI SLATFFFLYS FVRDVIHPYA 240 RNQQSDFYKI PIEIVNKTLP IVAITLLSLV YLAGLLAAAY QLYYGTKYRR FPPWLETWLQ 300 CRKQLGLLSF FFAMVHVAYS LCLPMRRSER YLFLNMAYQQ VHANIENSWN EEEVWRIEMY 360 ISFGIMSLGL LSLLAVTSIP SVSNALNWRE FSFIQSTLGY VALLISTFHV LIYGWKRAFE 420 EEYYRFYTPP NFVLALVLPS IVILGKIILF LPCISRKLKR IKKGWEKSQF LEEGMGGTIP 480 HVSPERVTVM 490 275 WO 03/087306 PCT/USO3/10462 Table LV(g). Amino acid sequence alignment of 98P4B6 v.1 (SEQ ID NO: 191) and 98P4B6 v.8 (SEQ ID NO: 192) Score = 888 bits (2294), Expect = 0.1Odentities = 444/444 (100%), Positives = 444/444 (100%) V.1: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS V.8: 1 MESISMMGSPKSLSETCLPNGINGIKDARKVTVGVIGSGDFAKSLTIRLIRCGYHVVIGS 60 V.1: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM V.8: 61 RNPKFASEFFPHVVDVTHHEDALTKTNIIFVAIHREHYTSLWDLRHLLVGKILIDVSNNM 120 V.1: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE V.8: 121 RINQYPESNAEYLASLFPDSLIVKGFNVVSAWALQLGPKDASRQVYICSNNIQARQQVIE 180 V.1: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA V.8: 181 LARQLNFIPIDLGSLSSAREIENLPLRLFTLWRGPVVVAISLATFFFLYSFVRDVIHPYA 240 V.1: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ V.8: 241 RNQQSDFYKIPIEIVNKTLPIVAITLLSLVYLAGLLAAAYQLYYGTKYRRFPPWLETWLQ 300 V.1: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY V.8: 301 CRKQLGLLSFFFAMVHVAYSLCLPMRRSERYLFLNMAYQQVHANIENSWNEEEVWRIEMY 360 V.1: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE V.8: 361 ISFGIMSLGLLSLLAVTSIPSVSNALNWREFSFIQSTLGYVALLISTFHVLIYGWKRAFE 420 V.1: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 EEYYRFYTPPNFVLALVLPSIVIL V.8: 421 EEYYRFYTPPNFVLALVLPSIVIL 444 276

Claims (46)

1. A composition that comprises, consists essentially of, or consists of: a) a peptide of eight, nine, ten, or eleven contiguous amino acids of a protein of Figure 2; b) a peptide of Tables VIII-XXI; c) a peptide of Tables XXII to XLV; or, d) a peptide of Tables XLVI to XLIX.

2. A composition of claim 1 that comprises a protein related to a protein of Figure 2.

3. A protein of claim 2 that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, or 99% homologous to an entire amino acid sequence shown in Figure 2.

4. A composition of claim 1 wherein the substance comprises a CTL polypeptide or an analog thereof, from the amino acid sequence of a protein of Figure 2.

5. A composition of claim 4 further limited by a proviso that the epitope is not an entire amino acid sequence of Figure 2.

6. A composition of claim 1 further limited by a proviso that the polypeptide is not an entire amino acid sequence of a protein of Figure 2.

7. A composition of claim 1 that comprises an antibody polypeptide epitope from an amino acid sequence of Figure 2.

8. A composition of claim 7 further limited by a proviso that the epitope is not an entire amino acid sequence of Figure 2.

9. A composition of claim 7 wherein the antibody epitope comprises a peptide region of at least 5 amino acids of Figure 2 in any whole number increment up to the end of said peptide, wherein the epitope comprises an amino acid position selected from: a) an amino acid position having a value greater than 0.5 in the Hydrophilicity profile of Figure 5, b) . an amino acid position having a value less than 0.5 in the Hydropathicity profile of Figure 6; c) an amino acid position having a value greater than 0.5 in the Percent Accessible Residues profile of Figure 7; d) an amino acid position having a value greater than 0.5 in the Average Flexibility profile of Figure 8; e) an amino acid position having a value greater than 0.5 in the Beta-turn profile of Figure 9; f) a combination of at least two of a) through e); g) a combination of at least three of a) through e); h) a combination of at least four of a) through e); or i) a combination of five of a) through e).

10. A polynucleotide that encodes a protein of claim 1. 277 WO 03/087306 PCT/US03/10462

11. A polynucleotide of claim 10 that comprises a nucleic acid molecule set forth in Figure 2.

12. A polynucleotide of claim 10 further limited by a proviso that the encoded protein is not an entire amino acid sequence of Figure 2.

13. A composition of claim 11 wherein the substance comprises a polynucleotide that comprises a coding sequence of a nucleic acid sequence of Figure 2.

14. A polynucleotide of claim 22 that further comprises an additional nucleotide sequence that encodes an additional peptide of claim 1.

15. A composition comprising a polynucleotide that is fully complementary to a polynucleotide of claim 10.

16. A method of generating a mammalian immune response directed to a protein of Figure 2, the method comprising: exposing cells of the mammal's immune system to a portion of a) a 98B4B6-related protein and/or b) a nucleotide sequence that encodes said protein, whereby an immune response is generated to said protein.

17. A method of generating an immune response of claim 16, said method comprising: providing a 98B4B6-related protein that comprises at least one T cell or at least one B cell epitope; and, contacting the epitope with a mammalian immune system T cell or B cell respectively, whereby the T cell or B cell is activated.

18. A method of claim 17 wherein the immune system cell is a B cell, whereby the induced B cell generates antibodies that specifically bind to the 98B4B6-related protein.

19. A method of claim 17 wherein the immune system cell is a T cell that is a cytotoxic T cell (CTL), whereby the activated CTL kills an autologous cell that expresses the 98B4B6-related protein.

20. A method of claim 17 wherein the immune system cell is a T cell that is a helper T cell (HTL), whereby the activated HTL secretes cytokines that facilitate the cytotoxic activity of a cytotoxic T cell (CTL) or the antibody-producing activity of a B cell.

21. A method for detecting, in a sample, the presence of a 98B4B6-related protein or a 98B4B6-related polynucleotide, comprising steps of: contacting the sample with a substance that specifically binds to the 98B4B6-related protein or to the 98B4B6 related polynucleotide, respectively; and, determining that there is a complex of the substance with the 98B4B6-related protein or the substance with the 98B486-related polynucleotide, respectively. 278 WO 03/087306 PCT/USO3/10462

22. A method of claim 21 for detecting the presence of a 98B4B6-related protein in a sample comprising steps of: contacting the sample with an antibody or fragment thereof either of which specifically bind to the 98B4B6-related protein; and, determining that there is a complex of the antibody or fragment thereof and the 98B4B6-related protein.

23. A method of claim 21 further comprising a step of: taking the sample from a patient who has or who is suspected of having cancer.

24. A method of claim 21 for detecting the presence of a protein of Figure 2 mRNA in a sample comprising: producing cDNA from the sample by reverse transcription using at least one primer; amplifying the cDNA so produced using 98B4B6 polynucleotides as sense and antisense primers, wherein the 9814B6 polynucleotides used as the sense and antisense primers serve to amplify a 98B4B6 cDNA; and, detecting the presence of the amplified 98B4B6 cDNA.

25. A method of claim 21 for monitoring one or more 98B4B6 gene products in a biological sample from a patient who has or who is suspected of having cancer, the method comprising: determining the status of one or more 98B4B6 gene products expressed by cells in a tissue sample from an individual; comparing the status so determined to the status of one or more 98B4B6 gene products in a corresponding normal sample; and, identifying the presence of one or more aberrant gene products of 988486 in the sample relative to the normal sample.

26. The method of claim 25 further comprising a step of determining if there are one or more elevated gene products of a 98B4B6 mRNA or a 98B4B6 protein, whereby the presence of one or more elevated gene products in the test sample relative to the normal tissue sample indicates the presence or status of a cancer.

27. A method of claim 26 wherein the cancer occurs in a tissue set forth in Table I.

28. A composition comprising: a substance that a) modulates the status of a protein of Figure 2, or b) a molecule that is modulated by a protein of Figure 2, whereby the status of a cell that expresses a protein of Figure 2 is modulated.

29. A composition of claim 28, further comprising a physiologically acceptable carrier.

30. A pharmaceutical composition that comprises the composition of claim 28 in a human unit dose form.

31. A composition of claim 28 wherein the substance comprises an antibody or fragment thereof that specifically binds to a protein of Figure 2. 279 WO 03/087306 PCT/US03/10462

32. An antibody or fragment thereof of claim 31, which is monoclonal.

33. An antibody of claim 31, which is a human antibody, a humanized antibody or a chimeric antibody.

34. A non-human transgenic animal that produces an antibody of claim 31.

35. A hybridoma that produces an antibody of claim 32.

36. A method of delivering a cytotoxic agent or a diagnostic agent to a cell that expresses a protein of Figure 2, said method comprising: providing the cytotoxic agent or the diagnostic agent conjugated to an antibody or fragment thereof of claim 4; and, exposing the cell to the antibody-agent or fragment-agent conjugate.

37. A composition of claim 28 wherein the substance comprises a polynucleotide that encodes an antibody or fragment thereof, either of which immunospecifically bind to a protein of Figure 2.

38. A composition of claim 28 wherein the substance comprises a) a ribozyme that cleaves a polynucleotide having a 98B4B6 coding sequence, or b) a nucleic acid molecule that encodes the ribozyme; and, a physiologically acceptable carrier.

39. A composition of claim 28 wherein the substance comprises human T cells, wherein said T cells specifically recognize a 98B4B6 peptide subsequence in the context of a particular HLA molecule.

40. A method of inhibiting growth of cancer cells that express a protein of Figure 2, the method comprising: administering to the cells the composition of claim 28.

41. A method of claim 40 of inhibiting growth of cancer cells that express a protein of Figure 2, the method comprising steps of: administering to said cells an antibody or fragment thereof, either of which specifically bind to a 98B4B6-related protein.

42. A method of claim 40 of inhibiting growth of cancer cells that express a protein of Figure 2, the method comprising steps of: administering to said cells a 98B4B6-related protein.

43. A method of claim 40 of inhibiting growth of cancer cells that express a protein of Figure 2, the method comprising steps of: administering to said cells a polynucleotide comprising a coding sequence for a 98B486-related protein or comprising a polynucleotide complementary to a coding sequence for a 98B4B6-related protein.

44. A method of claim 40 of inhibiting growth of cancer cells that express a protein of Figure 2, the method comprising steps of: 280 WO 03/087306 PCT/USO3/10462 administering to said cells a ribozyme that cleaves a polynucleotide that encodes a protein of Figure 2.

45. A method of claim 40 of inhibiting growth of cancer cells that express a protein of Figure 2 and a particular HLA molecule, the method comprising steps of: administering human T cells to said cancer cells, wherein said T cells specifically recognize a peptide subsequence of a protein of Figure 2 while the subsequence is in the context of the particular HLA molecule.

46. A method of claim 40, the method comprising steps of: administering a vector that delivers a nucleotide that encodes a single chain monoclonal antibody, whereby the encoded single chain antibody is expressed intracellularly within cancer cells that express a protein of Figure 2. 281