AU2008200628B2 - Nucleic acid and corresponding protein entitled 24P4C12 useful in treatment and detection of cancer - Google Patents

Description

I AUSTRALIA Patents Act 1990 FB RICE & CO Patent and Tradc Mark Attorneys AGENSYS, INC. COMPLETE SPECIFICATION STANDARD PATENT Invention Title: Nucleic acid and corresponding protein entitled 24P4C12 useful in treatment and detection of cancer The following statement is a full description of this invention including the best method of performing it known to us:- NUCLEIC ACID AND CORRESPONDING PROTEIN ENTITLED 24P4C12 USEFUL IN TREATMENT AND DETECTION OF CANCER CROSS-REFERENCE TO RELATED APPLICATIONS This application is a divisional application of Australian Patent Application No. 2002352976 filed on November 27, 2002, the contents of which are incorporated herein in their entirety by reference. FIELD OF THE INVENTION The Invention described herein relates to a gene and its encoded protein. tended 24P4C12, expressed in certain cancers, and to diagnostic and therapeutic methods and compositions useful in the management of cancers that express 24P4C12. BACKGROUND OF THE INVENTION Cancer is the second leading cause of human death next to coronary disease. Woddwide, miions 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 mllon new cases diagnosed per year. While deaths from heart disease have been decining 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 Iung prostate, breast colon, pancreas, and ovary represent the pdmary causes-of cancer death. These and virtually all other carinomas 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 expedence has shown that their fives 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 debitations 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 thepy, 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 mader that can accurately detect earty-stage, localized tumors remains a significant Imitation in the diagnosis and management of this disease. Although the serum prostate specific anfigen (PSA) assay has been a very useful lool, however its specificity and general utility Is widely regarded as lacidng In several important respects. Progress in identifying additional specific markers for prostate cancer has been improved by the generation of prostate canor xenografts that can recapitulate different stages of the disease In mice. The LAPC (Ls pgeles Bostate Cancer) xenografts are prostate cancer xenografts that have survived passage In severe combined immune deficient (SCID) mice and have exhibited the capacity to mlnic the transition from androgen dependence to androgen Independence (Klein of at., 1997, Nat. Med. 3:402). More recently Identfied prostate cancer markers Include PCTA-1 (Suet a., 1996, Proc. Nat. Acad. Sci. USA 93:7252), prostate-specific membrane (PSM) antigen (Pinto ot al. Clin Cancer Res 1996 Sep 2 (9): 1445 51), STEAP (Hubert of at, Proc Na Acad Sci U S A 1999 Dec 7;96(25): 14523-8) and prostate atem cel antigen (PSCA) (Reitereta., 1998, Proc Nat. Acad. Sci USA 95: 1735).

IA

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 irnnunotherapies, 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 malellemale ratio of 3:1 may be decreasing related to smoking pattems 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 canor 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 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. 2 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 canor 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. Local excision of ductal carcinoma in su (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 ol 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-oophorecdomy), and the uterus (hysterectomy). In some very early tumors, only the involved ovary wiR be removed, especialy 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. 3 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 defined 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 24P4C1 2, that has now been found to be over-expressed in the cancer(s) listed in Table 1. Northern blot expression analysis of 24P4C12 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 24P4C12 are provided. The tissue-related profile of 24P4C12 In normal adult tissues, combined with the over-expression observed in the tissues listed in Table I, shows that 24P4C1 2 is aberrantly over-expressed in at least some cancers, and thus serves as useful diagnostic, prophylactic, prognostic, and/or therapeutic target for cancers of the tissue(s) such as those listed in Table 1. The invention provides polynudeotides corresponding or complementary to aD or part of the 24P4C1 2 genes, mRNAs, and/or coding sequences, preferably in isolated form, including polynudeotides encoding 24P4C12-related proteins and fragments 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 contiguous amino adds: 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 24P4C12-related protein, as well as the peptides/proteins themselves; DNA, RNA, DNARNA hybrids, and related molecules, polynudeotides or oligonucleotides complementary or having at least a 90% homology to the 24P4C12 genes or mRNA sequences or parts thereof, and polynudeotdes or otigonudeotides that hybridize to the 24P4C1 2 genes, mRNAs, or to 24P4C12-encoding polynuclecddes. Also provided are means for Islating cDNAs and the genes encoding 24P4C12. Recombinant DNA molecules containing 24P4C12 polynucleotides, cells transfonneri or transduced with such molecules, and host-vector systems for the expression of 24P4C12 gene products are also provided. The invention further provides antibodies that bind to 24P4C1 2 proteins and polypeptide fragments thereof, including polydonal and monoclonal antibodies, murine and 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 nuclelc 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 nudelc 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 24P4C12 polynucleotides and proteins in various biological samples, as wel as methods for identifying cels that express 24P4C12. A typical embodiment of this invention provides methods for monitoring 24P4C12 gene products in issue 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 24P4C12 such as cancers of tissues listed in Table t, including therapies aimed at inhibiting the transcription, translation, processing or function of 24P4C12 as well as cancer vaccines. In one aspect, the invention provides compositions, and methods comprising them, for beating a cancer that expresses 24P4C12 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 4 the production or function of 24P4C12. Preferably, the carrier is a uniquely human carrier. In another aspect of the invention, the agent is a moiety that is immunoreactive with 24P4C12 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 occuning 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 24P4C12 and/or one or more than one peptide which comprises a helper T lymphocyte (HTL) epitope which binds an HLA dass I 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 stimulaling peptides as described above. In yet another aspect of the Invention, the one or more than one nudeic acid molecule may express a moiety that is immunologically reactive with 24P4C1 2 as described above. The one or more than one nuclel acid molecule may also be, or encodes, a molecule that inhibits production of 24P4C12. Non-limiting examples of such molecules Indude, but are not limited to, those complementary to a nudeotide sequence essential for production of 24P4C12 (e.g. antisense sequences or molecules that form a triple helx with a nucleotide double helix essential for 24P4C12 production) or a ribozyme effective to lyse 24P4C12 mRNA. Note that to determine the starting position of any peptide set forth in Tables VIll-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 Pepdde is used to obtain HLA peptides oi a particular for a particular variant. The position of each Search Peptide relative to its respective parent molecule is listed in Table VIl. Accordingly, if a Search Peptide begins at position W, one must add the value "X -1" to each position In Tables Vill-XXI and XXII to XUX 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 HLA peptide that occurs at least once In Tables Vill-XXI and at least once in tables XXII to XLIX, or an oligonudeotide that encodes the HILA peptide. Another embodiment of the invention is antibody epitopes, which comprise a peptide regions, or an oligonudeotide 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 Indudes 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 Hydrophilldty profile of Figure 5; 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 fulllength of that protein in Figure 3, that indudes 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; ill) 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 indudes an amino add 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; 5 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 indudes 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 ull 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-tum profile of Figure 9. BRIEF DESCRIPTION OF THE FIGURES Figure 1. The 24P4C12 SSH sequence of 160 nucleolides. Figure 2. A) The cDNA and amino acid sequence of 24P4C12 variant I (also called 24P4C12 v.Vor24P4C12 variant 1 ) Is shown in Figure 2A. The start methionine is underlined. The open reading frame extends from nucleic acid 6 2138 induding the stop codon. B) The cDNA and amino acid sequence of 24P4C12 variant 2 (also called 24P4C12 v.2') Is shown In Figure 2B. The codon for the start methlonine is underlined. The open reading frame extends from nucleic acid 6-2138 including the stop codon. C) The cDNA and amino acid sequence of 24P4C12 variant 3 (also called "24P4C12 v.3) is shown in Figure 2C. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 6-2138 Including the stop codon. D) The cDN4A and amino acid sequence of 24P4C12 variant 4 (also called 24P4C12 v.4") is shown in Figure 2D. The codon for the start methionine Is underlined. The open reading frame extends from nudeic acid 6-2138 including the stop codon. E) The cDNA and amino acid sequence of 24P4C12 variant 5 (also called "24P4C1 2 v.5') is shown in Figure 2E. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 6-2138 including the stop codon. F) The cDNA and amino acid sequence of 24P4C12 variant 6 (also called "24P4C12 v.6) Is shown in Figure 2F. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 6-2138 Including the stop codon. G) The cDNA and amino acid sequence of 24P4C12 variant 7 (also called "24P4C1 2 v.7") is shown in Figure 2G. The codon for the start methionine is underlined. The open reading frame extends from nudeic acid 6-1802 including the stop codon. H) The cDNA and amino add sequence of 24P4C12 variant 8 (also called 24P4C12 v.8") is shown in Figure 2H. The codon for the start methionine is underlined. The open reading frame extends from nuclelc add 6-2174 including the stop codon. I) The cDNA and amino acid sequence of 24P4C12 variant 9 (also called '24P4C12 v.9") is shown in Figure 21. The codon for the start methionine is underlined. The open reading frame extends from nucleic acid 6-2144 including the stop codon. Figure 3. A) Amino acid sequence of 24P4C12 v.I is shown in Figure 3A; it has 710 amino adds. B) The amino acid sequence of 24P4C12 v.3 is shown in Figure 38; it has 710 amino acids. C) The amino acid sequence of 24P4C12 v.5 is shown in Figure 3C; It has 710 amino acids. D) The amino acid sequence of 24P4C12 v.61s shown in Figure 30; it has 710 amino adds. 6 E) The amino acid sequence of 24P4C12 v.7 is shown in Figure 3E; it has 598 amino acids. F) The amino acid sequence of 24P4C12 v.8 is shown in Figure 3F; it has 722 amino acids. G) The amino add sequence of 24P4C12 v.9 is shown in Figure 3G; it has 712 amino adds. As used herein, a reference to 24P4C12 includes all variants thereof, including those shown in Figures 2, 3, 10, and 11, unless the context deadly Indicates otherwise. Figure 4. Alignment or 24P4C12 with human cholne transporter-like protein 4 (CTL4) (g114249468). Figure 5. Hydrophilicity amino acid profile of 24P4C1 2 determined by computer algorithm sequence analysis using the method of Hopp and Woods (Hopp T.P., Woods KR., 1981. Proc. NatI. Acad. Sci. U.S.A. 78:3824-3828) accessed on the Protscale website located on the World Wide Web at (.expasy.chlcgi-binlprotscale.pl) through the ExPasy molecular biology server. Figure B. Hydropathicity amino acid profile of 24P4C12 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-binlprotscale.pl) through the ExPasy molecular biology server. Figure 7. Percent accessible residues amino acid profile of 24P4C12 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.chicgi-bin/protscale.pl) through the ExPasy molecular biology server. Figure 8.. Average flexibility amino add profile of 24P4C12 determined by computer algorithm sequence analysis using the method of Bhaskaran and Ponnuswamy (Bhaskaran R., and Ponnuswamy P.K., 1988. Int. J. Pept. Protein Res. 32:242-255) 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. Beta-turn amino acid profile of 24P4C12 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 Word Wide Web at (.expasy.ch/cgi-bin/protscale.p) through the ExPasy molecular biology server. Figure 10. Schematic alignment of SNP variants of 24P4C12. Variants 24P4C12 v.2 through v.6 are variants with single nudeotide differences. Though these SNP variants are shown separately, they could also occur in any combinations and in any transcript variants that contains the base pairs. Numbers correspond to those of 24P4C1 2 v.1. Black box shows the same sequence as 24P4C12 v.1. SNPs are indicated above the box. Figure 11. Schematic alignment of protein variants of 24P4C12. Protein variants correspond to nucleotide variants. Nucleotide variants 24P4C12 v.2, v.4 In Figure 10 code for the same protein as 24P4C12 v.1. Nudeotide variants 24P4C1 2 v.7, v.8 and v.9 are spice variants of v.1, as shown in Figure 12. Single amino acid differences were Indicated above the boxes. Black boxes represent the same sequence as 24P4C12 v.1. Numbers underneath the box correspond to 24P4C12 v.1. FIgure 12. Exon compositions of transcript variants of 24P4C12. Variant 24P4C12 v.7, v.8 and v.9 are transcript variants of 24P4C12 v.1. Variant 24P4C12 v.7 does not have exons 10 and 11 of variant 24P4C12 v.1. Variant 24P4C12 v.8 extended 36 bp at the 3' end of exon 20 of variant 24P4C12 v.1. Variant 24P4C12 v.9 had a longer exon 12 and shorter exon 13 as compared to vacant 24P4C12 v.1. Numbers in "( ) underneath the boxes correspond to those of 24P4C12 v.1. Lengths of Introns and exons are not proportional. Figure 13. Secondary structure and transmembrane domains prediction for 24P4C12 protein variant I (SEQ ID NO: 112). k The secondary structure of 24P4C12 protein variant 1 was predicted using the HNN -Hierarchical Neural Network method (Guermeur, 1997, htplJpbilJbcp.frJogi-binJnpsa...automat.plpage=nps.inn.htl), accessed from the ExPasy molecular biology server (httpJhww.expasy.chltools). 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 7 secondary structure is also listed. B: Schematic representation of the probability of existence of transmembrane regions and orientation of 24P4C12 variant 1 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). C: Schematic representation of the probability of the existence of transmembrane regions and the extracelular and Intracellular orientation of 24P4C12 variant 1 based on the TMHMM algorithm of Sonnhammer, von Heine, and Krogh (Erik LL. 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 (httpJ/ww.expasy.chftools). Figure 14. 24P4C12 Expression by RT-PCR. First strand cDNA was generated from vital pool 1 (kidney, liver and lung), vital pool 2 (colon, pancreas and stomach), a pool of prostate cancer xenografts (LAPC-4AD, LAPC-4Al, LAPC-9AD and LAPC-9A), prostate cancer pool, bladder cancer pool, kidney cancer pool, colon cancer pool, ovary cancer pool, breast cancer pool, and cancer metastasis pool. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers to 24P4C12, was performed at26 and 30 cycles of amplification. Results show strong expression of 24P4C12 in prostate cancer pool and ovary cancer pool. Expression was also detected in prostate cancer xenografts, bladder cancer poo, kidney cancer pool, colon cancer pool, breast cancer pool, cancer metastasis pool, vital pool 1, and vital pool 2. Figure 15. Expression of 24P4C12 in normal tissues. Two multiple tissue northern blots (Clontech) both with 2 ug of mRNAlane were probed with the 24P4C1 2 sequence. Size standards in kilobases (kb) are Indicated on the side. Results show expression of 24P4C12 in prostate, kidney and colon. Lower expression is detected in pancreas, lung and placenta amongst all 16 normal tissues tested. Figure 16. Expression of 24P4C12 in Prostate Cancer Xenografts and Cell Unes. RNA was extracted from a panel of cell fines and prostate cancer xenografts (PrEC, LAPC-4AD, LAPC-4A, LAPC-9AD, LAPC-9AI, LNCaP, PC-3, DU145, TsuPr, and LAPC-4CL). Northern blot with 10 ug of total RNAnane was probed with 24P4C1 2 SSH sequence. Size standards In kilobases (kb) are indicated on the side. The 24P4C12 transcript was detected in LAPC-4AD, LAPC-4AI, LAPC 9AD, LAPC-9A, LNCaP, and LAPC-4 CL Figure 17. Expression of 24P4C12 In Patient Cancer Specimens and Normal Tissues. RNA was extracted from a pool of prostate cancer specimens, bladder cancer specimens, colon cancer specimens, ovary cancer specimens, breast cancer specimens and cancer metastasis specimens, as well as from normal prostate (NP), normal bladder (NB), normal kidney (NK), and normal colon (NC). Northern blot with 10 pg of total RNAJlane was probed with 24P4C12 SSH sequence. Size standards in kilobases (kb) are indicated on the side. Strong expression of 24P4C12 transcript was detected In the patient cancer pool specimens, and in normal prostate but not in the other normal tissues tested. Figure 18. Expression of 24P4C12 in Prostate Cancer Patient Specimens. RNA was extracted from normal prostate (N), prostate cancer patient tumors (T) and their matched normal adjacent tissues (Nat). Northern blots with 10 ug of total RNA were probed with the 24P4C12 SSH fragment Size standards in kilobases are on the side. Results show expression of 24P4C12 In normal prostate and all prostate patient tumors tested. Figure 19. Expression of 24P4C1 2 In Colon Cancer Patient Specimens. RNA was extracted from colon cancer cell lines (CL: Colo 205, LoVo, and SK-CO-), normal colon (N), colon'cancer patient tumors (T) and their matched normal adjacent tissues (Nat). Northern blots with 10 ug of total RNA were probed with the 24P4C12 SSH fragment Size standards In Idlobases are on the side. Results show expression of 24P4C1 2 In normal colon and all colon patient tumors tested. Expression was detected In the cell lines Colo 205 and SK-CO., but not In LoVo. 8 Figure 20. Expression of 24P4C12 in Lung Cancer Patient Specimens. RNA was extracted from lung cancer cell lines (CL' CALU-1, A427, NCI-H82, NCI-H146), normal lung (N), lung cancer patient tumors (T) and their matched normal adjacent tissues (Nat). Northern blots with 10 ug of total RNA were probed with the 24P4C12 SSH fragment Size standards in kilobases are on the side. Results show expression of 24P4C1 2 in lung patient tumors tested, but not in normal lung. Expression was also detected in CALU-1, but not in the other cell lines A427, NCI-H82, and NCI-H146. Figure 21. Expression of 24P4C12 in breast and stomach human cancer specimens. Expression of 24P4C12 was assayed in a panel of human stomach and breast cancers (T) and their respective matched normal tissues (N) on RNA dot blots. 24P4C12 expression was seen in both stomach and breast cancers. The expression detected in normal adjacent tissues (isolated from diseased tissues) but not in normal tissues (isolated from healthy donors) may indicate that these tissues are not fully normal and that 24P4C1 2 may be expressed in early stage tumors. Figure 22. 24P4C12 Expression in a large panel of Patient Cancer Specimens. First strand cDNA was prepared from a panel of ovary patient cancer specimens (A), uterus patient cancer specimens (B), prostate cancer specimens (C), bladder cancer patient specimens (D), lung cancer patient specimens (E), pancreas cancer patient specimens (F), colon cancer specimens (G), and kidney cancer specimens (H). Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers to 24P4C12, was performed at 26 and 30 cydes 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 24P4C12 in the majority of patient cancer specimens tested, 73.3% of ovary patient cancer specimens, 83.3% of uterus patient cancer specimens, 95.0% of prostate cancer specimens, 61.1% of bladder cancer patient specimens, 80.6% of lung cancer patient specimens, 87.5% of pancreas cancer patient specimens, 87.5% of colon cancer specimens, 68.4% of of dear cell renal carcinoma, 100% of papillary renal cell carcinoma. Figure 23. 24P4C12 expression in transduced cells. PC3 prostate cancer cells, NIH-3T3 mouse cells and 300.19 mouse cells were transduced with 24P4C12.pSRa retroviral vector. Cells were selected in neomycin for the generation of stable cell lines. RNA was extracted following selection in neomycin. Northern blots with 10 ug of total RNA were probed with the 24P4C12 SSH fragment. Results show strong expression of 24P4C12 in 24P4C12.pSRa transduced PC3, 3T3 and 300.19 cells, but not in the control cells transduced with the parental pSRa construct Figure 24. Expression of 24P4C12 in 293T cells. 293T cell were transiently transfacted with either pCDNA3.1 Myc-His tagged expression vector, the pSRO expression vector each encoding the 24P4C12 variant I cONA or a control neo vector. Cells were harvested 2 days later and analyzed by Western blot with antI-24P4C1 2 pAb (A) or by Flow cytometry (B) on fixed and permeabilized 293T cells with either the anti-24P4C1 2 pAb or anti-His pAb followed by a PE-conjugated anti rabbit IgG secondary Ab. Shown Is expression of the monomeric and aggregated forms of 24P4C12 by Western blot and a fluorescent shift of 24P4C12-293T cells compared to control neo ces when staIned with the anti-24P4C12 and anti-His pAbs which are directed to the intracellular NH3 and COOH termini, respectively. Figure 25. Expression and detection of 24P4C12 in stably transduoed PC3 cells. PC3 cells were Infected with retrovirus encoding the 24P4C12 variant I cDNA and stably transduced cells were derived by G418 selection. Cells were then analyzed by Western blot (A) or immunohistochemistry (B) with anti-24P4C12 pAb. Shown with an arrow on the Western blot is expression of a -94 kD band representing 24P4C12 expressed In PC3-24P4C12 cells but not in control neo cells. Immunohistochemical analysis shows specific staining of 24P4C1 2-PC3 cells and not PC3-neo cells which Is competed away competitor peptide to which the pAb was derived. Figure 26. Expression of recombinant 24P4C12 antigens in 293T cells. 293T cells were transiency transfected with Tag5 His-tagged expression vectors encoding either amino acids 59-227 or 319-453 of 24P4C12 variant I or a control vector. 2 days later supernatants were collected and cells harvested and lysed. Supematants and lysates were then subjected to Western blot analysis using an anti-His pAb. Shown is expression of the recombinant Tag5 59-227 protein In 9 both the supernatant and lysate. and the Tag5 319-453 protein in the cell lysate. These proteins are purified and used as antigens for generation of 24P4C12-specific antibodies. Figure 27. Monoclonal antibodies detect 24P4C12 protein expression in 293T cells by flow cytometry. 293T cells were transfected with either pCDNA 3.1 His-tagged expression vector for 24P4C1 2 or a control neo vector and harvested 2 days later. Cells were fixed, permeabilized, and stained with a 1:2 dilution of supernatants of the indicated hybildomas generated from mice immunized with 300.19-24P4C12 cells or with anti-His pAb. Cells were then stained with a PE conjugated secondary Ab and analyzed by flow cytometry. Shown is a fluorescent shift of 293T-24P4C12 cells but not control neo cells demonstrating specific recognition of 24P4C12 protein by the hybridoma supematants. Figure 28. Shows expression of 24P4C12 Enhances Proliferation. PC3 and 3T3 were grown overnight in low FBS. Cells were then incubated in low or 10% FBS as indicated. Proliferation was measured by Alamar Blue. Figure 29. Detection of 24P4C12 protein by immunohlstochemistry in prostate cancer patient specimens. Prostate adenocarcinoma tissue and Its matched normal adjacent tissue were obtained from prostate cancer patients. The results showed strong expression of 24P4C12 in tie tumor cells and normal epithelium of the prostate cancer patients' issue (panels (A) low grade prostate adenocarcinoma, (B) high grade prostate adenocarcinoma, (C) normal tissue adjacent to tumor). The expression was detected mostly around the cell membrane indicating that 24P4C1 2 is membrane associated In prostate tissues. Figure 30. Detection of 24P4C12 protein by immunohistochemistry in various cancer patient specimens. Tissue was obtained from patients with colon adenocarcnoma, breast ductal carcinoma, lung adenocarcinoma, bladder transitional cell carcinoma, renal clear cell carcinoma and pancreatic adenocarcnoma. The results showed expression of 24P4C12 in the tumor cells of the cancer patients' tissue (panel (A) colon adenocarcinoma, (B) lung adenocarcinoma, (C) breast ductal carcinoma, (D) bladder transitional carcinoma, (E) renal dear cell carcinoma, (F) pancreatic adenocarcinoma). Figure 31. Shows 24P4C12 Enhances Tumor Growth In SCID Mice. 1 x 106 PC3-24P4C1 2 cells were mixed with Matrigel and injected on the right and left subcutaneous flanks of 4 male SCID mice per group. Each data point represents mean tumor volume (n=8). Figure 32. Shows 24P4C12 Enhances Tumor Growth in SCID Mice. 1 x 106 3T3-24P4C12 cells were mixed with Matrigel and Injected on the right subcutaneous flanks of 7 male SCID mice per group. Each data point represents mean tumor volume (n=6). DETAILED DESCRIPTION OF THE INVENTION Outline of Sections I.) Definitions 11.) 24P4C12 Polynudleotides IlA) Uses of 24P4C12 Polynucleotides (IAI.) Monitoring of Genetic Abnormalities ILA2.) Antisense Embodiments IIA3.) Primers and Primer Pairs IlA4.) Isolation of 24P4C12-Encoding Nucele Acid Molecules I1A5.) Recombinant Nucleic Acid Molecules and Host-Vector Systems IlIl.) 24P4C2-related Proteins I.A.) Motif -bearing Protein Embodiments 1ll.B.) Expression of 24P4C12-related Proteins IlI.C.) Modifications of 24P4C12-related Proteins lll.D.) Uses of 24P4C12-related Proteins 10 IV.) 24P4C12 Antibodies V.) 24P4C12 Cellular Immune Responses VI.) 24P4C12 Transgenic Animals VII.) Methods for the Detection of 24P4C12 VIII.) Methods for Monitoring the Status of 24P4C12-related Genes and Their Products IX.) Identification of Molecules That interact With 24P4C12 X.) Therapeutic Methods and Compositions X.A.) Anti-Cancer Vaccines XB.) 24P4C12 as a Target for Antibody-Based Therapy XC.) 24P4C12 as a Target for Cellular Immune Responses X.C.1. Minigene Vaccines XC.. Combinations of CTL Peptides with Helper Peptides XC.3. Combinations of CTL Peptides with T Cell Priming Agents XC.4. Vaccine Compositions Comprising DC Pulsed with CTL andlor HTL Peptides XD.) Adoptive Immunotherapy X.E.) Administration of Vaccines for Therapeutic or Prophylactic Purposes Xl.) Diagnostic and Prognostic Embodiments of 24P4C12. Xfl.) Inhibition of 24P4C12 Protein Function XIlIA) inhibition of 24P4C1 2 With Intraceflular Antibodies XII.B.) Inhibition of 24P4C12 with Recombinant Proteins XiI.C.) Inhibition of 24P4C12 Transcription or Translation XII.D.) General Considerations for Therapeutic Strategies Xil.) identification, Characterization and Use of Modulators of 24P4C12 Xiv.) KITS/Articles of Manufacture I.) Definitions: Unless otherwise defined, an 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 darity 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 of a., Molecular Cloning: A Laboratory Manual 2nd. edition (1989) Cold. Spdng 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 Assodation (AUA) system, stage C1 - C2 disease under the WhitmoresJewett 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 compared to patients having clinically localized (organ-confined) prostate cancer. Locally advanced disease is clinically 11 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 patten" is intended for purposes herein to mean deleting one or more carbohydrate moietes found in native sequence 24P4C12 (either by removing the underlying glycosylation site or by deleting the glycosylation by chemical and/or enzymatic means), and/or adding one or more glycosylation sites that are not present in the native sequence 24P4C12. In addition, the phrase indudes qualitative changes in the glycosylation of the native proteins, involving a change in the nature and proportions of the various carbohydrate moleties present. The term "analog refers to a molecule which is structurally similar or shares similar or corresponding attributes with another molecule (e.g. a 24P4C1 2-related protein). For example, an analog of a 24P4C12 protein can be spedfically bound by an antibody or T cell that specifically bonds to 24P4C12. The term "antibody is usedln the broadest sense. 'Therefore, an"anbd can benaturally ocouningorman-made such as monoclonal antibodies produced by conventional hybidoma technology. Anti-24P4C12 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-24P4C12 antibodies and dones thereof (including agonist, antagonist and neutralizing antibodies) and and-24P4C12 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 coons having a usage frequency of less than about 20%. Nudeolde sequences that have been optimized for expression in a given host species by elimination of spurious polyadenylation sequences, elimination of exonfintron 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 'combinatodal 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 combinatodal 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 adds in a polypeptide compound). Numerous chemical compounds are synthesized through such combinatorial mixing of chemical building blocks (Gallop at 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 Indude, 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 blo- oligomers (PCT Publication WO 92/00091), benzodiazepines (U.S. Pat No. 5,288,514), dliversomers such as hydantoins, benzodiazepines and dipeptides (Hobbs et al.. Proc. Nat. Acad. Sd. -USA 90.6909-6913 (1993)), vinytogous polypeptides (Haghara et al., J. Amer. Chem. Soc. 114'568 (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 at al., J. Amer. Chem. Soc. 116:2661 (1994)), oligocarbamates (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), nudeic acid libraries (see, e.g., Stratagene, Corp.), peptide nucleic add libraries (see, e.g., U.S. Patent 5,539,083), antibody libraries (see, e.g., Vaughn et al., Nature Biotechnology 14(3): 309-314 (1996), and PCTUS96/1 0287), carbohydrate libraries (see, e.g., Liang et al., Science 12 274:1520-1522 (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; thlazolidinones 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, Wobum, 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 skied in the relevant art. In addition, numerous combinatorial libraries are themselves commercial 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 and/or causes destruction of cells. The term is intended to include radioactive isotopes chemotherapeutic agents, and toxins such as small molecule toxins or enzymaticaly active toxins of bacterial, fungal, plant or animal origin, Including fragments andfor variants thereof. Examples of cytotoxic agents include, but are not limited to auristatins, auromycins, maytansinolds, yttium, bismuth, ricin, ricin A-chain, combrestatin, duocarmycins, dolostatins, doxorubicin, daunorubicin, taxol, cisplatin, cc1065, ethidium bromide, mitomycin, etoposide, tenoposide, vincristine, vinblastine, colchicine, dihydroxy anthracin done, actinomycin, diphtheria toxin, Pseudomonas exotoxin (PE) A, PE4O, abrin, abrin A chain, modeocin A chain, alpha-sardn, gelonin, mitogellin, retstrictocin, phenomycin, enomycin, curicin, crotin, calicheamicin, Sapaonaria officinalis Inhibitor, and glucocorticoid and other chemotherapeutic agents, as well as radioisotopes such as At21, 1131, 1125, Y9, Rei8, Re'", SmIS 3 , BI22r 13, p32 and radioactive isotopes of Lu including Lu'. 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 nuclelc acid of Figure 2. The cancer protein can be a fragment, or alternatively, be the fullength 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 naturaly occuring allelic variants of a protein encoded by a nudeic add 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 disdoses high throughput screening methods for proteins; U.S. Patent No. 5,585,639 disposes high throughput screening methods for nucleic add 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. Fulerton, CA; Precision Systems, Inc., Natick, MA; etc.). These systems typically automate entire procedures, including all sample 13 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 dass 11 Major Histocompatibility Complex (MHC) protein (see, e.g., Stites, at at., IMMUNOLOGY, 8' 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% formamideI6XSSCIO.1% SDS/100 pg/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 acordance with the invention preferably do not contain materials normally associated with the peptides in their in situ environment. For example, a polynudeotide is said to be Isolated" when It is substantially separated from contaminant polynudeotides that correspond or are complementary to genes other than the 24P4C12 genes or that encode polypeptides other than 24P4C12 gene product or fragments thereof. A skilled artisan can readily employ nuleic acid isolation procedures to obtain an isolated 24P4C1 2 polynucleotide. A protein is said to be Isolated,' for example, when physical, mechanical or chemical methods are employed to remove the 24P4C12 proteins from cellular constituents that are normally associated with the protein. A skilled artisan can readily employ standard purification methods to obtain an isolated 24P4C12 protein. Altenatively, an isolated protein can be prepared by chemical means. The tern mammal' refers to any organism classified as a mammal, includng 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 'Inetastatic 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 sie 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, Over and brain. Metastatic ,prostate cancer is typically diagnosed by open or laparoscopic pelvic lymphadenectomy, whole body radionudide scans, skeletal radiography, andlar bone lesion biopsy. The term "modulator' or 'test compound" or 'drug candidate' or grammatical equivalents as used herein describe .any molecule, e.g., protein, oligopepfide, small organic molecule, polysaccharide, polynudeotide, 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 add or protein sequences, or effects of cancer sequences (e.g., signing, gene expression, protein interaction, etc.) In one aspect, a modulator will neutralize the effect of a cancer protein of the Invention. By *neutralize Is meant that an activity of a protein 14 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 paralel 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 banding, and typically indude at least an amine, carbony, 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 dass 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 add and the N-terminus is a free amine to aid in coupling, i.e., to cystelne. 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 adds to create a longer peptide/protein. The modulatory peptides can be digests of naturally occurring proteins as is outlined above, random peptides, or 'blased" random peptides. In a preferred embodiment, peptlde/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 acds, random nucleic acids, or basede" 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 monoclonall 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 *motir, as in biological motif of a 24P4C12-related protein, refers to any pattern of amino adds 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, "moif" refers to the pattem of residues In a peptide of defined length, usually a peptide of from about 8 to about 13 amino acids for a dass I HLIA motif and from about 6 to about 25 amino acids for a dass II HLA motif, which Is recognized by a particular HLA molecule. Peptude motifs for HLA binding are typically different for each protein encoded by each human HLA allete and differ In the pattern of the primary and secondary anchor residues. 15 A "pharmaceutical excipienr comprises a material such as an adjuvant, a carrier, p-l-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 "polynudeotide" means a polymeric form of nucleotides of at least 10 bases or base pairs in length, either ribonucleotides or deoxynudeotides 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 oligonucleolde". A polynudeotide 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 acds. 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 add at a specific position along a peptide sequence which is understood to provide a contact point between the immunogenic peplide and the HLA molecule. One to three, usually two, primary anchor residues within a peptide of defined length generally defines a "motir 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 dass 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 |1 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) Actinlum-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 radlolmmunotherapy Bismuth-212 (Bi-212) See Thorium-228 (Th-228) Bismuth-213 (Bi-213) See Thorum-229 (Th-229) Cadmium-109 (Cd-1 09) Cancer detection 16 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 radicimmunotherapy 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 Europlum-152 (Eu-1 52) Radiation source for food Irradiation and for sterlization of medical supplies Europium-154 (Eu-154) Radiation source for food irradiation and for sterilization of medical supplies Gadolinium-153 (Gd-153) Osteoporosis detection and nuclear medical quality assurance devices Gold-198 (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 lodine-125 (1-125) Osteoporosis detection, diagnostic imaging, tracer drugs, brain cancer treatment, radiolabeling, tumor imaging, mapping of receptors In the brain, interstiial 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 todine-131 (1-131)' Thyroid function evaluation, thyroid disease detection, treatment of thyroid cancer as well as other non malignant thyroid diseases (Le., Graves disease, goiters, and hyperthyroidism), treatment of leukemia, lymphoma. and other forms of cancer (e.g., breast cancer) using rediolmmunotherapy Iridium-192 (r-192) Brachytherapy, brain and spinal cord tumor treatment, treatment of blocked arteries (i.e., arteriosclerosis and restenosis), and implants for breast and prostate tumors Lutelium-177 (Lu-177) 17 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, To-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 Palladlum-103 (Pd-103) Prostate cancer treatment Platinum-195m (Pt-1 95m) Studies on blodistrIbution 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 nuclekc adds 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 diagnosisltreatment, radiolabeling, and treatment of blocked arteries (i.e., arteriosclerosis and restenosis) Radium-223 (Ra-223) See Actinlum-227 (Ac-227) Rhenium-186 (Re-186) Bone cancer pain relief, rheumatoid arthdtis treatment, and diagnosis and treatment of lymphoma and bone, breast, colon, and liver canors 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 Samarum-153 (Sm-153) Cancer radioimmunotherepy and bone cancer pain relief Scandium-47 (Sc-47) Cancer radiolmnunotherapy and bone cancer pain relief Seleniurn-75 (Se-75) 18 Radiotracer used in brain studies, imaging of adrenal cortex by gamma-scintigraphy, lateral locations of steroid secreting tumors, pancreatic scanning, detection of hyperactive parathyrold 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 Techrnetium-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 Thorum-229 (Th-229) Parent of Actinium-225 (Ac-225) and grandparent of Bismuth-213 (Bi-213) which are alpha emitters used in cancer radioimmunotherapy Thullum-170 (Tm-170) Gamma source for blood irradiators, energy source for implanted medical devices Tin-117m (Sn-1 17m) Cancer immunotherapy and bone cancer pain relief Tungsten-188 (W-188) Parent for Rhenium-188 (Re-1 88) which is used for cancer diagnoslics/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 radloimunotherapy Yttrium-90 (Y-90) Microseeds obtained from irradiating Yttrium-89 (Y-89) for river cancer treatment Yttrium-91 (Y-91) A gamma-emitting label for Yttrium-90 (Y-90) which Is used for canor radiolmmunotherapy (i.e., lymphoma, breast, colon, kidney, lung, ovarian, prostate, pancreatic, and inoperable liver cancers) 19 By 'randomized' or grammatical equivalents as herein applied to nuclec acids and proteins is meant that each nucleic acid and peptide consists of essentially random nuceotides and amino acids, respectively. These random peptides (or nucleic acids, discussed herein) can Incorporate any nuceotide 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 bloactive 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 nudeotides or amino acid residues are randomized within a defined class, e.g., of hydrophobic amino adds, 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 "reombinanr DNA or RNA molecule is a DNA or RNA molecule that has been subjected to molecular manipulation in vRRo. Non-limiting examples of small molecules Include compounds that bind or interact with 24P4C12, ligands induding hormones, neuropeptides, chemokines, odorants, phospholipids, and functional equivalents thereof that bind and preferably Inhibit 24P4C12 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, 24P4C12 protein; are not found in natural 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 nudeic 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 of 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 dilorIde/0.001 5 M sodium citrate/l.1 % sodium dodecyl sulfate at 500C; (2) employ during hybridization a denaturing agent, such as formamide, for example, 50% (v/v) formamide with 0.1% bovine serum albumin/0.1% Flcoll/O.1% polyvinylpyrrolidonel50 mM sodium phosphate buffer at pH 6.5 with 750 mM sodium chloride, 75 mM sodium citrate at 42 OC; or (3) employ 50% fomamide, 5 x SSC (0.75 M NaCl, 0.075 M sodium citrate), 50 mM sodium phosphate (pH 6.8), 0.1% sodium pyrophosphate, 5 x Denhard's solution, sonicated salmon sperm DNA (50 pg/m), 0.1% SDS, and 10% dextran sulfate at 42 cC, with washes at 420C in 0.2 x SSC (sodium chloridelsodium. citrate) and 50% formamide at 55 CC, 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 of 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 376C in a solution comprIsing: 20% formamide, 5 x SSC (150 mM NaCl, 15 mM trisodium citrate), 50 mM sodium phosphate (pH 7.6), 5 x 20 Denhardrs solution, 10% dextran sulfate, and 20 mg/mL denatured sheared salmon sperm DNA, followed by washing the filters in 1 x SSC at about 37-50C. 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: A 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 BY: B7, 6*3501-03, 8*51, B*5301, B*5401, 8*5501, B*5502, B*5601, B*6701, B*7801, B*0702, B*5101, B*5602 B44; B'3701, B*4402, B*4403, B'60 (B*4001), 861 (84006) Al A*0102, A*2604, A*3601, A*4301, A*8001 A4; A*24, A*30, A*2403, A*2404, A*302, A*3003 827; B*1401-02, B*1503, B*1509, B*1510, B*1518, B*3801-02, 0*3901, B*3902, B*3903-04, B*4801-02, B*7301, B'2701-08 B58; 81516, B*1517, B*5701, B*5702, 858 §12-_B*4601, 852, B*1501 (862), B*1502 (875), B*1513 (B77) Calculated population coverage afforded by different HLA-supertype combinations are set forth in Table IV (G). As used herein 'to trear 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 adds 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., atleast 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. HI.A class I peptides of the invention can be adrxed with, or inked to, HLA class I 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 calts. The term variant* refers toa molecule that exhibits a variation from a desgibed type or nonn, such as a protein that has one or more different amino add residues in the corresponding position(s) of a spedically described protein (e.g. the 24P4C1 2 protein shown in Figure 2 or Figure 3. An analog is an example of a variant protein. Splice isoforms and single nudeotides polymorphisms (SNPs) are further examples of variants. The "24P4C12-related proteins' of the invention include those specifically identified herein, as well as altec vagrants, conservative substitution variants, analogs and homologs that can be isdated/generated and characterized without undue experimentaion following the methods outlined herein or readily available in the art Fusion proteins that combine parts of different 24P4C12 proteins or fragments thereof, as well as fusion proteins of a 24P4C12 protein and a heterologous polypeptide 21 are also induded. Such 24P4C12 proteins are collecvely referred to as the 24P4C12-related proteins, the proteins of the invention, or 24P4C12. The term "24P4C127related protein" refers to a polypeptide fragment or a 24P4C12 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 acids; 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, 600, 625, 650, or 664 or more amino acids. ii.) 24P4C12 Polynucleotides One aspect of the invention provides polynucleotides corresponding or complementary to all or part of a 24P4C12 gene, mRNA, and/or codng sequence, preferably in isolated form, induding polynuceotides encoding a 24P4C1 2-related protein and fragments thereof, DNA, RNA, DNAIRNA hybrid, and related molecules, polynucleotdes or oigonudeotides complementary to a 24P4C1 2 gene or mRNA sequence or a part thereof, and polynudeotides or oligonucleotides that hybridize to a 24P4C12 gene, mRNA, orto a 24P4C12 encoding polynudeotide (collectively, "24P4C12 polynuceotides"). In all instances when referred to In this section, T can also be U in Figure 2. Embodiments of a 24P4C12 polynucleotide Indude: a 24P4C12 polynucleotide having the sequence shown in Figure 2, the nucleotide sequence of 24P4C12 as shown in Figure 2 wherein T is U; at least 10 contiguous nucleotides of a polynudeotide having the sequence as shown In Figure 2; or, at least 10 contiguous nucleotides of a polynudeotide having the sequence as shown in Figure 2 where T is U. For example, embodiments of 24P4C12 nudeotides comprise, without limitation: (1) a polynudeotide comprising, consisting essentially of, or consisting of a sequence as shown in Figure 2, wherein T can also be U; (11) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2A, from nucleotide residue number 6 through nucleotide residue number 2138, induding the stop codon, wherein T can also be U; (li) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown In Figure 28, from nucleotide residue number 6 through nudeotide residue number 2138, induding the stop codon, wherein T can also be U; (IV) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown In Figure 2C, from nuceotide residue number 6 through nucleotide residue number 2138, Induding the a stop codon, wherein T can also be U; (V) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2D, from nudeotide residue number 6 through nucleotide residue number 2138, induding the stop codon, wherein T can also be U; (VI) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2E, from nudeotide residue number 6 through nucleotide residue number 2138, Induding the stop codon, wherein T can also be U; 22 (VII) a polynucleotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2F, from nucleotide residue number 6 through nucleodide residue number 2138, induding the stop codon, wherein T can also be U; (VIII) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2G, from nucleotide residue number 6 through nucleotide residue number 1802, induding the stop codon, wherein T can also be U; (IX) a polynudeotide comprising, consisting essentially of, or consisting of the sequence as shown in Figure 2H, from nucleotide residue number 6 through nudeotide residue number 2174, 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 6 through nucleotide residue number 2144, including the stop codon, wherein T can also be U; (XI) a polynudeotide that encodes a 24P4C 12-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99 or 100% homologous to an entire amino add sequence shown in Figure 2A-l; (XII) a polynucleotide that encodes a 24P4C12-related protein that is at least 90, 91, 92,93, 94, 95,96, 97, 98, 99 or 100% identical to an entire amino add sequence shown in Figure 2A-I; (XIll) a polynudeotide that encodes at least one peptide set forth in Tables VIII-XXI and XXIIL-XIX; (XIV) a polynudeotide 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-D in any whole number increment up to 710 thatindudes 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; (XV) a polynudeotide 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-D in any whole number increment up to 710 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; (XVI) a polynudeotide 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-D in any whole number Increment up to 710 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; (XVII) a polynudeotide 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-D in any whole number Increment up to 710 that includes 1, 2, 3, 4, 5,6, 7, 8,9, 10, 11, 12, 13, 14, 15,16, 17, 18, 19, 20, 23 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; (XVIII) a polynudeotide 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 pepfide of Figure 3A-D In any whole number increment up to 710 that Indudes 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; (XIX) a polynudeolide 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 cf a peptide of Figure 3E In any whole number increment up to 598 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; (XX) a polynudeotide 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 in any whole number Increment up to 598 that Indudes 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 add positlon(s) having a value less than 0.5 in the Hydropathicity profile of Figure 6; (XXI) a polynudeotide that encodes 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 3E in any whole number Increment up to 598 that indudes 1, 2, 3,4, 5, 6, 7, 6, 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; (XXII) a polynudeotide 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 adds of a peptide of Figure 3E In any whole number Increment up to 598 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; (XXIl) a polynudeotide that encodes 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 3E In any whole number increment up to 598 that indudes 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 (XXIV) a polynudeotide 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 adds of a peptide of Figure 3F In any whole number Increment up to 722 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 add position(s) having a value greater Jhan 0.5 In the Hydrophilicty profile of Figure 5; 24 (XXV) 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 adds of a peptide of Figure 3F in any whole number Increment up to 722 that indudes 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; (XXVI) a polynudeotide that encodes 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 adds of a peptide of Figure 3F in any whole number increment up to 722 that indudes 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; (XXVIl) a polynudeoide 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 3F in any whole number Increment up to 722 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 add position(s) having a value greater than 0.5 in the Average Flexibiity profile of Figure 8; (XXVIII) 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 3F In any whole number increment up to 722 that indudes 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 positlon(s) having a value greater than 0.5 in the Beta turn profile of Figure 9 (XXIX) a polynudeotide 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 3G in any whole number increment up to 712 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; (OO) a polynudeotide 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 3G in any whole number increment up to 712 that indudes 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 polynudeotide 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 3G in any whole number increment up to 712 that Indudes 1, 2, 3,4,5,6, 7,8,9,10,11, 1213, 14,15,16,17,18,19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35 amino add position(s) having a value greater than 0.5 In the Percent Accessible Residues profile of Figure 7; (XXXII) a polynudeotide 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 3G In any whole 25 number increment up to 712 that indudes 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 add positions) having a value greater than 0.5 in the Average Flexibility profile of Figure 8; (XXXIll) a polynudeotide 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 3G in any whole number increment up to 712 that indudes 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 (XXXV) a polynucleotide that is fully complementary to a polynudeotide of any one of (I)-(XXXIl). (XXXV) a peptide that is encoded by any of () to (XXXiii); and (XXXVI) a composition compising a polynudeotide of any of (IHXXXIV) or peptide of (XXXV) together with a pharmaceutical excipient and/or in a human unit dose form. (XXXVII) a method of using a polynucleotide of any (IH XXXIV) or peptide of (XXXV) or a composidon of (XXXVI) in a method to modulate a cell expressing 24P4C12, (XXXVIII) a method of using a polynudeotide of any (IH XXXIV) or pepide of (XXXV) or a composition of (XXXVI) in a method to diagnose, prophylax, prognose, or treat an Individual who bears a ceU expressing 24P4C12 (XXXI) a method of using a polynudeodde of any ()4 XXXIV) or peptide of (XXXV) or a composition of (XXXVI) in a method to diagnose, prophylax, prognose, or treat an individual who bears a cel expressing 24P4C12, said cel from a cancer of a tissue listed in Table I; (XL) a method of using a polynudeotide of any (I)JMXV) or peptide of (XXXV) or a composition of (XXXVI) in a method to diagnose, prophylax, prognose, or treat a a cancer; (XLI) a method of using a polynudeotide of any (IHXXXUV) or peptide of (XXXV) or a composition of (XXXVI) in a method to diagnose, prophylax, prognose, or treat a a cancer of a tissue listed in Table I; and, (XLII) a method of using a polynucleotide of any (IHXXXIV) or peptide of (XXXV) or a composition of (XXXVI) in a method to identify or characterize a modulator of a cell expressing 24P4C1 2. As used herein, a range Is understood to disdose specifically all whole unit positions thereof. Typical embodiments of the invention disposed herein indude 24P4C12 polynudeotides that encode specific portions of 24P4C12 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, 225, 250, 275, 300,325, 350,375,400,425,450, 475,500, 525, 550, 575,600,625, 650,675, 700, 710 or more contiguous amino acids of 24P4C12 variant 1; the maximal lengths relevant for other variants are: variant 3,710 amino acids; variant 5, 710 amino adds, variant 6, 710 amino acids, variant 7, 598 amino acids, variant 8, 722 amino acids, and variant 9, 712 amino adds. 26 For example, representative embodiments of the invention disclosed herein include: polynudeotides and their encoded peptides themselves encoding about amino acid I to about amino acid 10 of the 24P4C12 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 10 to about amino acid 20 of the 24P4C12 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 20 to about amino acid 30 of the 24P4C12 protein shown in Figure 2 or Figure 3, polynudeotldes encoding about amino acid 30 to about amino acid 40 of the 24P4C1 2 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 40 to about amino acid 50 of the 24P4C1 2 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 50 to about amino acid 60 of the 24P4C12 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 60 to about amino acid 70 of the 24P4C12 protein shown in Figure 2 or Figure 3, polynucleotides encoding about amino acid 70 to about amino acid 80 of the 24P4C1 2 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 80 to about amino acid 90 of the 24P4C12 protein shown in Figure 2 or Figure 3, polynudeotides encoding about amino acid 90 to about amino acid 100 of the 24P4C12 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 aids), of amino acids, 100 through the carboxyl terminal amino acid of the 24P4C12 protein are embodiments of the Invention. Wherein it Is understood that each particular amino add position discloses that position plus or minus five amino acid residues. Polyrudeotides encoding relatively long portions of a 24P4C12 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 24P4C1 2 protein 'or variant" shown In Figure 2 or Figure 3 can be generated by a variety of techniques well known in the art. These polynudeotide fragments can include any portion of the 24P4C12 sequence as shown in Figure 2. Additional Illustrative embodiments of the invention disclosed herein include 24P4C12 polynudeotide fragments encoding one or more of the biological motifs contained within a 24P4C12 protein "or variant" sequence, including one or more of the motif-bearing subsequences of a 24P4C1 2 protein 'or variant sel forth in Tables Vill-XXI and XXII-XLIX. In another embodiment typical polynudleotide fragments of the invention encode one or more of the regions of 24P4C1 2 protein or variant that exhibit homology to a known molecule. In another embodiment of the invention, typical polynudeotide fragments can encode one or more of the 24P4C12 protein or variant N-glycosylation sites, cAMP and cGMP-dependent protein kinase phosphorylation sites, casein kinase il phosphorylation sites or N-myristoylation site and amidation sites. Note that to determine the starting position of any peptide set forth in Tables VIl-XXI and Tables XXII to XLIX (colectively 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 LVII. 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"lo each position in Tables Vil-XXI and Tables XXIi-IL 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. DA.) Uses of 24P4C12 Polvnucleotides hI.A.1.) Monitoring of Genetlc Abnormalities The polynuceotides of the preceding paragraphs have a number of different specific uses. The human 24P4C12 gene maps to the chromosomal location set forth in the Example entitled Chromosomal Mapping of 24P4C12." For example, because the 24P4C12 gene maps to this chromosome, polynucleotides that encode different regions of the 24P4C1 2 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 27 rearrangements have been identIfied as frequent cytogenetic abnonnalities 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 a/., P.NAS. 85(23): 9158-9162 (1988)). Thus, polynudeotides encoding specific regions of the 24P4C12 proteins provide new tools that can be used to delineate, with greater precision than previously possible, cytogenetic abnormalities in the chromosomal region that encodes 24P4C12 that may contribute to the malignant phenotype. In this context, these polynudeotides 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 a., Am. J. Obstet. Gynecol 171(4): 1055-1057 (1994)). Furthermore, as 24P4C12 was shown to be highly expressed In bladder and other cancers, 24P4C12 polynudeotides are used in methods assessing the status of 24P4C12 gene products in normal versus cancerous tissues. Typically, polynucleotides that encode specific regions of the 24P4C12 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 24P4C12 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 polynudeotides encoding specific regions of a protein to examine these regions within the protein. IiA.2.) Antisense Embodiments Other specifically contemplated nudeic acid related embodiments of the Invention disclosed herein are genonic DNA, cDNAs, rbozymes, and antisense molecules, as well as nucleic acid molecules based on an alternative backbone, or including alternative bases, whether delved from natural sources or synthesized, and include molecules capable of hbiting the RNA or protein expression of 24P4C12. For example, antisense molecules can be RNAs or other molecules, including peptide nucleic acids (PNAs) or non-nudeic add 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 24P4C12 polynudeotides and polynudeotide sequences disclosed herein. Antisense technology entails the administration of exogenous oligonucleotides that bind to a target polynudeotide located within the cells. The term "antisense" refers to the fact that such ollgonudeotides are complementary to their intracellular targets, e.g., 24P4C1 2. See for example, Jack Cohen, Oligodeoxynucleotides, Antisense Inhibitors of Gene Expression, CRC Press, 1989; and Synthesis 1:1-5 (1988). The 24P4C12 antisense oligonucleotides of the present invention include derivatives such as S-oligonudeotides (phosphorothioate derivatives or S-oligos, see, Jack Cohen, supra), which exhibit enhanced cancer cell growth inhibitory action. S-oigos (nucleoside phosphorothioates) are isoelectronic analogs of an oligonucleotide (O-oligo) in which a nonbddging 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 benzodithlol-3-one-1,1-dioxide, which is a sulfur transfer reagent. See, e.g., lyer, R. P. el a., J. Org. Chem. 55:4693-4698 (1990); and lyer, R. P. et al, J. Am. Chem. Soc. 112:1253-1254 (1990). Additional 24P4C12 antisense oligonudeotides of the present invention include morpholino antisense oligonucleotides known in the art (see, e.g., Partridge et al., 1996, Antisense & Nucleic Acid Drug Development 6:169-175). The 24P4C12 antisense oligonucleotides of the present invention typically can be RNA or DNA that is complementary to and stably hybridizes with the first 1005' codons or last 100 3'codons of a 24P4C1 2 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 24P4C12 mRNA and not to mRNA specifying other regulatory subunits of protein kinase. In one embodiment, 24P4C12 antisense oligonucleotides of the present invention are 15 to 30-mer fragments of the antisense DNA moleale that have a sequence 28 that hybridizes to 24P4C12 mRNA. Optionally, 24P4C12 antisense oligonucleotide is a 30-mer oligonudeotide that is complementary to a region in the first 10 5' codons or last 10 3' codons of 24P4C12. Alternatively, the antisense molecules are modified to employ ribozymes in the inhibition of 24P4C12 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 nudeotides 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 nudeic 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 24P4C1 2 polynudeotide in a sample and as a means for detecting a cell expressing a 24P4C12 protein. Examples of such probes indude polypeptides comprising al or part of the human 24P4C1 2 cDNA sequence shown In Figure 2. Examples of primer pairs capable of specifically amplifying 24P4C12 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 24P4C12 mRNA. The 24P4C12 polynudeotides 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 24P4C12 gene(s), mRNA(s), or fragments thereof; as reagents for the diagnosis andfor prognosis of prostate cancer and other cancers; as coding sequences capable of directing the expression of 24P4C12 polypeptides; as tools for modulating or inhibiting the expression of the 24P4C12 gene(s) and/or translation of the 24P4C12 transcript(s); and as therapeutic agents. The present 'nvention includes the use of any probe as described herein to identify and isolate a 24P4C12 or 24P4C1 2 related nudeic acid sequence from a naturally occurring source, such as humans or other mammals, as well as the isolated nudeic acid sequence per se, which would comprise all or most of the sequences found in the probe used. IL.A.4.) Isolation of 24P4C1 2-Encoding Nucleic Acid Molecules The 24P4C1 2 cONA sequences described herein enable the Isolation of other polynucleotides encoding 24P4C12 gene product(s), as well as the isolation of polynudeotides encoding 24P4C1 2 gene product homologs, alternatively spliced isoforms, allelic variants, and mutant forms of a 24P4C12 gene product as wel as polynudeotides that encode analogs of 24P4C12-related proteins. Various molecular cloning methods that can be employed to isolate full length cDNAs encoding a 24P4C12 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; Cunent 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 dones containing 24P4C12 gene cDNAs can be identified by probing with a labeled 24P4C12 cDNA or a fragment thereof. For example, in one embodiment, a 24P4C12 cDNA (e.g., Figure 2) or a portion thereof can be synthesized and used as a probe to retrieve overlapping and fulHength cDNAs corresponding to a 24P4C12 gene. A 24P4C12 gene itself can be isolated by screening genomic DNA libraries, bacterial artificial chromosome libraries (BACs), yeast artificial chromosome libraries (YACs), and the like, with 24P4C12 DNA probes or primers. ILA.5,) Recombinant Nucleic Acid Molecules and Host-Vector Systems The invention also provides recombinant DNA or RNA molecules containing a 24P4C12 polynudeotide, a fragment analog or homologue thereof, including but not limited to phages, plasmids, phagemids, cosmids, YACs, BACs, as wen as various viral and non-viral vendors well known in the art, and cells transformed or transfected with such recombinant DNA or RNA moecules. Methods for generating such molecules are wel known (see, for example. Sambrook et al, 1989, supra). 29 The invention further provides a host-vector system comprising a recombinant DNA molecule containing a 24P4C12 polynudeotide, fragment analog or homologue Ihereof 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 Indude various prostate cancer cell lines such as DU145 and TsuPrl, other transfectable or transdudble 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 polynudeotide comprising the coding sequence of 24P4C12 or a fragment, analog or homolog thereof can be used to generate 24P4C12 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 24P4C12 proteins or fragments thereof are available, see for example, Sambrook et at., 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 pSRkaneo (Muller ef al., 1991. MCB 11:1785). Using these expression vectors, 24P4C12 can be expressed in several prostate cancer and non-prostate cell lines, including for example 293, 293T, rat-1, NIH 3T3 and TsuPr1. The host-vector systems of the invention are useful for the production of a 24P4C1 2 protein or fragment thereof. Such host-vector systems can be employed to study the functional properties of 24P4C1 2 and 24P4C12 mutations or analogs. Recombinant human 24P4C12 protein or an analog or homolog or fragment thereof can be produced by mammalian cells transfected with a construct encoding a 24P4C12-related nudeotide. For example, 293T cells can be transfected with an expression plasmid encoding 24P4C12 or fragment, analog or homolog thereof, a 24P4C12-related protein is expressed in the 293T cells, and the recombinant 24P4C12 protein is isolated using standard purification methods (e.g., affinity purification using anti-24P4C12 antibodies). In another embodiment, a 24P4C12 coding sequence is subdoned into the retroviral vector pSRuMSVtkneo and used to infect various mammalian cell lines, such as NIH 3T3, TsuPrl, 293 and rat-1 In order to establish 24P4C1 2 expressing cell lines. Various other expression systems wel known in the art can also be employed. Expression constructs encoding a leader peptide joined in frame to a 24P4C12 coding sequence can be used for the generation of a secreted form of recombinant 24P4C12 protein. As discussed herein, redundancy In the genetic code permits variation in 24P4C12 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 polyadenytation signals, exonIntron splice site signals, transposon-like repeats, and/or other such well-characterized sequences that are deleterious to gene expression. The GC content of the sequence Is 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. CeP 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., 24P4C12-related Proteins 30 Another aspect of the present invention provides 24P4C12-related proteins. Specific embodiments of 24P4C12 proteins comprise a polypeptide having all or part of the amino acid sequence of human 24P4C12 as shown in Figure 2 or Figure 3. Alternatively, embodiments of 24P4C1 2 proteins comprise vacant, homolog or analog polypeptides that have alterations in the amino acid sequence of 24P4C1 2 shown In Figure 2 or Figure 3. Embodiments of a 24P4C12 polypeptide indude: a 24P4C12 polypeptide having a sequence shown in Figure 2, a peptide sequence of a 24P4C12 as shown in Figure 2 wherein T Is U; at least.10 contiguous nudeotides 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 24P4C12 peptides comprise, withoutlimitation: (I) a protein comprising, consisting essentially of, or consisting of an amino add sequence as shown in Figure 2A-I or Figure 3A-G; (I) a 24P4C12-related protein that is at least 90, 91, 92, 93, 94, 95, 96, 97,98, 99 or 100% homologous to an entire amino add sequence shown In Figure 2A-1: (ll) a 24P4C12-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-1 or 3A-G; (IV) a protein that comprises at least one peptide set forth in Tables Vill to XIJX, 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 VIl-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 Vill-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 Vill to XLIX collectively, with a proviso that the protein Is not a contiguous sequence from an amino acid sequence of Figure 2; (Vill) a protein that comprises at least one peptide selected from the peptides set forth In Tables Vill-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 add sequence of Figure 2; (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 adds of a protein of Figure 3A, 31, 3C, 3D, 3E, 3F, or 3G In any whole number Increment up to 710, 710, 710, 710, 598, 722, or 712 respectively that indudes 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 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 protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, or 3G In any whole number increment up to 710, 710, 710, 710, 598, 722, or 712 respectively, that Indudes 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 add positions) having a value less than 0.5 in the Hydropathicity profile of Figure 6; 31 (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, or 3G in any whole number increment up to 710, 710, 710, 710, 598, 722, or 712 respectively, 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 Percent Accessible Residues profile of Figure 7; (XII) a polypeptide comprising 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 protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, or 3G In any whole number increment up to 710, 710, 710, 710, 598, 722, or 712 respectively, 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 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, 35 amino adds of a protein of Figure 3A, 3B, 3C, 3D, 3E, 3F, or 3G in any whole number increment up to 710, 710, 710, 710, 598, 722, or 712 respectively, 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 Beta-turn profile of Figure 9: (XIV) a peptide that occurs at least twice in Tables VIlI-XXI and XXII to XLIX, collectively; (XV) a peptide that occurs at least three times in Tables VIII-XXI and XXII to XLIX, collectively; (XVI) a peptide that occurs at least four times in Tables VIII-XXI and XXI to XLIX, collectively; (XVII) a peptide that occurs at least five times in Tables VIllI-XXI and XXI to XLIX, collectively; (XVIII) a peptide that occurs at least once in Tables Vill-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; (() 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 VI-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 oligonudeotide encoding such peptide: I) a region of at least 5 amino acids of a particular peplide of Figure 3, in any whole number Increment up to the full length of that protein in Figure 3, that includes an amino add 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 Hydrophilcity profile of Figure 5; 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 add 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: ii) a region of at least 5 amino adds 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 add 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, 32 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 indudes 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 (INXXII), or an antibody or binding region thereof or a composition of (XXIII) in a method to modulate a cell expressing 24P4C12, (XXV) a method of using a peptide of (IHXXI) 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 24P4C1 2 (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 call expressing 24P4C12, said cell from a cancer of a tissue listed in Table I; (XXVII) a method of using a peptide of (INXXIl) or an antibody or binding region thereof or a composition of (XXIII) in a method to diagnose, prophylax, prognose, or treat a a cancer; (XXVIll) a method of using a peptide of (IHXXI) 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 Usted In Table I; and, (XXIX) a method of using a a peptide of (I)NXXI) or an antibody or binding region thereof or a composition (XXII) in a method to identify or characterize a modulator of a cell expressing 24P4C12. As used herein, a range is understood to specifically disclose all whole unit positions thereof. Typical embodiments of the invention disclosed herein include 24P4C1 2 polynucleotides that encode spedfic portions of 24P4C12 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, -. 225,250, 275, 300, 325,350,375, 400, 425, 450, 475, 500, 525, 550,575, 600, 625,650,675,700,710 or more contiguous amino acids of 24P4C12 variant 1; the maximal lengths relevant for other variants are: variant 3,710 amino acids; variant 5, 710 amino acids, variant 6, 710, variant7, 598 amino acids, variant 8, 722 ar'ino acids, and variant 9, 712 amino adds.. In general, naturally occuning allelic variants of human 24P4C12 share a high degree of structural identity and homology (e.g., 90% or more homology). Typically, allelic variants of a 24P4C12 protein contain conservative amino add substitutions within the 24P4C12 sequences described herein or contain a substitution of an amino acid from a corresponding posidonin ahomologueof 24P4C12. One dass of24P4C12 aldic variants are proteins that share ahigh degree of homology with atlieast a small regon of a particular 24P4C12 amino acid sequence, but further contain a radical departure from the sequence, such as a non-anservative subsitution, truncation, insertion or frame shift In comparisons of protein sequences, the terms, similarity, Identity, and homology eac have a distinct meaning as appreciated In the field of genetics. Moreover, orthology and paralogy can be imporant concepts descdbing the relationship of members of a given protein family In one organism to the members of the same family in other organisms. 33 Amino acid abbreviations are provided in Table ll. 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 (0) 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 add 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 IlIl herein; pages 13-15'Biochemistry' 2nd ED. Lubert Stryer ed (Stanford University); Henikoff ef 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 24P4C12 proteins such as polypeptides having amino acid Insertions, deletions and substitutions. 24P4C12 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 at., Nuct. Acids Res., 13:4331 (1986); Zolier et al., Nud. 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 doned DNA to produce the 24P4C1 2 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, seine, and cysteine. Alanine is typically a preferred scanning amino acid among this group because it elminates 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. As defined herein, 24P4C1 2 variants, analogs or homologs, have the distinguishing attribute of having at least one epitope that Is "cross reactive' with a 24P4C12 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 24P4C1 2 variant also specifically binds to a 24P4C12 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 24P4C12 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 a., Mol Immunol (1989) 26(9):865-73; Schwartz et aL, J Immunol (1985) 135(4):2598-608. Other classes of 24P4C1 2-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 24P4C12 protein variants or analogs comprises one or more of the 24P4C12 biological motifs described herein or presently known in the art. Thus, encompassed by the present Invention are analogs of 24P4C12 fragments (nucleic or amino acid) that have altered functional (e.g. 34 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 24P4C12 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 24P4C1 2 protein shown in Figure 2 or Figure 3. Moreover, representative embodiments of the invention disclosed herein include polypeptides consisting of about amino acid i to about amino acid 10 of a 24P4C12 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 10 to about amino acid 20 of a 24P4C12 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 20 to about amino acid 30 of a 24P4C12 protein shown in Figure 2 or Figure 3, polypepddes consisting of about amino acid 30 to about amino acid 40 of a 24P4C12 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 40 to about amino acid 50 of a 24P4C12 protein shown In Figure 2 or Figure 3, polypeptides consisting of about amino acid 50 to about amino acid 60 of a 24P4C12 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 60 to about amino acid 70 of a 24P4C12 protein shown In Figure 2 or Figure 3, polypeptides consisting of about amino acid 70 to about amino acid 80 of a 24P4C12 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 80 to about amino acid 90 of a 24P4C12 protein shown in Figure 2 or Figure 3, polypeptides consisting of about amino acid 90 to about amino acid 100 of a 24P4C12 protein shown In Figure 2 or Figure 3, etc. throughout the entirely of a 24P4C12 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 24P4C1 2 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 wel as that position plus or minus 5 residues. 24P4C 12-related proteins are generated using standard peptide synthesis technology or using chemical cleavage methods weil known in the art. Alternatively, recombinant methods can be used to generate nucleic acid molecules that encode a 24P4C12-related protein. In one embodiment, nucleic add molecules provide a means to generate defined fragments of a 24P4C1 2 protein (or variants, homologs or analogs thereof). lIl.A.) Motif-bearina Protein Embodiments Additional Illustrative embodiments of the invention disclosed herein indude 24P4C1 2 polypeptides comprising the amino acid residues of one or more of the biological motifs contained within a 24P4C1 2 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 a number of publicly available Internet sites (see, e.g., URL addresses: pfam.wusti.edul; searchlauncher.bcm.tmc.edulseq searchlstruo-predict.html; psortLims.u-tokyo.ac.jpl; cbs.dtu.dkl; ebi.ac.uklinterpro/scan.html; expasy.chltootslsaipsitl.html; EpmatrIx m and Epimerm, Brown University, brown.eduReseardiTB-HVablepimatrWepimatrixhtm; and BIMAS, birqas.dcrt.nih.govl.). Motif bearing subsequences of all 24P4C12 variant proteins are set forth and identified in Tables Vill-XXI and XXII XiX Table V sets forth several frequently occurring motifs based on pfam searches (see URL address pfam.wustI.edu). 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 24P4C12 motifs discussed above are useful In elucidating the specific characteristics of a malignant phenotype in view of the observation that the 24P4C1 2 motifs discussed above are associated with growth dysregulation and because 24P4C12 is overexpressed in certain cancers (See, e.g., Table I). Casein kinase 11, 35 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 of al, Lab Invest., 78(2): 165-174 (1998); Gaiddon et al., Endocrinology 136(10): 4331-4338 (1995); Hall et af., Nucleic Acids Research 24(6): 1119-1126 (1996); Peterzel et al., Oncogene 18(46): 6322-6329 (1999) and O'Brian, Oncol. Rep. 5(2): 305-309 (1998)). Moreover, both glycosylation end myristoylation are protein modifications also associated with cancer and cancer progression (see e.g. Dennis et al., Biochem. Blophys. 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. Nai. 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 VI-XXI and XXII-XUX. CTL epitopes can be determined using specific algorithms to identify peptides within a 24P4C1 2 protein that am capable of optimally binding to specified HILA aleles (e.g., Table IV; EpmabixTm and EpimerTm, Brown University, URL brown.edu/ResearchTB HIV..Lab/epimatixepimatrix.html; and BIMAS, URL bimas.dcrtnih.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 vftro 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 HILA Class I and HLA Class I1 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 a/.; Sette, Immunogenetics 1999 50(3-4): 201 212; Sette at 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 of at., J. Immunot. 1996 157(8): 3480-90; and Falk el al., Nature 351: 290-6 (1991); Hunt et al., Science 255:1261-3 (1992); Parker al al., J. Immunol. 149:3580-7 (1992); Parker et al., J. Immunol. 152:163-75 (1994)); Kastef al., 1994 152(8): 3904-12 Borras-Cuesta etal., Hum. Immunol. 2000 61(3): 266-278; Alexander of a., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander et al., PMID: 7895164, Ul: 95202582; O'Sullivan ot al., J. Immunol. 1991 147(8): 2663-2669; Alexander ot at., Immunity 1994 1(9): 751-761 and Alexander ot al., Immunol. Res. 1998 18(2): 79-92. Related embodiments of the invention include potypeptides comprising combinations of the different motifs set forth in Table VI, and/or, one or more of the predicted CTL epitopes of Tables V1I-XXI and XXlI-XLIX, and/or, one or more of the predicted HTL epitopes of Tables XLVI-XLX, 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 Indude a number of either N-terminal and/or C-terminal amino acid residues on either side of these motifs may be desirable (to, for example, incude a greater portion of the potypeptide 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 motifIs between about 1 to about 100 amino acid residues, preferably 5 to about 50 amino add residues. 24P4C1 2-related proteins are embodied in many forms, preferably in isolated form. A purified 24P4C12 protein molecule wil be substantially free of other proteins or molecules that impair the binding of 24P4C12 to antibody, T cell or 36 other ligand. The nature and degree of isolation and purification will depend on the intended use. Embodiments of a 24P4C1 2 related proteins include purified 24P4C12-related proteins and functional, soluble 24P4C12-related proteins. In one embodiment, a functional, soluble 24P4C12 protein or fragment thereof retains the ability to be bound by antibody, T cell or other ligand. The Invention also provides 24P4C12 proteins comprising biologically active fragments of a 24P4C12 amino acid sequence shown in Figure 2 or Figure 3. Such proteins exhibit properties of the starting 24P4C1 2 protein, such as the ability to elicit the generation of antibodies that specifically bind an epitope associated with the starting 24P4C12 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. 24P4C12-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 Doolitte, Eisenberg, Karplus-Sdiultz or Jameson-Wolf analysis, or based on immunogenicity. Fragments that contain such structures are particularly useful in generating subunit-specific antl-24P4C12 antibodies or T cells or in identiyng cethuar factors that bind to 24P4C12. For example, hydrophiicity profiles can be generated, and immunogenic peptide fragments identified, using the method of Hopp, T.P. and Woods. K.R., 1981, Proc. Nati. Acad. Sci. U.SA 78:3824-3828. Hydropathicity profiles can be generated, and Inmnunogenic 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-tum 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 24P4C12 protein that are capable of optimally binding to spedfied HLA alleges (e.g., by using the SYFPEITHI site at World Wide Web URL syfpelthi.bmi heidelberg.comf; the listings in Table IV(A)-(E); Epimatixm and Epimerm, Brown University, URL (brown.edu/ResearchiTB HIVJ.ablepimatrixpimatrix.html); and BIMAS, URL bimas.dcrtnih.gov). Illustrating this, peptide epitopes from 24P4C12 that are presented in the context of human MHC Class I molecules, e.g., HLA-A1, A2, A3, All. A24, B7 and B35 were predicted (see, e.g., Tables VII-XXI, XXIFXLIX). Specifically, the complete amino acid sequence of the 24P4C12 protein and relevant portions of other variants, ie., for HLA Class I predictions 9 flanking residues on either side of a point mutation or axon juction, and for HLA Class Il predictions 14 flanking residues on either side of a point mutation or axon junction corresponding to that variant were entered into the HLA Peptide Motif Search algorithm found In the Bioinformatics and Molecular Analysis Section (BIMAS) web site listed above; In addition to the site SYFPEITHI, at URL syfpeithi.bm 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 of al., Nature 351: 290 (1991); Hunt et aL, Science 255:1261-3 (1992); Parker of aL, J. Immunol. 149-3580-7 (1992); Parker at at., 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 dass 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 leudne (L) at the C-terminus (see, e.g., Parker et al., J. Immunol. 149:3580-7 (1992)). Selected results of 24P4C12 predicted binding peptides are shown in Tables VIll-XXI and XXII-XLIX herein. In Tables VIII XXI and XXI-XLVi, 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 XLV-XLIX, selected 37 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 370C at pH 6.5. Peptides with the highest binding score are predicted to be the most tightly bound to HLA Class I on the cefl surface for the greatest period of time and thus represent the best immunogenic targets for T-cefl 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 a, 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, Epimers and Epimatrim sites, or specified by the HLA dass I or class I 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 syfpelthi.bmi-heidelberg.oom/, or BIMAS, bimas.dcrtnih.gov/ are to be 'applied' to a 24P4C12 protein in accordance with the invention. As used in this context "applied" means that a 24P4C12 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 24P4C1 2 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 it motif are within the scope of the invention. Il.B.) Expression of 24P4C1 2-related Proteins In an embodiment described in the examples that follow, 24P4C1 2 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 24P4C12 with a C-terminal 6XHis and MYC tag (pcDNA3.1knycHIS, 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 24P4C12 protein in transfected cells. The secreted HIS-tagged 24P4C1 2 In the culture media can be purified, e.g., using a nickel column using standard techniques. III.C.) Modifications of 24P4C12-related Proteins Modifications of 24P4C1 2-related proteins such as covalent modifications are induded within the scope of this Invention. One type of covalent modification includes reacting targeted amino add residues of a 24P4C12 polypeptide with an organic derivatizing agent that is capable of reacting with selected side chains or the N- or C- terminal residues of a 24P4C12 protein. Another type of covalent modification of a 24P4C12 polypeptide induded within the scope of this invention comprises altering the native glycosylation patten of a protein of the invention. Another type of covalent modification of 24P4C1 2 comprises linking a 24P4C12 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 24P4C12-related proteins of the present Invention can also be modified to form a chimeric molecule comprising 24P4C12 fused to another,. heterologous polypeptide or amino acid sequence. Such a chimeic 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. Altenatively, a protein in accordance with the invention can comprise a fusion of fragments of a 24P4C12 sequence (amino or nucleic add) such that a molecule is created that is not, through its length, directly homologous to the amino or nucleic add sequences shown in Figure 2 or Figure 3. Such a chimeric molecule can comprise multiples of the same subsequence of 24P4C12. A chimeric molecule can comprise afusion of a 24P4C12-related protein with a polyhlsUdine epitope tag, which provides an epitope to which immobilized nickel can selectively bind, with 38 cytokines or with growth factors. The epitope tag is generally placed at the amino- or carboxyl- terminus of a 24P4C12 protein. In an alternative embodiment, the chimeric molecule can comprise a fusion of a 24P4C1 2-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 24P4C12 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. 10J. Uses of 24P4C12-related Proteins The proteins of the invention have a number of different specific uses. As 24P4C1 2 is highly expressed in prostate and other cancers, 24P4C12-related proteins are used in methods that assess the status of 24P4C1 2 gene products in normal versus cancerous tissues, thereby elucidating the malignant phenotype. Typically, polypeptides from specific regions of a 24P4C12 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 24P4C12-related proteins comprising the amino acid residues of one or more of the biological motifs contained within a 24P4C12 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, 24P4C12-related proteins that contain the amino acid residues of one or more of the biological motifs in a 24P4C12 protein are used to screen for factors that interact with that region of 24P4C12. 24P4C12 protein fragments/subsequences are particularly useful in generating and characterizing domain-specifc antibodies (e.g., antibodies recognizing an exiraceular or Intracellular epitope of a 24P4C12 protein), for Identifying agents or cellular factors that bind to 24P4C1 2 or a particular structural domain thereof, and in various therapeutic and diagnostic contexts, incuding but not limited to diagnostic assays, cancer vaccines and methods of preparing such vacdnes. Proteins encoded by the 24P4C12 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 igands and other agents and celutar constituents that bind to a24P4C12 gene product. Antibodies raised against a 24P4C12 protein or fragmentthereof are useful in diagnostic and prognostic assays, and imaging methodologies In the management of human cancers characterized by expression of 24P4C12 protein, such as those listed in Table 1. Such antibodies can be expressed intracelularly and used In methods of treating patients with such cancers. 24P4C12-related nucleic acids or proteins are also used in generating HTL or CTL responses. Various immunological assays useful for the detection of 24P4C12 proteins are used, including but not limited to various types of radioimmunoassays, enzyme-inked immunosarbent assays (EUSA), enzyme-inked immunofluorescent assays (ELIFA), immunocytochemical methods, and the like. Antibodies can be labeled and used as immunological imaging reagents capable of detecting 24P4C12-expressing cals (e.g., in radioscintigraphic inaging methods). 24P4C12 proteins are also particulary useful In generating cancer vaccines, as further described herein. IV.) 24P4C12 Antibodies Another aspect of the invention pviAdes antibodies that bind to 24P4C12- elated proteins. Preferred antibodies specifically bind to a 24P4C1 2-related protein and do not bind (or bind wealdy) to peplides or proteins that are not 24P4C12 related proteins. For example, antibodies that bind 24P4C12 can bind 24P4C12-related proteins such as the homologs or analogs thereof. 39 24P4C1 2 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 24P4C1 2 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 24P4C12 is Involved, such as advanced or metastatic prostate cancers. The invention also provides various Immunologica assays useful for the detection and quantification of 24P4C12 and mutant 24P4C12-related proteins. Such assays can comprise one or more 24P4C12 antibodies capable of recognizing and binding a 24P4C12-related protein, as appropriate. These assays are performed within various Immunological assay nornats wel known In the art, including but not imited to various types of radioimmunoassays, enzyme-linked immunosorbent assays (ELISA), enzyme-inked immunofluorescent assays (ELIFA), and the like. Immunological non-antibody assays of the invention also comprise T call imunogenicity assays (inhibitory or stimulatory) as well as major histocompalbility complex (MHC) binding assays. In addition, Immunological imaging methods capable of detecting prostate cancer and other cancers expressing 24P4C12 are also provided by the invention, induding but not limited to radioscntigraphic Imaging methods using labeled 24P4C12 antibodies. Such assays are cinicaly useful In the detection, monitoring, and prognosis of 24P4C12 expressing cancers such as prostate cancer. 24P4C1 2 antibodies are also used in methods for purifyng a 24P4C12-related protein and for Isolating 24P4C12 homologues and related molecules. For example, a method of purifying a 24P4C12-related protein comprises incubating a 24P4C12 antibody, whidihas been coupled to a solid matrix, with a lysate or other solution containing a 24P4C12-related protein under conditions that permit t 24P4C12 antibody to bind to the 24P4C12-related protein; washing the solid matrix to eliminate impurities; and eluting the 24P4C1 2-related protein from the coupled antibody. Other uses of 24P4C12 antibodies in accordance with the invention indude generating anti-diotypic antibodies that mimic a 24P4C12 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 24P4C12-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 24P4C12 can also be used, such as a 24P4C12 GST-4usion 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 used as an immunogen to generate appropriate antibodies. In another embodiment, a 24P4C12-related protein is synthesized and used as an Immunogen. In addition, naked DNA Immunizaion techniques known in the art are used (with or without purifed 24P4C12-related protein or 24P4C12 expressing calls) to generate an immune response to the encoded imunogen (for review, see Donnelly et al., 1997, Ann. Rev. Immunal. 15: 617-648). The amino acid sequence of a 24P4C12 protein as shown In Figure 2 or Figure 3 can be analyzed to select specific regions of the 24P4C12 protein for generating antibodies. For example, hydrophobicity and hydrophildty analyses of a24P4C12 amino acid sequence are used to Identify hydrophilic regions in the 24P4C12 structure. Regions of a 24P4C12 protein that show immunogenic structure, as wel as other regions and domains, can readily be identiled using various other methods known in the art, such as Choufasman, Gamier-Robson, Kyte-Doollttle, Elsenberg, Karplus-Schultz or Jameson-Wolf analysis. Hydrophilicity profiles can be generated using the method of Hopp, T.P. and Woods, KR., 1981, Proc. Nai. Acad. Scl. 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-tum profiles can be generated using the method of Deleage, G., Roux B., 1987, Protein 40 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 24P4C12 antibodies are further illustrated by way of the examples provided herein. Methods for preparing a protein or polypepide for use as an immunogen are well known in the art Also wellknown in the art are methods for preparing immunogenic conjugates of a protein with a carier, such as BSA, KLH or other cancer protein. In some circumstances, direct conjugation using, for example, cartiodlimide reagents are used; in other instances linking reagents such as those supplied by Pierce Chemical Co., Rockford, Il, are effective. Administration of a 24P4C12 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 fbmation. 24P4C12 monoclonal antibodies can be produced by various means well known in the art. For example, immortalized cellines that Reaete a desired monoconal antibody are prepared using the standard hybildoma tedinology of Kohler and Milstein or modifications that immortalize antibody-produdrng 8 calls, as is generally known. Immortaized cell lines that secrete the desired antibodies are screened by immunoassay in which the antigen is a 24P4C1 2-related protein. When the appropriate Immortalized cell culture is identified, the cels can be expanded and antibodies produced either from in Wiro 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 24P4C12 protein can also be produced In the context of chirneric or compleientiity determining region (CDR) grafted antibodies of multiple species origin. Humanized or human 24P4C12 antibodies can also be produced, and are preferred for use in therapeutic contexts. Methods for humanizing marine and other non-human antibodies, by substituting one or more of the non-human antibody CDRs for conesponding human antibody sequences, are well known (see for example, Jones et at., 1986, Nature 321: 522-525; Riechmann at at, 1988, Nature 332: 323-327; Vertoeyen et al., 1988, Science 239 1534-1536). See also, Carter et al, 1993, Proc. NaO. Acad. Sci. USA 89: 4285 and Sims et al., 1993, J. Imrnunol. 151: 2296. - Methods for producing fully human monoclonal antibodies Include phage display and transgenic methods (for review, see Vaughan et al., 1998, Nature Biotechnology 16: 535-539). Fully human 24P4C12 monoconal antibodies can be generated using zoning technologies employing large human Ig gene combinatorial libraries (i.e., phage display) (Grifiths and Hoogenboom, Building an in vitm knmune 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. jd., pp 65-82). Fully human 24P4C12 monoconal antibodies can also be produced using tiansgenic mice engineered to contain human unmunoglobulin gene loci as described In PCT Patent Application W098/24893, Kuchelapati and Jakobovits of 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 tie in vitro manipulation required with phage display technology and efficiently produces high affinity authentic human antibodies. Reactivity of 24P4C12 antibodies with a 24P4C12-related protein can be established by a number of well known means, inducing Western blot, Immunoprecipitation, ELISA, and FACS analyses using, as appropriate, 24P4C 12-related proteins, 24P4C12-expressing cells or extracts thereof. A 24P4C12 antibody or fragment thereof can be labeled with a detectable marker or conjugated to a second molecule. Suitable detectable markers indude, but are not limited to, a radioisotope, a fluorescent compound, a bloluminescent compound, chemiuminescent compound, a metal chelator or an enzyme. Further, bi-specific antibodies specific for two or more 24P4C12 epitopes are generated using methods generally known in the art Homodimeric anibodles can also be generated by cross-linking lechniques known in the art (e.g., Wolff et al., Cancer Res. 53:2560-2565). V.) 24P4C12 Cellular Immune Responses 41 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-resticted T cells (Buus, S. et al., Cell 47:1071, 1986; Babbitt, B. P. et al., Nature 317:359, 1985; Townsend, A. and Bodmer, H., Annu. Rev. Immunol. 7:601, 1989; Germain, R. N., Annu. Rev. Immunot. 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 al., J. Immunol. 160:3363, 1998; Rammensee, et a., Immunogenetics 41:178, 1995; Rammensee et a., SYFPEITHI, access via World Wide Web at URL (134.2.96.221/saipts.haserver.dliThome.htm); Sette, A and Sidney, J. Cur. Opin. Immunol. 10:478, 1998; Engelhard, V. H., Cun. Opin. Immunol. 6:13,1994; Sette, A. and Grey, H. M., Cuf. Opin. Immunol. 4:79, 1992; Sinigaglia, F. and Hammer, J. Cur. Biol. 6:52, 1994; Ruppert et aL, Col 74:929-937, 1993; Kondo et a., J. Immuno. 155:4307-4312,1995; Sidney et al., J. ImmunoL 157:3480-3490, 1996; Sidney et aL, Human Invnunol. 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 borne 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 at al., Immunity 8:305, 1998; Stem ef al., Structure 2:245, 1994; Jones, E.Y. Curr. Opin. Immunol. 9:75,1997; Brown, J. H. et al., Nature 364:33, 1993; Guo, H. C. et al., Proc. Natl. Aced. Sci. USA 90:8053, 1993; Guo, H. C. et al., Nature 360:364,1992; Silver, M. Let aL, Nature 360:367, 1992; Matsurnura, M. at al., Science 257:927, 1992; Madden at al., Cell70'1035, 1992; Fremont, D. H. et al., Science 257:919, 1992; Saper, M. A. , Bjorkman, P. J. and Wiley, D. C., J. Mot. Biol. 219:277, 1991.) Accordingly, the definition of class I and class I anele-specific HLA binding motifs, or class I or class 11 supermotifs allows identification of regions within a protein that are correlated with binding to particular HLA anfigen(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 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 imrnunogenicity. Various strategies can be utilized to evaluate cellular immunogenicity, including: 1) Evaluation of primary T ceU cultures from normal Individuals (see, e.g., Wentworth, P. A. qtal., Mot. linmundo. 32:603, 1995; Cells, E. et a., Prc. Natg. Acad. Sd. USA 91:2105,1994; Tsai, V. at al., J. Immunol. 158:1796,1997; Kawashima, I. et at., 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 vIro over a period of several weeks. T cells specific for the peptide become activated during this lime and are detected using, e.g., a lymphoidne- or 51 Cr-release assay involving peptide sensitized target cells. 2) Immunization of HLA transgenic mice (see, e.g.. Wentworth, P. A. of a., J. Immunol. 26:97, 1996; Wentworth, P. A at at., tnt. 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 vio in the presence of test peptide for approximately one week. 42 Peptide-specific T cells are detected using, e.g., a 51 Cr-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 andlor from chronically ill patients (see, e.g., Rehermann, B. et al., J. Ep. Med. 181:1047, 1995; Doolan, D. L. et al., immuniy 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 "naturaly", 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 "nalve" T cells. At the end of the culture period, T cell activity is detected using assays including 51Cr release Involving peptide-sensitized targets, T cell proliferation, or lymphokine release. VI.) 24P4C12 Transgenic Animals Nucleic acids that encode a 24P4C12-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 24P4C1 2 can be used to done genomic DNA that encodes 24P4C1 2. The doned genomic sequences can hen be used to generate transgenic animals containing cells that express DNA that encode 24P4C12. Methods for generating transgenic animals, particularly animals such as mice or rats, have become conventional in thb 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 24P4C1 2 transgene incorporation with tissue-spedfic enhancers. Transgenic animals that include a copy of a transgene encoding 24P4C12 can be used to examine the effect of increased expression of DNA that encodes 24P4C1 2. 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 24P4C12 can be used to construct a 24P4C12 'knock out" animal that has a defective or altered gene encoding 24P4C12 as a result of homologous recombination between the endogenous gene encoding 24P4C12 and altered genomic DNA encoding 24P4C12 Introduced Into an embryonic cell of the animal. For example,.cDNA that encodes 24P4C12 can be used to done genomic DNA encoding 24P4C12 in accordance with established techniques. A portion of the genomic DNA encoding 24P4C12 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., U et al., C 69.15 (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 &nbyonic Stem Cells: A Pradical Approach, E. J. Robertson, ed. (IRL, Oxford, 1987), pp. 113-152). A diimeric 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 gen 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, 43 for example, for their ability to defend against certain pathological conditions or for their development of pathological conditions due to absence of a 24P4C12 polypeptide. Vi1.1 Methods for the Detection of 24P4C12 Another aspect of the present invention relates to methods for detecting 24P4C12 polynudeotides and 24P4C12 related proteins, as wel as methods for identifying a cel that expresses 24P4C12. The expression profile of 24P4C1 2 makes it a diagnostic marker for metastasized disease. Accordingly, the status of 24P4C12 gene products provides information useful for predicting a variety of factors including susceptibility to advanced stage disease, rate of procession, and/or tumor aggressiveness. As discussed in detail herein, the status of 24P4C12 gene products in patient samples can be analyzed by a variety protocols that are well known in the art induding Immiohilstochemical analysis, the variety of Northern blotting techniques induding in siftu hybridization, RT-PCR analysis (for example on laser capture micro-issected samples), Western blot analysis and tissue array analysis. More particularly, the invention provides assays for the detection of 24P4C1 2 polynudeotides in a biological sample, such as serum, bone, prostate, and other tissues, urine, semen, cen preparations, and the like. Detectable 24P4C12 polynudeotides include, for example, a 24P4C12 gene or fragment thereof, 24P4C12 mRNA, alternative splice variant 24P4C12 mRNAs, and recombinant DNA or RNA molecules that contain a 24P4Ct 2 polynucleotide. A number of methods for amplifying and/or detecting the presence of 24P4C12 polynudeotides are well known in the art and can be employed in the practice of this aspectof the invention. In one embodiment, a method for detecting a 24P4C12 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 24P4C12 polynucleotides as sense and antisense primers to amplify 24P4C12 cDNAs therein; and detecting the presence of the amplified 24P4C12 cDNA. Optionally, the sequence of the amplified 24P4C12 cDNA can be determined. In another embodiment, a method of detecting a 24P4C12 gene in a biological sample comprises first isolating genomic DNA from the sample; amplifying the isolated genomic DNA using 24P4C12 polynudeotides as sense and antisense primers; and detecting the presence of the amplified 24P4C12 gene. Any number of appropriate sense and antisense probe combinations can be designed from a 24P4C12 nucleotide sequence (see, e.g., Figure 2) and used for this purpose. The invention also provides assays for detecing the presence of a 24P4C12 protein in a tissue or other biological sample such as serum, semen, bone, prostate, urine, cell preparations, and the like. Methods for detecting a 24P4C12-related protein are also wel known and indude, for example, immunoprecipitation, immunohlstochemical analysis, Western blot analysis, molecular binding assays, ELISA, ELIFA and the ike. For example, a method of detecting the presence of a 24P4C12-related protein In a biological sample comprises first contacting the sample with a 24P4C12 antibody, a 24P4C12-reactive fragment thereof, or a recombinant protein containing an antigen-binding region of a 24P4C12 antibody; and then detecting the binding of 24P4C12-related protein in the sample. Methods for identifying a cell that expresses 24P4C12 are also within the scope of the Invention. In one embodiment, an assay for Identifying a cell that expresses a 24P4C12 gene comprises deterting the presence of 24P4C12 mRNA in the cap. Methods for the detection of particular mRNAs in cells are well known and indude, for example, hybiiza 'on assays using complementary DNA probes (such as In slu hybridization using labeled 24P4C12 rboprobes, Northern blot and related techniques) and various nudeic acid amplification assays (sudi as RT-PCR using complementary primers specifc for 24P4C12, and other amplification type detcion methods, such as, for example, branched DNA. SISBA, TMA and the ke). Alternatively, an assay for identifying a call that expresses a 24P4C12 gene comprises detecting the presence of 24P4C 12-related protein in the 44 cell or secreted by the cel. Various methods for the detecon of proteins are well known in the art and are employed for the detection of 24P4C12-related proteins and cells that express 24P4C12-related proteins. 24P4C12 expression analysis is also useful as a tool for identifying and evaluating agents that modulate 24P4C12 gene expression. For example, 24P4C12 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 24P4C12 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 24P4C12 expression by RT-PCR, nucleic acid hybridization or antibody binding. VIII.) Methods for Monitorinq the Status of 24P4C12-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 24P4C12 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 24P4C12 in a biological sample of interest can be compared, for example, to the status of 24P4C12 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 24P4C12 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 at at, J. Comp. Neurol. 1996 Dec 9; 376(2): 306-14 and U.S. Patent No. 5,837,501) to compare 24P4C12 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. sailed 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 24P4C12 expressing cells) as well as the level, and biological activity of expressed gene products (such as 24P4C1 2 mRNA, polynudeotidas and polypeptides). Typically, an alteration In the status of 24P4C12 comprises a change in the location of 24P4C12 and/or 24P4C12 expressing cells and/or an increase In 24P4C12 mRNA and/or protein expression. 24P4C12 status in a sample can be analyzed by a number of means well known in the art, including without limitaton, immunohistociemical analysis, in sfu hybridization, RT-PCR analysis an laser capture micro-dissected samples, Western blot analysis, and issue array analysis. Typical protocols for evaluating the status of a 24P4C12 gene and gene products are found, for example In Ausubel at at ads., 1995, Current Protocols In Molecular Biology, Units 2 (Northern Blotting), 4 (Southern Blotting), 15 (Immunoblottig) and 18 (PCR Analysis). Thus, the status of 24P4C12 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 24P4C12 gene), Northern analysis and/or PCR analysis of 24P4C12 mRNA (to examine, for example alterations in the polynucleotide sequences or expression levels of 24P4C12 mRNAs), and, Western and/or Immunohistochemical analysis (to examine, for example alterations In polypepdde sequences, alterations in polypeptide localization within a sample, alterations in expression levels of 24P4C12 proteins and/or associations of 24P4C12 proteins with polypeptide binding partners). Detectable 24P4C12 polynudeotides Indude, for example, a 24P4C12 gene or fragment thereof, 24P4C12 mRNA, alternative spice variants, 24P4C12 mRNAs, and recombinant DNA or RNA molecaes containing a 24P4C12polynudeolide. The expression profile of 24P4C12 makes it a diagnostic marker for local and/or metastasized disease, and provides Inionnton on the growth or oncogenic potential ofabiological sample. In particular. the status of 24P4C12 provides 45 information useful for predicting susceptibility to particular disease stages, progression, andlcr tumor aggressiveness. The invention provides methods and assays for determining 24P4C12 status and diagnosing cancers thatexpress 24P4C12, such as cancers of the tissues listed In Table 1. For example, because 24P4C12 mRNA Is so highly expressed in prostate and other cancers relative to normal prostate tissue, assays that evaluate the levels of 24P4C1 2 mRNA transgipts or proteins in a biological sample can be used to diagnose a disease associated with 24P4C12 dysregulation, and can provide prognostic information useful in defining appropriate therapeutic options. The expression status of 24P4C1 2 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 24P4C1 2 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 24P4C12 in a biological sample can be examined by a number of well-known procedures in the art. For example, the status of 24P4C1 2 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 24P4C12 expressing cells (e.g. those that express 24P4C12 mRNAs or proteins). This examination can provide evidence of dysregulated cellular growth, for example, when 24P4C12-expressing cells are found in a biological sample that does not normally contain such cells (such as alymph node), because such alterations in the status of 24P4C12 in a biological sample are often associated with dysregulated celular 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 al., Prostate 42(4): 315-317 (2000);Su ef 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 24P4C1 2 gene products by determining the status of 24P4C12 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 24P4C12 gene products in a corresponding normal sample. The presence of aberrant 24P4C12 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 24P4C12 mRNA or protein expression in a test cell or tissue sample relative to expression levels in the corresponding normal cell or tissue. The presence of 24P4C12 mRNA can, for example, be evaluated in tissues Including but not limited to those listed in Table 1. The presence of significant 24P4C12 expression in any of these tissues is useful to indicate the emergence, presence andlor severity of a cancer, since the corresponding normal tissues do not express 24P4C12 mRNA or express it at lower levels. In a related embodiment, 24P4C12 status Is determined at the protein level rather than at the nucleic acid level. For example, such a method comprises determining the level of 24P4C12 protein expressed by cells in a test tissue sample and comparing the level so determined to the level of 24P4C1 2 expressed in a corresponding normal sample. In one embodiment, the presence of 24P4C12 protein is evaluated, for example, using immunohistochemical methods. 24P4C12 antibodies or binding partners capable of detecting 24P4C12 protein expression are used In a variety of assay formats well known in the art for this purpose. 46 In a further embodiment one can evaluate the status of 24P4C1 2 nucleotide and amino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules. These perturbations can indude Insertions, deletions, substitutions and the Ike. Such evaluations are useful because perturbations in the nudeotide and amino acid sequences are observed in a large nwber of proteins associated with a growth dysregulated phenotype (see, e.g., Marrogi etal., 1999, J. Cutan. Pathol. 26(8):369-378). For example, a mutation in the sequence of 24P4C12 may be indicative of the presence or promotion of a tumor. Such assays therefore have diagnostic and predictive value where a mutation in 24P4C12 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 add or amino acid sequences of 24P4C12 gene products are observed by the Northam, Southern, Westem, PCR and DNA sequencing protocols discussed herein. In addition, other methods for observing perturbations in nudeotide and amino acid sequences such as single strand oonfomnation 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 24P4C12 gene in a biological sample. Aberrant demethylation and/or hypermethytation 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 at at., 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 neoplasla (PIN) (Brooks et al., Cancer Epidemiol. Blomarkers Prev., 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 at at., Int. J. Cancer 76(6): 903-908 (1998)). A variety of assays for examining methylation status of a gene are wei known in the art For example, one can utilize, in Southem hybridization approaches, methylation-sensitive restricion 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 wil convert al unmethylated cytosines to uracil) followed by amplification using primers specific for methytated versus unmethylated DNA. Protocols involving methytation interference can also be found for example in Current Protocols In Molecular Biology, Unit 12, Frederick M. Ausubel at l. eds., 1995. Gene amplification Is an additional method for assessing the status of 24P4C12. Gene amplification Is measured in a sample directly, for example, by conventional Southern blotting or Northem blotting to quantitate the transcription of mRNA (Thomas, 1980, Proc. Nat. Aced. Sci. USA, 77:5201-5205), dot blotting (DNA analysis), or in situ hybridization, using an appropriately labeled probe, based on the sequences provided herein. Alternatively, antibodies are employed that recognize specific duplexes, induding 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 canr cer s using for example, Northern, dot blot or RT-PCR analysis to detect 24P4C12 expression. The presence of RT-PCR amplifiable 24P4C12 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 detec6on of cells expressing PSA and PSM (Verkaik at 47 al., 1997, Urol. Res. 25:373-384; dhossein et al., 1995, J. Clin. Oncol. 13:1195-2000; Heston at al., 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 deteding 24P4C1 2 mRNA or 24P4C12 protein in a tissue sample, Its presence indicating susceptibility to cancer, wherein the degree of 24P4C12 mRNA expression correlates to the degree of susceptibility. In a specific embodiment, the presence of 24P4C12 in prostate or other tissue is examined, with the presence of 24P4C12 in the sample providing an Indication of prostate cancer susdepitMty (or the emergence or existence of a prostate tumor). Similarly, one can evaluate the integrity 24P4C12 nudeotide and amino add sequences in a biological sample, in order to identify perturbations in the structure of these molecules sudi as insertions, deletions, substitutions and the like. The presence of one or more perturbations in 24P4C12 gene products in the sample is an indication of cancer susceptibilty (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 24P4C12 mRNA or 24P4C12 protein expressed by tumor calls, comparing the level so determined to the level of 24P4C12 mRNA or 24P4C12 protein expressed in a corresponding normal tissue taken from the same individual or a normal tissue reference sample, wherein the degree of 24P4C1 2 mRNA or 24P4C12 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 24P4C12 is expressed in the tumor cells, with higher expression levels indicating more aggressive tumors. Another embodiment is the evaluation of the integrity of 24P4C12 nudeotide 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 Ike. 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 ime. In one embodiment, methods for observing the progression of a malignancy in an individual over time comprise determining the level of 24P4C1 2 mRNA or 24P4C12 protein expressed by calls in a sample of the tumor, comparing the level so determined to the level of 24P4C12 mRNA or 24P4C12 protein expressed in an equivalent tissue sample taken from the same individual at a different time, wherein the degree of 24P4C12 mRNA or 24P4C12 protein expression In the tumor sample over ime provides information on the progression of the cancer. In a specific embodiment, the progression of a cancer Is evaluated by determinilng 24P4C12 expression in the tumor cells over time, where increased expression over time indicates a progression of the cancer. Also, one can evaluate the integrity 24P4C12 nudeodde and anino acid sequences in a biological sample in order to identify perturbations in the structure of these molecules sudi as insertions, deleions, substtutions and the Ike, 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 24P4C12 gene and 24P4C12 gene products (or perturbations in 24P4C12 gene and 24P4C12 gene products) and a factor that is associated with malignancy, as a means for diagnosing and prognosticating the status of a Issue sample. A wide variety of factors associated with malignancy can be utlized, such as the expression of genes associated with malignancy (e.g. PSA, PSCA and PSM expression for prostate cancer et,) as well as gross cytological observations (see, e.g., Bocking efal., 1984, Anal. Quant. Cytol. 6(2):74-88; Epstein, 1995, Hum. Pathol. 26(2):223-9; Thorson et a., 1998, Mod. Pathol. 11(6):543-51; Baisdien etal., 1999, Am.J. Surg. Patho.23(8):918-24). Methods for observing acoincidence between the expression of 24P4C12 gene and 24P4C12 gene products (or perturbations In 24P4C12 gene and 24P4C12 gene products) and another factor thatis associated with malignancy are useful, for example, because the presence of a set of spedfic factors that coincide with disease provides Information crucial for diagnosing and prognosticaing the status of a tssue sample. 48 In one embodiment, methods for observing a coincidence between the expression of 24P4C12 gene and 24P4C12 gene products (or perturbations in 24P4C12 gene and 24P4C12 gene products) and another factor associated with malignancy entails detecting the overexpression of 24P4C1 2 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 24P4C12 mRNA or protein and PSA mRNA or protein overexpression (or PSCA or PSM expression). In a specific embodiment, the expression of 24P4C12 and PSA mRNA in prostate tissue is examined, where the coincidence of 24P4C12 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 24P4C12 mRNA or protein are described herein, and standard nucleic acid and protein detection and quantification technologies are wel known in the art. Standard methods for the detection and quantification of 24P4C1 2 mRNA indude in stu hybridization using labeled 24P4C12 riboprbes, Northern blot and related techniques using 24P4C12 polynudeotide probes, RT-PCR analysis using primers specific for 24P4C12, and other amplification type detection methods, such as, for example, branched DNA, SISBA, TMA and the lke. In a specific embodiment, semi quantitative RT-PCR is used to detect and quantify 24P4C12 mRNA expression. Any number of primers capable of amplifying 24P4C12 can be used for this purpose, including but not limited to the various primer sets specifically described herein. In a specific embodiment, polydonal or monoclonal antibodies specifically reactive with the wild-type 24P4C12 protein can be used in an immunohistodemical assay of blopsied tissue. IX.) Identification of Molecules That Interact With 24P4C12 The 24P4C12 protein and nucleic acid sequences disclosed herein allow a skilled artisan to identify proteins, small molecules and other agents that interact with 24P4C12, as well as pathways activated by 24P4C12 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, 5,846,722 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 a, Nature 402- 4 November 1999, 83-86). Alternatively one can screen peptide libraries to identify molecules that Interact with 24P4C12 protein sequences. In such methods, peptides that bind to 24P4C12 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 24P4C1 2 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 libraries and screening methods that can be used to identify molecules that interact with 24P4C12 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. Alte'matively, ce lines that express 24P4C12 are used to identify proteln-protein Interactions mediated by 24P4C12. Such Interactions can be examined using Immunoprecipitation techniques (see, e.g., Hamilton 8.J., et al. Biochem. Biophys. Res. Commun. 1999, 261:646-51). 24P4C12 protein can be Immunoprecipitated from 24P4C12 expressing call Ines using anti-24P4C12 antibodies. Alternatively, antibodies against His-tag can be used In a cell line engineered to express fusions of 24P4C12 and a His-tag (vectors mentioned above). The Immunoprecipitated complex can be examined for protein association by procedures such as Westem blotting, 3S-methionine labeling of proteins, protein microsequencing, silver staining and two-dmensional get electrophoresis. 49 Small molecules and ligands that interact with 24P4C12 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 24P4C12'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 tumorienesis. Similar, small molecules that modulate 24P4C1 2-related ion channel, protein pump, or cell communication functions are identified and used to treat patients that have a cancer that expresses 24P4C12 (see, e.g., Hille, B., Ionic Channels of Excitable . Membranes 2d Ed., Sinauer Assoc., Sundeland, MA, 1992). Moreover, iigands that regulate 24P4C12 function can be identified based on their ability to bind 24P4C12 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, cels engineered to express a fusion protein of 24P4C12 and a DNA-binding protein are used to co-express a fusion protein of a hybrid ligand/small molecule and a cDNA library transcdptional 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 24P4C1 2. An embodiment of this invention comprises a method of screening for a molecule that Interacts with a 24P4C12 amino add sequence shown In Figure 2 or Figure 3, comprising the steps of contacting a population of molecules with a 24P4C12 amino acid sequence, allowing the population of molecules and the 24P4C12 amino acid sequence to interact under conditions that facilitate an Interaction, determining the presence of a molecule that interacts with the 24P4C12 amino acid sequence, and then separating molecules that do not interact with the 24P4C12 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 24P4C12 amino acid sequence. The identified molecule can be used to modulate a function performed by 24P4C12. In a preferred embodiment, the 24P4C12 amino acid sequence is contacted with a library of peptides. X.1 Therapeutic Methods and Compositions The identification of 24P4C12 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, 24P4C12 functions as a transcdption factor involved in activating tumor-promoting genes or repressing genes that block tumorigenesis. Accordingly, therapeutic approaches that inhibit the activity of a 24P4C12 protein are useful for patients suffering from a cancer that expresses 24P4C12. These therapeutic approaches generally fall into two classes. One class comprises various methods for Inhibiting the binding or association of a 24P4C12 protein with its binding partner or with other proteins. Another class comprises a variety of methods for inhibiting the transcription of a 24P4C12 gene or translation of 24P4C12 mRNA. X.A.) Anti-Cancer Vaccines The invention provides cancer vaccines comprising a 24P4C12-related protein or 24P4C12-related nudeic acid. In view of the expression of 24P4C12, cancer vaxines prevent and/or treat 24P4C12-expressing cancers with minimal or no effects on non-target tissues. The use of a tumor antigen in a vaccine that generates humorei 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 at aL, 1995, int J. Cancer 63:231-237; Fong at at., 1997, J. Immunol. 159-3113-3117). 50 Such methods can be readily practiced by employing a 24P4C12-related protein, or a 24P4C12-encoding nucleic acid molecule and recombinant vectors capable of expressing and presenting the 24P4C12 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., HeryIn et al., Ann Med 1999 Feb 31(1):66-78; Maruyama el 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 manmars immune system to an trnmunoreactive epitope (e.g. an epitope present In a 24P4C12 protein shown in Figure 3 or analog or homolog there) 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 24P4C12 Inmmunogen contains a biological motif, see e.g., Tables VIII-XXI and XXII-XLIX, or a peptide of a size range from 24P4C12 indicated in Figure 5, Figure 6, Figure 7, Figure 8, and Figure 9. The entire 24P4C1 2 protein, Immunogenic regons or epitopes thereof can be combined and delivered by various means. Such vaccine compositions can include, for example, lipopeptides (e.g.,Vitiello, A. et a., J. Clin. Invest. 95:341, 1995), peptide compositions encapsulated In poly(DL-lactlde-co-glycollde) ("PLG") microspheres (see, e.g., Eldrdge, et a., 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 at al., Ctin Exp Immunol. 113:235-243,1998), multiple antigen peptide systems (MAPs) (see e.g., Tam, J. P., Proc. Nall. Acad. Sd. 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., ad., p. 379,1996; Chakrabarti, S. et a., Nature 320:535. 1986: Hu, S. L et al., Nature 320:537, 1986; Kieny, M.-P. et a., AIDS BioaTechnology 4:790, 1986; Top, F. H. et al., J. Infect. Dis. 124:148,1971; Chanda, P. K. et a., Viology 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., Sam. Hematol. 30:16, 1993; Falo, L. D., Jr. at a., 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. ef al., Vaccine 11:293, 1993), lposomes (Reddy, R. et a., J. Immunol 148:1585,1992; Rock, K. L., Immunol. Today 17:131, 1996), or, naked or particle absorbed cDNA (Ulmer, J. B. et a., 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. ot 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 24P4C12-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. Induding use in combination with Immune adjuvants such as IL-2, IL-1 2, GM-CSF, and the like. Cellular Vaccines: CTL epitopes can be determined using specific algorithms to identify peptides within 24P4C12 protein that bind corresponding HLA alleles (see e.g., Table IV; Epher 7 " end Epimahlm, Brown University (URL brown.edulResearch/TB HIV_lablepimatrixtepimatrilhtml); and, BIMAS, (URL bImas.datnih.gov; SYFPEITHI at URL syfpeithi.bmi-heidelberg.coml). In a preferred embodiment, a 24P4C1 2 immunogen contains one or more amino acid sequences identified using tediques well known In the art, such as the sequences shown In Tables VIll-XXI and XUI-XLIX or a peptide of 8, 9, 10 or 11 amino adds 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 |1 motiflsupermotif (e.g., Table IV (B) or Table IV (C)). As is appreciated In the art the HIA Class I binding groove is essentially cosed 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 HILA Class 11 51 binding groove is essentially operi ended; therefore a peptide of about 9 or more amino acids can be bound by an HLA Class 11 molecule. Due to the binding groove differences between HLA Class I and I, 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 |1 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 24P4C12 protein) so that an immune response is generated. A typical embodiment consists of a method for generating an immune response to 24P4C1 2 in a host by contacting the host with a sufficient amount of at least one 24P4C12 8 cell or cytotoxic T-cell epitope or analog thereof; and at least one periodic Interval thereafter re-contacting the host with the 24P4C12 B cell or cytotoxic T-cel epitope or analog thereof. A specific embodiment consists of a method of generating an immune response against a 24P4C12 related protein or a man-made multiepitopic peptide comprising: administering 24P4C1 2 immunogen (e.g. a 24P4C1 2 protein or a peptide fragment thereof, a 24P4C12 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 PADRE"' peptide (Epimmune Inc., San Diego, CA; see, e.g., Alexander et a1., J. Immunol. 2000 164(3); 164(3): 1625-1633; Alexander at af., Immunity 1994 1(9): 751-761 and Alexander f al., Immunol. Res. 1998 18(2): 79-92). An alternative method comprises generating an Immune response in an individual against a 24P4C12 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 24P4C12 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 Epids; saponins; ectins; estrogenic compounds; hydroxylated lower alkyls; dimethyl sulfoxide; and urea Is also administered. In addition, an antildiotypic antibody can be administered that mimics 24P4C 12, in order to generate a response to the target antigen. Nucleic Aid Vaclnes: Vaccine compositions of the invention include nucleic acid-medated 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 24P4C12. Constructs comprising DNA encoding a 24P4C1 2-related proteinlimmunogen and appropriate regulatory sequences can be injected directly into muscle or skin of an individual, such that the cells of the musce or skin take-up the construct and express the encoded 24P4C12 proteinimmunogen. Altematively, a vaccine comprises a 24P4C12-related protein. Expression of the 24P4C1 2-related protein Immunogen results In the generation of prophylactic or therapeutic humoral and cellular immunity against cells that bear a 24P4C12 protein. Various prophylacuic and therapeutic genetic Immunization techniques known In the art can be used (for review, see Information and references published at Intemet address genweb.com). Nucleic acid-based delivery is described, for instance, in Wolff of. 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 (bupivicalne, 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). 52 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, vacdfnia, fOWIpox, canarypox, adenovirus, influenza, pollovirus, adeno-assodated virus, lenlivirus, and sindbis virus (see, e.g., Restifo, 1996, Curr. Opin. Immunol. 8:658-663; Tsang at a. J. Nal. Cancer Inst 87:982-990 (1995)). Non-viral delivery systems can also be employed by Introdudng naked DNA encoding a 24P4C12-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. Vacdnla vectors and methods useful in Immunization protocols are described in, e.g., U.S. Patent No. 4,722,848. Another vector is BCG (Bacifle Calmette Guerin). BCG vectors are described in Stover at 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 yphi vectors, 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 24P4C1 2-related nudeic acid molecule. In one embodiment, the full length human 24P4C12 cDNA is employed. In another embodiment, 24P4C12 nucleic acid molecules encoding specific cytotoxic T lymphocyte (CTL) and/or antibody epitopes are employed. Ex Vivo Vaodnes Various ex vvo strategies can also be employed to generate an immune response. One approachlnvolves the use of antigen presenting cells (APCs) such as dendritic cals (DC) to present 24P4C12 antigen to a patient's immune system. Dendritic cells express MHC class I and il molecules, B7 oD-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 dinical trial to stimulate prostate cancer parents' Immune systems (Tjoa at at., 1996, Prostate 28:65 69; Murphy at al., 1996, Prostate 29:371-380). Thus, dendritic cells can be used to present 24P4C12 peptides to T cells in the context of MHC class I cr 11 molecules. In one embodiment, autologous dendritic cells are pulsed with 24P4C12 peptides capable of binding to MHC class I and/or class Il molecules. In another embodiment, dendritic cells are pulsed with the complete 24P4C12 protein. Yet another embodiment involves engineering the overexpression of a 24P4C12 gene in dendritic ceNs 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-assocated virus, DNA transfecion (Rbas 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 24P4C12 can also be engineered to express immune modulators, such as GM CSF, and used as immunizing agents. X.B.) 24P4C12 as a Target for Antibody-based Therapy 24P4C12 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 24P4C12 Is expressed by cancer cells of various lineages relative to corresponding normal ceas, systemic administration of 24P4C12-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 24P4C1 2 are useful to treat 24P4C12-expressing cancers systemically, either as conjugates with a toxin or therapeutic agent, or as naked antibodies capable of inhibiting cell proliferation or function. 53 24P4C12 antibodies can be introduced into a patient such that the antibody binds to 24P4C12 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 celular cytotoxicity, modulation of the physiological function of 24P4C12, inhibition of ligand binding or signal transduction pathways, modulation of tumor cell differentiation, alteration of tumor angiogenesis factor profies, 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 24P4C1 2 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 ot 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. 24P4C12), 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-cytotoxlc 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 24P4C12 antibody) that binds to a marker (e.g. 24P4C12) expressed, accessible to binding or localized on the cell surfaces. A typical embodiment is a method of delivering a cytotoxic andlor therapeutic agent to a cell expressing 24P4C12, comprising conjugating the cytotoxic agent to an antibody that immunospecifically binds to a 24P4C12 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 parenteraty 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-24P4C12 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 (Aren et a., 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 a., 1992, Cancer Res. 52:2771-2776), B-cell lymphoma (Funakoshi et al., 1996, J. Immunother. Emphasis Tumor Immuno. 19:93-101), leukemia (Zhong ef aL., 1996, Leuk. Res. 20:581-589), colorectal cancer (Moun et aL, 1994, Cancer Res. 54:6160-6166; Velders af aL, 1995, Cancer Res. 55:4398-4403), and breast cancer (Shepard et al., 1991, J. Cin. Immunol. 11:117-127). Some therapeutic approaches involve conjugation of naked antibody to a toxin or radioisotope, such as the conjugation of YOt or 1 1 3 'to anti-CD20 antibodies (e.g., Zevalin'", IDEC Pharmaceuticals Corp. or Bexxar-r", Coulter Pharmaceuticals), while others involve co-administration of antibodies and other therapeutic agents, such as Herceptinmi (trastuzumab) with paditaxel (Genentech. Inc.). The antibodies can be conjugated to a therapeutic agent To treat prostate cancer, for example, 24P4C1 2 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 I, Wyeth-Ayerst, Madison, NJ, a recombinant humanized IgG4 kappa antibody conjugated to antitumor antibiotic 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 24P4C12 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 54 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 a. (Cancer Res. 51:4575-4580, 1991) describe the use of various antibodies together with chemotherapeutic agents. Although 24P4C12 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 chernotherapeutlc 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 chemotherapeuic agent very well. Cancer patients can be evaluated for the presence and level of 24P4C1 2 expression, preferably using Immunohlstochemical assessments of tumor tissue, quantitative 24P4C12 imaging, or other techniques that reliably indicate the presence and degree of 24P4C12 expression. lmmunohistochemical analysis of tumor biopsies or surgical specimens is preferred for this purpose. Methods for imunohistochemical analysis of tumor tissues are well known in the art. Anti-24P4C12 monoclonal antibodies that treat prostate and other cancers indude those that Initiate a potent Immune response against the tumor or those that are directly cytotoxic. In this regard, anti-24P4C12 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-24P4C12 mAbs that exert a direct biological effect on tumor growth are useful to treat cancers that express 24P4C12. 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-24P4C1 2 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 humantmouse 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 24P4C1 2 antigen with high affinity but exhibit low or no antigeniity in the patient. Therapeutic methods of the invention contemplate the administration of single anti-24P4C12 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 24P4C12 mAbs can be admipistered concomitantly with other therapeutic modalities, including but not limited to various chemotherapeutic agents, androgen-blockers, immune modulators (e.g., L-2, GM-CSF), surgery or radiation. The anti 24P4C12 mAbs are administered in their "naked' or unconjugated form, or can have a therapeutic agent(s) conjugated to them. Anti-24P4C12 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, Intradennal, and the like. Treatment generally involves repeated administration of the anti-24P4C12 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, 55 .3,.4,.5,.6,.7,.8,.9., 1, 2,3,4, 5,6, 7, 8, 9,10,15,20, or 25mg/kg body weight. In general, doses in the range of 10-1000 mgn mAb per week are effective and well tolerated. Based on clinical experience with the HerceptinM mAb in the treatment of metastatic breast cancer, an Initial loadng dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mgfkg IV of the anti 24P4C12 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 Indude, for example, the binding affinity and half life of the Ab or mAbs used, the degree of 24P4C12 expression in the patient, the extent of circulating shed 24P4C12 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. Cptionally, patients should be evaluated for the levels of 24P4C12 in a given sample (e.g. the levels of circulating 24P4C12 antigen and/or 24P4C12 expressing ells) 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). Antidiotypic anti-24P4C12 antibodies can also be used in anti-cancer therapy as a vaccine for Inducing an immune response to cells expressing a 24P4C1 2-related protein. In particular, the generation of ani-idiotypic antibodies Is well known In the art; this methodology can readily be adapted to generate and-idiotypic ant-24P4C12 antibodies that mimic an epitope on a 24P4C124elated protein (see, for example, Wagner et aL., 1997, Hybridoma 16: 33-40; Foon et Al., 1995, J. Clin. Invest 96:334-342; Hedyn et a., 1996, Cancer Immunol. Immunother. 43-65-76). Such an anti-idiotypic antibody can be used in cancer vaccine strategies. XC.) 24P4C1 2 as a Target for Cellular Immune Responses Vacaines 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 andgenic determinants of the pathogenic organism or tumor-related peptide targeted for an Immune response. The composition can be a naturaly 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, albunins such as human serum albumin, tetanus toxoid. polyamino adds such as poly L-Iysine, poly L.-glutamic acid, influenza, hepatitis B virus core protein, and the like. The vaccines can contain a physiologically tolerable (i.e., acceptable) 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-glyoerylcysteinlysery- serine'(PsCSS). Moreover, an adjuvant such as a synthetic cytosine-phosphorothiolated-guaninecontaining (CpG) oligonudeotides has been found to Increase CTL responses 10- to 100-fold. (see, e.g. Davila and Celis, J. Immunol. 165:539-547 (2000)) 56 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 cels that express or overexpress 24P4C12 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 11 epitopes in accordance with the invention. An alternative embodiment of such a composition comprises a dass I and/or class il epitope in accordance with the invention, along with a cross reactive HTL epitope such as PADRETm (Epimmune, San Diego, CA) molecule (desaibed 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 dendriic 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 vlvo. 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. lie 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 11 a similar rationale is employed; again 3-4 epitopes are selected from at least one TAA (see, e.g., Rosenberg ot al., Science 2781447-1450). 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 inmunogenicity for HLA Class I an ICso of 500 nM or less, often 200 nM or less; and for Class I an ICso of 1000 nM or less. 3.) Sufficient supermotif bearng-peptides, or a sufficient array of allele-spedfic 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. 5.) Of particular relevance are epitopes referred to as nested epitopes." Nested epitopes ocar 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 Il 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, 57 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. Spaer 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 concem is a junctional epitope that is a "dominant epitape." 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 I binding peptide be conserved In a designated percentage of the sequences evaluated for a specific protein antigen. XC.1. MInigene Vaccines A number of different approaches are available which aflow simultaneous delivery of multiple epitopes. Nucleic adds encoding the peptides of the Invention are a particularly useful embodiment of the invention. Epitopes for Inclusion in a mhigene 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 ef aL, J. Immunol. 162:3915-3925,1999; An, L. and Whitton. J. L, J. Vrol. 71:2292, 1997; Thomson, S. A. et al., J. Immunol. 157:822, 1996; Whitton, J. L of al., J. Viro. 67:348,1993; Hanke, R. at al., Vaccine 16:426,1998. For example, a multi-epitope DNA plasmid encoding supermotif and/or motif-bearing epitopes derived 24P4C1 2, the PADRE® universal helper T cell epitope or multiple HTL epitopes from 24P4C12 (see e.g., Tables VIII-XXI and XXI 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 vitm 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 cels 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 elements can be Incorporated Into the minigene design. Examples of amino acid sequences that can be reverse translated and Induded In the minigene sequence include: HLA class I epitopes, HLA class I epitopes, antibody epitopes, a ubiquitination signal sequence, and/or an endoplasmic reticulum targeting signal. In addition, HLA presentation of CTL and HTIL 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. 58 The minigene sequence may be converted to DNA by assembling oligonucleotides that encode the plus and minus strands of the minigene. Overapping oligonudeotides (30-100 bases long) may be synthesized, phosphorylated, purified and annealed under appropriate conditions using well known techniques. The ends of the oligonudeotides 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 doning site for minigene insertion; a polyadenylation signal for efficient transcription termination; an E. col origin of replication; and an E. coli 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 infusion 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. col strain, and DNA is prepared using standard techniques. The orientation and DNA sequence of the minigene, as wel 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- 2, GM CSF), cytokine-inducing molecules (e.g., LeIF), costimulatory molecules, or for HTL responses, pan-DR binding proteins

(PADRE

T

", Epimmune, San Diego, CA). Helper (HTL) epitopes can be joined to intraocular 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 11 pathway, thereby Improving HTIL induction. In contest to HTL or CTL induction, specifically decreasing the Immune response by co-expression of immunosuppressive molecules (e.g. TGF-p) may be beneficial in certain diseases. Therapeutic quantities of plasmid DNA can be produced for example, by fermentation in E. co, followed by purification. Aliquots from the working cel 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 bloseparation technologies such as solid phase anion-exchange resins supplied by QIAGEN, Inc. (Valencia, California). If required, supercolled DNA can be isolated from the open circular and linear forms using gel electrophoresis or other methods. 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 dinical 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 ipids, glycolipids, and fusogenic liposomes can 59 also be used in the formulation (see, e.g., as described by WO 93/24640; Mannino & Gould-Fogerite, Bio Techniques 6(7): 682 (1988); U.S. Pat No. 5,279,833; WO 91/06309; and Feigner, et al., Proc. Nat' 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 disperson, 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 wil 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 (51Cr) labeled and used as target cells for epitope-specific CTL lines; cytolysis, detected by s"Cr release, Indicates both production of, and HLA presentation of, minigeneencoded 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, Intrapedtoneal (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 t 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 CTILs. 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 acvity 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 typical selected from, e.g., Ala, Gly, or other neutral spacers of nonpolar amino adds 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 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. 60 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 If molecules. Examples of such amino acid bind many HLA Class Il molecules include sequences from antigens such as tetanus toxoid at positions 830-843 (QYIKANSKFIGITE; SEQ ID NO: 29), Plasmodium falciparum circumsporozoite (CS) protein at positions 378-398 (DIEKKIAKMEKASSVFNWNS; SEQ ID NO: 30), and Streptococcus 18kD protein at positions 116-131 (GAVDSILGGVATYGAA; SEQ ID NO: 31). 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., PADRE70, Epimmune, Inc., San Diego, CA) are designed, most preferably, to bind most HLA-DR (human HLA dass 11) molecules. For instance, a pan-DR-binding epitope peptide having the formula: AKXVAAWTLKAAA (SEQ ID NO: 32), where T is either cydohexytalanine, 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 halg ife, 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 palmritic 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. Upids have been identified as agents capable of priming CTL in vivo. For example, palmitic acid residues can be attached to the E-and x- 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 lipdated peptide can then be administered either directly in a micelle or particle, incorporated Into a liposome, or emulsified in an aduvant, e.g., incomplete Freund's adjuvant In a preferred embodiment, a particularly effective Immunogenic composition comprises patmitic 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. coli lipoproteins, such as tripalmitoyl-S glycerycysteinlyseryl- 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 t'PaCSS, for example, and the lipopeptide administered to an individual to prime speciiicaUy an immune response to the target antigen. Moreover, because the Induction of neutralizing antibodies can also be primed with PsCSS-conjugated epitopes, two such compositions can be combined to more effectively elicit both humoral and cell-mediated responses. XC.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 patients blood. A pharmaceutical to facilitate harvesting of DC can be used, such as Progenipoietina (Pharnacia-Monsanto, St. Louis, MO) or GM-CSFIIL-4. After putsing the DC with peptides and prior to reinfusion into patients, the DC are washed to remove unbound peptides. In this embodimenta vaccine comprises peptide-pulsed DCs which present the pulsed peptide epitopes complexed with HILA molecules on their surfaces. 61 The DC can be pulsed ex vivo with a cocktail of peptides, some of which stimulate CTL responses to 24P4C12. Optionally, a helper T cel (HTL) peptide, such as a natural or artificial loosely restricted HLA Class Il 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 24P4C12. X.D. Adoptive Immunotherapy Antigenic 24P4C12-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 nudeic acid in accordance with the invention. Ex vivo CTL or HTL responses to a particular antigen are induced by incubating in tissue culture the patients, or genetically compatible, CTL or HTL precursor cels 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 (CT) or facilitate destruction (HTL) of their specific target cell (e.g., a tumor cel). Transfected dendritic cels may also be used as antigen presenting cells. X.E. AdministratIon of Vaccines for Therapeutlc or Prophylactic Pumoses Pharmaceutical and vaccine compositions of the Invention are typically used to treat and/or prevent a cancer that expresses or overexpresses 24P4C1 2. 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 win 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 24P4C12. 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 24P4C12-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., induding, but not limited to embodiments such as peptide cocktails, polyepitopic polypeptides, minigenes, or TAA-specific CTLs or pulsed dendriic cells) delivered to the patient may vary according to the stage of the disease or the patien's health status. For example, in a patient with a tumor that expresses 24P4C12, a vaccine comprising 24P4C12-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. 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 62 upon the patients 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 neoplasla, 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, ife-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 irnmunogencity of the vaccine can be assessed by measuring the specific activity of CTL and HTi. obtained from a sample of the patient's 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 canter, preferably an aqueous carrier. A variety of aqueous carriers may be used, e.g., water, buffered water, 0.8% saline, 0.3% glydne, hyaturonic 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 Iyophilized, the lyophilized preparation being combined with a sterile solution prior to administration. The compositions may contain pharmaceutically acceptable auxiflary 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 deate, 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 wekgt, and will be selected primarily by fuid 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 votumelquantity 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, 170 Edition, A Gennaro, Editor, Mack Publishing Co., Easton, Pennsylvania, 1985). For example a peptide dose for initial Immunization can be from about I 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 nuceic add administered IM (or SC or ID) in the amounts of 0.5-5 mg at multiple sites. The nucleic acid (0.1 to 1000 pg) 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 5x10 9 pfu. 63 For antibodies, a treatment generally involves repeated administration of the anti-24P4C1 2 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 wel tolerated. Moreover, an initial loading dose of approximately 4 mg/kg patient body weight IV, followed by weekly doses of about 2 mglkg IV of the anti- 24P4C1 2 mAb preparation represents an acceptable dosing regimen. As appreciated by those of skiD 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 Immunogenldty of a substance, the degree of 24P4C12 expression in the patient, the extent of circulating shed 24P4C12 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 hvention, as well as the health status of a particular patient. Non-limiting preferred human unit doses are, for example, 500pg - 1mg, 1mg - 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 polynudeotides 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 polynudeotide 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 polynuceotide of about 20 bases, a dosage range may be selected from, for example, an Independenly 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. Generay, parenteral routes of administration may require higher doses of polynudeotide 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 10 to about 5 x 1010 cells. A dose may also about 100 cells/m 2 to about 1010 cells/m 2 , or about 10s cells/m 2 to about 108 cellsh. 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 lymphold tissue; 2) to target selectively to diseases cells; or, 3) to Increase the half-life of the peptide composition. Uposomes include emulsions, foams, micelles, insoluble monolayers, liquid crystals, phospholipid dispersions, lamellar layers and the like. In these preparations, the 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 cels, 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 64 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 veside-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 ability and stability of the lposomes In the blood stream. A variety of methods are available for preparing liposomes, as described in, e.g., Szoka, el aL, Ann. Rev. Biophys. Boeng. 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 igand 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, infer 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 aliphatc 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. XI.) Diagnostic and Prognostlc Embodiments of 24P4C12. As disclosed herein, 24P4C12 polynudeotides, 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 Ested in Table I (see, e.g., both its specific patten of tissue expression as well as its overexpression in certain cancers as described for example in the Example entitled 'Expression analysis of 24P4C12 In normal tissues, and patient specimens'). 24P4C1 2 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 ef at., J. Urol. 163(2): 503-5120 (2000); Polascik of al., J. Urol. Aug; 162(2)293-306 (1999) and Fortier et al, J. Net 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 at at., Int J Mol Med 1999 Jul 4(1):99-102 and Minimoto etal., Cancer Detect Prev 2000;24(1):1-12). Therefore, this disclosure of 24P4C12 polynucleotides and polypeptides (as well as 24P4C12 polynucleotide probes and anti-24P4C12 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 essays directed to examining conditions associated with cancer. Typical embodiments of dagnostic methods which utilize the 24P4C12 polynudeotides, 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 polynudeotides are used as probes 65 (for example in Northern analysis; see, e.g., Sharief ef al., Biochem. Mol. Biol. Int. 33(3):567-74(1994)) and primers (for example in PCR analysis, see, e.g., Okegawa et a., J. Urol. 163(4): 1189-1190 (2000)) to observe the presence and/or the level of PSA mRNAs in methods of monitoring PSA overexpresslon or the metastasis of prostate cancers, the 24P4C12 polynucleotides described herein can be utilized in the same way to detect 24P4C12 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 and/or 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 24P4C1 2 polypeptides described herein can be utlized to generate antibodies for use in detecting 24P4C12 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 lymph node), assays which examine a biological sample for the presence of cells expressing 24P4C12 polynudeotides and/or polypeptides can be used to provide evidence of metastasis. For example, when a biological sample from tissue that does not normally contain 24P4C12-expressing cells (lymph node) is found to contain 24P4C12-expressing cells such as the 24P4C12 expression seen in LAPC4 and LAPC9, xenografts isolated from lymph node and bone metastasis, respectively, this finding Is indicative of metastasis. Alternatively 24P4C12 polynudeotides and/or polypepides can be used to provide evidence of cancer, for example, when cells in a biological sample that do not normally express 24P4C12 or express 24P4C12 at a different level are found to express 24P4C12 or have an increased expression of 24P4C12 (see, e.g., the 24P4C12 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 Ussue restricted marker (in addition to 24P4C12) such as PSA, PSCA etc. (see, e.g., Alanen et al., Pathol. Res. Pract. 192(3): 233 237 (1996)). Just as PSA polynuleotide fragments and polynudeotide variants are employed by skilled artisans for use in methods of monitoring PSA, 24P4C12 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 prmers 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 of a., Methods Mol. Bol. 98:121-154 (1998)). An additional illustration of the use of such fragments is provided In the Example entitled 'Expression analysis of 24P4C1 2 In normal tissues, and patient specimens," where a 24P4C12 polynudeotide fragment is used as a probe to show the expression of 24P4C12 RNAs in cancer cells. In addition, variant polynudeotide sequences are typical used as primers and probes for the corresponding mRNAs in PCR and Northern analyses (see, e.g., Sawai et a., Fetal Diagn. Ther. 1996 Nov-Dec 1-1(6):407-13 and Current Protocols In Molecular Biology, Volume 2, Unit 2, Frederick M. Ausubel et al. eds., 1995)). Polynudeotide fragments and variants are useful in this context where they are capable of binding to a target polynudeotide sequence (e.g., a 24P4C1 2 polynucleotide shown In Figure 2 or variant thereof) under conditions of high stringency. Furthermore, PSA polypeptides which contain an epitope that can be recognized by an antibody or T cell that specifically binds to that epitope a used in methods of monitoring PSA. 24P4C12 polypeplide fragments and potypeptide 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 -66 such as fusion proteins being used by practitioners (see, e.g., Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubel ef 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 24P4C12 biological molifs discussed herein or a motif-bearing subsequence which is readily identified by one of skill In the art based on motif 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 24P4C1 2 polypeptide shown in Figure 3). As shown herein, the 24P4C12 polynudeotides and polypeptides (as well as the 24P4C12 polynudeotide probes and anti-24P4C12 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 1. Diagnostic assays that measure the presence of 24P4C12 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 24P4C12 polynucleotides and polypeptides (as well as the 24P4C12 polynucleotide probes and anti 24P4C1 2 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 24P4C12 polynucleotides disposed 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 24P4C12 gene maps (see the Example entitled "Chromosomal Mapping of 24P4C12" below). Moreover, In addition to their use in diagnostic assays, the 24P4Ci2-related proteins and polynucleolides disposed 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, 24P4C12-related proteins or polynudeofides of the invention can be used to treat a pathologic condition characterized by the over-expression of 24P4C12. For example, the amino acid or nudeic acid sequence of Figure 2 or Figure 3, or fragments of either, can be used to generate an immune response to a 24P4C1 2 antigen. Antibodies or other molecules that react with 24P4C12 can be used to modulate the function of this molecule, and thereby provide a therapeutic benefit. XI.I Inhibition of 24P4C12 Protein Function The invention includes various methods and compositions for inhibiting the binding of 24P4C1 2 to Its binding partner or Its association with other protein(s) as well as methods for inhibiting 24P4C12 function. XIIA.) Inhibition of 24P4C12 With Intracellular Antibodies In one approach, a recombinant vector that encodes single chain antibodies that specifically bind to 24P4C12 are introduced Into 24P4C12 expressing cells via gene transfer technologies. Accordingly, the encoded single chain anti 24P4C12 antibody is expressed Intracellularly, binds to 24P4C12 protein, and thereby Inhibits its function. Methods for engineering such intracquular single chain antibodies are well known. Such Intracellular antibodies, also known as "intrabodies", are spedfically targeted to a particular compartment within the cell, providing control over where the inhibitory 67 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 a., 1995, Proc. Nati. Acad. Sd. USA 92: 3137-3141; Beerl l al.. 1994, J. Biol. Chem. 289: 23931-23936; Deshane at 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 poypeptide, 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 polynudeotide 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 reticulum (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 indude a nuclear localization signal. Upid 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 24P4C1 2 in the nucleus, thereby preventing its activity within the nucleus. Nuclear targeting signals are engineered into such 24P4C12 intrabodies in order to achieve the desired targeting. Such 24P4C12 intrabodies are designed to bind specifically to a particular 24P4C12 domain. In another embodiment, cytosolic intrabodles that specifically bind to a 24P4C12 protein are used to prevent 24P4C12 from gaining access to the nucleus, thereby preventing it from exerting any biological activity within the nucleus (e.g., preventing 24P4C12 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). XIl.B.1 Inhibition of 24P4C12 with Recombinant Proteins In another approach,'recombinant molecules bind to 24P4C12 and thereby inhibit 24P4C12 function. For example, these recombinant molecules prevent or inhibit 24P4C1 2 fmm 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 24P4C12 specific antibody molecule. In a particular embodiment, the 24P4C12 binding domain of a 24P4C12 binding partner is engineered into a dimeric fusion protein, whereby the fusion protein comprises two 24P4C12 igand binding domains Inked to the Fc portion of a human IgG, such as human IgG1. Such IgG portion can contain, for example, the CH2 and CH3 domains and the hinge region, but not the C1 domain. Such dmeric fusion proteins are administered in soluble form to patients sullering from a cancer associated with the expression of 24P4C12, whereby the dimeric fusion protein specifically binds to 24P4C12 and blodcs 24P4C12 Interaction with a binding partner. Such dimeric fusion proteins are further combined Into multimeric proteins using known antibody linking technologies. XII.C.) Inhibition of 24P4C12 Transcription or Translation The present invenicn also comprises various methods and compositions for inhibiting the transcription of the 24P4C12 gene. Similarly, the invention also provides methods and compositions for Inhibiting the translation of 24P4C12 mRNA Into protein. 68 In one approach, a method of inhibiting the transcription of the 24P4C12 gene comprises contacting the 24P4C12 gene with a 24P4C12 antisense polynucleotide. In another approach, a method of inhibiting 24P4C12 mRNA translation comprises contacting a 24P4C12 mRNA with an antisense polynucleotide. In another approach, a 24P4C12 specific ribozyme is used to deave a 24P4C12 message, thereby inhibiting translation. Such antisense and ribozyme based methods can also be directed to the regulatory regions of the 24P4C12 gene, such as 24P4C12 promoter and/or enhancer elements. Similady, proteins capable of inhibiting a 24P4C12 gene transcription factor are used to inhibit 24P4C12 mRNA transcription. The various polynudeotides and compositions useful in the aforementioned methods have been described above. The use of antisense and ribozyme molecules to inhibit transcription and translation Is wel known in the art Other factors that inhibit the transcription of 24P4C12 by interfering with 24P4C1 2 transcriptional activation are also useful to treat cancers expressing 24P4C12. Similarly, factors that interfere with 24P4C12 processing are useful to treat cancers that express 24P4C12. Cancer treatment methods utilizing such factors are also within the scope of the invention. Xi.D.) General Considerations for Therapeutic Strateqls Gene transfer and gene therapy technologies can be used to deliver therapeutic polynucleotide molecules to tumor cells synthesizing 24P4C12 (Le., antisense, ribozyme, polynudeoddes encoding Intrabodes and other 24P4C12 Inhibitory molecues). A number of gene therapy approaches are known In the art Recombinant vectors encoding 24P4C12 anbsense polynudeotides, ribozymes, factors capable of interfering with 24P4C12 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 diemotherapy (or other therapies) and/or less frequent administration, an advantage for all patients and particulaly for those that do not tolerate the toxicity of the chemotherapeutic agent wel. 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 vito and i vivAo assay systems. In vitro assays that evaluate therapeutic activity indude 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 24P4C12 to a binding partner, etc. In vivo, the effect of a 24P4C12.theapeutic 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 issues are introduced Into immune compromised animals, such as nude or SCID mice (ein at al., 1997, Nature Medicine 3:402-408). For example, PCT Patent Application W098/16628 and U.S. Patent 6,107,540 describe various xenograft models of human prostate cancer capable of recapitulating the development of primary tumors, micrornetastasis, 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 vim 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-bearng 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. The therapeutic compositions used in the practice of the foregoing methods can be formulated into pharmaceucal compositions comprising a carrier suitable fir the desired delvery method. Suitable carriers indude any material that when combined with the therapeutic composition retains the ant-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 69 pharmaceutical carriers such as sterile phosphate buffered saline solutions, bacteriostatic water, and the like (see, generally. Remington's Pharmaceutical Sciences 16h 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 polyvinytchloride 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 wil vary with the method and the target cancer, and will generally depend on a number of other factors appreciated In the art. X)(i Identification. Characterization and Use of Modulators of 24p4C'2 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 ldenfy 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 and/or 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 agenivnduced proteins and used to target novel therapeutics to the treated cancer tissue sample. Modulator-related Identification and Screening Assays: Gene Exgression-related Assavs Proteins, nucleic acids, and antibodies of the Invention are used in screening assays. The cancer-associated proteins, antibodies, nucleic acids, modified proteins and cels 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 throughput screening techniques to allow monItoring for expression profile genes after treatment with a candidate agent (e.g., Davis, GF, etal, J Biol Screen 7:69 (2002); Zlokamik, et al., Science 279:84-8 (1998); Heid, Genome Res 6:986 94,1996). 70 The cancer proteins, an tibodies, 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 alow 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 blochips 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 assodated 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, 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. 71 As noted above, gene expression monitoring is conveniently used to test candidate modulators (e.g., protein, nudeic 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 blochIp. 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 nudeotides is performed. Generally. the nudeic 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 add 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 stdngency 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, nudease 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 cel comprising a 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. 72 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., oell-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 kientified, 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 Lhmitation 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 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 morphologicay by the formation of a disoriented monolayer of cells or cells In 73 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 modulalors 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. Nati. 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 Tumar-speelfic Marker Levels to Identify and Oharacterize 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, Anglogenesis 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. Biot. Chem. 249:4295-4305 (1974); Strickland & Beers, J. Blol. 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 (ad.) 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 Matrioel to Identify and Characterize Modulators The degree of invasiveness into Matigel 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 cels 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 fiflter, is rated as invasiveness, and rated histologically by number of cells and distance moved, or by prelabeling the cells with 125 and counting the radioactivity on the distal side of the filter or bottom of the dish. See, e.g., Freshney (1984), supra. Evaluation of Tumor Growth In Vi, to Identify and Characterize Modulators 74 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 One. 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., Glovaneila et al., J. Natl. Cancer Inst 52:921 (1974)), a SCID mouse, a thymectomized 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 108 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., Students 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 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 nudelc 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 at (Davis GF, supra; Gonzalez, J. & Negulescu, P. Curr. Opin. Biotechnol. 1998: 9:624). 75 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. Atematively, cels comprising the cancer proteins are used in the assays. Thus, the methods comprise combining a canor 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", 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 stericaly 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 cels. A wide variety of assays can be used for this purpose, including proliferation assays, cAMP assays, labeled in itro protein-protein binding assays, electrophoretic mobility shift assays, immunoassays for protein binding, functional assays (phosphorylation assays, etc.) and the like. 76 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., 112, 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, rigands, 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*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 proteInscf 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 whch 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. 77 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 proteln-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 Polynudeotides 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 oligonudeotide or its conjugated version into the call. Aftematively, a polynudeotide modulator of cancer can be Introduced Into a cell containing thelarget nuceic add sequence, e.g., by formation of a polynudeotide-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 Nudeotides 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 nudear 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 polynudeotide to the mRNA reduces the translation and/or stability of the mRNA. In the context of this Invention, antisense polynudeotides can comprise naturally occurring nudeotides, or synthetic species formed from naturally occurring Subunits or their dose homologs. Antisense polynudeotides may also have altered sugar moleties or Inter-sugar linkages. Exemplary among these are the phosphorothloate 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 nudeotides of the Invention. See, e.g., Isis Pharmaceuticals, Carlsbad, CA; Sequitor, Inc., Natick, MA. Such anlisense polynudeotides can readily be synthesized using recombinant means, or can be synthesized in vitro. Equipment for such synthesis is sold by several vendors, Induding Applied Biosystems. The preparation of other olligonudeotides such as phosphorothioates and alkylated derivatives is also well known to those of skill in the art Anisense molecules as used herein include anbsense or sense oligonudeotides. Sense oligonudeofides can, e.g., be employed to block transcription by binding to the anti-sense strand. The antisense and sense oligonudeotide 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 nudeotides, preferably from about 12 to 30 nucleotides. The ability to derive 78 an antisense or a sense oligonucleolide, 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 nudeotide 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 ibozymes, hairpin ribozymes, RNase P, and ahead 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., Nuc. Adds 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 94126877; Ojwang et al., Proc. Nall. Acad. Sd. USA 90:63404344 (1993); Yamada et al., Human Gene Therapy 1:39-45 (1994); Leavitt et a1., Proc. Nall. Aced 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 Screeninq 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 US97101019. Regulatable gene therapy systems can also be used. Once the modulator has been administered to the cels, 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 transcdpt 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 diferentially 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, neovasculazation, hormone release, transcriptional changes to both known and uncharacterized genetic markers (e.g., by Northem blots), changes In cell metabolsm such as cell growth or pH changes, and changes In intracellular second messengers such as cGNIP. 79 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 call. 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, Bestfil, 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 partiolar when chromosomal abnonnalities such as translocations, and the like are identified in the cancer gene locus. XIV.) KitslArticles 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 nudeic add, 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 blotin-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 wi typically comprise the container described above and one or more other ontainers comprising materials desiable 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 spedfic therapy or non-therapeutic application, such as a diagnostic or laboratory application, and can also indicate directions for either ve or in vimno use, such-as those described herein. Directions and or other Information can also be Included on an Insert(s) or label(s) which is Induded with or on the kit. The terms *kit and "artide 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 molecle(s), nucleic add sequence(s), and/or antibody(s), e.g., materials useful for the diagnosis, prognosis, prophytaxis and/or treatment of neoplasias of tissues such as those set forth In Table I Is provided. The article of 80 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), nudeic add 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 specfically binding 24P4C1 2 and modulating the function of 24P4C12. - 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 1. The article of manufacture can further comprise a second container comprising a pharmaceufically-acceptable buffer, such as phosphate-buffered saline, Rngers solution andlordextrose 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 Fragment of the 24P4C12 Gene 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 the LAPC-9 AD prostate cancer xenograft. The gene 24P4C12 was derived from an LAPC-9 AD minus benign prostatic hyperplasia experiment. The 24P4C12 SSH cDNA of 160 bp is listed in Figure 1. The full length 24P4C12 cDNAs and ORFs are described in.Figure 2-with the protein sequences listed in Figure 3. 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 (Ufe Technologies, Glbco BRIL) using 10 ml g issue 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. Olioonudeotides: The following HPLC purified oligonudeotides were used. DPNCDN (cDNA synthesis primer: 5'TTTTGATCAAGCTTo3' (SEQ ID NO: 33) 81 Adaptor 1: 5'CTAATACGACTCACTATAGGGCTCGAGCGGCCGCCCGGGCAG3'(SEQ ID NO 34) 3'GGCCCGTCCTAG5' (SEQ ID NO: 35) Adaptor 2 5'GTAATACGACTCACTATAGGGCAGCGTGGTCGCGGCCGAG3' (SEQ ID NO: 36) 3'CGGCTCCTAG5' (SEQID NO: 37) PCR primer 1: 5'CTAATACGACTCACTATAGGGC3' (SEQ ID NO 38) Nested Primer (NP)1: 5'TCGAGCGGCCGCCCGGGCAGGA3' (SEQ ID NO: 39) Nested primer (NP)2: 5'AGCGTGGTCGCGGCCGAGGA3' (SEQ ID NO: 40) Supression 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 and nonnal tissues. The gene 24P4C12 sequence was derived from LAPC-4AD prostate cancer xenograft minus begin prostatic hyperplasia cDNA subtraction. The SSH DNA sequence (Figure 1) was identified. The cDNA derived from a pool of normal tissues and benign prostatic.hyperplasla was used as the source of the *driver' cDNA, while the cDNA from LAPC-4AD xenograft 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 xenograft 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. PT1 117-1, Catalog No. K1804-1). The resulting cDNA was digested with Dpn 11 for 3 hirs at 37C. Digested cDNA was extracted with phenolldiloroform (1:1) and ethanol precipitated. Driver cDNA was generated by combining In a 1:1 ratio Dpn Il digested cDNA from the relevant tissue source (see above) with a mix of digested cDNAs derived from the nine normal tissues: stomach, skeletal muscle, lung, brain, liver, kidney. pancreas, small intestine, and heart. Tester cDNA was generated by diluting 1 p of Dpn |1 digested cDNA from the relevant tissue source (see above) (400 ng) In 5 p1 of water. The diluted cDNA (2 pi, 160 ng) was then ligated to 2 pl of Adaptor 1 and Adaptor 2 (10 pM), in separate igation reactions, in a total volume of 10 p1 at 1600 ovemight, using 400 u of T4 DNA ligase (CLONTECH). Ligation was terminated with 1 p1of 0.2 M EDTA and heating at 720C for 5 min. The first hybridization was performed by adding 1.5 pl (600 ng) of driver cDNA to each of two tubes containing 1.5 p1 (20 ng) Adaptor 1- and Adaptor 2- ligated tester cDNA. In a final volume of 4 pI, the samples were overlaid with mineral oil, denatured in an MJ Research thermal cyder at 98C for 1.5 minutes, and then were allowed to hybridize for 8 hrs at 8C. The two hybridizations were then mixed together with an additional I p of fresh denatured driver cDNA and were allowed to hybridize 82 ovemighl at 68C. The second hybridization was then diluted in 200 i of 20 mM Hepes, pH 8.3,50 mM NaCl, 0.2 mM EDTA, heated at 700C for 7 min. and stored at -200C. PCR Amplification, Cloning and Seouencina 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 p1 of the diluted final hybridization mix was added to 1 pl of PCR primer 1 (10 pM), 0.5 p1 dNTP mix (10 pM), 2.5 pI 10 x reaction buffer (CLONTECH) and 0.5 p1 50 x Advantage cDNA polymerase Mix (CLONTECH) in a final volume of 25 p1. PCR 1 was conducted using the following conditions: 75oC for 5 min., 940C for 25 sec., then 27 cycles of 94oC for 10 sec, 66WC for 30 sec, '72CC 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, i sA from the pooled and diluted primary PCR reaction was added to the 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 94CC for 10 sec, 68C for 30 sec, and 720C for 1.5 minutes. The PCR products were analyzed using 2% agarose gel electrophoresis. The PCR products were inserted Into pCR2.1 using the TIA vector cloning kit (Invitrogen). Transformed E. colf were subjected to blue/white and 9mpicillin 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 NPi and NP2 as primers. PCR products were analyzed using 2% agarose gel electrophoresis. Bacterial clones were stored i 20% glycerol in a 96 wel 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 pg of mRNA with dligo (dT)12-18 priming using the Gibco-BRL Superscript Preampfification system. The manufacturer's protocol was used wich Included an Incubation for 50 min at 42CC with reverse transcriptase followed by RNAse H treatment at 370C for 20 min. After completing the reaction, the volume can be Increased to 200 pl 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'atategocgegctetcgtcgacaa3' (SEQ ID NO: 41) and 5'agccacacgcagctcattgtagaagg 3'(SEQ ID NO: 42) to ampify p-actin. First strand cDNA (5 p) were amplified in a total volume of 50 p1 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 IX 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 940C for 15 -sec, followed by a 18, 20, and 22 cycles of 94oC for 15, 65C for 2 min, 72aC for 5 sec. A final extension at 72CC was carried out for 2 min. After agarose gel electrophoresis, the band intensities of the 283 b.p. 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 an tissues after 22 cydes 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 24P4C12 gene, 5 p 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 24P4C12 SSH sequence and are listed below' 24P4C12.1 5'- AGATGAGGAGGAGGACAAAGGTG - 3' (SEQ ID NO: 43) 83 24P4C12.2 5'- ACTGCTGGGAGGAGTACCGAGTG -3' (SEQ ID NO: 44) Example 2: Isolation of Full Length 24P4C12 Encodino cDNA The 24P4C12 SSH cDNA sequence was derived from a substraction consisting of LAPC-4AD xenograft minus benign prostatic hyperplasla. The SSH cDNA sequence (Figure 1) was designated 24P4C12. The isolated gene fragment of 160 bp encodes a putative open reading frame (ORF) of 53 amino adds and exhibits significant homology to an EST derived from a colon tumor library. Two larger cDNA ones were obtained by gene trapper experiments, GTE9 and GTF8. The ORF revealed a significant homology to the mouse gene NG22 and the C.elegans gene CEESB82F. NG22 was recently Identified as one of many ORFs within a genonic BAC done that encompasses the MHC class III in the mouse genome. Both NG22 and CEESB82F appear to be genes that contain 12 transmembrane domains. This suggests that the gene encoding 24P4C12 contains 12 transmembrane domains and is the human homologue of mouse NG22 and C. elegans CEESB82F. Functional studies in Ce. elegans may reveal the biological role of these homologs. If 24P4C1 2 is a cell surface marker, then it may have an application as a potential imaging reagent and/or therapeutic target in prostate cancer. The 24P4C12 v.1 of 2587 bp codes for a protein of 710 amino acids (Figure 2 and Figure 3). Other variants of 24P4C12 were also identified and these are listed in Figures 2 and 3.24P4C12 v.1, v.3, V.5 and v.6 proteins are 710 amino acids in length and differ from each other by one amino acid as shown in Figure 11. 24P4C12 v.2 and v.4 code for the same protein as 24P4C12 v.1. 24P4C1 2 v.7, v.8 and v.9 are alternative splice variants and code for proteins of 598, 722 and 712 amino acids in length, respectively. Example 3: Chromosomal Mappinq of 24P4C12 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 Al), human-rodent somatic cell hybrid panels such as is available from the Coriel Institute (Camden, New Jersey), and genomic viewers utilizing BLAST homologies to sequenced and mapped genomic clones (NCBI, Bethesda, Maryiand). 24P4C12 maps to chromosome 6p21.3 using 24P4C12 sequence and the NCBI BLAST tool located on the Word Wide Web at (.ncbi.nlm.nih.gov/genome/seqlpage.cgi?F=HsBasthtml&&ORG=Hs). Example 4: Expression Analysis of 24P4C12 Expression analysis by RT-PCR demonstrated that 24P4C12 is strongly expressed in prostate and ovary cancer patient -specimens (Figure 14). First strand cDNA was generated from vital pool I (kidney, liver and lung), vital pool 2 (colon, pancreas and stomach), a pool of prostate cancer xenografts (LAPC-4AD, LAPC-4A, LAPC-9AD and LAPC-9Ai), prostate cancer pool, bladder cancer pool, kidney cancer pool, colon cancer pool, ovary cancer pool, breast cancer pool, and cancer metastasis pool. Normalization was performed by PCR using primers to actin. Semi-quantitative PCR, using primers to 24P4C1 2, was performed at 26 and 30 cycles of ampification. Results show strong expression of 24P4C1 2 in prostate cancer pool and ovary cancer pool. Expression was also detected In prostate cancer xenografts, bladder cancer pool, kidney cancer pool, colon cancer pool, breast cancer pool, cancer metastasis pool, vital pool 1, and vital pool 2. Extensive northern blot analysis of 24P4C12 in multiple human normal tissues is shown in Figure 15. Two multiple tissue northem blots (Clontech) both with 2 pg of mRNAAane were probed with the 24P4C12 SSH sequence. Expression of 24P4C12 was detected in prostate, kidney and colon. Lower expression is detected in pancreas, lung and placenta amongst all 16 normal tissues tested. 84 Expression of 24P4C12 was tested in prostate cancer xenografts and cell lines. RNA was extracted from a panel of cell lines and prostate cancer xenografts (PrEC, LAPC-4AD, LAPC-4Al, LAPC-9AD, LAPC-9A, LNCaP, PC-3, DU145, TsuPr, and LAPC 4CL). Northem blot with 10 pg of total RNAiane was probed with 24P4C12 SSH sequence. Size standards in kilobases (kb) are indicated on the side. The 24P4C12 transcript was detected in LAPC-4AD, LAPC-4A, LAPC-9AD, LAPC-9A, LNCaP, and LAPC-4 CL Expression of 24P4C12 in patient cancer specimens and human normal tissues is shown in Figure 16. RNA was extracted from a pool of prostate cancer specimens, bladder cancer specimens, colon cancer specimens, ovary cancer specimens, breast cancer specimens and cancer metastasis specimens, as well as from normal prostate (NP), normal bladder (NB), normal kidney (NK), and normal colon (NC). Northern blot with 10 pg of total RNAfane was probed with 24P4C1 2 SSH sequence. Size standards in kilobases (kb) are indicated on the side. Strong expression of 24P4C12 transcript was detected in the patient cancer pool specimens, and In normal prostate but not in the other normal tissues tested. Expression of 24P4C12 was also detected in individual prostate cancer patient specimens (Figure 17). RNA was extracted from normal prostate (N), prostate cancer patient tumors (T) and their matched normal adjacent tissues (Nat). Northern blots with 10 pg of total RNA were probed with the 24P4C12 SSH fragment Size standards in kilobases are on the side. Results show expression of 24P4C12 in normal prostate and all prostate patient tumors tested. Expression of 24P4C12 In colon cancer patient specimens Is shown in figure 18. RNA was extracted from colon cancer cell lines (CL: Colo 205, LoVo, and SK-CO-), normal colon (N), colon cancer patient tumors (T) and their matched normal adjacent tissues (Nat). Northern blots with 10 pg of total RNA were probed with the 24P4C12 SSH fragment. Size standards in kilobases are on the side. Results show expression of 24P4C1 2 in normal colon and all colon patient tumors tested. Expression was detected In the cell lines Colo 205 and SK-CO-, but not In LoVo. Figure 20 displays expression results of 24P4C12 In lung cancer patient specimens. Ma was extracted from lung cancer cell lines (CL CALU-1, A427, NCI-H82, NCI-H146), normal lung (N), lung cancer patient tumors (T) and their matched normal adjacent tissues (Nat). Northern blots with 10 pg of total RNA were probed with the 24P4C12 SSH fragment Size standards in kilobases are on the side. Results show expression of 24P4C12 in lung patient tumors tested, but not in normal lung. Expression was also detected In CALU-1, but not in the other cell lines A427, NCI-H82, and NCI H146. 24P4C12 was assayed in a panel of human stomach and breast cancers (T) and their respective matched normal tissues (N) on RNA dot blots. 24P4C12 expression was seen in both stomach and breast cancers. The expression detected in normal adjacent tissues (isolated from diseased tissues) but not in normal tissues (isolated from healthy donors) may Indicate that these tissues are not fully normal and that 24P4C12 may be expressed in early stage tumors. The level of expression of 24P4C12 was analyzed and quantitated in a panel of patient cancer tissues. First strand cDNA was prepared from a panel of ovary patient cancer specimens (A), uterus patient cancer specimens (B), prostate cancer specimens (C), bladder cancer patient specimens (D), lung cancer patient specimens (E), pancreas cancer patient specimens (F), colon cancer specimens (G), and kidney cancer specimens (H). Normalization was performed by PCR using primers to actin. Semi-quantitative PCR using primers to 24P4C1 2, was performed at 26 and 30 cycles of amplification. Samples were run on an agarose get and PCR products were quantitated using the Alphalmager software. Expression was recorded as absent, low, medium or strong. Results show expression of 24P4C12 in the majority of patient cancer specimens tested, 73.3% of ovary patient cancer specimens, 83.3% of uterus patient cancer specimens, 95.0% of prostate cancer specimens, 61.1% of bladder cancer patient specimens, 80.6% of lung cancer patient specimens, 87.5% of pancreas cancer patient specimens, 87.5% of colon cancer specimens, 68.4% of dear cell renal carcinoma, 100% of papillary renal cell carcinoma. 85 The restricted expression of 24P4C12 in normal tissues and the expression detected in prostate cancer, ovary cancer, bladder cancer, colon cancer, lung cancer pancreas cancer, uterus cancer, kidney cancer, stomach cancer and breast cancer suggest that 24P4C1 2 is a potential therapeutic target and a diagnostic marker for human cancers. Example 5: Transcrpt Variants of 24P4C12 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 spiced differently from the same transcript In eukaryotes, when a mulli-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 zoning experiment, or by use of full-length transcript and EST sequences. First, all human ESTs were grouped into dusters 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 done, that portion of the variant Is very useful for antigen generation and for further zoning 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 at compbio.onl.gov/Grail-binEmptyGrailForm) and GenScan (URL at genes.mitedu/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., et at., Identification of human chromosome 22 transcribed sequences with ORF expressed sequence tags, Proc. Nai Aced 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 zoning, 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 pro-messenger RNA produces multiple forms of mature caprine alpha(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 LightCyder technology, Clin Chem. 2001 Apr;47(4):654-60; Jia, H.P., et al., Discovery of new human beta defensins using a genomlcs-based approach, Gene. 2001 Jan 24; 263(1-2):211-8. For PCR-based and 5' RACE Validation: Brigle, K.E., et al., Organization of the murine reduced folate carrier gene and Identification of variant splice forns, Biochem Blophys Acta. 1997 Aug 7; 1353(2): 191-8). It is known in the art that genomic regions are modulated In cancers. 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. 86 Disclosed herein Is that 24P4C12 has a particular expression profile related to cancer. Alternative transcripts and splice variants of 24P4C12 may also be involved in cancers in the same or different tissues, thus serving as tumor-assocated markerslantigens. The exon composition of the original transcript, designated as 24P4C12 v.1, is shown in Table LI. Using the fuD length gene and EST sequences, three transcript variants were Identified, designated as 24P4C12 v.7, v.8 and v.9. Compared with 24P4C12 v.1, transcript variant 24P4C1 2 v.7 has spliced out exons 10 and 11 from variant 24P4C1 2 v.1, as shown In Figure 12. Variant 24P4C12 v.8 inserted 36 bp in between 1931 and 1932 of variant 24P4C12 v.1 and variant 24P4C12 v.9 replaced with 36 bp the segment 1136-1163 of variant 24P4C12 v.1. Theoretically, each different combination of exons In spatial order, e.g. exons 2 and 3, is a potential splice variant. Figure 12 shows the schematic alignment of exons of the four transcript variants. Tables LII through LXIII are set forth on a variant by variant basis. Tables UI, LVi, and LX show nudeolide sequences of the transcript variant Tables Lill, LVII, and LXI show the alignment of the transcript variant with the nucleic add sequence of 24P4C12 v.1. Tables LIV, LVIII, and LXII lay out the arnino acid translation of the transcript variant for the Identified reading frame orientation. Tables LV, LIX, and LXIII display alignments of the amino acid sequence encoded by the splice variant with that of 24P4C12 v.1. Example 6: Single Nucleotide Polymorphisms of 24P4C12 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 pars: A/T, CIG, G/C and TIA. 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. SNPs that occur on a cDNA are called cSNPs. These cSNPs may change amino acids of the protein encoded by the gene and thus change the functions of the protein. Some SNPs cause inherited diseases; others contribute to quantitative variations in phenotype and reactions to environmental factors Including diet and drugs among individuals. Therefore, SNPs 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 0ct 11(5):637-641; M. Pirmohamed and B. K. Park, 'Genefic susceptibility to adverse drug reactions,' Trends Pharmacol. Sci. 2001 Jun; 22(6):298 305; J. H. Riley, C. J. Allan, E. Lal and A. Roses, * The use of single nucleotide polymorphisms in the isolation of common disease genes,' Pharmacogenomics. 2000 Feb; 1(l):39-47; R. Judson, J. C. Stephens and A. Wndemuh, 'The predictive power of haplotypes in clinical response,' Pharmacogenomics. 2000 feb: 1(1):15-26). SNPs are identified by a variety of art-accepted methods (P. Bean, 'The promising voyage of SNP target discovery,' Am. Cin. Lab. 2001 Oct-Nov; 20(9):18-20; K. M. Weiss, "In search of human varIation," Genone Res. 1998 Jul; 8(7):691-697; M. M. She, *Enabling large-scale pharmacogenetic studies by high-throughput mutation detecton and genotyping technologies," Clin. Chem. 2001 Feb; 47(2):164-172). For example, SNPs are 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 SNPs 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). SNPs can be verfied and genotype or haplotype of an individual can be determined by a variety of methods including direct 87 sequencing and high throughput microarrays (P. Y. Kwok, *Methods for genotyping single nucleotide polymorphisms," Annu. Rev. Genomics Hum. Genet. 2001; 2:235-258; M. Kokods, 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, five SNPs were identified In the original transcript, 24P4C12 v.1, at positions 542 (GIA), 564 (GIA). 818 (C/T), 981(A/G) and 1312 (A/C). The transcripts or proteins with alternative alleles were designated as variants 24P4C12 v.2, v.3, v.4, v.5 and v.6, respectively. Figure 10 shows the schematic alignment of the SNP variants. Figure 11 shows the schematic alignment of protein variants, corresponding to nucleotide variants. Nucleotide variants that code for the same amino acid sequence as variant 1 are not shown in Figure 11. These alleles of the SNPs, though shown separately here, can occur in different combinations (haplotypes) and in any one of the transcript variants (such as 24P4C12 v.7) that contains the sequence context of the SNPs. Example 7; Production of Recombinant 24P4C12 In Prokarvotic Systems To express recombinant 24P4C12 and 24P4C12 variants In prokaryotic cells, the full or partial length 24P4C12 and 24P4C12 variant cDNA sequences are cloned into any one of a variety of expression vectors known in the art The full length cDNA, 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 24P4C12, variants, or analogs thereof are used. A. In im transcription and translation constructs: 2.Cl; To generate 24P4C12 sense and anti-sense RNA probes for RNA in siftu Investigations, pCRll constructs (Invitrogen, Carlsbad CA) are generated encoding either all or fragments of the 24P4C12 cDNA. The pCRII vector has Sp6. and T7 promoters flanking the insert to drive the transcription of 24P4C1 2 RNA for use as probes in RNA in situ hybridization experiments. These probes are used to analyze the cel and tissue expression of 24P4C1 2 at the RNA level. Transcribed 24P4C12 RNA representing the cDNA amino acid coding region of the 24P4C1 2 gene is used in i vitro translation systems such as the TnT" Coupled Reticulolysate System (Promega, Corp., Madison, WI) to synthesize 24P4C1 2 protein. B. Bacterial Constructs' pGEX Constructs: To generate recombinant 24P4C1 2 proteins in bacteria that are fused to the GlutathIone S transferase (GST) protein, all or parts of the 24P4C12 cDNA or variants are cloned into the GST- fusion vector of the pGEX family (Amersham Pharmaca Biotech, Piscataway, NJ). These constructs allow controlled expression of recombinant 24P4C12 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 aftiity 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 proteolyic cleavage site, such as the PreScssionTm recognition site in pGEX-6P-1, may be employed such that it permits cleavage of the GST tag from 24P4C12-related protein. The ampicillin resistance gene and pBR322 origin permits selection and maintenance of the pGEX plasmids in E coli. pMAL Constructs: To generate, in bacteria, recombinant 24P4C12 proteins that are fused to maltose-binding protein (MBP), all or parts of the 24P4C12 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 24P4C12 protein sequences with MBP fused at the amino-terminus and a BX His epitope tag at the carboxy 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 ant-MBP and anti-His antibodies. The 6X His epitope tag is generated by adding 6 histidine codons to the 3'conIng primer. A Factor Xa recognition site permits cleavage of the pMAL 88 tag from 24P4C12. 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 24P4C12 in bacterial cels, all or parts of the 24P4C12 cDNA protein coding sequence are doned into the pET family of vectors (Novagen, Madison, Wi). These vectors allow tightly controlled expression of recombinant 24P4C12 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"' 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 24P4C1 2 protein are expressed as amino-terminal fusions to NusA. C. Yeast Constructs: pESC Constructs: To express 24P4C12 in the yeast species Saccharomyces cerevislae for generation of recombinant protein and functional studies, all or parts of the 24P4C12 cDNA protein coding sequence are cloned into the pESC family of vectors each of which contain I of 4 selectable markers, HIS3, TRPI, LEUZ 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 24P4C12. In addition, expression In yeast yields similar post-translational modifications, such as glycosylations and phosphorylations, that are found when expressed In eukaryotic lls. pESPConstructs: To express 24P4C12 in the yeast species Saccharomycespombe, all or parts of the 24P4C12 cDNA protein coding sequence are cloned into the pESP family of vectors. These vectors allow controlled high level of expression of a 24P4C12 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 Flagw epitope tag allows detection of the recombinant protein with anti Flag"m antibody. Example 8: Production of Recombinant 24P4C12 In Higher Eukarvtic Systems A. Mammalian Constructs: To express recombinant 24P4C12 in eukaryotic cells, the ful or partial length 24P4C12 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 24P4C12 are expressed In these constructs, amino acids Ito 710, 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 24P4C12 v.1 through v.6; amino acids I to 598, 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 24P4C12 v.7. amino acids 1 to 722, 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 24P4C12 v.8, amino acids 1 to 71Z 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 24P4C12 v.9, variants, or analogs thereof. The constructs can be traisfected Into any one of a wide variety of mammalian cells such as 293T cells. Transfected 293T cell lysates can be probed with the anti-24P4C12 polyclonal serum, described herein. .cDNA3.1MycHis Constructs; To express 24P4C12 in mammalian cells, a 24P4C12 ORF, or portons thereof, of 24P4C1 2 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) polyadenylatlon signal and transcription termination sequence to enhance mRNA stability, along with the SV40 orign 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 89 resistance gene and ColE1 origin permits selection and maintenance of the plasmid in E coli. Figure 24 demonstrates expression of 24P4C1 2 from the pcDNA3.1/MycHis construct in transiently transfected 293T cells. vcDNA41HisMax Constructs: To express 24P4C12 in mammalian cells, a 24P4C12 ORF, or portions thereof, of 24P4C1 2 are doned 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-rm and six histidine (6X His) epitopes fused to the amino-terminus. The pcDNA4fHisMax 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 coli. pcDNA3.1ICT-GFP-TOPO Construct: To express 24P4C1 2 in mammalian cells and to allow detection of the recombinant proteins using fluorescence, a 24P4C1 2 ORF, or portions thereof, with a consensus Kozak translation initiation site are cloned into pcDNA3.1ICT-GFP-TOPO (Invitrogen, CA). Protein expression is driven from the cytomegalovirus (CMV) promoter. The recombinant proteins have the Green Fluorescent Protein (GFP) fused to the carboxyl-terminus facilitating non-Invasive, In vivo detection and cell biology studies. The pcDNA3.lCT-GFP-TOPO 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 CoEl origin permits selection and maintenance of the plasmid in E. coi. Additional constructs with an amino terminal GFP fusion are made in pcDNA3.1/NT-GFP-TOPO spanning the entire length of a 24P4C12 protein. . pTa&5: A 24P4C1 2 ORF, or portions thereof, were cloned into pTag-5. This vector is similar to pAPtag but without the alkaline phosphatase fusion. This construct generates 24P4C12 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 24P4C1 2 protein were 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 24P4C12 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 coli. Figure 26 shows expression of 24P4C12 from two different pTag5 constructs. PAPtag: A 24P4C1 2 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 24P4C12 protein while fusing the IgGx signal sequence to the amino-terminus. Constructs are also generated in which alkaline phosphatase with an amino terminal IgGx signal sequence is fused to the amino-terminus of a24P4C12 protein. The resulting recombinant 24P4C12 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 24P4C12 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 coi. PsecFc: A 24P4C1 2 ORF, or portions thereof, Is also cloned Into psecFc. The psecFc vector was assembled by zoning the human immunoglobuin G1 (1gG) Fc (hinge, CH2, CH3 regions) into pSecTag2 (Invitrogen, California). This construct generates an IgGI Fc fusion at the carboxyt-terminus of the 24P4C12 proteins, while fusing the IgGK signal sequence to N-terminus. 24P4C1 2 fusions utilizing the murine IgG1 Fc region are also used. The resulting recombinant 24P4C12 proteins are optimized for secretion into the media of transfected mammalian cells, and can be used as 90 immunogens or to Identify proteins such as ligands or receptors that Interact with 24P4C12 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 ampidllin resistance gene permits selection of the plasmid In E coli. SRa Constructs: To generate mammalian cell lines that express 24P4C12 constitutively, 24P4C12 ORF, or portions thereof, of 24P4C12 were cloned into pSRct constructs. Amphotropic and ecotropic retroviruses were generated by transfection of pSRoL constructs into the 293T-10A1 packaging line or co-transfection of pSRoL 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, 24P4C12, into the host cellines. Protein expression is driven from a long terminal repeat (LTR). The Neomycn resistance gene present In the vector allows for selection of mammalian cells that express the protein, and the ampiciltin resistance gene and ColE1 origin permit selection and maintenance of the plasmld In E. coll. The retroviral vectors can thereafter be used for Infection and generation of various ca lines using, for example, PC3, NIH 3T3, TsuPri, 293 or rat-1 cells. Figure 23 shows RNA expression of 24P4C1 2 driven from the 24P4C12pSRa construct in stably transduced PC3, 3T3 and 300.19 cells. Figure 25 shows 24P4C12 protein expression in PC3 cells stably transduced with 24P4C12pSRa construct. Additional pSRa constructs are made that fuse an epitope tag such as the FLAGm tag to the carboxyl-terminus of 24P4C12 sequences to allow detection using anti-Flag antibodies. For example, the FLAGm sequence 5' gat tac aag gat gac gac gat aag 3 (SEQ ID NO: 45) is added to cloning primer at the 3' end of the ORF. Additional pSRcL constructs are made to produce both amino-terminal and carboxyt-terminal GFP and mycBX His fusion proteins of the full-length 24P4C1 2 proteins. Additional Viral Vectors: Additional constructs are made for viral-mediated delivery and expression of 24P4C1 2. High virus titer leading to high level expression of 24P4C12 is adieved In viral delivery systems such as adenoviral vectors and herpes amplicon vectors. A 24P4C1 2 coding sequences or fragments thereof are amplified by PCR and subdoned into the AdEasy shuttle vector (Stratagene). Recombination and virus packaging are performed according to the manufacturers instructions to generate adenoviral vectors. Alternatively, 24P4C1 2 coding sequences or fragments thereof are cloned into 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 cels. Regulated Expression Systems: To control expression of 24P4C12 in mammalian cells, coding sequences of 24P4C12, or portions thereof, are doned 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 24P4C12. These vectors are thereafter used to control expression of 24P4C12 in various cell lines such as PC3, NIH 3T3, 293 or rat-1 cells. B. Baculovirus Expression Systems To generate recombinant 24P4C12 proteins in a baculovirus expression system, 24P4C12 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-24P4C12 is co-transfected with helper plasmid pBac-N-Blue (Invilrogen) Into SF9 (Spodoptera fruglpetda) insect cells to generate recombinant baculovirus (see Invitrogen instruction manual for details). Baculovirus is then collected from cell supernatant and purified by plaque assay. Reombinant 24P4C1 2 protein is then generated by Infection of HighFive insect cells (Invilrogen) with purified baculovirus. Recombinant 24P4C12 protein can be detected using antl-24P4C12 or anti-His-tag antibody. 24P4C12 proteIn can be purified and used in various cell-based assays or as immunogen to generate polyconal and monoclonal antibodies specific for 24P4C12. 91 Example 9: Antlaenicity Profiles and Secondary Structure Figures 5-9 depict graphically five amino acid profiles of the 24P4C12 variant 1, 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, Hydrophiicity, (Hopp T.P., Woods KR., 1981. Proc. Nati. Acad. Sci. U.S.A. 78:3824 3828); Figure 6, Hydropathidty, (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-tum (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 the 24P4C12 protein. Each of the above amino acid profiles of 24P4C12 were generated using the following ProtScale parameters tor 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. Hydophilicity (Figure 5), Hydropathcity (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-tum (Figure 9) profiles determine stretches of amino adds (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 24P4C12 protein and of the variant proteins indicated, e.g., by the profiles set forth in Figure 5, Figure 6, Figure 7, Figure 8, and/or Figure 9 are used to prepare immunogens, either peptides or nucleic acids that encode them, to generate therapeutic and diagnostic anti-24P4C12 antibodies. The immunogen can be any 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 or more than 50 contiguous amino adds, or the corresponding nudeic acids that encode them, from the 24P4C12 protein variants listed in Figures 2 and 3. In partiaolar, peptide immunogens of the invention can comprise, a peptide region of at least 5 amino adds of Figures 2 and 3 in any whole number increment that indudes an amino acid position having a value greater than 0.5 In the Hydrophillidly profile 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 Hydropathiidty profile of Figure 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 profile 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 profile 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-tum profile of Figure 9. Peptide immunogens of the invention can also comprise nudeic adds that encode any of the forgoing. AD immunogens of the invention, peptide or nudelec add, can be embodied in human unit dose form, or comprised by a composition that includes a pharmaceutical excpient compatible with human physiology. The secondary structure of 24P4C12 variant 1, namely the predicted presence and location of alpha helices, extended strands, and random coils, are predicted from the respective primary amino add sequences using the HNN Hierarchical Neural Network method (Guermeur, 1997, http-lpbiibcp.frlgi-ininpsa_automat.pl?pagenpsajnn.html), 92 accessed from the ExPasy molecular biology server (httpJ/www.expasy.ch/tools). The analysis indicates that 24P4C1 2 variant 1 is composed of 53.94% alpha helix, 9.44% extended strand, and 36.62% random coil (Figure 13a). Analysis for the potential presence of transmembrane domains in 24P4C12 variants were carried out using a variety of transmembrane prediction algorithms accessed from the ExPasy molecular biology server (http:/Aww.expasy.ch/toois/. Shown graphically are the results of analysis of variant I depicting the presence and location of 10 transmembrane domains using the TMpred program (Figure 13b) and TMHMM program (Figure 13c). The results of each program, namely the amino acids encoding the transmembrane domains are summarized in Table L. Example 10: Generation of 24P4C12 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 subcutaneous or intraperttoneal Injections. In addition to Immunizing with the full length 24P4C12 protein, 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 the Example entitled "Antigenicity Profiles). Such regions would be predicted to be hydrophilic, flexible, in beta-tum conformations, and be exposed on the surface of the protein (see, e.g., Figure 5, Figure 6, Figure 7, Figure 8, or Figure 9 for amino acid profiles that indicate such regions of 24P4C12 and variants). For example, 24P4C12 recombinant bacterial fusion proteins or peptides containing hydrophilic, flexible, beta-tum regions of 24P4C12 variant proteins are used as antigens to generate potyclonal antibodies in New Zealand White rabbits. For example, such regions include, but are not limited to, amino adds 1-34, amino acids 118-135, amino acids 194-224, amino acids 280-290, and amino acids 690-710, of 24P4C12 variants 1. 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 1-14 of 24P4C1 2 variant 1 was conjugated to KLH and used to immunize a rabbit This antiserum exhibited a high tiler to the peptide (>10,000) and recognized 24P4C12 in transfected 293T cells by Western blot and flow cytometry (Figure 24) and in stable recombinant PC3 cels by Western blot and Immunohistochemistry (Figure 25). Altemaively the Immunizing agent may indude a! or portions of the 24P4C12 variant proteins, analogs or fusion proteins thereof. For example, the 24P4C1 2 variant I 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. Such fusion proteins are purified from induced bacteria using the appropriate affinity matrix. In one embodiment, a GST-fusion protein encoding amino acids 379-453, encompassing the third predicted extracellular loop of variant 1, is produced, purified, and used as immunogen. Other recombinant bacterial fusion proteins that may be employed Indude maltose binding protein, LacZ, thioredoxin, NusA, or an immunoglobulin constant region (see the section entitled Production of 24P4C12 In Prokaryotic Systems" and Current Protocols In Molecular Biology, Volume 2, Unit 16, Frederick M. Ausubul et al. eds., 1995; Unsley, P.S., Brady, W., Umes, 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 Example entitled "Production of Recombinant 24P4C12 in Eukaryotic Systems'), and retains post-translational modifications such as glycosylations found in native protein. In two embodiments, the predicted 1st and third extracellular loops of variant 1, amino acds 59-227 and 379-453 respectively, were each doned into the Tag5 mammalian secretion vector and expressed in 293T cells (Figure 26). Each recombinant protein is then purified by metal chelate chromatography from tissue culture 93 supematants and/or lysates of 293T cells stably expressing the recombinant vector. The purified Tag5 24P4C12 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 Upid A, synthetic trehalose dicorynomycolate). In a typical protocol, rabbits are Initially immunized subcutaneously with up to 200 pg, typically 100-200 pg, 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 pg, typically 100-200 pg, 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. To test reactivity and specificity of immune serum, such as the rabbit serum derived from immunization with a KLH conjugated peptide encoding amino acids 1-14 of variant 1, the full-length 24P4C12 variant 1 cDNA is doned into pCDNA 3.1 myc-his or retroviral expression vectors (invitrogen, see the Example entitled "Production of Recombinant 24P4C12 in Eukaryotic Systems"). After transfection of the constructs Into 293T cells or transduction of PC3 with 24P4C1 2 retrovirus, cell lysates are probed with the anti-24P4C12 serum and with anti-His antibody (Santa Cruz Biotechnologies, Santa Cruz, CA) to determine specific reactivity to denatured 24P4C12 protein using the Western blot technique. As shown in Figures 24 and 25 the antiserum specifically recognizes 24P4C12 protein in 293T and PC3 cells. In addition, the immune serum is tested by fluorescence microscopy, flow cytometry, and immunohistochemistry (Figure 25) and immunopredpitation against 293T and other recombinant 24P4C12-expressing cells to determine specific recognition of native protein. Western blot, Immunoprecipitation, fluorescent microscopy, immunohistochemistry and flow cytometric techniques using ceUs that endogenously express 24P4C12 are also carried out to test reactivity and specificity. Anti-serum from rabbits immunized with 24P4C12 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 24P4C1 2 fusion protein encoding amino adds 379-453 of variant 1 Is first purified by passage over a column of GST protein covalendy coupled to AffiGel matrix (BioRad, Hercules, Caif.). The antiserum is then affinity purified by passage over a column composed of a MBP-fusion protein also encoding amino acids 379-453 covalently coupled to Affigel matrx. The serum Is then further purified by protein G affinity chromatography to isolate the IgG fracton. 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. Example 11: Generation of 24P4C12 Monoclonal Antibodies (mAbs) In one embodiment, therapeutic mAbs to 24P4C1 2 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 24P4C12 variants, for example those that would disrupt the interaction with Igands and substrates or disrupt its biological activity. Immunogens for generation of such mAbs Include those designed to encode or contain the entire 24P4C12 protein variant sequence, regions of the 24P4C12 protein variants predicted to be antigenic from computer analysis of the amino acid sequence (see, e.g., Figure 5, Figure 6, Figure 7, Figure 8, or Figure 9, and the Example entitled "Antigenicity Profiles"). immunogens indude peptides, recombinant bacterial proteins, and mammalian expressed Tag 5 proteins and human and urine IgG FC fusion proteins. In addition, cells engineered to express high levels of a respective 24P4C12 variant, such as 293T-24P4C12 variant i or 300.19-24P4C12 vacant Imurine Pre-B cells, are used to immunize mice. 94 To generate mAbs to 8 24P4C12 variant, mice are first immunized intraperitoneatly (IP) with, typically, 10-50 pg of protein immunogen or 107 24P4C12-expressing cells mixed In complete Freund's adjuvant Mice are then subsequently immunized IP every 2-4 weeks with, typically, 10-50 sg of protein immunogen or 107 cels mixed in incomplete Freund's adjuvant. Alternatively, MPL-TDM adjuvant is used in immunizations. In one embodment, mica were immunized as above with 300.19-24P4C12 cells In complete and then incomplete Freund's adjuvant, and subsequently sacrificed and the spleens harvested and used for fusion and hybridoma generation. As is can be seen in Figure 27, 2 hybridomas were generated whose antibodies specifically recognize 24P4C1 2 protein expressed in 293T cells by flow cytometry. 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 24P4C12 variant sequence Is used to immunize mice by direct injection of the plasmid DNA. In one embodiment, a Tag5 mammalian secretion vector encoding amino acids 59-227 of the variant 1 sequence (Figure 26) was used to immunize mice. Subsequent booster immunizations are then carded out with the purified protein. In another example, the same amino acids are cloned into an Fc-fusion secretion vector in which the 24P4C12 variant I sequence Is fused at the amino-terminus to an igK leader sequence and at the carboxyl-erminus 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 in combination with purified proteins as above and with cels expressing the respective 24P4C12 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, immunohistochemistryg 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 24P4C1 2 variant 8 specific monoclonal antibodies, a peptide encoding amino acids 643-654 (RNPITPTGHVFQ) (SEQ ID NO: 46) of 24P4C12 variant 8 is synthesized, coupled to KLH and used as immunogen. Balb C mice are initialy immunized intrapedtoneally with 25 pg of the KLH-24P4C1 2 variant 8 peptide mixed in complete Freund's adjuvant. Mice are subsequently immunized every two weeks with 25 pg of the antigen mixed in incomplete Freund's adjuvant for a total of three immunizations. ELISA using the free peptide determines the reactivity of serum from immunized mice. Reactivity and specificity of serum to fuU length 24P4C12 variant 8 protein is monitored by Western blotting, immunoprecipitation and flow cytometry using 293T cells transfected with an expression vector encoding the 24P4C1 2 variant 8 cDNA compared to cells transfected with the other 24P4C1 2 variants (see e.g., the Example entitled "Production of Recombinant 24P4C12 in Eukaryotic Systems). Other recombinant 24P4C12 variant 8-expressing cells or cells endogenously expressing 24P4C12 variant 8 are also used. Mice showing the strongest specific reactivity to 24P4C12 variant 8 are rested and given a final injection of 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 (Hariow and Lane, 1988). Supernatants from HAT selected growth wells are screened by ELISA, Western blot, immunoprecipitation, fluorescent microscopy, and flow cytometry to identify 24P4C12 variant 8-specific antibody-producing clones. A similar strategy is also used to derive 24P4C12 variant 9-specific antibodies using a peptide encompassing amino acids 379-388 (PLPTQPATLG) (SEQ ID NO: 47). The binding affinity of a 24P4C12 monoclonal antibody is determined using standard technologies. Affinity measurements quantify the strength of antibody to epitope binding and are used to help define which 24P4C1 2 monoclonal antibodies.preferred for diagnostic or therapeutic use, as appredated by one of skill in the art. The BlAcore system (Uppsala, Sweden) is a preferred method for determining binding affinity. The BlAcore system uses surface plasman resonance (SPR, Welford K. 1991, Opt. Quant. Elect 23:1; Morton and Myszka, 1998, Methods in Enzymology 295: 268) to 95 monitor bimolecular interactions in real time. BlAcore analysis conveniently generates association rate constants, dissociation rate constants, equilibrium dissociation constants, and affinity constants. Example 12: HLA Class I and Class il Binding Assays HLA class I and class 1i binding assays using purified HLA molecules are performed in accordance with disclosed protocols (e.g., PCT publications WO 94120127 and WO 94103205; Sidney et al., Current Protocols in Immunology 18.3.1 (1998); Sidney, et al., J. Immunol. 154:247 (1995); Sette, et al., Mol Immunol. 31:813 (1994)). Briefly, purified MHC molecules (5 to 500 nM) are incubated with various unlabeled peptide inhibitors and 1-10 nM '2l-radiolabeled probe peptides as described. Foiowing 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 HILA concentrations. Since under these conditions [labeI]<[HLA] and ICsomtHLA, the measured ICso values are reasonable approximations of the true Ko values. Peptide inhibitors are typically tested at concentrations ranging from 120 Ngmi to 1.2 ngtmt, 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 IC5o 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 motf-bearing peptides (see Table IV). Example 13: Identification of HLA Supermotif- and Motf-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 24P4C12 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 il supermotifs or motifs are performed as follows. 'AD translated 24P4C12 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 I 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: 96 "AG'= au x a2i xax...... xas where al is a coefficient which represents the effect of the presence of a given amino acid (i) 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 essentialy 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 j 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 at al., J. Mol. Biol. 267:1258-126, 1997; (see also Sidney el al., Human immunol. 45:79-93, 1996; and Southwood et al., J. Immuno. 160:3363 3373, 1998). Briefly, for all i positions, anchor and non-anchor alike, the geometric mean of the average relative binding (ARB) of all peptides carrying j is calculated relative to the remainder of the group, and used as the estimate of J. For Class I 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 supertve cross-reactive Deptides Protein sequences from 24P4C12 are scanned utilizing motif Identification software, to Identify 8-, 9- 10- and 11 mer sequences containing the HLA-A2-supermotii 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 to bind purified HLA-A*0201 molecules in vm (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 supermollf-bearino epitopes The 24P4C12 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 s 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-87 supermotif beadno evitopes The 24P4C12 protein(s) scanned above Is also analyzed for the presence of 8-, 9- 10-, or 1 1-mer peptides with the HLA-87-supermotif. Corresponding peptides are synthesized and tested for binding to HLA-8*070Z the molecule encoded by the most common B7-supertype allele (i.e., the prototype B7 supertype allele). Peptides binding 8*0702 with ICso 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, *5101, B*5301, and 8*5401). Peptides capable of binding to three or more of the five B7 supertype alleges tested are thereby identified. 97 Selection of Al and A24 motif-bearing epitopes To further increase population coverage, HLA-Al and -A24 epitopes can also be incorporated into vaccine compositions. An analysis of the 24P4C12 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 Immuno-geniclty Cross-reactive candidate CTL A2-supermotif-bearing peptides that are identified as described herein are selected to confirm In vftm immunogenicity. Confirmation is perfonned using the following methodology: Tsrqet 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 tine 721.221, is used as the peptide-loaded target to measure activity of HLA-A2.1-restricted CTL. This cell ine is grown In RPMI-1640 medium supplemented with antibiotics, sodium pyruvate, nonessential amino acids and 10% (vlv) 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 penlcilin/streptomycin). The monocytes are purified by plating 10 x 10s PBMClwell 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 supermatants. 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 nglml of GM-CSF and 1,000 UlmI of IL-4 are then added to each well. TNFa Is added to the DCs on day 6 at 75 ngiml and the cells are used for CTL induction cultures on day 7. Induction of CTL with DC and Peptide: CD8+ T-oells are isolated by positive selection with Dynal immunomagnedc beads (Dynabeads@ M-450) and the detacha-bead@ reagent Typically about 200-250x10 6 PBMC are processed to obtain 24x10 5 CD8+ T-cells (enough for a 48-well plate culture). Briefly, the PBMCs are thawed in RPMI with 30pgmi DNAse, washed once with PBS containing 1% human AB serum and resuspended In PBS/1% AB serum at a concentration of 20x10cells/ml. The magnetic beads are washed 3 times with PBSAB serum, added to the cells (140pl beads/20x0 cells) and incubated for 1 hour at 4"C with continuous mixing. The beads and cels are washed 4x with PBSAB serum to remove the nonadherent cells and resuspended at 100x10 cellsmil (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 6 /mi in the presence of 3pghnl R2- microglobuln for 4 hours at 20*C. The DC are then irradiated (4,200 rads), washed 1 time with medium and counted again. Setting up Induction culrs 0.25 ml cytokine-generated DC (at 1x105 cells/il) are co-cultured with 0.25mil of CD8+ T-cefls (at 2x0s cell/ml) In each well of a 48-well plate in the presence of 10 nglml of IL-7. Recombinant human IL-10 is added the next day at a final concentration of 10 ng/ml and human IL-2 Is added 48 hours later at iD IUlmi. . Resimulation of the Induction cultures with peptide-pulsed adherent cogs: Seven and fourteen days after the primary Induction, the cells are restimulated with peptide-pulsed aierent cells. The PBMCs are thawed and washed twice 98 with RPMI and ONAse. The cells are resuspended at 5x106 cells/mi 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 1Opg/ml of peptide in the presence of -3 pg/ml 8 2 microglobulin in 0.25ml RPMI/5%AB per well for 2 hours at 37*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-1O is added at a final concentration of 10 ng/ml and recombinant human 112 is added the next day and again 2-3 days later at 501U/ml (Tsai et a/., Crit/cal Reviews in Immunology 18(1-2):65-75, 1998). Seven days later, the cultures are assayed for CTL activity in a 5 1 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 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 5 1 C release. Seven days after the second restimulation, cytotoxicity is determined in a standard (5 hr) 1Cr release assay by assaying individual wells at a single E:T. Peptide-pulsed targets are prepared by incubating the cells with 1Opg/mi peptide overnight at 37 0 C. Adherent target cells are removed from culture flasks with trypsin-EDTA. Target cells are labeled with 20OpCi of 6 1 Cr sodium chromiate (Dupont, Wilmington, DE) for I hour at 37*C. 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 cel line used to reduce non specific lysis). Target cells (100 pl) and effectors (100p) are plated in 96 well round-bottom plates and incubated for 5 hours at 37*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 1 Cr release sample)/(cpm of the maximal 5 1 Cr release sample cpm of the spontaneous 5 '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 isdefined 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 Peptide-speeific and Endogenous Recognition Immulon 2 plates are coated with mouse anti-human IFNy monoclonal antibody (4 pg/mi 0.1M NaHCO3, pH8.2) overnight at 4'C. The plates are washed with Ca2, Mg 2 ,4ree PBS/0.05% Tween 20 and blocked with PBS/1 0% FCS for two hours, after which the CTLs (100 pIwell) and targets (100 pilwell) 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 1x1 06 cells/ml. The plates are incubated for 48 hours at 37'C with 5% C02. 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 pl of biolinylated mouse anti-human IFN gamma monoclonal antibody (2 microgramml in PBS/3%FCS0.05% 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 mlcroliter/well developing solution (TMB 1:1) are added, and the plates allowed to develop for 5-15 minutes. The reaction is stopped with 50 microlitertwell 1M H3P04 and read at 01D450. 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. 99 CTL Expansion. Those cultures that demonstrate specific lytic activity against pepide-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: 1x10 irradiated (4,200 rad) PBMC (autologous or allogeneic) per ml, 2x10 5 irradiated (8,000 rad) EBV- transformed cells per ml, and OKT3 (anti-CD3) at 30ng per nd in RPMI-1640 containing 10% (vlv) human AB serum, non-essential amino acids, sodium pyruvate, 25pM 2-mercaptoethanol, L-glutamine and penicilinistreptomycin. Recombinant human IL2 is added 24 hours later at a final concentration of 2001Ulml and every three days thereafter with fresh media at 50lU/ml. The cells are spit If the cell concentration exceeds 1x1O 6 nlm and the cultures are assayed between days 13 and 15 at E ratios of 30, 10, 3 and 1:1 in the s 1 Cr release assay or at 1x1 6 /ml In the in situ FNy 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 5x10' CD8' cells are added to a T25 flask containing the following: 1x10 autologous PBMC per ml which have been peptide-pulsed with 10 pg/ml peptide for two hours at 37C and Irradiated (4,200 rad); 2x10 5 irradiated (8,000 rad) EBV-transformed cells per ml RPMI-1640 containing 10%(v/v) human AB serum, non-essential AA, sodium pyruvate, 25mM 2-ME, L-glutamine and gentamicin. Immunogenicity of A2 supermotif-bearina neptides 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 spedfic CTI-s 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 24P4C12. 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/A1 I immunogenicity HLA-A3 supermotif-bearing cross-reactive binding peptides are also evaluated for rimunogenicity using methodology analogous for that used to evaluate the immunogenidty of the HLA-A2 supermotif peptides. Evaluation of B7 Immunoaenicit Immunogenidty 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-Al, HLA-A24 etc. are also confirmed using similar methodology Example 15: ImplementatIon of the Extended Supemotif to Improve the Binding Capacity of Native Epitopes by Creatine Analoas HLA motifs and supermotifs (comprising primary and/or secondary residues) are useful In the identification and preparation of higIhy cross-reacive 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.' Analooino at Primary Anchor Residues Peptide engineering strategies are implemented to further Increase the cross-reactivity of the epitopes. For example, the main andcors of A2-supemotif-bearing peptides are altered, for example, to Introduce a preferred L, 1, V. or M at position 2, and I or V at the C-terminus. 100 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 resticted by the capacity of the parent wild type (WT) peptide to bind at least weakly, i.e., bind at an ICso of 5000nM or less, to three of more A2 supertype alleges. The rationale for this requirement is that the Wr 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 a., J. Immunol. 157:2539, 1996; and Pogue ot aL., Proc. Nal. Acad. Sc. USA 92:8166,1995). In the cellular screening of these peptide analogs, it is important to confirm that analog-speclfic CTLs are also able to recognize the wild-type peptide and, when possible, target cels that endogenously express the epitope. Analoninq of HLA-A3 and B7-supermotif-bearinq neptides 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 S 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. 87 supermolif-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 supermof-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. Analocing at Secondary Anchor Residues Moreover, HLA supermolifs are of value In engineering highly cross-reactive peptides and/or peptides that bind HILA 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 P8MC from patients with 24P4C12 expressing tumors. Other analoging strategies 101 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 sufficently 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 24P4C12-derlved sequences with HLA-DR binding motifs Peptide epitopes bearing an HLA class i supermotif or motif are identified and confirmed as outlined below using methodology similar to that described for HLA Class I peptides. Selection of HLA-DR-suoernotif-bearino evitooes. To identify 24P4C12-derived, HLA dass i HTL epitopes, a 24P4C12 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 adds total). Protocols for predicting peptide binding to DR molecules have been developed (Southwood of al., J. Immunol. 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 of 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 DRI, DR4w4, and DR7, can efficiently select DR cross-reactive peptides. The 24P4C12-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: DRI, 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, DR5wI 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. 24P4C12-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 specifilty of the DR3 motif, peptides binding only to 'DR3 can also be considered as candidates for inclusion in a vaccine formulation. To elliclently Identify peptides that bind DR3, target 24P4C12 antigens are analyzed for sequences carrying one of the two DR3-specific binding motifs reported by Geluk et al. (J. Immunol. 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 i pM. Peptides are found that meet this binding criterion and qualify as HLA dass I high affinity binders. DR3 binding epitopes Identified in this manner are induded in vaccine compositions with DR supermotif-bearing peptide epitopes. 102 Similarly to the case of HLA dass I motif-bearing peptides, the class il 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 oflen improves DR 3 binding. Example 17: lmmunoaenlcitv of 24P4012-derlved HTL epitones This example determines immunogenic DR supermotif- and DR3 motif-bearing epitopes among those identified using the methodology set forth herein. Immunogeniaty of HTL epitopes are confirmed ina 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 viro primary induction using normal PBMC or 2.) recall responses from patients who have 24P4C1 2-expressing tumors. 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 vacdne 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 af)) (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=1-(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-od 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, Al, A31, A*3301, and A'6801. Although the A3-like supeutype 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 A0201, A*0202, A*0203, A0204, A*0205, A*0206, A*0207, A*6802, and A*6901. Finally, the B7-like supertype-confirmed alleles are: B7, B*3501-03, B51, B*5301, B'5401, B*5501-2, B*5601, B*6701, and 8*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 alleges are represented with an average frequency of 39% in these same ethnic populations. The total coverage across the major ethnicilles when Al and A24 are combined with the coverage of the A2-, A3- and 87-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 Il 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 of al., J Immunal. 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. 103 With a sufficient numberof epitopes (as disclosed herein and from the art), an average population coverage is predicted to be greater than 95% in each of fve major ethnic populations. The game theory Monte Carlo simulation analysis, which is known in the art (see e.g., Osborne, M.J. and Rubinsten, 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 Endogenouslv Processed Antlaens After Primina This example confinns 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 .supermotit-bearing epitopes, are re-stimulated in viftro using peptide-coated stimulator cells. Six days later, effector cells are assayed for cytotoxicity and the cell lines that contain peptide-specific cytotoxic activity are further re-stimulated. An additional sIx days later, these cell fines are tested for cytotoxic activity on 'ICr 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, L.e. cells that are stably transfected with 24P4C1 2 expression vectors. The results demonstrate (hat CTL lines obtained from animals primed with peptide epitope recognize endogenously synthesized 24P4C12 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*O201Kb transgenic mice, several other transgenic mouse models including mice with human All1, which may also be used to evaluate A3 epitopes, and B7 aleles 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 Conlunated Epitopes In Transgenic Mice This example Illustrates the induction of CTLs and HTLs in transgenic mice, by use of a 24P4C12-derived CTL and HTL peptide vaccine compositions. The vaccine composition used herein comprise peptides to be administered to a patient with a 24P4C12-expressing tumor. The peptide composition can comprise multiple CTL and/or HTL eitopes. 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. Immunizalion procedures: Immunization of transgenic mice is performed as described (Alexander et al., J. Immunal. 159:4753-4761, 1997). For example, A2/KO nice, which are ransgenic for the human HILA 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 tali) with a 0.1 ml of peptide In Incomplete Freund's Adjuvant, or if the peptide composition is a lipldated CTLJHTL 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 pepide. Cell nes: Target cells for peptide-specific cytotoxicity assays are Jurkat cells transfected with the HLA-A2.1/K chimeric gene (e.g., Vitiello et al., J. &p. Med. 173:1007,1991) 104 In vitro CTL activation: One week after priming, spleen cells (30x10 6 cellstflask) are co-cultured at 37*C with syngeneic, irradiated (3000 rads), peptide coated lymphoblasts (10x106 cells/flask) in 10 ml of culture mediumIT25 flask. After six days, effector cells are harvested and assayed for cytotoxic activity. Assay for cytotoxic activity: Target cells (1.0 to 1.5x10) are incubated at 37'C in the presence of 200 pl of 51Cr. After 60 minutes, cells are washed three times and resuspended in RIO medium. Peptide is added where required at a concentration of 1 pg/ml. For the assay, 104 5 1 Crlabeled 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'C, a 0.1 ml aliquot of 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 rdease)/(maximum release - spontaneous release). To facilitate comparison between separate CTL assays run under the same conditions, % 51Cr release data is expressed as lytic units/10 6 cells. One lylic unit is arbitrarily defined as the number of effector cells required to achieve 30% lysis of 10,000 target cells in a six hour 5 1 Cr release assay. To obtain specific lytic units1l 06, the lytic units/105 obtained in the absence of peptide Is subtracted from the lytic units/06 obtained in the presence of peptide. For example, if 30% 5'Cr release Is obtained at the effector (E): target (T) ratio of 50:1 (i.e., 5x105 effector cells for 10,000 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 entided "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 HTIL response is induced upon administration of such compositions. Example 21: Selection of CTL and KTIL epitopes for Inclusion in a 24P4C12-specific vaccine. This example ilustrates a procedure for selecting peptide epitopes for vaccine compositions of the Invention. The peptides In the composition can be In the form of a nuclelc 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 flowing principles are utilized when selecting a plurality of epitopes for Inclusion in a vaccine compositon. 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 24P4C12 clearance. The number of epitopes used depends on observations of patients who spontaneously clear 24P4C12. For example, If it has been observed that patients who spontaneously dear 24P4C12-expressing cals generate an immune response to at least three (3) epitopes from 24P4C12 antigen, then at least three epitopes should be included for HLA class -1. A similar rationale is used to determine HLA class 11 epitopes. Epitopes are often selected that have a binding affinitty of an ICso of500 nM or less for an HLA dass I moleule, or for dass 11, 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.govi. 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. 105 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 peplide 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 multiepitopic, peptide can be generated synthetically, recombinantly, or via cleavage from the native source. Altematively, 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 end 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 24P4C12, thus avoiding the 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 dears cells that bear or overexpress 24P4C12. Example 22: Construction of "Mininene" Multi-Epitope DNA Plasmids This example discusses the construction of a minigene expression plasmid. Minigene plasmids may, of course, contain various configurations of 8 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, -87 supermotif-bearing peptide epitopes and HLA-Al and -A24 motif-bearing peptide epitopes are used in conjunction with DR supermoif-bearing epitopes and/or DR3 epitopes. HLA class I supermotif or motif-bearing peptide epitopes derived 24P4C12, are selected such that multiple supermotifskmotifs are represented to ensure broad population coverage. Similarly, HLA class I epitopes are selected from 24P4C12 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 infusion 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 I protein may be fused to one or more HTL epilopes as described In the art, wherein the CLIP sequence of the U protein is removed and replaced with an HLA dass I epitope sequence so that HLA dass I epitope is directed to the endoplasmic reticulum, where the epitope binds to an HLA dass 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 mlnigene 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 disdosed herein. The sequence encodes an open reading frame fused to the Myc and His antibody eplitope tag coded for by the pcDNA 3.1 Myc-His vector. 106 Overlapping oligonudeotides that can, for example, average about 70 nudeotides in length with 15 nucleotide oveiaps, are synthesized and HPLC-purified. The oligonudeotides encode the selected peptide epitopes as well as appropriate tinker nudeotides, 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, anneaing temperature (50 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 pg of each of two oligonucleotides are annealed and extended: In an example using eight oligonucleotides, Le., four pairs of primers, oligonudeotides 1+2, 3+4, 5+6, and 7+8 are combined in 100 p1 reactions containing Pfu polymerase buffer (1x= 10 mM KCL, 10 mM (NH4)2SO4, 20 mM Tris-chlorde, 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. 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 vito by determining epitope presentation by APC following transduction or transfection of the APC with an epitope-expressing nucleic acid construct. Such a study determines 'antigenicity' 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 eptpe-HLA class I complexes on the cell surface. Quantitation can be perfomed by directly measuring the amount of peptide eluted from the APC (see, e.g., Sijts of al., J. ImmunoJ. 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 ilto 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 et al., immunity 1:751-761, 1994. For example, to confirm the capadty 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 (pepfide epitopes encoded in the minigene or the polyepitopic peptide), then assayed for peptide-specific cytotoxic activity In a 5'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 rninigene vaccine and polyepitopic vaccine. It is, therefore, found that the minigene elicits immune responses directed toward the HLA-A2 supennotif peptide epitopes as does the polyepitoplc 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-97 motif or supermotif epitopes, whereby it is also found that the mrilgene elicits appropriate Immune responses directed toward the provided epitopes. 107 To confirm the capacity of a class il 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-Abirestricted 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 cels, 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 at 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., Bamett at at., Aids Res. and Human Refroviruses 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 ef al., Vaccine 16:439 445,1998; Sedegah at al., Prc. Natl. Aced. Sci USA 95:7648-53,1998; Hanke and McMichael, Immunol. Letters 66:177 181, 1999; and Robinson et a., Nafure 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, A2.1A(b transgenic mice are immunized IM with 100 pg of a DNA minigene encoding the 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 pfulmouse 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 vaccinla 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 EUSPOT assay. Additionally, splenocytes are stimulated in vfro with the A2-restricted peptide epitopes encoded in the minigene and recombinant vaccinia, then assayed for peptide-specific activity in an alpha, beta andlor 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-A1 1 or HLA-87 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 inductionn 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 24P4C12 expression in persons who are at risk for tumors that bear this antigen. For example, a polyepitopic peptide epitope composition (or a nudelc add 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 IndMduals at risk for a 24P4C12-assodated 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- Ito about 50,000 pg, generally 100-5,000 pg, 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 24P4C12-associated disease. Alternatively, a composition typically comprising transfecing agents is used for the administration of a nudelc: add based vaccine in accordance with methodologies known in the art and disclosed herein. 108 Example 25: Polyepitopic Vaccine Compositions Derived from Native 24P4C12 Sequences A native 24P4C1 2 polyprotein sequence is analyzed, preferably using computer algorithms defined for each class I and/or class I supermotif or motif, to identify 'relatively shor" 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 pepfide, 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 24P4C12 antigen and at least one HTL epitope. This polyepitopic native sequence is administered either as a peptide or as a nucleic acid sequence which encodes the pepide. Alternatively, an analog can be made of this native sequence, whereby one or more of the epitopes comprise substitutions that alter the cross-reacvity and/or binding affinity properties of the polyepitopic peptide. The embodiment of this example provides for the possiblity 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. Additonally, 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 24P4C12, 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: Polvepitopic Vaccine Compositions from Multiple Antiens The 24P4C1 2 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 24P4C12 and such other antigens. For example, a vaccine composition can be provided as a single polypepUde that Incorporates multiple epitopes from 24P4C12 as well as tumor-associated antigens that are often expressed with a target cancer associated with 24P4C12 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 vito. 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 HTI. directed to 24P4C12. Such an analysis can be performed in a manner described by Ogg at 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. 109 In this example highly sensitive human leukocyte antigen tetrameric complexes (tetramers") are used for a cross sectional analysis of, for example, 24P4C12 HLA-A*0201-specific CTL frequencies from HLA A*0201-positive individuals at different stages of disease or following immunization comprising a 24P4C12 peptide containing an A'0201 motif. Tetrameric complexes are synthesized as described (Musey et al., N. Eng. 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, 2-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 tetraimer-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 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 readly indicating the extent of Immune response to the 24P4C1 2 epitope, and thus the status of exposure to 24P4C12, or exposure to a vaccine that elicits a protective or therapeutic response. Example 28: Use of Peotlde Elptopes 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 24P4C12-associated disease or who have been vaccinated with a 24P4C1 2 vaccine. For example, the class I restricted CTL response of persons who have been vaccinated may be analyzed. The vaccine may be any 24P4C12 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 Ficoli-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 (500/mt), 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 I pg/ml to each well as a source of T cel help during the first week of stimulation. In the migroculture 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/mI final concentration of rlL-2 are added to each wel. On day 7 the cultures are transferred into a 96-well fiat-bottom plate and restimulated with peptide, rL-2 and 105 Irradiated (3,000 red) 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 stCr release, based on comparison with non-diseased control subjects as previously described (Rehermann, at at., Nature Med. 2:1104,1108, 1996; Rehermann et aL, J. lIn. Invest. 97:1655-1665, 1996; and Rehernann et al. J. Clin. Invest. 98:1432 1440,1996). 110 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, ef a/. J. WIo. 66:2670-2678, 1992). Cytotoxicity assays are performed in the following manner. Target cells consist of either aflogenele 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 5 'Cr release assay using U-bottomed 96 well plates containing 3,000 targets/well. Stimulated PBMC are tested at effectorltarget (Err) 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-resricted CTL populations have been stimulated by previous exposure to 24P4C12 or a 24P4C12 vaoine. Similarly, Class il restricted HTL responses may also be analyzed. Purified PBMC are cultured in a 96-well flat bottom plate at a density of 1.5x10 5 cells/we and are stimulated with 10 pg/mI synthetic peptlde of the invention, whole 24P4C12 antigen, or PHA. Cels 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 1OUknl 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 3

H

thymidine Incorporation In the presence of antigen divIded by the 3H-thymldlne incorporation in the absence of antigen. Example 29: Induction Of Specific CTL Response In Humans A human clinical rial for an immunogenic composition comprising CTL and HTL epitopes of the invention is set up as an IND Phase 1, dose escalation study and carried out as a randomized, double-Wind, 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 pg of peptide composition; Group 11: 3 subjects are Injected with placebo and 6 subjects are Injected with 50 pg peptide composition; Group 1I1: 3 subjects are injected with placebo and 6 subjects are injected with 500 pg 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 peplide 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 dinical 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. 111 Example 30: Phase || Trials In Patients Expressinq 24P4C12 Phase I trials are performed to study the effect of administering the CTL-HTL peptide compositions to patients having cancer that expresses 24P4C1 2. The main objectives of the trial are to determine an effective dose and regimen for inducing CTLs in cancer patients that express 24P4C12, to establish the safety of Inducing a CTL and HTL response in these patients, and to see to what extent activation of CTILs improves the dinical 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 reversibiity) 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 24P4C12. Clinical manifestations or antigen-specific T-cell responses 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 24P4C12 associated disease. Example 31: Induction of CTL Responses Usinq 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 peptide mixture 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 nudelc 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 pg) 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 fowIpox virus administered at a dose of 5-101 to 5x10 9 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 we 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 24P4C12 is generated. Example 32: Administration of Vaccine Compositions Usina 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 vfo. 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 vvo. The Induced CTL 112 and HTL then destroy or facilitate destruction, respectively, of the target cells that bear the 24P4C12 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 ProgenipoieUnT (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 100 DC per patient are typically administered, larger number of DC, such as 107 or 10 can also be provided. Such cell populations typically contain between 50-90% DC. In some embodiments, peptide-loaded PBMC are injected into patients without purification of the DC. For example, PBMC generated after treatment with an agent such as Progenipoietiny" are Injected into patients without purification of the DC. The lotal 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 immunoluorescence analysis with specific anti-DC antibodies. Thus, for example, if Progenipoietin'm 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 Progenlpoietin 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 CTLHTL responses Alternatively, ex vivo CTL or HTL responses to 24P4C1 2 antigens can be induced by incubating, in tissue culture, the patients, 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 faciitate destruction (HTL) of their specific target cells, I.e., tumor cells. Example 33: An Alternative Method of Identifying and Confirming Motif-Bearina 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 cels express only a single type of HLA molecule. These cells can be transfected with nucleic acids that express the antigen of Interest, e.g. 24P4C12. Peptides produced by endogenous antigen processing of peptides produced as a result of transfectiori will then bind to HLA molecules within the cel 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 ef at., J. Immuno. 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 nuclelc acids that encode 24P4C12 to isolate peptides corresponding to 24P4C12 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 cel. 113 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 Polynucleotldes Sequences complementary to the 24P4C12-encoding sequences, or any parts thereof, are used to detect, decrease, or inhibit expression of naturally occurring 24P4C12. 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 24P4C1 2. 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 24P4C1 2-encoding transcript. ExamPle 35: Purification of Naturally-occurrina or Recombinant 24P4C12 Usina 24P4C12-Specflc Antibodies Naturally occurring or recombinant 24P4C12 is substantially purified by immunoaffinity chromatography using antibodies specific for 24P4C12. An immunoaffinity column is constructed by covalently coupling anti-24P4C12 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 24P4C12 are passed over the Immunoaffinity column, and the column Is washed under conditions that allow the preferential absorbance of 24P4C12 (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/24P4C12 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 24P4C12 24P4C12, or biologically active fragments thereof, are labeled with 1211 Bolton-Hunter reagent (See, e.g., Bolton at a. (1973) Biochem. J. 133:529.) Candidate molecules previously arrayed In the wells of a multi-well plate are incubated with the labeled 24P4C12, washed, and any welts with labeled 24P4C12 complex ere assayed. Data obtained using different concentrations of 24P4C1 2 are used to calculate values for the number, affinity, and association of 24P4C12 with the candidate molecules. Example 37: In Vvo Assay for 24P4C12 Tumor Growth Promotion The effect of the 24P4C1 2 protein on tumor cell growth is evaluated in vivo by evaluating tumor development and growth of cels expressing or lacking 24P4C12. For example, SCID mice are injected subcutaneously on each lank with I x 106 of either 3T3, prostate, colon, ovary, lung, or bladder cancer cell lines (e.g. PC3, Caco, PA-1, CaLu or J82 cells) containing tkNeo empty vector or 24P4C12. At least two strategies may be used: (1) Constitutive 24P4C12 expression under regulation of a promoter, such as a constitutive promoter obtained from the genomes of viruses such as polyoma virus, fowIpox virus (UK 2,211,504 published 5 July 1989), adenovirus (such as Adenovirus 2), bovine paplloria 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 inmunoglobulin 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, tetracycline, etc., provided such promoters are compatible with the host cell systems. Tumor volume is then monitored by caliper 114 F measurement at the appearance of palpable tumors and followed over Ume to determine if 24P4C12-expressing cells grow at a faster rate and whether tumors produced by 24P4C1 2-expressing cells demonstrate characteristics of altered aggressiveness (e.g. enhanced metastasis, vascularization, reduced responsiveness to chemotherapeutic drugs). As shown in figure 31 and Figure 32, 24P4C12 has a profound effect on tumor growth in SCID mice. The prostate cancer cells PC3 and PC3-24P4C1 2 were injected subcutaneously In the right flank of SCID mice. Tumor growth was evaluated by caliper measurements. An Increase in tumor growth was observed in PC3-24P4C12 tumors within 47 days of injection (fig 31). In addition, subcutaneous injection of 3T3-24P4C12 Induced tumor formation in SCID mice (Figure 32). This finding is significant as control 3T3 cells fail to form tumors, indicating that 24P4C12 has several tumor enhancing capabilities, induding transformation, as well as tumor Initiation and promotion. Example 38: 24P4C12 Monoclonal Antibody-mediated Inhibition of Prostate Tumors in Vivo. The significant expression of 24P4C12 in cancer tissues, together with Its restrictive expression In normal tissues and cell surface localization, make 24P4C12 a good target for antibody therapy. Similarly, 24P4C12 is a target for T cell based immunotherapy. Thus, the therapeutic efficacy of anti-24P4C12 mAbs In human prostate cancer xenograft mouse models is evaluated by using recombinant cell lines such as PC3-24P4C12, and 3T3-24P4C12 (see, e.g., Kaighn, M.E., et al., Invest Urol, 1979. 17(1): p. 16-23), as well as human prostate xenograft models such as LAPC9 (Saffran et al, Proc Natl Acad Sci U S A. 2001, 98:2658). Simlarly, anti-24P4C12 mAbs are evaluated in xenograft models of human bladder cancer colon cancer, ovarian cancer or lung cancer using recombinant cell lines such as J82-24P4C12, Caco-24P4C12, PA 24P4C1 or CaLu-24P4C12, respectively. Antibody efficacy on tumor growth.and metastasis formation is studied, e.g., in a mouse orthotopic bladder cancer xenograft model, and a mouse prostate cancer xenograft model. The antibodies can be unconjugated, as discussed in this Example, or can be conjugated to a therapeutic modality, as appreciated in the art. Anti-24P4C12 mAbs inhibit formation of prostate and bladder xenografts. Anti-24P4C12 mAbs also retard the growth of established orthotoplc tumors and prolonged survival of tumor-bearing mice. These results indicate the utility of anti-24P4C12 mAbs in the treatment of local and advanced stages of prostate, colon, ovarian, lung and bladder cancer. (See, e.g., Saffran, D., el al., PNAS 10:1073-1078 or www.pnas.org/ogi/dol/10. 1073/pnas.051624698). Administration of the anti-24P4C12 mAbs led 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 24P4C12 as an attractive target for Immunotherapy and demonstrate the therapeutic potential of ani-24P4C12 mAbs for the treatment of local and metastatic cancer. This example demonstrates that unconjugated 24P4C12 monoclonal antibodies are'effective to inhibit the growth of human prostate, colon, ovarian, lung and bladder cancer tumor xenografts grown in SCID mice; accordingly a combination of such efficacous monoclonal antibodies is also effective. Tumor inhibition using multiple unconjugated 24P4C12 mAbs Materials and Methods 24P4C1 2 Monoclonal Antibodies: Monoclonal antibodies are raised against 24P4C12 as described in the Example entitled 'Generation of 24P4C12 Monoclonal Antibodies (mAbs)." The antibodies am characterized by ELISA, Western blot FACS, and immunoprecipitation for their capacity to bind 24P4C12. Epitope mapping data for the anti-24P4C12 mAbs, as determined by EUSA and Western analysis, recognize epltopes on the 24P4C12 protein. lmmunohlstochemical analysis of prostate cancer tissues and cells with these antibodies is performed, 115 The monoclonal antibodies are purified from ascites or hybridoma tissue culture supematants by Protein-G Sepharose chromatography, dialyzed against PBS, filter sterilized, and stored at -20 0 C. Protein determinations are performed by a Bradford assay (Blo-Rad, Hercules, CA). A therapeutic monoconal 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 SCABER, J82, A498, 769P, CaOvi or PA1 tumor xenografts. Cell Lines The prostate, colon, ovarian, lung and bladder cancer carcinoma cell lines,, Caco, PA-1, CaLu or J82 cells as well as the fibroblast line NIH 3T3 (American Type Culture Collection) are maintained in media supplemented with L-glutamine and 10% FBS. PC3-24P4C12, Caco-24P4C12, PA-24P4C12, CaLu-24P4C12 or J82.24P4C12 cells and 3T3-24P4C12 cell populations are generated by retroviral gene transfer as described in Hubert, R.S., et al., Proc Nati Acad Sci U S A, 1999. 96(25): 14523. Xenograft Mouse Models. Subcutaneous (s.c.) tumors are generated by injection of 1 x 10 6 cancer 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. Tumor sizes are determined by 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. Orthotopic Injections are performed under anesthesia by using ketamine/xylazine. For bladder orthotopic studies, an incision is made through the abdomen to expose the bladder, and tumor cells (5 x 105) mixed with Matrigel are injected into the bladder wall In a 10-pl volume. To monitor tumor growth, mice are palpated and blood Is collected on a weekly basis to measure BTA levels. For prostate orthopotic models, an incision is made through the abdominal musces to expose the bladder and seminal vesicles, which then are delivered through the incision to expose the dorsal prostate. Tumor cells e.g. LAPC-9 cells (5 x 10) mixed with Mabigel are injected into the prostate in a 10-pi volume (Yoshida Yet al, Anticancer Res. 1998,18:327: Ahn et al, Tumour Biol. 2001, 22:146). To monitor tumor growth, blood is collected on a weekly basis measuring PSA levels. Similar procedures are followed for lung and ovarian xenograft models. The mice are segregated Into groups for the appropriate treatments, with anti-24P4C12 or control mAbs being injected i.p. Anti-24P4C12 mAbs Inhibit Growth of 24P4C1 2-Expressino Xenograft-Cancer Tumors The effect of anti-24P4C12 mAbs on tumor formation is tested on the growth and progression of bladder, and prostate cancer xenografts using PC3.24P4C12, Caco-24P4C12, PA-24P4C12, CaLu-24P4C12 or J82-24P4C12 orthotopic models. As compared with the s.c. tumor model, the orthotopic model, which requires injection of tumor cells directly in the mouse prostate, colon, ovary, lung and bladder, 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, K, 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 slowed us to follow the therapeutic effect of mAbs on clinically relevant end points. Accordingly, tumor cells are Injected Into the mouse organs, and 2 days later, the mice are segregated into two groups and treated with either a) 200-500pg, of anti-24P4C12 Ab, or b) PBS three times per week for two to ive weeks. A major advantage of the orthotopic cancer models Is the ability to study the development of metastases. Formation of metastasis in mice bearing established orthotopic turnors is studies by IHC analysis on lung sections using an 116 antibody against a tumor-specific cell-surface protein such as antl-CK20 for bladder cancer, anti-STEAP-1 for prostate cancer models (Lin S et al, Cancer Detect Prev. 2001;25:202; Saffran, D., et al., PNAS supra). Mice bearing established orthotopic tumors are administered 10OOpg injections of either anti-24P4C12 mAb or PBS over a 4-week period. Mice in both groups are allowed to establish a high tumor burden, to ensure a high frequency of metastasis formation In mouse lungs. Mice then are kiled and their bladders, livers, bone and lungs are analyzed for the presence of tumor cels by IHC analysis. These studies demonstrate a broad anti-tumor efficacy of anti-24P4C12 antibodies on initiation and progression of prostate and kidney cancer in xenograft mouse models. Anti-24P4C1 2 antibodies inhibit tumor formation of tumors as well as retarding the growth of already established tumors and prolong the survival of treated mice. Moreover, anti-24P4C1 2 mAbs demonstrate a dramatic inhibitory effect on the spread of local bladder and prostate tumor to distal sites, even in the presence of a large tumor burden. Thus, anti-24P4C12 mAbs are efficacious on major clinically relevant end points (tumor growth), prolongation of survival, and health. Example 39: Therapeutic and Diagnostic use of Anti-24P4C12 Antibodles in Humans, Anti-24P4C1 2 monoclonal antibodies are safely and effectively used for diagnostic, prophylactic, prognostic and/or therapeutic purposes in humans. Westem blot and immunohistochemical analysis of cancer tissues and cancer xenografts with anti-24P4C12 mAb show strong extensive staining in carcinoma but significantly lower or undetectable levels in normal tissues. Detection of 24P4C12 in carcinoma and in metastatic disease demonstrates the usefulness of the mAb as a diagnostic and/or prognostic indicator. Anti-24P4C12 antibodies are therefore used in diagnostic applications such as immunohistochemistry of kidney biopsy specimens to deted cancer from suspect patients. As determined by flow cytometry, anti-24P4C12 mAb specifically binds to carcinoma cells. Thus, anti-24P4C12 antibodies are used In diagnostic whole body imaging applications, such as radiolmmunoscintigraphy 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 24P4C1 2. Shedding or release of an extracellular domain of 24P4C12 Into the extracellular milieu, such as that seen for alkaline phosphodiesterase 810 (Meerson, N. R., Hepatology 27:563-568 (1998)), allows diagnostic detection of 24P4C12 by anti-24P4C12 antibodies in serum and/or urine samples from suspect patients. Anti-24P4C12 antibodies that specifically bind 24P4C1 2 are used in therapeutic applications for the treatment of cancers that express 24P4C12. Anti-24P4C12 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 antU-24P4C12 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 "24P4C1 2 Monoclonal Antibody-mediated Inhibition of Bladder and Lung Tumors In VWo"). Either conjugated and unconjugated anti-24P4C12 antibodies are used as a therapeutic modality in human einical 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-24P4C12 Antibodies n vi yo Antibodies are used in accordance with the present Invention which recognize an epitope on 24P4C12, and are used In the treatment of certain tumors such as those listed in Table 1. Based upon a number of factors, including 24P4C12 expression levels, tumors such as those listed in Table I are presently preferred indications. In connection with each of these indications, three cinicat approaches are successfully pursued. 117 I.) Adjunctive therapy: In adjunctive therapy, patients are treated with anti-24P4C1 2 antibodies in combination with a chemotherapeutic or antineoplastic agent and/or radiation therapy. Primary cancer targets, such as those listed in Table 1, are treated under standard protocols by the addition anti-24P4C12 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-24P4C12 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). 11.) Monotherapy In connection with the use of the anti-24P4C12 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. Ill.) Imaging Agent Through binding a radionuclide (e.g., iodine or yttrium (1131, Y9) to anti-24P4C12 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 wel as, metastatlc lesions of cells expressing 24P4C1 2. In connection with the use of the anti-24P4C12 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 (M ln)-24P4C12 antibody is used as an imaging agent in a Phase I human clinical trial in patients having a carcinoma that expresses 24P4C12 (by analogy see, e.g., Divgl 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-24P4C12 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-24P4C12 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-24P4C12 antibodies that are fully human antibodies, as compared to the chimeric antibody, have slower dearance; accordingly, dosing in patients with such fully human anti-24P4C12 antibodies can be lower, perhaps In the range of 50 to 300 mgkn2, and still remain efficacious. Dosing In mghn 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 al sizes from infants to adults. Three distinct delivery approaches are useful for delivery of anti-24P4C12 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 dearance of the antibody. Clinical Development Plan (CDP) Overview. The CDP follows and develops treatments of anti-24P4C12 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-24P4C12 antibodies. As will 118 be appreciated, one criteria that can be utilized in connection with enrollment of patients is 24P4C12 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 inmunogenic 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 24P4C12. Standard tests and follow-up are utilized to monitor each of these safety concerns. Anti-24P4C12 antibodies are found to be safe upon human administration. Example 41: Human Clinical Trial Adlunctive Therapy with Human Antl-24P4C12 Antibody and Chemotherapeutic Agent A phase I human cinical trial is initiated to assess the safety of six intravenous doses of a human anti-24P4C12 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 of single doses of anti-24P4C12 antibodies when utilized as an adjunctive therapy to an antineoplastic or chemotherapeutic agent as defined herein, such as, without limitation: cisplatin, topotecan, doxorubidn, adriamycin, taxol, or the like, is assessed. The trial design incuded delivery of six single doses of an anti-24P4C1 2 antibody with dosage of antibody escalating from approximately about 25 mg/n 2 to about 275 mg/m 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 mghn 2 mgm 2 mgn 2 mg rn 2 mg/m 2 mg/m 2 Chemotherapy 4 + + + + + (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, (ii) toxicity to normal cells that express 24P4C12. Standard tests and follow-up are utilized to monitor each of these safety concerns. Patients are also assessed for dinical outcome, and particularly reduction In tumor mass as evidenced by MRI or other imaging. The anti-24P4C12 antibodies are demonstrated to be safe and efficacious, Phase 11 trials confirm the efficacy and refine optimum dosing. Example 42: Human Clinical Trial: Monotherapy with Human Antl-24P4CI2 Antibody Anti-24P4C1 2 antibodies are safe in connection with the above-discussed adjunctive trial, a Phase 11 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-24P4C12 antibodies. Example 43: Human Clinical Trial: Diannostic Imaging ith Anti-24P4C12 Antibody Once again, as the adjunctive therapy discussed above Is safe within the safety criteria discussed above, a human cinical trial is conducted concerning the use of anti-24P4C1 2 antibodies as a diagnostic imaging agent The protocol is 119 designed in a substantially similar manner to those described in the art, such as in Divgi et al. J. Nail. Cancer tnst. 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 24P4C12 to Known Senuences The 24P4C1 2 protein of Figure 3 has 710 amino acids with calculated molecular weight of 79.3 kDa, and pl of 8.9. Several variants of 24P4C12 have been identified, induding 4 SNPs (namely v.1, v.3, v.5, v.6) and 3 splice variants (namely v.7, v.8 and v.9) (figures 10 and 11). 24P4C12 variants v.3, v.5, and v.6 differ from 24P4C12 v.1 by 1 amino acid each, at aa positions 187, 326 and 436, respectively. Variant v.7 carries a deletion of 111 aa long starting at aa 237, while variant v.8 and v.9 contain insertions at as 642 and 378, respectively. The 24P4C12 protein exhibits homology to a previously cloned human gene, namely NG22 also known as chorine transporter-like protein 4 (gi 14249468). It shows 99% identity and 99% homology to the CTL4 protein over the length of that protein (Figure 4). 24P4C1 2 is a multi-transmembrane protein, predicted to carry 10, 11 or 13 transmembrane domains. Bloinformatic analysis Indicates that the 24P4C12 protein localizes to the plasma membrane with some endoplasmic reticulum localization (see Table 1). Recent evidence indicates that the 24P4C1 2 protein is a 10 transmembrane protein that localizes to the cell surface (O'Regan S et al PNAS 2000, 97:1835). Choline as an essential component of cell membranes that plays an important role in cell integrity, growth and survival of normal and tumor cells. Choline accumulates at increased concentration In tumor cels relative to their normal counterparts and as such constitutes a tool for the detection of cancer cells by magnetic resonance imaging (Kurhanewicz J et al, J Magn Reson Imaging. 2002.). In addition to its role in maintaining membrane integrity, choline mediates signal transduction event from the membrane to the nucleus (Spiegel S, Milstien S. J Membr Biol. 1995,146:225). Choline metabolites include sphingosylphosphorycholine and lysophosphatidylcioline, both of which activate G-protein coupled receptors (Xu Fetal Blochim Blophys Acta 2002,1582-81). In addition, choline results in the activation of kinase pathways Induding Raf-i (Lee M, Han SS, Cell Signal 2002,14:373.). Choline also plays a role in regulating DNA methytation and regulation of gene expression. For example, choline methabolites regulate the expression of cytokines and chemokines essential for tumor growth (Schwartz BM et al, Gynecol Oncol. 2001, 81:291; Denda A at al, Carcinogenesis. 2002, 23:245). Due to its effect on cell signaling and gene expression, choline controls cell growth and survival (Holmes-McNary MOet al, J Biol Chem. 2001, 276:41197; Albright et al, FASEB 1996,10:510). Choline deficiency results in cel death, apoptosis and transformation, while accumulation of choline Is associated with tumor growth (Zelsel S et a], Carcinogenesis 1997, 18:731). eAcordingly, when 24P4C1 2 functions as a regulator of tumor formation, cell proliferation, invasion or cell signaling, 24P4C12 is used for therapeutic, diagnostic, prognostic and/or preventative purposes. Example 45: 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). In particular, choline have been reported to activate MAK cascades as wel as G proteins, and been associated with the DAG and ceramide and sphingophosphorylchollne signaling pathway (Cummings et al, above). In addition, choline transmit its signals by regulating choline-kinase and phospholipase activity, .:-resulting in enhance tumorigenic effect (Ramirez et al, Onoogene. 2002, 21:4317; Lucas et al, Oncogene. 2001, 20-.1 110; Chung T at al, Cell Signal. 2000, 12:279). Using immunoprecipitation and Westem blotting techniques, proteins are identified that associate with 24P4C1 2 and mediate signaling events. Several pathways known to play a role in cancer biology can be regulated by 24P4C12, including phospholipid pathways such as P13K, AKT, etc, adhesion and migration pathways, including FAK, Rho, RaO-1, etc, as well as mitogenidsurvival 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). Using Western blotting and other techniques, the ability of 120 24P4C12 to regulate these pathways is confirmed. Cells expressing or lacking 24P4C12 are either left untreated or stimulated with cytokines, androgen and anti-integrin antibodies. Cell lysates are analyzed using anti-phospho-spedlic antibodies (Cell Signaling. Santa Cruz Biotechnology) in order to detect phosphorylation and regulation of ERK, p3B, AKT, P13K, PLC and other signaling molecules. To confirm that 24P4C12 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. NFkB4uc, NFkB/Rel; Ik-kinase/SAPK; growthlapoptosis/stress 2. SRE-luc, SRFITCFIELK1; MAPKlSAPK; growth/differentiation 3. AP-1-uc, FOS/JUN; MAPKJSAPK/PKC; growth/apoptosls/stress 4. ARE-luc, androgen receptor; steroids/MAPK; growth/differentiation/apoptosis 5. p534uc, p53; SAPK; growth/differentiation/apoptosis 6. CRE-luc, CREB/ATF2; PKAlp38; growth/apoptosis/stress 7. TCF4uc, TCF/Lef; 5-catenin, Adhesionlinvaslon 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 tudferin substrate and luminescence of the reaction is monitored in a luminometer. Signaling pathways activated by 24P4C12 are mapped and used for the identification and validation of therapeutic targets. When 24P4C12 is involved in cell signaling, it is used as target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 46: 24P4C12 Functions as a Choline transporter Sequence and homology analysis of 24P4C12 Indicate that 24P4C12 carries a transport domain and that 24P4C12 functions as a choline transporter. In order to confirm that 24P4C12 transports choline, primary and tumor cells, indudeing prostate, colon, bladder and lung lines, are grown In the presence and absence of 3 H-choline. Radioactive choline uptake is measured by counting incorporated counts per minutes (cpm). Parental 24P4C12 negative cells are compared to 24P4C12 expressing cels using this and similar assays. Similarty, parental and 24P4C12-expressing cells can be compared for chollne content using NMR spectroscopy. These assay systems can be used to identify small molecules and antibodies that interfere with choline uptake and/or with the function of 24P4C12. Thus, compounds and small molecules designed to Inhibit 24P4C1 2 function and downstream signaling events are used for therapeutic diagnostic, prognostic and/or preventative purposes. Example 47: Reaulation of Transcription The cell surface localization of 24P4C12 and its ability to regulate DNA methylation Indicate that it 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 24P4C12. For this purpose, two types of experiments are performed. 121 In the first set of experiments, RNA from parental and 24P4C1 2-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, pheromones, or growth factors are compared. Differentially expressed genes are identified in accordance with procedures known in the art. The differentialy 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 acivation is evaluated using commercially available (Stratagene) luciferase reporter constructs Induding: NFkB-luc, SRE-luc, ELK1-luc, ARE-luc, p53-tuc, 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, 24P4C12 plays a role in gene regulation, and it is used as a target for diagnostic, prognostic, preventative and/or therapeutic purposes. Example 48: Involvement in Tumor Proaression The 24P4C1 2 gene can contribute to the growth of cancer cells. The role of 24P4C12 in tumor growth is confirmed in a variety of primary and transfected cell lines including prostate, and bladder cell lines, as well as NIH 3T3 cells engineered to stably express 24P4C12. Parental cells lacking 24P4C12 and cells expressing 24P4C12 are evaluated for cell growth using a well-documented proliferation assay (Fraser SP, et al., Prostate 2000;44:61, Johnson DE, Ochieng J, Evans SL Anticancer Drugs. 1996, 7:288). Such a study was performed on prostate cancer cells and the results are shown in figure 28. The growth of parental PC3 and PC3-24P4C12 oelis was compared in low (0.1%) and 10% FBS. Expression of 24P4C12 Imparted a growth advantage to PC3 cells grown in 10% FBS. Similarly, expression of 24P4C12 in NIH-3T3 cells enhances the proliferation of these cells relative to control 3T3-neo cells. The effect of 24P4C1 2 can also be observed on cell cycle progression. Control and 24P4C12-expressing cells are grown in low serum ovemight and treated with 10% FBS for 48 and 72 hrs. Cells are analyzed for BrdU and propidium Iodide Incorporation by FACS analysis. To confirm the role of 24P4C12 in the transformation process, Its effect In colony forming assays is investigated. Parental NIH-3T3 cells lacking 24P4C12 are compared to NIH-3T3 cells expressing 24P4C12, 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 24P4C12 in Invasion and metastasis of cancer cells, a well-established assay is used. A non-limiting example is the use of an assay which provides a basement membrane or an analog thereof used to detect whether cells are invasive (e.g., a Transwell Insert System assay (Becton Dickinson) (Cancer Res. 1999; 59:6010)). Control cels, Including prostate, and bladder cell lines lacking 24P4C12 are compared to cells expressing 24P4C12. Cells are loaded with the fluorescent dye, calcein, and plated in the top well of a support structure coated with a basement membrane analog (e.g. the Transwell Insert) and used In the assay. Invasion Is determIned by fluorescence of cells In the lower chamber relative to the fluorescence of the entire cell population. 24P4C12 can also play a role in cell cycle and apoptosis. Parental celis and cells expressing 24P4C12 are compared for differences in cell cycle regulation using a we-established rdU 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 Gi, S, and G2M phases of the ceil cycle. Alternatively, the effect of stress on apoptosis Is evaluated in control parental cells and cels expressing 24P4C12, Including normal and tumor prostate, colon and lung cells. Engineered and parental cells are treated with various chemotherapeutic agents, such as etoposide, futamide, etc, and protein synthesis inhibitors, such as cycloheximide. Cells 122 are stained with annexin V-FITC and cell death is measured by FACS analysis. The modulation of cell death by 24P4C12 can play a critical role in regulating tumor progression and tumor load. When 24P4C1 2 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 Antiogenesis Angiogenesis or new capilary 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, 24P4C1 2 plays a role In angiogenesis (DeFouw L et 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 endotheat cell tube formation and endothelial cell prolferation. Using these assays as well as in vitro neo-vascularization, the role of 24P4C12 In anglogenesis, enhancement or inhibition, is confirmed. For example, endotheflial cells engineered to express 24P4C12 are evaluated rising tube formation and proliferation assays. The effect of 24P4C12 is also confirmed In animal models in vivo. For example, cells either expressing or lacking 24P4C12 are implanted subcutaneously in immunooompromised mice. Endothellal cell migration and angiogenesis are evaluated 5-15 days later using immunohistochemistry techniques. 24P4C1 2 affects angiogenesis and it is used as a target for diagnostic, prognostic, preventative andlor therapeutic purposes. Example 50: Involvement In Adhesion Cell adhesion plays a critical role in tissue colonization and metastasis. The presence of leucine rich and cysteine rich motifs in 24P4C12 is indicative of its role in cell adhesion. To confirm that 24P4C12 plays a role in cell adhesion, control cells tacking 24P4C12 are compared to cels expressing 24P4C12, using techniques previously described (see, e.g., Haler et a], Br. J. Cancer. 1999, 80:1867; Lehr and Pienta, J. Nad. Cancer Inst. 1998,90:118). Briefly, in one embodiment, cells labeled with a fluorescent indicator, such as calcein, are incubated on tissue culture wells coated with media alone or with matrix proteins. Adherent cells are detected by fluorimetric analysis and percent adhesion is calculated. This experimental system can be used to identify proteins, antibodies and/or small molecules that modulate cell adhesion to extracellular matrix and cell-cell interaction. Since cell adhesion plays a critical role In tumor growth, progression, and, colonization, the gene involved in this process can serves as a diagnostic, preventative and therapeutic modality. Example 51: Detection of 24P4C12 protein In cancer Patient specimens To determine the expression of 24P4C12 protein, specimens were obtained from various cancer patients and stained using an affinity purified polyclonal rabbit antibody raised against the peptide encoding amino acids 1-14 of 24P4C12 variant 1 and conjugated to KLH (See, Example 10: Generation of 24P4C12 Polyclonal Antibodies.) This antiserum exhIbited a high titer to the peptide (>10,000) and recognized 24P4C12 in transfected 293T cells by Western blot and low cytometry (Figure 24) and in stable recombinant PC3 cells by Western blot and immunohistodiemistry (Figure 25). Formalin fixed, paraffin embedded tissues were cut into 4 micron sections and mounted on glass slides. The sections were dewaxed, rehydrated and treated with antigen retrieval solution (0.1 M Tris. pH10) at high temperature. Sections were then incubated in potyclonal rabbit anti-24P4C12 antibody for 3 hours. The slides were washed three times in buffer and further incubated with DAKO EnVision+'" peroxidaseconjugated goat anti-rabbit immunoglobulin secondary antibody (DAKO Corporation, Carpenteria, CA) for I hour. The sections were then washed in buffer, developed using the DAB kit (SIGMA Chemicals), counterstalned using hematoxylin, and analyzed by bright field microscopy. The results showed expression of 24P4C12 in cancer patients' tissue (Figures 29 and 30). Tissue from prostate cancer patients showed expression of 24P4C12 in the 123 tumor cells and in the prostate epithelium of tissue normal adjacent to tumor (Figure 29). Generally, expression of 24P4C12 was high in all prostate tumors and was expressed mainly around the cell membrane indicating that 24PC12 is membrane associated in prostate tissues. All of the prostate samples tested were positive for 24P4C12. Other tumors that were positive 5 for 24P4C12 included heart, skeletal muscle, liver, brain, spinal cord, skin, adrenal, lymph node, spleen, salivary gland, small intestine and placenta. None demonstrated any expression of 24P4C12 by immunohistochemistry. Normal adjacent to tumor tissues were also suited to determine the presence of 24P4C12 protein by immunohistochemistry. These included, breast, lung, colon, ileum, bladder, kidney and pancreas. In some of the tissues from these organs 10 there was weak expression of 24P4C12. this expression may relate to the fact that the samples were not truly normal and may indicate a precancerous change. The ability to identify malignancy in tissue that has not undergone obvious morphological changes is an important diagnostic modality for cancerous and precancerous conditions. These results indicate that 24P4C1 2 is a target for diagnostic, prophylactic, prognostic 15 and therapeutic applications in cancer. Throughout this application, various website data contact, publications, patent applications and patents are referenced. (Websites are referenced by their Uniform Resource Locator, or URL, addresses on the World Wide Web). The present invention is not to be limited in scope by the embodiments disclosed 20 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 25 embodiments can be practiced without departing from the true scope and spirit of the invention. Throughout this specification the word "comprise", or variations such as "comprises" or "comprising", will be understood to imply the inclusion of a stated element, integer or step, or group of elements, integers or steps, but not the exclusion of any other element, integer or step, or group of elements, integers or steps. 30 Any discussion of documents, acts, materials, devices, articles or the like which has been included in the present specification is solely for the purpose of providing a context for the present invention. It is not to be taken as an admission that any or all of these matters form part of the prior art base or were common general knowledge in the field relevant to the present invention as it existed before the priority date of each claim of this application. 124 TABLES: TABLE 1I: Tissues that Express 24P4C12: a. Maignant Tissues i Prostate Blad der Kidney Lung Colon Ovary Breast Uterus Stomach TABLE 11: Amino Acid Abbreviations SINGLE LETTER THREE LETTER FULL______NAME ___ F Phe phenylalanlne L Leu ucn S Ser en Y Tyr trsn C Cys _________________ W Trp tytpa P Pro poline H His histidlne 0 Gln glutainine R Arg argine Ilie isoleucine M Met methionine T Thr threonine N Asn asparagine K Lys lysine V Val valine A AJa alanine D Asp aspartic acid E Glu glutamic acdd G I Gly gfydne 125 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.chImanualblosum62.htmlI) A C D E F G H I K L M N 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 -2 A 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 -3 G 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 -2 N 7 -1 -2 -1 -1 -2 -4 -3 P 5 1 0 -1 -2 -2 -1 0 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 7 Y 126 TABLE IV: HLA Class till MotiflSuperMOtifiS TABLE IV (A): HIA Class I SupermotifsMotlfs SUPERMOTIF POSITION POSITION POSITION 2 (Primary Anchor) 3 (Primary Anchor) C Terminus (Pnimary Anchor) Al TIL VMS FWY A2 LIVMATQ lVMATL A3 VSMATUJ RK A24 YFWIVLMT FIYWtM B7 P __________VILFMWYA B27 RHK ______ ___FYLWMIVA B44 ED _____ ___FWYLUMVA M5 ATS _________FWYLIVMA B62 01! VAP _________FWYMIVLA MOTIFS Al TSM y Al IDEAS V A2-1 LMVQIAT VLIMAT A3 LMVISATFCGD _________KYRJIFA All VrMLISAGNCDF _________KRYH A24 YFWM ___ ____FLIW A13101 MVTAIJS RK M'3301 MVALFIST RK A6801 AVTMSLI_______ RJ( 8*0702 P LMFWYAIV B'3501 p ________ LMFWYIVA B51 P UVFWYAM E85301 P IMFWYALV B*5401 IP ATIVLMFWY Bolded residues are preferred, italicized residues are less preferred: A peptlde is considered motl-beaing If It has pimary anchors at each primary anchor position for a motif or supermotif as specified in the above table. TABLE IV (8): HLA Class 11 Supermnotif 1 6 9 W F. Y, V,L A, V1.L, P.C, S, T A, V,1, L, C,S, T,M. Y 127 TABLE IV (C): HLA Class I Motifs MOTIFS 1* anchor 1 2 3 4 5 1* anchor 6 7 8 9 DR4 preferred FMYLJVW M T I VSTCPAUM MH MH deleterious W R WDE DRI preferred MFLIVWY PAMQ VMATSPLC M AVM deleterous C CH FD CWD GDE D DR7 preferred MFUVWY M W A IVMSACTPL M IV deleterious C G GRD N G PM MOTIFS 1* anchor 1 2 3 1* anchor 4 5 1* anchor 6 Moif a preferred UVMFY D MoWif b preferred LIVMFAY DNOEST KRH DR Supemiotif MFUJVWY VMSTACPU Italicized residues indicate less preferred or'tolerated" rescues TABLE IV (D): HLA Class I Supermotifs POSITION: 1 2 3 4 5 6 7 8 C-terminus

SUPER

MOTIFS A1 1* Anchor 1* TIL VMS FWY A2 1* Andor 1* Anhor UVMATQ UVMAT A3 Preferred 1 * Anchor YFW YFW YFW P I Anchor VSMATI (4/5) (3/5) (4/5) (4/5) RK deleterious DE (315); DE P (5/5) (415) A24 1* A * Anchor YFWIVLMT FlYWLM B7 Preferred FWY (5/5) 1* Anchor FWY FWY 1*Anchor LIVM (3/5) P (4/5) (315) 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 ~ * Anchor *Anch RHK FYL WMIVA B44 i Achor 1* Anchor ED FWYLIMVA B58 1* Anchor 1* Anchor ATS FWYUVMA 862 1* Anco 1*Anchor QjVMP FWYMIVLA Itajicized residues indicate less preferred or 'tlerated' residues 128 TABLE IV (E): HLA Class I Motifs POSITION i 2 3 4 5 6 7 8 9 C terminus or C-tenninus Al preferred GYYW 1*Anchor DEA YFW P DEON YFW 1*And 9-mner STM y deleterious DE RHKLIVMP A G A Al preferred GRHK ASTCUVM 1*Anchor GSTC ASTC LIVM DE l'Anchor 9-mer DEAS Y deleterious A RHKDEPYFW DE PON RHK PG GP Al preferred YFW 1*Anchor DEAQN A YFWQN PASTC GDE P 1*Anchor 10- STM Y mer deleterious GP RHKGUVM DE RHK ONA RHKYFW RHK A Al preferred YFW STCLIVM IAnc A YFW PG G YFW 1*Anchor 10. DEAS Y mer deleterious RHK RHKDEPYFW P G PRHK QN A2.1 preferred YFW 1*Anco YFW STC YFW A P 1*Anchor 9-mer LMIVQAT VUMAT deleterious DEP DERKH RKH DERKH POSITION: 1 3 4 5 6 7 8 9 C Terminus A2.1 preferred AYFW 1*Anchor LVM G G FYWL 1*Anchor 10- LMIVQAT ViM VUMAT mer deleterious DEP DE RKHA P RKH DERK RKH H A3 preferred RHK l'Anchor YFW PRHKYF A YFW P 1*Anchor LMVISATFCGD W KYRHFA deleterious DEP DE All preferred A lAnchor YFW YFW A YFW YFW P 1Aco VTLMISAGNCD KRYH F deleterious DEP A G A24 preferred YFWRHK *Anc STC YFW YFW *Ancho 9-mer YFWM FUW deleteious DEG DE G QNP DERH G AQN K A24 Preferred 1*Ancho P YFWP P l*Anchor 10- YFWM FUW mer Deleterious GDE ON RHK DE A QN DEA A310 Preferred RHK *Ancho YFW P YFW YFW AP . Dr MVTAUS RK DeleteriousDEP DE ADE DE DE DE A330 Preferred oAnch YFW AYFW 1' 1 MVALFIST RK DeleteriousGP DE A680 Preferred YFWSTC *Anho YFWLIV YFW P 1Ai r 1 AVTMSI M RK deleterious GP DEG RHK A 8070 Preferred RHKFWY 1*Anch RHK RHK RHK RHK PA *Anche 2 P LMFWYAJ deleterious DEQNP DEP DE. DE GDE ON DE 129 POSMON 1 3 4 5 6 7 8 9 C terminus or C-tem~nus Al preferred GFYW I*Anchor DEA YFW P DEON YFW loArchor 9-er STM y deleterious DE RHKLIVMP A G A Al preferred GRHK ASTCLIVM l*Ancho GSTC ASTC LIVM DE 1*A&c 9-mer DEAS Y deleterious A RHKDEPYFW DE PQN RHK PG GP B350 Preferred FWYLIM j~I*nh FWY FWY' I P LMFWY/V A deleterious AGP G G B51 Preferred UVMFWY' 1*Anh FWft STC FWY G FWY I *Anch P UVFWYA A4 deleterious AGPOER DE G DEON GDE HKSTC B530 preferred LIVMVFWY £'Anh FWY STC FIW UIVMFW FWx' £*Ar~ 1 P Y IMFWYAL V deleterious AGPQN G RHKQN DE B540 preferred PFWY J*nh FWYUVM UIVM ALIVM FWYA V*Andio I P P ATIVLMF WY deleterious GPQNDE GDESTC RHKDE DE QNDGE DE 130 TABLE IV (F): ummary of HLA-supertypes all phenotypic frequencies of HLA-supertypes in different ethnic populations Specificity Phenotypic frequency pe position 2 Terminu aucasian A Bla apan 'n ispani e 7 V 3.2 5.1 .1 3.0 9.3 9.5 A3 LMVST 7.5 2.1 5.8 2.7 3.1 .2 A2 lLMVT LMVT 5.8 9.0 2.4 5.9 3.0 2.2 24 V * )3.9 8.9 .6 0.1 8.3 0.0 D44 ) LIMV 3.0 1.2 2.9 9.1 9.0 7.0 1 - (LVMS) 7.1 6.1 1.8 4.7 6.3 5.2 27 HK .WI 8.4 6.1 3.3 3.9 5.3 3.4 62 L IVMP WY (MI 2.6 .8 .5 5.4 1.1 8.1 58 TS 11 0.0 5. .6 .0A 0.3 TABLE IV (G): Cacuated poputaton coverage afforded by different HLA-supertop combinations HLA-supertypes Phenotypic frequency aucasian A Blacks Janese Inese anic ervee 3.0 16.1 87.5A. .3 8.2 A9 A3 and B7 .5 8.1 100.0 .5 .4 .3 A3, 87. A24, 9 . 100.0 .89.9. nd Al ,A3,137, A24.,

.

.

000. 9. Al. 827. B62, nd B 58 ________ ________________________ otiIndicate the residues defining supeutype specificites. The motifs "nororate residues determined on the basis of ublished data to be recognized by muliple alleles within the supertype. Residues Wthin brackets are additional residues lso predicted to be tolerated by multiple alleles within the supertype. Table V. Frequently Occurring Motifs -a-ertvrg. % ypesePhe pntial Function 4udeic acid-binding protein functions as aanscription factor, nuclear location C22 4%Z3.0 finger, C22 type 13obable Aytochrome b(N- andane bound odase, generate Aochrme b N 49% 9 erm9na./b6/peB pero9de domains are one hundred amino acids ong and Include a conserved lo19% Immunoglobulin domain ntradomaln disulfide bond. e repeats of about 40 residues, aach containing a TrpOAsp motif unction In signal transduction and WD40 18% domain, G-beta r tam interaction iay function In targeting signaling 02 23%___ PDZ domain wlcles to sub-membranoujs sites JI 8% Leuctne Rich Repeat Mort sequence mothf Involved in Nudeitac-protein interactions ins ed catalytic core common to nth sefnneghreonine and tyrosine protein kinases containing an ATP kinase 23% Ptemn kinase domain Inding site and a cabdytic site 131 lIeckstuin homology involved in ntracellular signaling or as constituents PH 16% H domain f th cytoskeleton 30-40 amino-acid long found in t 3xtracellular domain of membrane EGF 34% GF-ike domain nd proteins or in secreted proteins Reverse transaiptase :RNA-dependent DNA Rvt 49% lymerase) .ytoplasmic; protein, associates integral Mk 25% k repeat mbrane protons to the cytoskeleton 4ADH- membrane associated. Involved in Jbicquinonelplastoquinone xoton translocation across the 3xidoredgql 32% complex 1), various chains membrane cium-binding domain, consists of a12 sidue loop flanked on both sides by a EIhand 24% F hand 2 residue alpha-helical domain letroviral aspary partyl or acid proteases, centered on Ryp -9% protease ca c aspa residue xtracelluiar structural proteins Involved n formation of connective tissue. The :otagen triple helix repeat ieuence consists of the G-X-Y and the Colagen. 42% 20 Cois ypeptide chains forms a trile~ helixt tdaed In the extreluar lgand ing region of receptors and is about 0 amino acid residues long with two *of cysteines involved in disulfide n3 % ribronectin type If domain mnds een hydrophobic transmembrane egons with the N-terminus located transmembrne receptor xtraelpulairlywhile the Cterminus Is NADH- 1embra as~ciae.Ivovdi (mrodopsin family) a asmic. Si nal through G proteins Table VI: Motifs and Post-translational Moddficaonons of c24P4C12 N-glysesylation site 29 h32 NRSC (SEQ ID NO: 48) 69 -72 NSTG (SEQ IDNG. 49) 155e- 158 NMAV (SEQ ID NO, c ) 197 200 NDTf (SEQ IDNOn t 51) 298- 301 NLSA (SEQ ID NO: 52) 393- 396 NISS (SEQ I1) NO: 53) 405 -408 NTSC (SEQ ID NO, 54) 416 -419 NSSC (SEO ID NO: 55) 678- 681 NGSL (SEQ ID NO: 56) Protein kinase C phosphorylaivon site 22 -24 SIR~ 218 -220 SvK 430 -432 SsK 494 -496 TIR 573 -575 SaK 619-621 SgR CasAin kinase be phosphorylation site 31 -34 SCID (SEQ ID NO: 57) 102- 105 SVAE (SEQ ID NO: 58) 119 -122 SCPE (SEQ ID NO, 59) 135-138 1VGE (SEQ ID NOy 60) 304 -307 SE (SEQ ID NO 41) 132 Tyrosine kinase phosphorylation site 6 - 13 RDEDDEAY (SEQ ID NO: 62) N-myristoylation site 72 -77 GAYCGM (SEQ ID NO: 63) 76 -81 GMGENK (SEQ ID NO: 64) 151 -156 GVPWNM (SEQ 10 NO: 65) 207 -212 GLIDSL (SEQ ID NO: 66) 272- 277 GIYYCW (SEQ ID NO: 67) 287 -292 GASISQ (SEQ ID NO' 68) 349 - 354 GQMMST (SEQ ID NO: 69) 449- 454 GLFWTL (SEQ ID NO: 70) 467 - 472 GAFASF (SEQ ID NO: 71) Amidation site 695 - 698 IGKK (SEQ ID NO: 72) Leucine zipper pattern 245 -266 LFILLLRLVAGPLVLVULGVL (SEQ ID NO: 73) Cystelne-dch region 536 - 547 CIMCCFKCCLWC (SEQ ID NO: 74) Table VII: Search Peptides variant 1, 9-mers, 10-mers, 15-mers (SEQ ID NO: 75) MGGKQRDEDD EAYGKPVKYD PSFRGPIKNR SCTDVICCVL FLLFILGYIV VGIVAWLYGD PRQVLYPRNS TGAYCGMGEN KDKPYLLYFN IFSCILSSNI ISVAENGLQC PTPQVCVSSC PEDPWTVGKN EFSQTVGEVF YTKNRNFCLP GVPWNMTVIT SLQQELCPSF LLPSAPALGR CFPWTNVTPP ALPGITNDTT IQQGISGLID SLNARDISVK IFEDFAQSWY WILVALGVAL VLSLLFILLL RLVAGPLVLV LILGVLGVLA YGIYYCWEEY RVLRDKGASI SQLGFTTNLS AYQSVQETWL AALIVLAVLE AILLLMLIFL RQRIRIAIAL LKEASKAVGQ MMSTMFYPLV TFVLLLICIA YWAMTALYLA TSGQPQYVLW ASNISSPGCE KVPINTSCNP TAHLVNSSCP GLMCVFQGYS SKGLIQRSVF NLQIYGVLGL ETLNWVLAL GQCVLAGAFA SFYWAFHKPQ DIPTFPLISA FIRTLRYHTG SLAFGALILT LVQIARVILE YIDHKLRGVQ NPVARCIMCC FKCCLWCLEK FIKFLNRNAY IMIAIYGKNF CVSAKNAFML LMRNIVRVVV LDKVTDLLLF FGKLLVVGGV GVLSFFFFSG RIPGLGKDFK SPHLNYYWLP IMTSILGAYV IASGFFSVFG MCVDTLFLCF LEDLERNNGS LDRPYYMSKS LLKILGKKNE APPDNKKRKK Variant 3: 9-mers GRCFPWTNITPPALPGI (SEQ ID NO: 76) 10-mers LGRCFPWTNITPPALPGIT (SEQ ID NO: 77) 15-mers PSAPALGRCFPWTNITPPALPGITNDTTI (SEQ ID NO: 78) Variant 5: 9-mers VLEAILLLVLIFLRQRI (SEQ ID NO: 79) 10-mers AVLEAILLLVLIFLRQRIR (SEQ ID NO: 80) 15-mers ALIVLAVLEAILLLVLIFLRQRIRIAIAL (SEQ ID NO: 81) Variant 6: 9-mers GYSSKGLIPRSVFNLQI (SEQ ID NO: 02) 10-mers QGYSSKGLIPRSVFNLQIY (SEQ ID NO: 83) 15-mers 133 LMCVFQGYSSKGLIPRSVFNLQIYGVLGL (SEQ ID NO: 84) Variant 7 9-mers SWYWILVAVGQNIMSTM (SEQ ID NO: 85) 10-mers QSWYWILVAVGQMHSTMF (SEQ ID NO: 86) 15-mers FEDFAQSWYWILVAVGQMMSTMFYPLVT (SEQ ID NO: 87) Variant 8 9-mers NYYWLPIMRNPITPTGHVFQTSILGAYV (SEQ ID NO: 88) 10-mers LNYYWLPIMRNPITPTGHVFQTSIEGAYVI (SEQ ID NO: 89) IS-mers FKSPHLNYYWLPIMRNPITPTGHVFQTSILGAYVIASGFF (SEQ ID NO: 90) Variant 9 9-mers YWAMTALYPLPTOPATLGYVLWASNI (SEQ ID NO: 91) 10-mers AYWAMTALYPLPTQPATLGYVLWASNIS (SEQ ID NO: 92) 15-mers LLICIAYWAMTALYPLPTOPATLGYVLWASNISSPGCE (SEQ ID NO: 93) 134 Tables VillV - -: Table VAII-V9e-HLA-A9mers. Table Vill-V-HLA.AI-9mers 24P4C12 242 Table VIII-VI-HIA-Ai.gmers- Each peptide is a portion S of SEQ Each peptide is a portion of SEQ 24P4C12 ID NO: 3; each s position is ID NO: 3; each start position is Each peptide is a portion of SEQ specified, the length of peptide is specified, the length of peptide is ID NO: 3; each start positis 9 amino acids, and the end 9 amino acds, and the end specified, the length of peptide Is position for each peptide is the position for each peptide is the 9 amino acids, and the end start position plus eight start position plus eight position for each peptide is the Start Start Subsequence start position plus eight. 593 KVMLLLFF 0.500 133 S EVFY [0.150 Start Subsequence Score 58 YGDPRQVLY J[i5000~I 0.500 613 _____ 0.15 S361 ICCVFLLF 0.5001 66 CDTFCFI~oo 501 WVGIVAWLY 0,500O 488 1 ISAFIRTLR 77 MGENKDKPY 11.2505 77594 NDPI[120 1861 NVTPPALPG 0.500 1631 QQELCPSFL 0.135 594 VTDLLLFFG 6.250ISG 0125 38 VLEAILLNLM .228877 GASISLGF 0.500 485 FPSAFIR 0.125 363 VLLUICIAY If2.50] ~ LFELR]W~ i) TGVY .2 F318 VLEALLMIA 2.500] 187 jjVTPPALPGI 0.500 607~ VGGVGV1.SF 0.125 489 3 SAFIRT~RY 20] UMLIFLR 05 2. KNAFMLLMR 0.125 6 7 KSLLKILGK 1 .500 272 I C E 1 266 LGVLAYGIY 0.125 470 AS 521 1 YIDHKLRGA S050F A F0 LFLLFILGY 0.125 1 _222 I _FEDFA QSWY_ _ _ 1.250| 0.125 [~ 3] --- AS Y fI -- 398 GCEKVPINT 10.450 F i-61 VV0S FF 0.125 32 iCTDVICcVL 1.250 I360 IVTFVLIC 0.125 5 CIQRDEDDAl 1.250 1 [ SF-12E DE Y] 1. 5 338 ][ I L I E S 1 . 0 156 1 M TV ITSL QQ 0.125 125.1 PEDPWNGK [ 0 6 NNGSLDRPY 0.125 37i 79 LATSGQPQY 1.000 | 700 EAPPDNKKR |S1.000S39 EDPWI 0.300 5581| NAYIMIAJY i1.000 3M 1 ITNDTrIQO 0.125] 542 || KCCLWCLEK |1.000 629 P0250 452 WTLNVLAL 1 0.125 7 1 DEDDEAYGK I 1.000 [14 10.250 353 [|1 YLV 0.2] 11[ EAYGKPVKY l0.250 43 QIYGVLGLF L 0.100 670 FLEDLERNN I 0.9001 |_ _ 11 __M o 276 I CWEEYRVLR 10.900 67 NGSLDRPYY 0.250 207 0.100 F5181 ILEYlDHKL || 0.900 9 M F4-11 ISLEIIIK 1-07-7 513 IARVILEY 0.250 407 SCNPTAHLVI1 0.1001 417 I SSCPGLMCV || 0.750 | TPIA 92 CPNTi 1437 1RSVFNLQIY 0.750 48 TPIA10 RcwrvR5.6 F801 NKDKPiLii 0 FIC EDPWTVG1 0225 354 |[~Ii25 0100 i~~j(~ 12 065 ~ K ES 0225 23 LGVLGVLAY 0.625| 263IfLGV.GLAYIf0.65] 136 ][VGEVFYTKN][ 0225 Table VII.V3-HLAAI.Smers. 546 WCLEKFIKF 0.500 |]C F243 11 SLLFILLLR I O.50 VC|LPAA F.0 441 243 LLFILLR1 0.00] 147] FCIPGPWN 0 __ Each peptide is a portion of SEQ 238 || VALVLSLLF 1 0.500 N 3 579I MLLMRNIVR 00 spedfied, the lengthofpeptides 465 LAGAFASFY 0.500 9 amino adds, an e 421 GLMCVFQGY - r VIVLEYIDHK [0.200 posi.0on for each pde is the . 424 NCVFQGY start po nsition us elghL 508J_ ILTLVIAR 10500 394][ ISSPGCEKV [art Subsuence Score 135 Table Vill-V3-HLA-Ai -9mers- 6 - ________ 0.200 Table Vill.V8LA-AI*9mers 24P4C12 2 YSSKGLIPR 0.075 24P4C12 Each peptde is a portion of SEQ P Each peptide is a portion of SEQ ID NO: 7; each start position is LIPRSVFNL 0.005 ID NO: 17; each start position is specified, the length of peptides specified, the length of peptide is 9 amino acids, and the end [.H _ SSK S 0003 9 amino acids, and the end position for each peptide is the 4111 SKGLIPRSV 0.001 position for each peptide is the start position plus eight. 9 L start position plus e Start Subsequence I Score L -55- start Subsequence Score 9 31ITPPALPGI 0I.2.] [j GYSSKGLI .oo] 18I VFQTSILGA 0.0oA031 8 NTPPALPG 0.500 10 TNPITPTGHV OJO3 23| RCFPWTNIT 10.100 to VIII-V7-LAAi-9mers- 15 1 TGHVFQTSI 0.003 6| WTNITPPAL 0.050 |24P4C12 [9 TRNPITPTGH 1 0.003 TNITPPALP -0.001 Each peptide is a portion of SEQ [14 1 PTGHWQTS 1 0.003 1 ] GRCFPWTNI 1 0.001 ID N: 15; each start position is 7 1 IMRNPiTPT H o.ooi CPTIP 000 specified, the length of peptide is ___ IfYW3MRP F0.0 CFPWTNITP 0.0009 amino acids, and the end 5 PWTNITPPA 0.000 position for eadh peptide is the I GHVFQTSIL 11 0.0011 FPWTNITPP 0.000 start position plus eight 2 1 YW.PIMRN Start ubsequencef Score 6I IRPT 100 Table IIIVS.LAA197 IfVAVGQMMST 0.050 _ ________ Table Vill-V-HLA-A LVAVG MS 0.050 Table VII-V9-LAA-9mers 24P4C12 I 1 L-8 _ ]AVGQMMSTM 1 0.010] I441 Each peptide is a portion of SEQ IILVAVGQMM 0 1 Each peptideIs a portion of SEQ ID NO: 3; each startApositi0.010 ID NO: 19; each start position is specified, the length of peptide is 4. A0 specified, the length of peptide Is 9 amino adds, and the end L II YWILVAVGQ 0.001 9 amino acids, and the end position for each peptide is the II SWYWLVAV 0001 positionforeachpeptideIs the start position plus eight. E _____ _ Ia t u Srt Subseuence Score I Sa I S q j S 1 VLEAILLLV | 4.500 Table VillfBHIA19mers 117FPTQPATLGY 62 1 6 I[ LLLVUFLR |[ 24P4C12 . | 0.125 P :41[ AILLLVF 500peptideisaportionofSEQ 15 11 ATLOYVIWA F015 8 I LVLIFLROR 1 0.100 ID NO: 17; each start position is H YPLPTOPAT 0.o5o = .0Q 0 specified, the length of peptide is j T Y020 =571 ILLLVUFL 0 aino acds,andtheend 3 i EAILLLVLI Iposito or each peptide is the F-971 VUFLRQRI S0010rtSubsquence[5core] 0.01 S LEAILLLV |000311 PITPTGHVF 1 QPATLGYVL 0.005 19_ _ FQT[ILGAY 0.0751 17 ]LGYVLWASNI 0.005 Table VIl-V6-HILA-Ai-9mers- 20 QTSILGAYV 0.050 10 LPTQPATLG 11 0 1 24P4C12 1 Each peptide Is a portion of SEQ I 0 ID NO- 13; each start position is specified, the length of peptideIs 1 NYYM.PIMR 0.s2 Fl[ TQPATG 00 9 amino acids, and the end 1 T 113 F]AMTALYPLP1 position for each peptide is the 18 GYVLWASNI 1 start position plus eight 7.PA0 4 i KLIPRS || 0.004EN[YLTP Start suenc~e11 5 GYSKGP || 0.005 1 YWAMTALYP 136 [Table IX-VM4LAAlmers- Table IX.VI .HLA-A10mers 24134C12 j1 24134C12 Table IX-VI-HLA-Almers* 1 Each peptide is a portion of SEQ Each peptide is a portion of SEQ 2413402 I0 NO: 3; each start position is 10 NO: 3; each start position is Each peptide is a portion of SEQ specified, the length of peptide Is specified, the length of peptide is ID NO: 3; each start position is 10 amino acids, and the end 10 amino acids, and the end specified, the length of peptide is position for each peptide is the position for each peptide is the 10 amino acids, and the end start position plus nIne, start position plus nine. position for each peptide Is the Start Subsequence [Score Start ][Subsequence~ Scare stat ps~tonpl~ n~e.609 IIGVGVLSFFFF 186] [i~ NVTPPALPGI 1 0.200j ~ Score] F 3 5 3 77STFYPLvrF 0501 618 SGRIPGLGK]I0.1501 591(VDYGKi1500 464] VILAGAFASFY [0.500 1 r 1 73 1FPAPOLGRCF 1 0.5 1322I TVCVF~j ~ 5 [ILLMLIFLR jE 0500 [118 ISSCPEOPTV105 1M20 1rCPEDPWTVGKH 9.0035 J[ VICCVLFLLF 1 [ 0125 WTGN F 0.1251 1518 B ILEYIDIIKLR F60- I EJGGGLS I.500 [1 7 JNNSLRPY 0.125 F--0 1SDPYMSK[ 1 521 YIDHKLRGVQ I~ 0 GGVVLS00] 0125 I 1 ~ ~ ~ ~ . 69 INAPNK .0 6 CVDTLFLCrFL I[ 0.500 26 KGAS IS Q LGF .2 318 ~305 1[ ~ 661 IMCVDTLFCF Ii0.500] 80][ K K Y L ~ O 2 39 ] S FITR L 3q 0 S I VLM GVA YGY j[.5 0 360] VTFVLLLICI 0.12S~ 3r ] V1FUFI GY If i 49 R[ IWVGIVAW LY II 0.500 ] 196 ][ T D T Q GI] 1 5 1362 KI FVLLLICIAY j 2-0 F667 ILCFLEDLER 050198 j Dfl'IQ ISG I0.125 I' f 16 jVEFTKR471[SCNPTAHLVN J (-5001 F-931IG~tLA]"15 21 IFvEvrnlQRWf 2.205 7 ELCPSF .500 ~ iTYIYYCWEEY 9[001251 ~~~ 77] F]MGN KPYL1 0,45 1 382SGQPQvW02I 1 2.000]jT)[ CLKFIKFIJ 120D50 467 HGAFASFWAF[ 0010 1 6 !R.DD00]K ~ 337I AIALLKEASK 48700 1 LIA [RL 0.100 417 1SSCPGLMCVF R1.500 1 9~1 KSLLKILGKK 64 0.00 VLYPSTGA 0.100 1132 j FSOTVGEVFYO 10DO ]VQrL~u 07) ~ ~ M S f010 I49-] FM A 1 1.0 0]18 KYDPSFRGPI R01 5o 1272 IG Y W E R[ A O A~i[FAF~wAFH1l07 JIjGMGENKDKPY20] JF j RRI1ALi' _ F3rIFAVAMTAL- [.0 ] 57 RAYMAY 0.-2507 1 612 II VLSFFFR] 00100 1 7 IIYLTSGQ [Ta00] 590Jyj4 0.250LL 147 HFCLPGVP WNM[ 0010 6710 [FAE NNG [PT I 6770 M NGLRY 0.250 I 216 11 DISVKIFEDF IF-0100 1 1 0 3 [VAENGLQCPTI 0 0m 578 1FMLLMRNIVR I 76 53 ] IVAWLYGDPR][ 0.100] 2271 WYRLRD[ 09050 1871 VPPALPGiT 110250 r132611 MLIFLRQRIR H[ 0.100 :~~~:~rz LSLILL [F] 43I ~ ] jj4]CL WCLEKFIK [Ej10]j 163 [ QQELCPSFLL 11 006751 VLAGFAS1 0,0 58 IIYGDPRQvLYPI 0.625 74 6-RLYCGMGEK 0.200 266 i LGVLAYGIYY f0625 72 GACGMGEN 0.200 342 !IVGMMSTMFYII 02 423 IMCVFQGYSSKI 0.200 Tbe 24P4C12 171 LLPSAPALGR 1(.0] 621 II RIPGLGKDFK It Each peptide Is a portion of SEQ 507 .500 1- -] 0.0 IDNO- 7; each start position is 23 UVLVQIAF 0050 FI170 II FLLPSAPALG I0.200] specified, the length of pelptide is 237211ALVLSLLFI1O.001 __7____ 001_10lamino acids, and the end 32 EIL.UF -050 1611 ASLQQELCPSFT 0,200 position for each peptide Is the If UDSLNARDI - 0.0 j-VAPV ___ sta0t boion plus rdne.

FStarti 4I usqec f~j] [j SSKGLIP!RSV 0.0021 (2 ]NYYWLPIMRN 0.00 ,FoJ ITPPALPGIT ]1~5) [9 IPRSVFNLQI 0.001 [W]!6 TGHVFQTSIL ]0.003 S9 J[NITPPALPGI I~ O GYSSKGLIP 0.001 [17 U~ GHVFTSILG 110.D0l L rRCFPWIWI'P F -o81 UPSFNQ 0.06__ LPIMRNPITP 0.O001 IA.TNITPPALPG 10.013) _________ 1RNPITPTG ]01 F7-WrPTPPALP 0.0051 Table IX.V7HLA-A1.l0mers. 7 j[ PJMN ]- 0.0001 1L5 FPWmrIPPAlJ~ol 24P4C12 I3 YYWLPIMRNP70.000 [2: [GRCFPWThf O 1 Each peptide is a portion of SEQ -1-=GRFPTIi ID NO: 15; each start position is LGRFP--] TOOO I____ 0 specified, the length of peptide Is TaleIXV-HL.AM-l0mm-3 6 PWTNITPPAL 0.00 10 amino adds, and the en 7 24P4C12 4 JrCFPWThITPP If000j position for each peptide is the Each peptide is a portion of SEQ sttposition pus nine.- ID NO: 19; each start position Is Star Susqec cr specified, the length of peptide is Table IXV5HLA-AI-l0mers- I D______ latino acids, and the end . 2413402 1 ~1( AVGQMMSTMF] 1001 position for each peptide Is the Each peptide is a portion of SEQ [6 jILVAVGQMMS 110.050 start poiton pus nine. 10 NO: I t; each start position is 7 JrLVAVGQMMST 0.050 Start Subsequence Score specified, the length of peptide Is ______ 10 min acds an th-en J VAVGQMMSTM 0.010 11 ]LPTQPAThGY 0.6251 position for each peptidle is the 59 WILVAVGQMM 0.010 7 ALYP[.PTQPA 10. 1'00 start position plus nine. 1i JrSWYWILVAV 0.039 YPLPTQPATL 10.050 SStart i[ Subsequencej 2i Scorywi~r AvG IF5551 5 *[MTALYPLPTQ 0.050 VLA1LV 111v~i~~J 4.500 1 4 (YMLGQj 10 12 [PTQPATLGYV 0.025 16 I( ILLVIIFLR 1 00 3 1 WYW(LVAVGQ (oT J AMTALYPPT.. 0.025 F4j -FEALLLVLIF7 0.500 J 16 [ATGV AS 0.025 [.LiI LLVLIFLRQR M 0.100 Table IX-V8-HL.A.AIlmers- ir LGYVLWASN 0.2 10~ VL0.1QRR 00--o 2402 15j PATLGYVLWA 0.5 7) Fu1---LiFLR5Q][____ Each peptide Is a portion of SEQ __[QPATLGYVLW j00D5 AV.0JLLV 0 ID NO: 17; each start position is I Fqspecified, the length of peptide Is 10= M03 [T [AIULVIIFI a 0.050 10 ainino acids, and the end 18 JLIGYVIWA-SNI 1 4 i LVLIFLR0Rl 0.010 position for each peptide is the 3 WAMTALYPLP 10.002 0.0 start position plus nine. 2T 11 YWAMTALYPL 1001 ~= = ~ -Start If Subsequence iSc-OT7 10-11 PLPTQPATLG I 0.0011 ITable lX-V6HLAA-10mers- 1i. If LNYYWLPIMR 10.125 6 1 TALYPLPTQP ]0.001 24P4C12 13 IfFTPTGHVFQT 0.125I LYPLPTQPAT 0.0 Each peptcde is a portion of SEQ 121 QTSILGAYVI 0.050 H 9 GYVEWASNIS 0.0011 ID NO: 13; each start position is 18 HVF-TSILGA 0.050 0.0] specified. the length of peptie is 11ATAX NNkTHIFI1.2 10 amino acids, and the end __fNIPGV .2 position for each peptide is!the '1 VFTILA 0.025 _ _________ stau position plus nine. 12i 11 PITPTGHVFQ 10.020 Table X-VI4ILA..A0201.9mers . !1 Subsequence i[ e] 5 WLPIMRNPIT 0o.020 24P4C12 7 1I GLIPRSVFNL Jr00] 4 LYWLPIMRNPI 0.01 Each peptide Is a portion of SEQ 2 IfGYSKGLIR J oos J IfMRNITPTH 0005ID NO:- 3; each start position is 2 GIRVN .0 20 FQNTG 0.005 spcified, the length of peptide is ___ ______ rGN 1 03 9 amino acids, and the end 5__ SKGUPRSVF~J 0.005 [i I PTGHVFQTSI 10.00311 position for each peptide Is the ~3~'I ~I 14 _fTPTGHVFQTS O00031 I start position plus eight. 10I 11 0.003 10 IfRNP TGV 0.0031 j Subsequene Joe 138 TableOVI-HLA-A0201-9mers- Table X-V1-HLA-A0201.gmers- Table X-VI-HLA.A0201.9mers1 24P4C12 24RC12 24P4C12 Each peptide is a portion of SEQ Each peptide is a portion at SEQ Each peptide is a portion of SEQ ID NO. 3; each start position is U) NO. 3; each start position is ID NO: 3; each start position is speciied, the length of peptide is specified, the length of peptide is specified, the length of peptide Is 9 amino acids, and the end 9 amino acds, and the end 9 anino acids, and the end position for each peptide is the position for each peptide is the position for each peptide is the start psition pus ei hL start position plus eight start psition tlus elg t. Sta squnl IIcore] Star[ Subsequence Score IStardj ESu bse uence ScoR GLFWTLNWV 237 638 L O.28 3238.LLIL 19 456j WLALGQCV 103.5 49 CVVLF1 322 ILLLMLJFFL 1 91 1 580 LLMRNIVRV . 09 5 _73FI1 29 448 GVLGLFWrL __5 14811 PVPN 72 F597 LLLFFGKLL )O - I 1 1 ___A 25 LVLVLILGV 88.0 23 CLPAGVWNM .3 544 CLWCLEKFI 76.2VL_ 6 5 74 6601 GMVCV.FL .85 291 SQLGFTTNL 04 '5798 II UFFGKLLV 82. 9.7 6I 3LYNF . t2 688 YMSKSLLIKI 8.7 a YLLYFNIFS11 65 1770 FLLPSAPAIL 3 51 r 177] ALGRCFPWT 7.7 506 ALILTLVQI 39 86 LLYFNIFSC . 3 1 211 .5 252 LVAGPLVLV 79_ 578 FMLLMRNIV 50.5 5 29~~L~ 107 GLCT 95 3 LVALGVALV 7 24 LLFILLLRLM" 90 1 VLSLLF KLRGVNPV 41 FLLFILGYl 21 08 43 LIQRSVFNL 6 1 i 95 ILSSNIlSV 27 9f . 61 265f VLGVLAYGI ~1773 60 VLILGVLGV 04.78 CLEKFIKFL .72 326 MLIFLRQR IP76 56 WLYGDPRQV 261 4.7 42 LLilGlV 1793 21 65 V3SGFS 6 AsM7 42 LLFILGYI 61 2 VISL FIL IM4 5 YG L L W 16.411 179.1 564 AIYGKNFCV 3 13193.9 29 ALVLSL.FI i3. 6 lVAG L 18 ___________4 M MTFP.59 LTLVQIARV 1 0 LLVVGGVGV 11MFP 2' 60 3IWGVV182 1 1 36 ILICIAYWA r6.5 n S PLDPWV 13961 589 VVLDKVTDL 110.8 .1 F _____ M 4 ILGYIWGI L49ICK 1306 Ta VXAYG-V1L-A F2 K19mr 139 Table X-VI-HLA-A0201-9mers- Table XVi-HLA.A0201.9mers- Table X-V5.HLA.A0201.gmars. 24P4C12 24P4C12 24P4C12 Each peptide Is a portion of SEQ EachpeptideisaportionofSEQ EachpeptideisaportionofSEQ ID NO: 3; each start position Is ID NO: 3; each start position is ID NO: 11; each start position is specfied, the length of peptide Is specified, the length of peptide is specified, the length of peptide is 9 amino acds, and the end 9 amino acids, and the end 9 aino acids, and the end position for each peptide is the position for each peptide is the position for each peptde is the start position plus eight. start position plu t start osiboon lusel L iiart Sub uence score tr ISubsequence re] Subseuence Sco 26 AQSWYWILV 8536 CIMCCFKCC 1402 4] A rj 036 8 246 fFILLLRLVA Jj4.7671 EZ3 1 EAILLLVI I .02 452] WT 1161 757 YPLMVLL 4510 i LVLIFR 426 I FQGYSSKGL 9 Table X-V3-HLA-A0201.9mors- Table X-V6-ILA-A0201-9mers. S FLNRNAYM24PC12 24P4C12 S642 ] MTSILGAYV 9.032 Each peptide i a portion of SEQ of SEQ 164 1 OELCPSFLL 8.914 ID NOr. 7; each start position Is I0 NOr 13; each statposition is 1693 KILGKKNEA 8.846 specified, the length of peptide Is specified, the length of peptide is 251_ RLVAGPLVL 8.7591 9 amino acids, and the end 9 amino adds, and the end M position for each peptide is the position for each peptide is the 501 L A LI 8.759 1 start position plus eig t I start poiin tlus e L I 25FIT 8.759 t 487 S USFIt H179 *~*I Subsequence Score stairt] subsequence Sicore] L442L LQIYGVLGL 8.469 [ WmrmPA. 1.366 7 UPRSVFNL 6.61 262 ILGVLGVLA 8.446 ITPPALPGI 0.567 - 3 521 YIDHKLRGV 18.094 2 f RCFPWNIT 0.074 6 GLIPRSVFN [q.410 373 AMTALYLAT 8.073 NITPPALPG 0.010 4 SKGUPRSV 0.0 242 LSLLFILLL 7.6661 [ FPWTNITPP 0009 5 KGLIPRSVF 0.003 134 QTVGEVFYT I 7.!594 1 GRCFPWTNI 0.0021 2 YSSKGLIPR o0ooi] 191 ALPGITNDT H 7.452If 0.0001 9 PRSVFNLQI 590 VLDKVTDLL 5.11| PWTNITPPA 0.0001 SI RS 110.00 362 FVLLLICIA 6.977 L CFPWTNITP a 0 8 JI I 20_ TIQQGISGL71 6.756GY 200 __PJ7~ _ _ _ _ 1 GSKLIP [0 83 KYLFNI ]F&63l Table X.V5.HLA.A0201.9mors V 83 _KPY lLLYFN i~ .3 314- IVLAVLEAI 6A1I24P4C12 able X.V7.HLA.A02D1.9mers 383 GOPOYVIWA 6.372 Each peptide is a portion of SEQ 2PC 22511 FAQSWYWIL 16.2951 ID N 11; each startposition is Each peptde is a portion of SEQ qSj Tspecified, the legt oflpeptide Is ID N0r 15; each start position Is 289|| SISQLGFTT 9 amIno acds, and the end specified, the length of peptide Is 364 LLLICIAYW 5.929 posft for each peptide Is the amin adds, and the end 596 01--LLFFGKL 5,564 start sition lus eight position for each peptide s the SGVLSFFFFSr u nce start position plus eht. 282 VLRDKGASI 1t5.526art ISubquce Score 154 WNMTVITSL 1|5.459| 774 8446 380 || ATSGQPQ |5313|3 612 VLSFFFFSG . 35 'AVGQM 1 100 ISVAENGL 4.993 1__ 7 VAGQMMST 0405 1581 VITSLOQEL 4.993 ( 1 SWYMLVAV 0.071 FGAULTLV X Lr 6 LVAVGQMMS 0011 Eah7 i 0sU8 0 o 140 Table X-V7-HLA-A0201-9mers- Each peptide is a portion of SEQ Table XM-HLA.A0201.lomers. 24P402 ID NO: 19; each Stat position is 24P4C12 Each peptide is a portion of SEQ specified, the length of peptide is Each peptide is a portion of SEQ ID NO: 15; each start position is 9 amino acds, and the end ID NO: 3; each start position Is specified, the lgt of peptide i position for each peptide is the specified, the length of peptide is 9 amino acids, and the end start pin uselgt. 10aminoaddsandtheend position for each peptide is the Start I b uence ore position for each peptide Is the start position plus eight. 2 11.61 srt position olus nine. Start Subse uence e Start 1Subseuence_ Score r2 1 WYWILVAVG [|0.12 0TQPATLGYV 00 11 48 3 i] YWILVAVGQ 00.000| ~ W1LVVGQW~i I15j ATLGYWWA jr 4130 ]J7 48~~ Table X-V8-HLA-A02019mers- TLGYVLWAS 2 641 jjTI j] 69.6 24P4C12 7!7 YPLPTQPAT 0. 1 ' 69 Each peptide is a portion of SEQ 9 PLPTQPATL 04701 54 WCLEKFIKFL ID NO: 17; each start position is MTALYPLPT 0.1761 71 specified, the length of peptide is 1 ir 597 9 amino acids, and the end FE 82 position for each peptide is the 6 12.5 start position plus eight. 3 ][ P 0.16 598 L Start I Subsequence ||Scorel 171 LGYVLWASN I.004 5 7.9 1 1 TALYPILPTQ 10.0021 __0 4 WILPIMRNPI 0 f I I 1f] 1B][ GYVLWAS'II 2401 VLLFIL 17.4 F20|| QTSILGAYV |5.313 ___________ = 1 LYPILPTQPA 0.0011 1 1 1 0 7 |iMRNPITPT 1.5991 LPTQPATLG 0.0011 649 1 ASFrj 01 13 ITPTGHVFQT 0.649 M 0 0 ff I 15 J TGHVFQTSI |0.259 1 [PTGVW 00013 tGIRVN 4 10i NPITPTGHV 0.0597 5 LPIMRNPIT 034ILTLVQARV 18 i VFQTSILGA 0.013 Table XI-VI-HLA.A020140mers- 1.9 19 FQTSILGAY 1 0.0101 24PC12 48 161 GHVFQTSIL |0.006 EachpeptideisaportionofSEQ 12ID NO: 3; each start position is FILGYI 1 [2__| YYWLPIMRN 0.001 speiied, the length of peptide is Vi VT 'Y~.PMR1000 lamilno adds, and the end 339 ALXE 17 | HFQTSILG |IOO1Iil 14 17 Ef MIFTI .0 position for each peptide Is the- _____ 9 || RNPfTPTGH 0.000 start Positioous nine. T43.0 6 PIMRNPITP 0.000| tR 01r F11-11PITPTGHVF 0.000TMFYPLVTFV 35 1 . 2 LFILLLRLV 42 14|11 PTGHVFQTS 0.000 F 109 } 8 MRNPITPTG |0.000| 5 YLLYFNIFSC 9i 97 3I YWLPIMRNP . 000|8 1 || NYYWLPIMR |0.000| 579 MLLMRNIVRV I100. 4 YIWIAWI 17. Table X-V9-MLA-A0201-9mers- 603 KLLVVGGVGV 98 24P4C12 I a p 358 1599 11 39 amin acids, and theG L end I WMIVAV~ 60 137.4L29 2=51 MMSTMFYPLV 67 141 Table XJ-V1-HLA-A0201-10mers- able xJ.vi.HLAA02O1-1Omers- able XI.VI-A0201.lmm 2PI12 24P4C12 4C1 Eac pptdeIs prtonofSEQ Each peptide is a portion of SEQ 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 ID NO: 3; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 1 am no acds, and the end 10 amino acids, and the end 10 amino acids, and the end position for each pepide is the position for each peptide is the position for each peptide Is the start position Plus nine. start Position Ohs nin start position plus nine. [ t Subsequence ~ trJ~jIScorol [Start[ Subseqec FcR sri]Sbeuence Score] 56I WYDPQL 28.9 9 478] KPQOIPTFPL 11.60] 56 WLYGDPRQVL F 26 8 [ 1 1 iIIVALVLSLLF , It2 239 ALVLSLLFIL 1.1 1 _____ 4 1448 gLGLFWTLNWV 6F12 _12J[ ALIVLAVLEA 11,2 350 QMMSTMFYPL 28.04 6 22

-

1142 5 LLMRNIVRW T8I 554 3 64 VLYPRNSTGA FLNR 1 MM LIILY A 1 _ _ 571 44IAIYGKNFCV 9FW525 133 5S9TVGEVFYTL 5543 44105 YGVILG1FWTL 9.141 16ll 59 LLLFFGKLL 52 M LATSGQPQYV 9.032] 325 LQQELCPSFL 39 7 LIFLRQRIRI 9.023 b80 240 II SLFL '!24]L LLRLVAGPLV 8.986] 580 m oiLLMRNIVRds, and heend stn357 YPLVIFVLLL 4 [epid i theR YI 8.90 r 5 2315 VLALEILLC '64 50 W I 267 GVLAYYVYC 11 6 [457 ]~VLALGQCVLA 8.446 44IGFWLW 36.12TLQIRIL 8.5 304 EVIDHWLAI 17.562 ILSSNIISVA j7.964 554 11 IM I 1.97- 657 r SVFGMVDTL C L7.794 24~~lL 2 LLLRLVAGPL 2251 FAQSWYWILV 17.W54 32 YPVTL 593 KVLLLFFG 6.865 44.1GIWI 5 17.14 368 jr CIAYWAMTAL 6.756! 13 LVEFT A 5011 SLJAFGALILT 0 562 1MAYKF 6.3871 133k SQVEVY 1 363 Hs XQj5929 267 GVLAILYYC 17.VLICA 1.791 FN jj V 1L71. 36 I CCVLFLLFI 5.5651 438.52F318IYGV iLLLLRL452PL 231 WIVLVI -g" 6 VLKTD 6 292 I LFTLS .6 3 45 ILGYIWGI V A 1 VALAL 481 [35* ALGViV SL 9.135 3931 NISSPGCEKV 4.6861 4i 9.13 659 FGMCVDTLFL 10 AI 4 14 CLPGVPWNMT . 26 VLILGVLGVL 4.452 1 4 18 CLGVPWNT 2.6 _26 LILGVLGVLA 4.297 -W-39 8 5021 LA4 292l CIMCCFKCCL 4 108 LQCPTPQVCV 1198 14 ___ *8 142 able XI-V3-HLA-A0201-10mers Each pepe is a portion of SEQ FTSILGAYV 24P4C12 ID NO: 13; each startpositionis Each peptide Is a portion of SEQ specified, the length of peptide is ID NO: 7; each start position is 10 a WLPIMRNPIT 4 specified, the length of peptide is position for each peptide is the 13 ITPTGHVFQT 2.347 10 amino adds, and the end start tion US nin position for each peptide Is the Start Subseuence start position Plus nine. [ 1 H S2 Start Subs ence S corej 7 74 21 [j SIL .059 '9 GNITPPALPGI F 6 [KGLIPRSVFN 0.3s 10 L PPTGHV 0.059 5 FPWNITPPA |1.238 9 IPRSVFNLQI 0.0 16 TGHVFQSIL007 1i LGRCFPWTNI [.015 8 LIPRSVFNLQ 0.007 4 YWLPIMRNPII 0.025 10 N ITPPALPGIT |0.009 3 YSSKGLIPRS a.oo| 15 PTGHVFQTSI 0.012] 7 1 WTNITPPALP SSKGLIPRSV .3 8 IMRNPITPTG .007 8 8 f TNITPPALPG 000 | i IIQGYSSKGUP .0 1471 TPTGHVFQTS 0.001 2 GRCFPWTNIT 0.000 5 SKGLPRSVF 0.0 1 11 L WLPIMR 0.001 3 i RCFPWTNITP 0.000 2 GYSSKGLIPR 0.o00 12 PII 0.00] 6 Ji PWTNITPPAL 0.000 10PRSVNQY 0.0 Npm'TGHVF 0.000 4 J CFPWTNITPP 0000 6 LPIMRNPITP 0.000 able XW ALA-A0201A00mers- 2 T -LAAD2010mers- 24P4C12 17 GHVFQTSILG 0.000 24P402 Each peptide is a portion of SEQ 3 YYWL 0.000 Each peptidle Is a portion of SEQ ID NO: 15;, each start position is F197N VFOTSIWAY 0,F. 00 0 ID NO: 11; each start position is specified, the length of peptide 9 MRNPITPTGH specified, the length of peptide is 10 amino acds, and the end 10 amino adds, and the end posibon for each peptide Is the position for each peptide is the stptsition tus nine, able Xt-HLAA0201-l0mers start position plus nine. Start Subuenoe Sce 24P4C12 S Subse uence Scre Each peptide is a portion of SEQ SW Sbeqec 12. 5_ WILVV M1 6 ID NO: 19; each start position is 1 AVLEAILLLV specified, the length of peptide Is -0 1r QSYLA 8.6-7 IF 10 amino acids, and the end 5 AILLLVLIFL 1I 42 posit for each peptide is the

-

LVLIFLRQRI 8 VAVGQMMSTM start sitlon us nin 911 LLFRR .4 6 ILVAVGQMMS 0.127 IStart Subseuence Scre 2 9 VLEA)LLLVL 12.192| VQMTFF-07 58 6 i ILLLVLIFLR 91.2511 . I L. 11 - 8 3 || LEAILLLVLI 1 0.793 ! 31 W GL aV J 0.0[ AMTALYPLPT 5.382 7 I LLLVLIFLRQ I0.178| H I LAVG 0.00 9 YPLPTQPATL 2.373 1 8 1 LLVLFLRQR 10.0440 13 ] TQPAThGYVL 0.888 a L IFLRRIR 0.002 able XImV-rsLA-A201.0mers- 18 1 IGYVLWASNI 0.370 1 4 I EAUVLIF 0.000Mn 24P4C12 J 17 1f TLGYVLWASNJ0.12 Each peptide is a portion of SEQ 16 ATLGYVLWAS .066 able XI-VS- A021-0mers- ID NO: 17; each start position Is 12 ]f fri LGYV 0.035 2P4C12 specified, the length of peptide is 10 amino acids, and the end r 0 position for each peptide is the 15 P!TLGV ] 0.019 start positionplusnne WAMTALYPLP 0.005 Start Score LYPLPTQPAT 1 143 [10 PLP PATLG 0.002 Table XII.V1.HLAA3-9mers- T e XH..V14lLA-A-9mers 11 LPTQPATLGY 0.001 24P4C12 24P4C12 5 MTALYPLPTO 0.001 Each peptide is a portion of SEQ Each peptide Isa portion of SEQ 6___ 00i ID NO: 3; each start position is ID NO: 3; each start position Is 6 I i!!~! 0 J~*2 1 specified, the length of peptide is specified, the length of peptide is 14 QPATLGYVLW 0.1 9 amino acids, and the end 9 amino acds, and the end 1 || AYWAMTALYP .000 position for each peptide Is the position for each peptide is the 19-]_GYVLWASNIS 10.000] start position plus eight _trtoionihL..... Start SusI unI or Start Subeqence Score Table XII-Vi-HLA-A3-9mers- 272 ] IY 6.000 501 SLAFGAUL 1.200 24P4C12 351 M 5 662 CVDTLFLCF 1200 Each peptide is a portion of SEQ 47 A 4.500 349 GQMMSTMFY 1.080 ID NO: 3; each start positions 4 43 QIYGVIGLF 1.012 specified, the length of peptide is 86 LLYFNIFSC 32100 AILLLNLF 0.900 9 amino acids, and the end position for each peptide is the 446 GvLGLFwTL 3.645 590 VLDKVTDLL 0.900 start stion lus el ht. 660 II L 3. 326 MLIFLRQRI 0.900 Start Subs uence Score 633 HLNYYWLPI 3.600 268 VLAYGIYYC 0.900 421 GLMCVFQGY 1.00 542 KCCLWCLEK 3.600 107 GLQCPTPQV 0.900 0_J ~J . 9 241[ WLSLLFILL- 3.600 631 LSFFFFSGR 0.90D~ 135 TVGEVFYTK 0.503.000 318 VLEAILLLM 0.9D0 033 NISSPGCE< 3.000 (232 ILVALGVAL 0.900 207 GUDSLNAR .0 3 L Q 2. 518 ILEIDHKL 0.900 __jj7.00 45 ILGYIWGI 2.700 452 WTLNWL 0.810 323 LLLMLIFLR [22 ILLLMLFL [.70 596 DLLLFFGKL 0.7 243-I P.00 239 AiVLSLLFI 2.00 645 ILGAYVIAS 0.720 241 LFLL 0 641]1 IMTSILGAY 2.700 258[ VLVLILGVL 0.6081 354 TIY7T 5 598 LLFFGKLLV 2.000 49TMF V TF608 0 ~ L 2601 VULGVLGV 1.800 41 FI~Lj I 0.8 690 ((SLLKILGKK .25 26 VLGVLAYGI 1.801) 54 VAWLYGDPR I ___IL_______ 5131 QIARVILEY [ieOo 665 IITLFLCFLED 10.6001 VILEYIDHK .25 609 GVGVLSFFF 1.800 95 I 0.600 8.0 537Zi IMCCFKCCL 1.800 457] VLALGOCVL 0.600 363 VLLLICIAY 1 50 I 1.800 282 VLRDKGASI 0.600 585 IVRVLK 8.00 686 11 YMSKSLLKI 1. 554 FLNRNAYIM 0.600 0 251 RLVAGPLVL 1.800 39 VLFLLFILG 10.600 5w YMAYG .0 593 KVTDLLLFF 1.800 315 JVIAVLEAIL 10.600 0358 PLVTFVUL 1.620 638 IfWLPIMTSIL o.600 508 ILTLVQIAR 544 CLWCLEKFI 1.500 434 IQRSVFNE 0.540 IL o6 : KSLLKILGK 1.350 61 VLFFS 0.540 579 MLLMRNIVR 0 525 1.350 611 GVLFFFS 0.486 .80~ 170 FU.PSAPAL 1.350 647] GAYViASGF 0.450 267 GVLAYGIYY 8 260I 547 [ CLEKFIKFL 1.350 580 1 LANVRV 0.450 424 CVQ1SK 0.00 597[ U.LFFG)KA. 1.350 3641 LLCAYW 0.450 424 CVFQGYSSKUCIAYWA 1.350 564 AIYGKNFCV 244 ULLLRL 9.o0 ALILTLVQI 1.350 237 GVALVLSLL A05 4L64 JI VAFASF 9.000 14soLPVWM 1.5 38 LI CVLFLLFIL 0.405 144 Table XI-V1-HLA-A3-9mers. Tabe XII.VS-HLAA39mers1 Table XJI-VT-HLA-A3-9mers 24P4C12 j 24KC12 24P4C12 Each peptide is a portion of SEQ ach peptide is a portion of SEQ Subsequence Score ID NO: 3; each start position Is ID N& 11; each start position Is f AVGQMMSTM 0.030 specified, the length of peptide is specified, the length of pepe is r 9 amino acids, and the end 9 amino acids, and the end 4 WILVAVGQM D.027 position for each peptide is the position for each peptide is the [6 LVAVGQMMS 0.00 start position plus eight. start sition us al 1. 7 VAVGQMMST 0.007 Start I Subsequence iScore Start Subsequence Sco I SWYWILVAV 0.002 2041 GISGdDSL 0.405, 0 2 WYWILVAVG 0.000 35 VICCVLFLL |005 5 ILLLVLIFL 4.050 3 YWLVAVGQ 10.000 317-11 AVLEAILLL 10.4051 F4] AJVLIF 1.800 240 I LVLSLFIL 0[.405[[ VLaIFLRQRI 0.900 Table XII.VS.HLAA39mers 6681 [LCFLEDLER 0.400 1 WALLLV ] 2402 388 i VLWASNISS 0.400 LLLIFLRQ .270 Each peptide i a portion of SEQ --7 ]RLR 0.0 VIFRR 020 I NO: 17: each start position is 49 SAIFIRTILRY 0.400QR 12 ____________ secitie, the length of peptide is 211 I SLNARDISV | 0.4002 AILLLL 0.005 9 a adds and the end 85 YUYFNIFS 0.3603 EAILLLVLI [.04 position for each peptide is the start position plus eigh TableXil-V3-HLA-A39mors- - XII.V6LAA34mers- Str Sub Score 24P4C12 i24M 4 WLPIMRNPI 0.600 Each pepUde is a portion of SEQ Each peptide is a portion of SEQ 7 if I TT 225 ID NO: 7; each start position Is ID NO: 13; each start position is W1][ FQTSILGAY 081 specified, the length of peptide is specified, the length of peptde is 9 amino adds, and the erd 9 amino acids, and the end 1041 position for each peptide is the position for each peptide is the 11 [ ITPTGHVFi1.0301 start position plus ei t.ht 1 1 HVFQTSILG 0.020 Start if S Start Subsequence orl13 PTGHVFQT 0 1i 9 TPLPI 06 7 IfLlPRSVFNLI. 0.540 1 20 1 I TSILGAYV 0. 0 10 6 .L WTNIPAL .30 6 GPRSVFN 0.13516T GHVFQTSIL 0.003 2 RCFPWTNIT 0.022 2 YSSKGLPR F f i.5..I TGHVFQTSl 0.002 8 i NITPPALPG 009 15 KGLIPRSVF 013 L I..i LPIMIRNPIT 10.002 1 1 GRCFPWThI 040031 ( 8 IPRSVFNLQ [FO 00Ij F-0-1 NPT H 11.01 4- T- URUFN rNp 1[0 2 003IK LPIS F -001 r -2 IP(H F 7 11 TNITPPALP 0000 9 P VFNLQI 0. 14 PTGHVFQTS 3 F CFPWTNITP 00o I SKGLIP 0.000 18If VFQSILGA 0.001 w 1 ITPPA 1=516M1 Table Xl-V5-HLA-A3-9mers- Table Xll.W.HLA-A3-9mers- 9 If 24P4C12 24P4C12 8IfMRNPITPTG 0.000 Each peptide is a portion of SEQ Start Subseuence Scoe 3 1 YWLPIMRNP o510oJ ID NO:11; eadistart position is EachpeptideisaportionofSE specified, the length of peptide is ID N& 15; each start position 9 amino acids, and the end specified, the length of peptide Ta 24PA position for each peptide is the 9 amino acids, and the end start position plus eight. position for each peptide Is the SD NO- 1 e start position plus eight 6 7.00)FL E5 11ILVAVGQMM 10.40 145 Each peptide is a portion of SEQ-1 Table Xlll..LA.A3.l0mers. Table XIIIVI.HLA.A3.10mers ID NO: 19; each.start position Is24 24P4C12 specified, the length of peptide is Each peptide is a portion of SEQ Each peptide is a tion of SEQ 9 amino acids, and the end ID No. 3; each stan position is ID NO: 3; each start position is position for each peptide ise specified, the length of peptide is specified, the length of peptide is start tion US ei h 10 amino acds, and the end 10 amino adds. and the end Start IISubs. uence Scorel position for each peptide is the position for each peptide is the 15 ATLGYVLWA 0.405 start sition us ne. start position tus ni. 16 TLGYVLWAS 0.270 Start Subsequence Score 4 TALYPLPTQP 0.000 3 T 3.000 S PTOPATLGY 322 ILLLMLFLR 7 72 Ii GENK 3.000 2 PLPTPATL 0.060 0 IF 12.700 2 WAMTALYPL 0.041 58 NIVRWVLDK 7.0 0 660 GMCVDThFLC 2700 4 TAIVOIOT = 3 467 GAFASFYWAF 2.700 S AMTALYPLP 0.020 4 GLIQRSVFNL 0 243 SLLFILLLRL 2.700 13 IfQPATLGYVL 0.01] -40 83 KPYLLYFNIF 2.0700 18 I GVLWSN 0.0862i ILGVLGVI.AY 42 __ ILILFILGYIWV 2.000 12 TQPATLGWV 0.003 271 8C.~Ih00 I 518[ ILEYIDHKLR .001 [8 ]3YPLPTQPAT 0.002 272.I L9...EY 0 161] SLQQELCPSF 2.000 5s j TALYPLPTQ 0.001 464 VLAGAFASFY 8.1 1 337 AIAW(KEASK 2.000 LY-TP 0.00k 362 FVLLLIC lAY 1.800 10__I LPTQPATLG 0.000 665] TLFLCFLEOL 10 1 650 VlASGFFSVF 1.800 14 PATLGYVLW .000 .50-- 180 LGVWSN .0 RVILEYIDHK n 507 LLnVQIAR 1.18001 SWAMTALYP 0329 0RQRIRJ 18 0.0) 86 1 LLYFNIFSCI 0 M 18I VLEAIU.LML 1.800 Table XIllV1-HLA-A3-10mers- 171 LLPSAPALGR 1120 6 GLGKDFKSPH 11.800 24P4C12 309 WLAAUVLAV 1.800 Each peptide is a portion of SEQ 57 1 .0 [MLLMrNIV Izo32 L-VE o180 ID NO: 3; each start position is M [469 FASFYWAFHK 1.80 spedfied, the length of peptide is 76 GMGENKDKPY 9.000 64 VLYPRNSTGA 1.500 10 amino acids, and the end 59 ___________ position for each peptide is the 364 1 LICIAYWA 1.350 start sition us nine. 3.0 QMMSTMPIPL 8.0 657 SVFGMCVDTL 1.350 Start ubs e Score 667 FLCFLEDLER 8.000 85 YLLYFNIFSC 1.350 00. 56 1WLYGDPRQVL 6.750 1 ~~A s i~I 544 CLWCLEKFIK 3000 33 RRAL .0 2 JEFQWU30 I ~ 2~!~I OO 331 6.00 264 33GVLGVLAYGI 31.2151 39 VLFLLFILGY315 VLAVLEAILL 1.200 0L99 241 0 VLSULFO-LL 2370 T] GVAIVI.SUJF 1.2001 680 SLDRPYYMSK 2 IMIAIYGKNF 554 FLNRNAYIMI .200 uU239 ALVLSLLFIL 4.050 Se] LKTL. 120 612 VLSFFFFSGR 5.00 IWGIVAWLY 4.050 265 LGVLAYGIY 1.0 378 [YLATSGQPQY 4.000 [IC1FL 1.200 134 OTVGEVFYTK 441 NLQIYG L 31 II _______ ~53 IVAWLYGOPR 1.200 211 SLNARDISVK 0 S 0 598TFFGaW 3.00 26 VLAYGIXVYCW GLWRNWL .01 621 3.RPLKDK ~ Ii~ .0 Eah etie sa orin4f6 E Table Xll-VI-HLA-A3-l0mers- Table XIII-V-HLA-A3A1mers- Each peptide is a portion of SEQ 24P4C12 24P4Ci2 ID NO: 13; each start position is Each peptide Is a portion of SEQ FStart Sub ue Score specified, the length of peptide is ID NO: 3; eachids, and the end spafed te enthofpetieEsach peptide is a poto of SEQ 10oaitinfor acetdds and the p tnID NO 7; each startpi position fo thaet p eptid is h 10 amino acids, and the end specified, the length of peptide is pstonpsnne position for each peptide is the 10 amino acids, and the end Start ifSubsequence Sco0re] start posito pus nine, position for each peptide is the 1 LPSVN 4 S Subsequnce I )start position plus nine. 0 F275| YCWEEYRVLR [09 90 NITPPALPGI .1351 2 LIPR 0.036 232- ILVALGVALV 0.900] 5 r NiTPPA .15 9 NLOI 0.036] | 325 ] LMLIFLRORI 0.900 3 RCFPWTNITP 0.003 8 LIPRSVFNLQ JO 009] 463 | CVLAGAASF !F0.900| [i-i63 0VAGFS ,900 :-10 IITPPALPGI- 5 SKLIPRSVF J03 |525-|| KLRGVQNPVA 0.900 WTNITPPALP 0 PRSVFNLQIY 0.001 5061 AL0LTLVQ1A 0.900 1 IP 1 603 IKLLWGGVGV 0.900 2 GRCFPWINIT 0.001 4][ SSKGLIPRSV 0.000 633 HLNYYWLPIM 0.9008 I 1 F ][ OGYSSKGUP T 0 510 TLVQIARVIL 0.900 [6 P .13 KGLIPRSVFN 0.000 |365 LLICIAYWAM 40.9004 CF ITPP FLLFILGYIV 0.900 Table XJII.7-HLAA3.0mers 512 - VQIAiViLEY l0.810 Table Xi5-6]ILA-A3.10mers- 24P4C12 604 --LLWGGVGVL 0.810 24P4C12 I SubseuenceS 251 IRLVAGPLVLV 0.67 Each peptide is a portion of S]EQ Each peptide is a portion of SEQ ID NO. 11; each start position is 10 NO: 15; each start position is |F260-11 VULGVEGVI. 110.5080 260 VULVLGL 0608 specified, the length of peptide is specified, the length of peptide is r ]44 ] FILGYIVVGI 0.608 10 amino ads, and the end amino acids, and the end 107-] GLQCPTPOVC 00 position for each peptide Is the position for each peptide is the 327 LIFLRQRIRI 10.600 start position plus nine, tart position plus nine.

F3261 MLIFLRQRIR 0.600 Start [useunce SIor 1 9 H AVGQMMSTMF f0.200j 326-Fo E NUROIN 0 06 F597 LLLFFGKLLV 0.600 6 1 [IUIV FLR 7 1GQMMS 0.1201 F487 | LISAFIRTLR 0.600 | L5][ jI1VGQMM1045 1I20-1 CPEDPW VGK l0.600 FJ1 LLVLIFLRQR 270 1 ST0.0 J 351 T MMSTMFYPLV I0.6002 VLEAILLLVL [l [iwf 1 1I240 l VLSLLFILL I 0.540 ] i WIFLRQRIR 0.600 8 VAVGQMMSTM 252 I LVAGPLVLVL 0I . 5 2 | 360 i VTFVLLCI 00.450| 7 LVLIFLQ 0.270 4] YWILVAVGQM 363 VU.ICAY 0.50 kVLAILL 100.l3 WYWILVAVGQ 10.000 579 MLLMRNIVRV 90.0.o 95e ILSSNIISVA 3-HLA3 1 r Is -LLLVUF 0.054 Table XI-V-HLA-A3lmers I EE[PLEAI4LVLI 10.003 42C412 Table XltV3-HL-A-A3lOMts. _Each peptide is a portion of SEQ 244C12 1] Table XiI-V6DHLANA3ch s mers- ID NO: 17; each start position is I , 24P4C12 specific the length of peptide Is :ia I 10 amino acids, and the end position for each peptide is the ~start position plus nine. Str u ec Score] LGRCFPHVFQTS.0.300 147 Table XIll-VB-HLA-A3-10mers- | Table XII-V944LA-A3.0mers- able XVVI-HLAAI101 9mers 24P4C12 24P4C12 24P4C12 Each peplide is a portion of SEQ Each peptide Is a portion of SEQ Start Subseuence ID NO: 17; each start position is ID NO: 19; each start position i 6 SLLKILGK 0.180 specified, the length of peptide Is specified, t length of peptde is 10 amIno acds, and the end 10 amino acds, and the end posion r a peptide is the position for each peptide is the 9 GVGVLSFFF start position plus nine. start pin lus nine. 485 11 FPLISAFIR start I Subsequence [Score start sbuncelscore [446][ GVLGLFWTL 01 15 WLPIMRNPIT 0.100| 15 PATLGYWWA 0.004 267][ I 21 i QTSILGAYVI 0.0901 10 If T)ATGJ0.00- 27.1 1nI'CWEEYR I.16o Ill LNYYWLPIMR 10.080 2 0 [9W]f ILILVOIAR 13 | lTPTGHIVFQO 5 IMTALYPLPTQ 0.002. 668 LCFLEDLER 4516 11|| NPITPTGHVF |0.030 14 f QPATLGYVLW 0 [698] KNEAPPDNK 0.120 8]| IMRNPITPTG 10.030 12 1 PG WJILGY 47011 YWFK FR 15L| PTGHVFQTSI 1|].0091 6 00 F593 K 0.12 201| FQTSILGAYV |0.006 3 FWAMTALYPLP 0.000 701I1 APPDNKKRK 0.1000 PIONNIM>IYPY l ai)0 PIMRNPITPT 11.0 1I AYWAMTALYP 0.0001 59 5 F TDWY-FGK _0._0 14_ TPTGHVFQTS 0.003 1 GYVLWASNIS 0.0 38 [ CVLFLLFIL 0.090 [1i97[ VFQTSILGAY 0.003 8 LYPLPTOPAT 0.000 2 4 YWUIMRNPI 0.001 54 GDPR Rnntn 6 LPIMRNPITP 0.00 _172 I LPSAPALGR 0.080 FIT][ TGHVFQTSIL 0.001 able XIV.VI-HLA.AI 101-9meis 349 GQMMSTMFY 0072 r2 7 NYYWLPIMRN 0.000, 24P4C12 334 IRIAIALLK 0 [~][ MRNPITPTG [~~J start ISubsequence Score IfLCEFK i I ID9 MRNPITPTNGO: 3. ach sa potion s 545 K 0.060 12 PITPTGHVFQ 0.000| E ach t t portion f SEQ F 0_060, 17 GHVFQTSILG 0.000 specified, the length of peptide Is f AVLEAJLLL 0.060 10 RNPITPTGHV 0.000 9 amino acids, and the end 699 NEAPPDNKK 0.060 13 W1yWL.PIMRNP 0 oooj position for each pepflide . a is te15 GVPWVNMTV1 10.0601 sta sn ne 237 1!GVALVLSLL 0.0601 Table XIl-V9-HLA-A3-10mers- 15 D V4 257 LVILVLVULGV I 0 24P4C12 I I 4.000 DPSFRGPIK 0.060 Each peptide Is a portion of SEQ 44 CVFOGYSSK 4.000 KNAFMLLMR 0048 10 NO: 19; each start position is 6 YIM YGK 1 21 i specified, the length of peptide is 6 [ YYMSKSLLK 1.600 10 amIno acids, and the end 542 KCCLWCLEK 1.200 position for each peptide is the 7161 PVKYOPSFR k.0401 start position plus nine. 6 0F SVQETWLAA 0.040 Riat Subsequence ore, 51 VILEYIDHK 0.600 [19 1 SGRIPGLGK 0.040 7 l ALYPLPTQPA 2.250 [ 1 M'CGMVGENK 0.400 50 1 GIVAWLY 0.040 4 AMTALYPLPT 0.600 393 1 NISSPGCEK 0.400 1i fLPTQPATLGY 0.08 6621 LDLNR 0.6 CVDTLFLCF 0.040 F 13] TQPATLGYVL 5 323 LULMLIFLR 0.360|0.054 16 | ATLGYVLWAS |0.030 3KESK 0.300 83 KPYLLYFNI 0 17 |TLGYVLNA5N 0.240 472 GYIGIVA 0.036 9 I YPLPTQPATL ||0.013 243 SLLFIWR 0.40! 2 T abl X251-V9-HLA-A3-10mers I!.IIS oq I~GLspcFKi0.200 te383 legGQPQYVLWA 0.036 148 able XIV.VI-HLA-A1I01-9mers able XIV.V6HLA-AI 101 *Smers 24P4C12 able XIV-V3-NLA-AIIOI-9mers 24P4C12 Start|| Subsequence [Soe24P4C12 - St Subsequence 49i 0.0301 Start Subseguence l$0ore 7 UPRSVFNL 34 IVLAVLEAI 0.030 Each peptide Is a portion of SEQ 2 ~ YSSKGLIPR O0081 456T WVLALGQCV 0.3 SID NO: 7; each start position '3 1 GYSSKGLP 10.0021 _______________ pecified, the length of peptide is 589 VVLDKVTDL 0.030 9 amino acids, and the end 6 GLIPRSVFN 0.002 452 WTNWVLAL [.030 position for each peptide is the 5 KRSW]0.001 141 || YTKNRNFCL 10.030 st position plus eight 8 _ 0.00 498 I HTGSLAFGA 0.0301 9 ITPALPGI 01 9 0 65 iLVVGGVGVL lgo0.030FNO)1000 _11q2 6G]000§1 W11flTPPAL 0.0101 4 SKGISV 10.00 362 FVLLUCIA l0.030| 2 0.01 3 SSKGLIPRS 611 GVLSFFFFS 00.0271 8 = ].SK0 F5137 0 = GP i0.001 able XIV-V7[FLA-AG 101.9mers 564 i AYGKNFCV 0.024 4 F 24P4C12 272 G0YYCWEEY 0.0241 ] 11 CFPWTNIT Each peptide Is a poion of SEQ 60 DPRQVLYPR l0.024| L-7 TNITPPAL ID NO: 15; each start position is 421 GLMCVFQGY [024 D.2 PWTNITPPA specified, the length of peptide is 467. 9 amino adds, and the end 467 1 SW 0 Jposition for each peptiIs the 449 GLFWTLNWV 0.024 able JV-V-HLA-AIIOI.9mers start Po s siht. 660 0.024 24P412S 4 RY GAF 0.024 Each peptide is a portion of SEQ RYTGLA ] 002 ID NO: 11; each start position is 8- MMS7M .2 511 LVQIARVIL 10.020 specified, the length of peptde is 5 ILAVGQMM 10.006 218 SVKIFEDFA0. 9 amino adds, and the end 4 0.02LVAVGQM O06 233201 position for each peptide Is the 0.60 2MS0.0 ~ ]J SFRGPKNR 0.020start position plus e'.t ~ 2 I F2271 SFIRGPIKNIR |0.020|2 WWIVV 75 1 CGMGENKDK | Sa - S 7 1 VAVGQMMST 0.001 -414-|| LVNSSCPGL 10.020 6 If 1031 1 9 SWYWLVAV 10.00 F252 iLVAGPLVLV LVUFLRQR 0.060 WILVAVGQ .020 5711[ CVSAKNAFM 0.020V 0.012 AVGQMMSTM | ILLLVLIFL .012 able XIV-V0.0LA2A0I01.9mers 53W ARCIMCCFK 10.020|LAILV .082P41 527 R CIMCCFK 0.0 1 9 =IFR 0.006 Each peptide is a portion of SE 57.l| RGVQNPVAR 10.018| 34 DVICCVLFL 0.018 = 1 LLVLIFLRQ [ID NO 17: each start position is 693 1 .02 - I LEAILLLVL 0 specified, the length of peptide is 011 IL 0 1 'LLL 9 amnino adds, and the end 461 0CYIA F o018 I 0 position for each peptide is the 4 11 start Position plus eht 1 1 RQRIRIAIA |0 018 able -HLA-A 9mers Stan Subsuence 10 DEAYGKPVK I 08 24C12 NYYWLPIMR I 0.32D iolJ2 DEAYGKVK 0.01 Start Subs uence Score20 QTSILGA YV ooo 442 LQWYGVLGL 0.018 Each peptide Is a portion of SEQ 7 HVFQTSILG 00 255 GPLVLVLIL ID0 13; each startPositionis 1 598 1 __________0.016 Specified. the leOt of peptidle Is9 FTSLA 006 42 LLFILGYIV 0.016 9 amino acds, and end VFQTSILGA .004 244.. LLIW. RL IF-16 position for each peptide is the 4 L~ 0.0 244 j LLFILLLRL 00.016| ~ ~ eh PTTH .0 3 2 7 1D N e ach start p ositio n i 149 r able XIV-V8-HLA-A1 101-9mers. able XIV.BHLAA1101-9mers Table XVV1-AIl1-l0mers 24P4C12 24P4C12 24P4C12 Each peptide is a portion of SEQ Each peptide Isa portion of SEQ Each peptide Is a portion of SEQ ID NO: 17; each start position is ID NO: 1; each start position is ID NO: 3; each start position Is specified, the length of peptide is specified, the length of peptide is specified, the Length of peptide is 9 amino acids, and the end 9 amino acids, and the end 10 amino acds, and the end position for each peptide is the position for each peptide is the position for each peptide is the start position plus eight. start position plus eight start position plus nine. | Start j Subsequence scorer] Start Sub Score] [tart Subsequence Score 2j_ YYWLPIMRN |10.002] 1411 PATLGYWW 0. (64 PYYMSKSLLK LJLLRNPITPTGH 0.001 FF 1- LGYVLWASN 1 667 I .FL1117REO.160 [121 [rPTGHF EE =Ii YWAMTALYP 0.00 LU]!- ILLPSAPALGR 0.160] S16I GHVFQTSIL ||00 I0 RDEDDEAYGK 1 L TPTGHVFOT Table0X_._I-A10-0mers- 981! K 0.120 |i] 1 24P4C12 14 || PTGHVF 0.120 1 7E IMRNPM [10 Each peptide is a portion of SEQ r GVALSLLF 0.120 _________ .0 ID NO: 3; each start position Is 174 IYCGMGENKDK 0.100 specified, the length of pepide id 15 11 TGHVFQTSI 0.000 10 am acids, and the end 689 ILGKK 0.090 6 FIMRNPITP 0.000 position for each peptide is the YVIASGFFSV 0.090 14 PTGIVfQTS start position plus nine. RVLRDKGASI 0.090 8 MRNPITPTG 0S0s0uncStart Subsequence Score |ScorFq2| 31 YWLPIMRNP |0.00 | 516 RVILEYIDHK 9.000 FT8[ LISAIRTLR 0.080 1v8LLLFFGK [3.000 1 YCWEEYRVLR OVA ||0 able X.V9.HLAAiIOI.mers 13N[ QTVGEVTK j3.000 [438][ SVFNWMQTYGALYP |00 24P4C12 F33 || G2.0 0.60970 K6EAPPDNK Each peptide Is a portion of SEQ 5-44 ][I CLWCLEKFIK 2.400 392[ SNISSPGCEK o.060 ID NO: 19; each start position is |06.210 RIPGLGKDFK 1.200 04 CVSAINAFML 0.060 specified, the length of peptide is 55 [AIIIG 1.0 I2911LIGLV10.0 amino acids, and the end1 YMIIG 1.200 r -2-9 LLLVG . positi each peptide Is the GAYCGMGENK 1.200 491 IWGIVAWI 0.060 start position pseiGh 58411 NIVRWVLDK 1 1240 10.0L0L2L |0.060 [Start Subse uence I [601 SLDRPYYMSK 0.800 r~L 317 AVLEAILLLM 10.060 15 I ATLGYVLWA 0.030 IF ASFYWAFHK 0.600 0 1 FVLICIAY 0.060 18 GYVLWASNI 0.018 2721j GIYYCWEEYR 10.480 433 GLIQRSVFNL 0.0541 .2 WAMTALYPL 0.008 [428[!GYSSKGLIQR 0.480 449 GLFWTINWVL 0.048 12 TQPATLGYV 0.006 337Jj AIALKEASK 0.400 RTIRYHTGSL 0.045 8 |YPLPTOPA 0.004 3 W0.4001 518 0.040 131 OPATLGYVL 2.00 0~f] .. R4p!Wy! 10.400 25 LVAGPLVINL 0.0401 [ IMTALYPLPT 10.002 322 HL ILILMLIFLR 0.360 61 FSGPGLGK 0 [11 PTOPATLGY 0.002 r 423][ MCVFQGYSSK 0.300 68 SWLK 040 [6T ALYPLPTQP 0.001 507A 00.2401 606 WGGVGVLSF 0.0401 [16 ThGYVLWAS 0.001 578 1 L U.NY R J 2401 541 FKCCLWCI.EK 0.0401 1811 YPLPTQPAT 90.000 15 1 KPVKYDPSFR 0.180 233 LVALGVALVL 0 .o40oj _5 7 TALYPLPTQ ||0.000 284 1 GGI 0.8 0 ol LTQATLG q0.0001 609 1 GVGVPFj 0.18 0.030 150 Table XV-VI-A110110mers- Table XVVIAI I0l-l0mers- T X- V SHL-A1101. 24P4C1224P4C12 mers-24C12 Each peptide Is a portion of SEQ Each peplide is a portion of SEQ Each peptide Is a portion of SEQ ID NO, 3; each start position is ID NO: 3; each start positon is ID NO. 11; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptde Is 10 amIno acids, and the end 10 amino acids, and the end 10 amino adds, and the end position for each peptide is the position for each peptide is the position for each peptide is the start position plus nine. start sition us nine. Start || Subsequence SScorec ore enceScore 157 |1 TVITSLQQEL O.030 267 GVLAYGIYYC [87 L LI F0 1 1 4-63 CVLAGAFASF |0.030| I Jj LLJ 0001 F588| VVVLDKVTDL 0.0301Table XV-V3LAAiO 700I EAPPDNKKRK .0mers-24P4C12 Table XVV6-HLA|AI.O00 314 IVLAVLEAL Each pepde Is a portion of SEQ 0mers-24P4C2 456 WVLALGQCVL 0.030 ID NO: 7; each start position Each peptide is a portion of SEQ specified, the length of peptide is ID NO: 13; each start position is 27| LVLVUILGVL |0.030en 34) LV VU G L O 10 amino acids, and thsn pecified, the length of peptide Is 34 [ DVICCVLFLL |0.0271 position for each pepde Is the 10 amino acids, and the end '611 I GVLSFFFFSG 0.027 start Position plus nine, position for each peptide is the 59 I GDPRQVLYPR 024 Str Subsequence Score start siton us nine. 220 I KIFEDFAQSW 10.0241 NITPPALPGI Start Subseuence Score 654 [GFFSVFGMCV |0.024| 5 FPWThITPPA 0 2 GYSSKGLIPR 0.480 548 LEKFIKFLNRT0241 RCFPWTNITP 0.002 7 GUPRSVFNL 0.054 467 ] GAFASFYWAF |0.024 r WThITPPALP 0.001 9 IPRSVFNLQI 0.004 674 I LERNNGSLDR 10.024| ITP0.00 1 8 LIPRSVFNLQ 0.000 347| AVGQMMSTMF 10.020| 4 CFPWTNITPP 0.0 5___ 566 1 YGKNFCVSAK |0.02o 1. GPWl 000 6 KGLIPRSVFN 0.000 353 I STMFYPLVTF 0.020 F |I PPG0.000 VF [.00 J IVRWVVVKV 0.620 L PRSVFNLQJY [.00 1701 11 APPDNKI(RKK 10.020 6.00[ F 4 I1 SSKGLIPRSV0.0 304_j| SVQETLM L 0.020 I 0.0200 I 380 IASGQYLIo0oTable XV-V5-HLA-AiIOI. ___________ _30|ATSGQPQYVL |0.020| 662 CVDTLFLCFL 0.020 |1mers-2414412 Table XV4V.ILA-A1IO1. Each peptide is a portion of SEQ lmr-441 414 | LVNSSCPGLM 0.020 ID NO: 11; each start position I cpeIs-a pn S I 19 YDPSFRGPIK 0.020 specified, the length of peptide is IDE 5 ach pel sa position 116 CVSSCPEDPW 0.020 10 amino acids, and the end ID the enh of postioe is 186 NVTPPALPGl 0.020 positn feac peptide Is the 1acifd, the ed 642 MTSILGAYVI 0.020 position for each peptide the - ~~Start Subsequence scorestr Iio nne 512_ jVQARVILEY 0.018 p ls I 1~ I KQDPTL 0.18 [6 j ILLLVLIFLR 0.360 Start IISubsequence Sicore] F4781 KQDIPTFPL 0.1 47 i YIWIVW 018j1 AVLEAILLLV 0.0601 9 AVGOMMSTMF 000 47 ____ 00 9 V 0 WNYAVGQMM 0.006 461 GQCVLAGAFA 0.018S 239 I~ALVE~FII |01L IR .012 8 IVAVGQMMST 4 KQRDEDDEAY 0.018 AIL11 VLIFL. 0.012 8IVAVGQMMS 0.001 3 KLLVGGVGV 0.018 wL AuLuLvi. 0.01 6 ILVAVGQ 0.0 553 KFLNRNAYIM 0.018 2 EAILLLV 0.002 3 0.000 163 QQELCPSFLL E001 ILIV 7 =02 SY VA_00 151 Table XV-V7-HLA-A1OI- Each peptide is a portion of SEQ Table XVI-VI-HLA.A24-9mors l10mers-24P412 j ID NO: 19; each start position Is 24PC12 Each peptide Is a portion of SEQ specified, the length of peptide is Each peptide is a portion of SEQ ID NO:. 15; each start position is 10 amino acids, and the end ID NO. 3; each start position is specified, the length of peptide is position for each peptide Is the specified, the length of peptide is 10 amino adds, and the end Stpotition plus nine. 9 amino acids, and the end position for each peptide is the Start Subsequence Score] position for each peptide is the start sition lus nine. 13 TQPATLGYVL 0.012 start tion lus el t Start Subs uence Score 7][ ALYPLPTOPA 0.00 Start Subseuence Score 4 YWLVAVGQM 0.000 i117 LPTOPATLGY 0.004 [ 03 iLVAVG 0.000 9 ][ YPLPTQPATL 0 ______________16][ATLGYVLWAS 003 666 LFLCFLEDL 0 Table XV-V8-HLA-A11011- 14 QPATLGYVLW 0.002 10mers-24P4C12 GS 0 LFWTLNWVL'0 Each peptide is a portion of SEQ - AYWAMTALYP 0.002 ID NO: 17; each start position is - 3 AFGALIL specified, the length of peptide is 12 PT'AThGW 0.00 10 amino acids, and the end 5 MTALYPLPTQ 0.014 PYLLYFNIF position for each peptide Is the 4 1 ANTALYPIPT 0.00 start position plus nine. 8 LYPIPTOPAT 1 540 C 0 * 11 0.3 -tartce 1Scoe 181 LGIWASNI 0.010.02 20H0 15 I YVWA0.00 684 PYYMSKSLL 0FL. 1 LNYYWLPIMR 110032 j0i 0jt 0.003,LYVWSN0.0 00 13 IQTTLGAYVI 0.020 3 W 617 F LfjG 0 19 FQTSILGAY 0.006 2 a 11 FJj NPITPTGHVF 0.003 TALYP2'O 0.000 6 5 8 VFGMCVDTL 00 10 RNTPTGHV 0.001: ALPPO ].0 S PTGHVFQT 0.00 PLPTQPATLG O. 1500 F-1][ VFQTSILGAY 0.002 5 KFLNRNAYI 0 5 NYYWLPIMRN 0.002 Table XVI-ViHLA-A24-Smers- 251 RLVAGPLVL 12.00 S M RNPITPTGHV 0.001 24P4C12 0.000 (15]( PTGHVFQTSI 0.001 Each pepide Is a portion of SEQ 58 ]2 F-6 ]1 LPIMRNPITP 0.001 ID NO: 3; each start position is specified, the length of peptide is 4 TFPUSAF 0 7 WLPIMRNPIT 0 9 amino adds, and the end position for each ppde is the .5 F-4- 7 YWLPIMRNPI 0.000 start position plus eig . F-9-11 MRNPITPTGH 0.000 Start Subs uence ore 0.50 14 I I TGHVQTS '6-.0[00 20.0 3 0 1_ AYQSVQETW 0% __ AL 36 0YPLPTPA .0 16 ~ ~ ~ ~ ~ 1 ATLGYVLWAS.00 0038 AAFWA 1.1 17~1 QPATLGYVLW 0.0.02 7 I PIMIRNPITT 0.000 1 YGVL N 00 VFYTKNRNF 0 SIP 0496 ARYHTGSLAF I0.0 1 2 P2 PTT A L 0 0 0 . 0

-

91 41MTLPLT 0.011 TFLCI .0 68AYVAIASGFF 00 36 lmr.4C12 87 44811SC 0 VGF~ .4 II1750 258 V]1 ILGVVL 8.400] 3816 GYVIWASNI M500 49_ I IWVGIVAWL H8.400] 152 Table XVI-V1-HLA-A24-9mers- Table XVIVI-HLA-A24-9mers. Each peptide is a portion of SEQ 24P4C12 2412402 ID NO: 7; each start position is Each peptide Is a portion of Each peptide is a portion of SEQ specified, the length of peplide is ID NQ 3; each start posion is ID NO: 3; each start position i 9 ammo acds, and the end specified, the length of peptide is specified, the length of peptde is position for each peptide Is the 9 amino acids, and the end 9 amin acids, and the end position for each peptide is e post for each peplide is the tSharte] Subsuence Score start position plus eighL start ion us hig I 6 Start Subsequence Score Start[ S uence Score] 971 ITPPALPGI 1.800 154 i WNMTVITSL 8.400| 452 WTLNWVLA. 6.000] [T2[ RCFPWTNIT 10.288 31 1] AAIVILAVYE4 28.4001 i ] II .000 = GRCFPwTNI .0 P 261605 6-000] 3 CFPWTNITP 0.075 440 I FNLQIYGVL I8.400| 638 . TNITPPALP .01 42i7 VALGVALVL |8.00| [ 511 VOJARL 6. 68311 RPYYMSKSL | 1 163 QQELCPSFL 6.000 8 NITPPALPG 0.012 333 | RIRIAIALL ||8.000| 291 SQLGFTTNL . 4 FPWTNITPP 0.010 596 | DLLLFFGKL 7.920 j 434 1IRSVFN N L _ 65 ||. LYPRNSTGA 7.500 432 KGLIQRSVF 6.000 Table )VI.V5.HLA-A24-9mers 328 ] IFLRQRIRI 7. 225 FAQSWYWIL 6.000 24P4C1 2 317 | AVLEAILLL 7.200 322 ILMLIFL 6.00 Each peptide is a portion of SEQ [2551 GPLVLVLIL 7.2001 593 KVTDLLLFP 5.760 ID NO: 11; each start position is _______ ___________ specified, the length of peptide is 38 | CVLFLLFIL 7.200 24 VSLLFILL 5.760 9 amino acids, and the end 240| LVLSLLFIL 17.200 9 H VAGPLVLVI 5.760 position for each peptide is the 232][ ILVALGVAL 7.200 237 GVALVLSLL 5.600 start p ion pls eight 589 1[ VVLDKVTDL I7.200 228 1 SWYWLVAL 5.600 Ss e M170][ FLLPSAPAL 7.200 24 H LLRLVAGPL 5.600 5 ILLLVLIFL 6.400 357 j YPLVTFVLL 17.20 31 CCFL 5604 ALVU 3.0 236 i LGVALVLSL 7.200 1 32 1 CTDVICVI 5.600 9 VJFLRQ 21[60 621 l RIPGLGKDF 7.200 1 590 VLDKVTDLL 5.600 3 EMLLL [18 _158_ VITSLQQEL 6.336 217 F 5.040 2 LEULyV j 0.480 305 1 VQETWLAAL 6.000 224 DFAQSWYWI 5.000 1 VLEAILLV 0.21 157 [KPVKYDPSF 6.000 6 SFFFFSGRI .000 7 f 54 CLEKFIKFL 6.000 274 CWEEYRV 5.000 6 Lf H 1 59I1 LLLFFGKLL 6.000 631 YYWLPIMTS 5.000 8 LVUFLRO .015 565 j IYGKNFCVS 6.000 370 AYWAMTALY 5. _34 j DVICCV1L 6.000 AFMLL 4.800 Table XVI.V&HLA-A24-9mers 308 TWLAALIVL 6.000 MSTFYPL 4.800 24P4C12 184 j WTNVTPPAL 6.000 315 VLAVLEAIL 4.800 Each peptide isa portion of -11 IVEG 4.0 ID NO. 13; each start position is 316 LAVLEAILL 6000 specified, the length of peptide is 200 TIQQGISGL 6.000 2 GISGLIDSL 4800 9 amino acds, and the end 635 NYYWLPIMT 6.000 687 4800 position for each peptide is the 140 FYTKNRNFC 6.000 4600 S 673 I DLERNNGSL 6.000 499 1 4800] Score 442 || LQIYGVLGL 16.000 5 [K P7 6. 0 14 LVNSSCPGL 6.0 Table XVI-V3.HLA-A24-9mers LI PRSVFNL 444 IYGVLGLFW 116.0000 24P4C12 1_ _ _ _ _ _ _ _ _ _ 0 50011 153 Table XVI-V6-HLA-A24-9mers- Table V8-HLAA24-9mers- Table XVI-V9+LA-A24-9mers. 4 24P4C12 24P4C12 24P4C12 Each peptide is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 13; each start position is ID NO: 17; each start position is ID NO: 19; each start position is specfied, the length of peptide is specified, the length of peptide Is specified, the length of peptide is 9 ammo acids, and the end 9 amino adds, and the end 9 amino acids, and the end position for each peptide is the position for ea peptide Is thi position for each peptide is the start position olus eight start ton lus eght start position plus eih. Start Subseqne Score Start Subsequence Score [Start 1 Subseauence 6 GLIPRSVIFN I NWLPIMR 0600 5 TALYPLPTQ 3 SSKGLIPRS 0.120 1 LT HV 0.240 6 ALQP 11TI 8 IPRSVFNLQ 0.020 1 T NPiTPTGHV 3 AMJJ YPL SKGLIPRSV 0.014 5I LPIMRNPIT 0.15 [ 1 M iPTii1Ii .010 YSSKGLIPR 0.010 1 1 FOTSLGAY 0.140 1 4 , 010 9 PRSVFiNLQl 20 QTSILGAYV 0120101 'TPj .01 Oj _______________13 Hi WTrolvForJ 0.1001 ________ Table XVI-V7HLA-A24-9mers. 7 IMRNPITPT 0.1001 Tabe 24Ci2 24P4C12 9 RNPITPTGH 0.00 20402 Each peptide is a portion of SEQ 3 YWLPIMRNP 0. Each peptideisaportionof SEQ ID NO' 15; each start position is 1 ID NO.3; each stat position Is specified, the length of peptide is specified, the length of peptide is 9 amino acds, and the end 12 1 ITPTGHVFQ 0015) 10 ammo acids, and the end position for each peptide is the 7i H LG 0.010 position for each peptide Is the 8 003start position plus eigt. position plus eight 8 MR1 TT p .0)sat Wnlus nine. . Start || S e n Scorel PMRNPITP 0.002 S Subsequence Score 5i GQM 1.260 356 FYPLVFVLL 6 f4 | WLVAVGQM 0.750| T 2 || WYWILVAVG 0.60024P4C12 301 AYQSVQETL 00 8 || AVGQMMSTM | w Eachpeptide5Is0apo0ionofSEQ 7 1 VAVGQMMST 0.150 ID NO: 19; each start position is 87 LYFNIFSCIL 1ill SWYWILVAV |0.140 specfied,thelengthofpeptldeis F-79 amino adds, and the end 140 FYTXRNFCL .0 position each peptide is the 00 IL1391 YWILVAVGQ I0.021 start position plus eght 274 Y 0 Start 11 Subsequence Score F__0_ Table XVI-V8-HLA-A24-9ers- 00 24P4C12 Each peptide Is a portion of SEQ 7 .P. 9.00 ID NO: 17; each start position is WAMTALYPL 6.000 specified, the length of peptide is 13 OPATLGYVL 4.800 6 YYMSKSL 50 9 amino acids, and the end 0 position for each peptide is the [ PLPTQPATL 0.600 stat Position plus eight 8I YPLPTOPAT 0.180 636 YYWLPIMTSI 00 Start I Subsequence Score 15 ][ATLGYVLWA 0.150 2 YYWLPIMRN 5.000 12 TPATLGYV 0.1 F 4 WLPIMRNPI 1.800 16 TLGYVLWAS 0.140 3 MFYPLVTFVL '15 TGHVFQTSI 1.000 17 LGYVLWASN 0.120 is H FTIG O774 1MTALYPLPT 0.100 j169 SFLSPA n0 ]~~I1 GVQSL 06011 PTQPATLGY 0.018 14 11 GVFQTSILG S0. 0 0 154 Table XVII-VI-HLA.A24-10mers- Table XVIl.V1-HLA.A24-1Omers. Table XVII-Vi-HLAA24-10mers. 24P4C12 24P4C12 241402 Each peptide is a portion of SEQ Each peptide is a portion oSEQ Each peptide is a portion of SEQ ID NO: 3; each start position is ID NO: 3, each start position is ID NO: 3; each start position Is specified. the length of peptide is specified, the length of peptide is specified, the length of peptide Is 10 amino acids, and the end 10 amino adds, and the end 10 amino acids, and the end position for each peptide is the Position for each peptide is the position for each peptide is the start position plus nine. statsition us nine, start sition us nine. -S-tall Subsequence [Score Start Subseuence [scre Start Subsequence Score 65 ~ '1 LYPRNSTGAY 7.5D 500 [so] SLAFOALIL 6. 000 __________ r 553 KFLNRNAYIM 7.0 3 [KYLLYFNIF 5.6 616 FFFSGRIPGL 05.60 224 DFAQSWYWIL 200 SVQETWLAA 7.200 233 LVALGVALVL 5.6 U.4 231) WILVALGVAL 7.200 227 1 OSWYWILVAL 560-01 478 KPQDIPTFPL FJ1437[ YWLPIMTSIL 7.200) 661 MCVDTLFLCF 5.184 131 iEFSQTVGEVF 1 16 LQQELCPSFL 7.200 565 IYGKNFCVSA 5.000

SE

1 2239 ALVLLfL 7.200 279 EYRVLRDKGA 5.000 1400 318I VLEAILLLML 7.200' 635 IfNYYWLPIMTS 15.000 658 VFGMCVD314]f IVLAVLEAIL 720 273 I YYCWEEYRV 5.0001 569 NFCVSAI(NAF F-712.00 1 37 17.200 444 IYGVLGLFWT 5.000 1. 546 11 jCEKIKLj 7.J I 686 IIYMSKSLLKIL -4.80D 14 63 SPLYYL350 OMS1FP ~ ~ 7 .2001 56 ~IWLYGDPRQvL 4.800 -99 1 ... II EN L 7.200 2351 ALGVALVLSL 4.8W0 493 RTLY jGS 203~ 11 QGISGUDSL 7.200 252 IILVAGPLVLVL 4.8001 -II 11.20 243[ SLLFILLLRL 7.0I491 LFTNV 480 331 RQRIRIAIAL 0229 WW[LVALGV 7.000 502 LAFGALILTL 4.8001 51731 SCTVICCVL 6.720 625 LGKDFKSPHL 4.80 8441] GW E6.000[] 81 HTGSI.AFGAL F4. 800I 35711 rLq1[70 [ H VSAKNAFMLL ]R4.80W 4 FIU LGYI "5 -P~FVL]600 0 tr641 LLWGGVGVL 16.000 j5421 KCCLWCLEKF 4.4001 589 WLDKVTDLL 10.08 510 TVQARV1L 6000 442 ifIYGVII4.0 L F596 If DLLLFFGKLL 6.0 F368 ifCIAYWAMTAL 4.000O TVITSLQIQEL 19.5040 157 EY1I14KLRGEV 9.504 536 If CIMCCFKCCL 6.000 (241 IfVISILFILL 14000] 52 EYIDHKLRGV 19.000 600 386 ||QYVLWASNIS 09.000| 58 WLKVD .0 386 Hf QYVLWASNIS 81.040 [337] GLQRSVFNL 6.000 Table XVII.V3-HI.A.A24-10mers. 445 YGVGLFVTL 8.640 659 FGMCVDTLFL 6.000 24P4C12 S LVSLLFILLLAGQCVL 6.000 Each peptide s a portion of SEQ 1 2 I U.VAGPL 8.400 413 IfiP 60 ID NO.7; each start position is 257 3 LVLVULGVL 8.400I specified, the length of peptide is 482901 ISQLGF11NL 6.000 10 amino acids, and the end :i~111 YWGVAW. A773257 MLLMUFL 6.000 position for each peptide Is the L260 JVULGVLGL .,40 ~][VULVLGI 8400 [31 If L 1111LL 6.000 startt osltk us nine. LGVALVLSLL .LYGDPRQVLY 6000 Start Subsequence re V34 I 9DVICCVLFLL 8.400] [91 6 NITPPAGl 1.200 |63 RPYYMSKSLL ||8.000| = FCLSI .=0- -1 48 1 AYVIA GFFS 7.500 1 11 M GEKDKPYL 600 1 LGRCFPW T I 01.00D 648IfAYLASFF 7500 163] FQQELCPSFUL.6000 ~ 6 JPWTNITPPAL [O.400) T 4- 1 GYIVYIVAW 17.5001 1F1991 TTlQQGISGIL.0600O ~ 0.~ 155 Table XVI-V3-HLA-A24-10merso Table XVII-V6-HLA.A24-mers-I 41 YWLPIMRNPI 12.1601 24P4C12 24P4C12 - ::]I Each peptide is a portion o SEQ Each peptide is a portion of SEQ 21 if QISILGAYVI 1.0001 ID NO: 7; each start position is ID NO, 13; each start position Is 3 ' IMRNP 0.700 specified, the length of peptide is specified, the length of peptide is 10 amino acids, and the end 10 amino adds, ard the end 10 L RNPIGH I position for each peptide is the position for each peptide is the 14__ TPTGHVFQTS 02 start position plus nine. start position plus nne. 5 WLPIMRNPI 1 o-isoj Stat Sbsguence Score Start Subsuence Score 1 GHVFQT 0.150 5 FPWTNITPPA 10.1401 . 6 H RSWN J 20 F I E120 4 ]CFPWTNITPP 0.075 5 11 SKGLIP .200 18 HVFQTSILGA 0.100 31i RCFPWTNITP 0.024| 4 SSKGLIPRSV 0.4571 PTGFQTSI 10 8 | TNITPPALPG 0015 3 1 YSSKGLIPRS 2I LPIMRNPITP|[0 WTNI TPL 0.1 81 LIPRSVFNLQ 0.30 1l PIMRNPITPT 05 SGRCFPWThIT 0012 11 QGYSSKGLIP 10.0101 8 1IMRNPITPG 10.0141 _____________10 IfPRSVFNLQIY IR 10 II LNYYWLPIMR 0.0121 Table XVl-A24-10 mers- le A24-0 e - H 1.002] 24P4C12TalXVIV.LA4.mrs] 1 Each peptide is a portion of SEQ 24P4C12 12 1 PH VQ 0.00I ID NO:11: each start position is P1dUM specified, the length of peptide is ID NO: 15; each start position is 10 amino acids, And the end specified, the length of peptide is Table XVII.V9.HLAA24-l Omers-I position fo each peptide Is the 10 amino acids, and the end 24P4C12 s position lus nine. position for each peptide is the Each peptide isa portion of SEQ start ore nin ID NO: 19; each start position Is StSatarrt S[bseuence Score specified, the length of peptide is S VLEAILLLVL 7.200 AVGQMMSTMF 2.000 10 amino acids, and the end - -~- ~"position for each peptide Is the 4 EAILILLVLIF 3.600 _5 I1LVAVGQMM 1.260 us nine. 9 LVUFLRQRI 2.160 4 ir YIiVVGQM rI.750 Start I Subsuence icre ~j AVLEAILLLV 0.252 'M H .750 19 GYVLWASNIS LEAJLLLVLI 0.120| 3 WYW1LVAVGQ 0.700 8 LYPLPTQPAT 7.500 7 __ LLLVUFLRQ |0.025 6 ILVAVGQMMS 0.150 13 TQPATLGYVL 7.200 61 1 VILLLVIFLR 0.018 0.140 YPLPTQPATI.] DI 10 VLIFLRQRIR 0.015 R LVAVGQMMST 0.0 2 YWAMTALYPL . 4.000 81| LLVUFLRQR 0.0151 SWYWLVAVG 0.012 18 LGYVLWASNI 1.001 1 AYWAMTALYP 050 Table XVII-V6HLA-A24-10mers- Table XVII-VS4ILA-A24-10mors- 16 ATLGYVLWAS 24P4C12 24PC12 Each peptide is a portion of SEQ EachpeptideisaportionofSEQ 7 ID NO: 13; each start position is ID NO, 17; each startposition Is specfed, the length of peptide is specified, the length of peptide is [ TLYVL 0 10 amino acids, andtheend I0aminoacids,andtheend 14 QPATLGYVLW 0.100 position for each peptide Is the position for each peptide the LPTQATLGY 00 start position plus nine. start p on us nine. PTQPATLGYV 0.018 Start Subsequence reuence Sre 7 GLIPRSVFNL 7.200NYYWLPIMRN [TALYPLP ] 0.018 9 IPRSVFNLQI 1.000 16 TGVQTSIL 4.000 IN 21 GYS GUPR 0 11 NPITPTGha 3.000 15 0.0s0 10 amino acid, ad thPen 1|SG R F|2 1SGPRV6 .4 Table XVII-V9-HILA-A24-1l0mers- l VI HLA.B7.9me able XVIIl-V1.HL-B7.9mers. 24P4C12 24P4C12 1 241402 Each peptide Isa portion of SEQ Each peptide isa portion of SEQ Each peptide is a portion of SEQ ID NO: 19; each start position Is ID NO: 3; each start position is ID NO: 3; each start position is specified, dhe length of peptide is specified, the length of peptide is specified, the length of peptide Is 10 amino acids, and the end 9 amino ad and the end 9 amino acids, and the end position for each peptide is the position for each peptide is the position for each peptide is the start position plus nine. start sition pus eght sition lus eight Start I 5uisequenceS-ore Start S core start Subseuence Scorel 10 H PLPTdPATIG 0.002 20.00 241 VLSLLFILL4.000 _______________ It ... 236 LGVALVLSL 4.0001 Table XVlII-VI-HLA-B7.9mers- 605 LWGGVGVL ' 440 FNLQIYG 4. 24P4C12 P7 rvPA Each peptide is a portion of SEQ 34 DVICCVLFL .12 597 LLLYFGKLL r ID NO: 3; each start position is 0 ________ 40 specified, the length of peptide Is 589 L .00 9 amino acids, and the end _ 0 275 1YCWEEYRVL position for each peptide is the 34iV 1500 170 FLLPSAPAL start position plus eight QMMSTM Start S uence1 Score 5 S 12.00 VLRDKGASI 255 GPLVLVL 0.00 0 158 ](VITSLQQEL 40 253 VAGPLVLVL 12.00 [537 IfIMCCFKCCL ]4.000 631 SPHLNYW P000101 . 5 83 ~~12-.0__ __ 0 5660 GMCVDTLFL 14.000 SIAYWAMTA. [7457] VLALGQCVL 4.000 357 YPLVTFVLL -225 FAQSYWL I 12.00 F499 TGSLFGAL Igp 683j RPVYM S- 1 0_____ lI YPRNSTGAY 114.D0 63 RPYYMSKS 0" 00 0.0211 - ADSK r_ _ _i.o [Wf KNRNFCL ]IDD 317 AVLEAILLL[r 5 LNRNAYIMI 4.000 249 LLRVILVGP L200 FQGYSSKGL114.000 311 _4 -LAGLI 24 I LLR 4.0 = 41 WNMTVITSL [242LVNS G 4.0 494 GLG TL D.0 RTL 4.000 24P4C1 Each LA E AILL d p of SEQ 9333 dRIRIAIAm 0aci s ad 0 0 ____ 234 IIVALGVALVL 3510 3 f1 MMSTMFYPL 4.000 3WO5 LQIYGVLGL 4.00 34 DVICCVLF 0 jj 396 SPGCEKVPI 80 00 200 TIQQGISGL 4.000 1I LVIARVIL v.00 83 KPYLLYFNI 8.000 44 UQRSVFNL 4.000 __A______408 - TSCNPTAHL 8.000 501 ILAGAIL 14.000 414 LVNSSCPGL Pu0 381 TSGQPQYVL 16.000I 32 .j1 ILLLMLIFL 14.000 -H20.__20 571 CVSAKNAFM PLVLj . RLVAGPLVL 4.000 381J CVLOLLF 11-0 221 LILGVLGVL 4200204 GISGLIDSL 4.000 9 IWIVAWL 00 315 VLAVLEAILL 400 1 VSAKNAFML 4.0 I] 80 291 SLGFTrNL 4.000 6 MSKSLLKIL 4.000 0.6 1 0638 WLPIMTSILT 4.000 100 IISVAENGL 4.000 .0258 VLVLILGVL 4.000 2 ILVALGVAL 4.000 237 GVALVfSLL 452 WTLNWVLAL 4.000 H YQSVETWL 4.000 2 KN SCTDVI 4I00 35 11 VICCVlFl 4 157 Table XVIII-VI-HLA-B7-9mers- Table XVIII.VS-HLAB7.gmers. able XVIII-VHLA-B7-gmers 24P4C12 F 24P4C12 14P4C12 Each peptide Is a portion of SEQ Each peptide i a portion of SEQ Each peptide is a portion of SEQ ID NO: 3; each start position is ID NQ 7; each start position is ID NO: 13; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide Is 9 amino acids, and the end 9 amino acids, and the end 9 amio acids, and the end position for each peptide is the position for each peptide Is the position for each peptide is the start position plus eig ht. start sition us ei L start ition lus el ht. SStrtarti[ Score Start Subsquence |Sscore 25| GPKNRST 3.000 8 G [.5 9L RSWNL I.OI 482 IPTFPLISA |3.000CFPWTNIT jO 001 I GYjJP .001 344 || ASKAVGQMM |3.000 5 IPTiTPP 110001 343I| EASKAVGQM 13.000 Table XVII-W.HLA-B7.9mem. 149 || LPGVPWNMT |30001 Table XVIII-3.0HLA070mers00 2400402 f .58-1 LMRNIVRVV 2.000 I 24P4C12 EachpeptideisaportionofSEQ 152 IVPWNMTVIT l2.00 Each peptide is a portion of SEQ ID NO: 15; each start position s 531 NPVARCIMC 2.000 ID NO: 11; each stan position Is specified, the length of peptide is B. specid, the length of peptide is 9 amino acids, and the end 188 I1 TPPALPGIT 2.000 9 amino acids, and the end position for each peptide is the 112 |i TPQVCVSSC H2.0001 position for each peplde is the start sition pus el h. 60 I DPRQVLYPR | start po plus eight Subseuence Score 5-25I KLRGVQNPV 2.000 | tart I Subs__uence Score 15.00 314 1 IVLAVLEAI 2.000 5 11 I4.0 0P 167- l CPSFLLPSA 2.0001 1. 2-J0 a5 L ILVAVGQMM 1.000 151 I GVPWNMTVI 12.0001 21 110|600 4 ]7WILV GM 1.000 192 I LPGITNDTT 2.000 1 110.400 7 VAVGQMMST 0.300 359 If LVTFVLLLI |2.000 A ILVI .6 _ ____ _ 359 _v_ [4 _LL__F 006 6 LVAVGQMMS 0.1001 252 ILVAGPLVLv 1.50 LLLV 0.060 | 0 SWWILVAV 0.020 [L VLLV S L F I j . 2 0 J 0 .0 5 0 E 3 _ _ _ _ _ _ _ _ _ _ _ _ _ _go 451 FIRTLRYHT 1.50 VAVG 530 QNPVARCIM 1.500 7 LLVUFLRQ .010 2 239 A.VLL.FI 1.200

-

Tal XVIIV LAB-9mers 55FI iVQETWLAAL 1.2001 X1 able XVIII-V6.HLA-X7lmVrs. 324P4C12 h12 Eachpep is a portion of SEQ Table V3-HLAB7-9mrs- ID NO: 17; each start position is 4P4C12 Each peptide is a portion of SEQ specified, the length of peptide Is Each peplide is a portion of SEQ ID NO. 13; each start position Is 9 amn acids, and the end 10 N~r 7; each start position Is specified, the length of peptide is position for each peptide is the 9 9aaminoaaids, and the end specified, the length of peptide Is posinfor achide, s the start oibon pus eig L position for each peptide is the rel 10 I NubseuGHV Score start position plus eight. star I Start SubsLIPRSVFNL 4.0001 5 LPIMRNPIT 2.00 6 WTNITPPAL 4.000U F [T j ITPL.G 040 1 5 fKGLIPRSVF 1 7 1 IMRNP!~IPT 1.500 9 fTPPALPGI 0.40010-45 4 7 1 FPWTNITPP T0.200 6 1 GLIPRSVFN 4 WVPIMRNPI 0.600 2 I RCFPWTNIT 0.100| 4 SKGLIPRSV 0.0201 IN 1 I GRCFPWNI 0.060 GGHFQTSIL TNITrPPALP 0.015 [7If YSSKGUJPR 000 .I TSLAV .0 158 17F HVFQTSILG 0.050 Each peptide is a portion of SEQ Table XIX-VI-HLA-B7mr r-179 FQTSILGAY 0.020 ID NO: 3; each stat position Is 24P4C1 18 VFQTSILGA 0.010 specifed, the length of peptide is Ea peptde is a portion of SEQ I10 amino acids, and the end ID NO: 3; each start position is 12.. ITPTGHVFQ 0.010 position for each peptide is the specified, the length of peptide is 9 RNPITPTGH 0.010 staPipsne. 0 andno acids, and the end 6 PIMRNPITP 0.003 [tart Subseuence position for each peptide is the 2 YYWLPIMRN 0.003 120.0 star postbonplus nin 11 I PITPTGHVF 0.002 100 r Subseuence 14 PTGHVFQTS 0.002 683 RPYYMSKSLL -zr YWLPIMRNP 0.001 -0 12.00 8 MRNPITPTG 0.001 3 T LFJ 8 [23 ALVLSLLFIL 0 1 NYYWLPIMR 10.ij 0 659 FGMCVDTLFL 0 1 ______ _ 33 IRORIRIAAL M0F Table XVIV9-HLA-B7-9mers- [ 254 AGPLVLVUL 200 24P412 571 CVSAKNAFML 0 Each peptide is a portion of SEQ 257 GVL 350 QMMSTMFYPL ID NO: 19; each start position is F_ _ _ _ 02.0 specified, the length of peptide is - 235 ALGVALVLSL 0 9 amino acids, and the end 456 ]j AGjC j _ 0 position for each peptide is the 0 536 CIMCCFKCCL start position pus eight. VV.KVTDL10 Start Suseuec W 16il LALE I 20( 13 QPATLGYVL 0 010 LAALIVLAVL WAMTALYPL 36.000 7 E~~ j4~~M~ 5 IVRVWWK IV~ 81 YPLPTQPAT j I2j00j0 6TGAC 1_ _ I PLPTQPATL 0.400 -WRQ o 10 LPIQPNTL_ 0-100_ 314 ifUVLAVLEAIL 192 LPGITDT 8. LP1TQ11 ATLG V 0.300 -1 -r i 6.. . L~10 TLVIARVIL 6.10 ol 515 ATLGYVLWA |0.300! 2 11CVDTFLCFL 6.0001 12 TQPATLGYV |0.200|I 029][ Q __j F4 _ Mia~LNPY l0 10inn F5 TALYPLPT 0.1045| 25 VAGPLVIA 405 [NTSCNPTAHL 6.000 F T1 GYVLWASAI 0.040 SMCVDTL 44 [ LSSCIPGM 5.000 3 AMTALYPLP 0.030 P 413 1[ HLVNSSCPG 4.000 30 SV1.TWLAA- .00 _23]( QGISGLIDSL 4.000 6 ALYPLPT.P 0. 304 1 SVQETWL.0 17 LGYVLWASN 0.020| 0 00 isLWA S 0.00 34 DvCC FLLr 6868 YMSKSLLKIL 4.000. 1 711 ~ 23 L_________99 ][NIISVAENGL 4.000 7 | LYLTOPA 0.015| 233 LVALGvALv._roo1 665 TLFLCFLEDL 4.000 14 T PATLGYVLW 0.006| I 0290 ISQLG L 4.000 1_ yWWAy 11AA4 0 j 441 IiNLQIYGVLGL 14.000 11 ITPALY ~ 0.002|r Table~5.0 630I.L.7.~es-1 KSPHLNYYWL 4.000 __________________ 317 AVLEAILLLMI 031IfVWAL 400 24P4C12 321 17 AILL M2UFL2361 LGVALVLSLL_~.0 -2w0 ~A961 DLPFFGKLL4. E ach GALLTL pd60 DPRQVLYPRN 4.000 159 Table XIX-V1 -HLA-B7-1 0mers- Table XIX-Vl.HLA-B7-lOmers- Each peptide is a portion of SEQ 2434C12 24P4C12 IDNO: 11; eachstartpostion is Each peptide is a portion of SEQ Each peptide isa portion of SEQ specified, the length of peplide is ID NO: 3; each start position is ID NO: 3; each start position is 10 amino acids, and the end specified, the length of peptide is specified, the length of peptide is position for each peptide Is the 10 amino ads, and the end 10 amino acids, and the end start position plus nin position for each peptide is the position for each peptide Is the Start S ubs uence S start position plus nine. start pion us nine. 5 12.00 Start Subs uence Score Start Subs. ence score 243 SLLFILRL [4-.0 143 KNRNFCLPGV 2.000 9-- LVLIFLRQRI 3.000 37 CCVLFLLFIL 14.000 ILGA 2.000, 1 AWEAILLLV 3 F449 |GLFWTLNWVL 14.000 249U LLRLVAGPLV 2 VLEALLLVL 1.200 162-| LOOELCPSFL 4.000 172 LPSAPALGRC - 4 EAIUIVLIF 625 LGKDFKSPHL 4.000 [85 FPUSAFIRT [0I 3 LEAILLLVLI 0.040 [227- QSWYWILVAL 4.000 264 GVLGWAYGI 2.00 7 7J L I LR-] 0.010 [ TGSLAFGAL 4.000 531 NPVARCIMCC 2.000 48 YIWGIVAWL 4.000 163 QQELCPSFLL 1.80| 10 VIIFIRORIR 0.010 60411 LLWGGVGVL 4.000 529 VQNPVARCM5 8 LUROR 0.010 149 )LPGVPWNMTV 4.000 576 NAFMLLMRNI 260 i VLILGVLGVL |4.000| 1 AYWAMTALYL 11W0] Table XXV64LA-B7-lOmers A493 RTLRYHT514M 318 4.000 1.200 2402 248 5 L RLI 4 Each peptide isa portion of SE r--31F -I~AL M~n i Table )OX-V3-HLA-B7l0mers- ID NO: 13; each start position is 500 11 GS GLLJ4.00O 4Pj1 specified, the length of peptide is 500 GSLAFGAL 4.000ds, and the end 546 1 WCLEKF[KFL ||4.0001 Each peptide is a portion of SEQ position for each peptide Is the 241 1 VLSLLFILLL 4.6006 ID NO: 7; each Start position is start position plus nine. 539____________________ speiie, the length of peptide Is Start t[Subsequence EcR 5 CFKCL IRCL M4.0001 i acids, and the end 445 YGVLGLFWTL 4.000 position r each peptide is the 9 IPRSVFNLQI 307 ETWLAAUVL 4.000 sta i pu n, 1t 435 ~J SNL9140 StartIs euence diScore 7400 72 VSAKNAFMLE 4 O1 LGRCFPWTNI 6.000 110.2 433 i GLIQRSVFNL |5] FPWTNITPPA 2.04.0 0-I KGUPRSVFN 020 517 i VILEYIDHKL 14.00 9 ]NITPPALPGI 0.4001 IR 0 199 TTIQQGISGL 4.0 10 ITPPALPGIT 0.1004.0 3 I SCITUCCVL 4.00[ PWTNIPPAL 0.040 1 ]f 1 L178 [RFWN .D TNITPPALPG 0.015 5 = I(LI v 17 i LGRCFPWTNV 13.000 0052 GSKLP .0 343 EASKAVGQMM 3.000 7 WTNITPPALP 346 KAVGQMMSTM 3.000 3 RCFPWTNITP 0.010 jPRSVFNLOIY 0.00 581 LMRNIVRWV 3.000 2 GRCFP (1.010 ~ f AKAMLM .004 CFPWTNITPP 10.0011 Table XIX.V7-HLAB71 Cmers-I 573 SAKNAFMLLM 3.000 4C1 652 ASGFFSVFGM. 13.000 ---I ASGableG 3.000-7-0m Each peptide is a portion of SEQ 402 VPINTSC T 2000 T4PA12 I NO: 15; each start position Is 1821 FPWTNVTPPA 2.000 peafied, 528 I GVQNPVARCI 2000 10 aino adds, and the end 281 _____ _Each poston for each peptide is the 1886)1 NVTPPALPGI N000 start ition lus nine. 160 Start |Sub Each peptide is a portion of SEQ Table XSueeHnAne c35.emeres. 8 1 VAVGQMMSTM 3.000 ID NO: 19; each start position is 24P4C12 5 WILVAVGQMM j 1.000 specified, the length of peptide is Each peptide is a portion of SEQ 10 amino acids, and the end I O ;ec tr oiini 7 ||LVN900MMST |0.500| psto o ahppiei h I O ,ec tr oiini 9 1 " QMST L position pepms is specified, the length of peptide is :1 !~~hi03i tr osfoMlu ie 9 aminvo acids, and the end 1 QSWiYlLVAV |tat0.200|nc Sor Ii I QSWWILVV 0.00J ___ Subequ Nce icR position for each peptide is the 4 .I YWILVAVGQM 10.1001 0.00 start ition pls eh 6 I020 __L_____ 0 Start S ~FI-3I1 TQPATLGYVL 1400 DO 3 WYWILVAVGQ 0.001 T0 0 LAVGQ n A LYPI.PTOPA 0. 450 D __ 357 PVF 0.00 Table XIX-V8-HLA-B7-10mers- 14 QPATGYVLW 0.400 255 GPLVLVLIL 0.00 24P4C12 I 2 -YwAMTALYPL 0.400 F 0 Eadh peptide Is a portion of SEQ I [ LGYVIWASNI 0.400 631 SPHLNYYWL ID NO: 17; each start position is 4 -1 AMTALYPLPT 0.300 spedfied, the length of peptide Is 16.00 10 amino adds, and the end - 1 L . - [ _________ 0 position for each peptide is the 16 ATLGYVLWAS 0.060 R1 start position plus nine. 6 TALYPLPTQP 0.030 0 Start Sub 15 PATLGSVLcWA 0.030 ore00 16 TGHVFQTSIL 4.000 12 PTQPATLGYV 0.020 18 1 HVFQTSLGAO.500 1711 L PTQ 0.015 - NSTGAYCGM 1000 11 NPITPTGHVF ||0.400|YLPO UV1 21 QTSILGAYVI 0.40 LYPLPTPAT 0.010 573 SAKNAFMLL 9.0 14][ TPTGHVFOTS 10.4001 0.0 IMCCF 9.000 10 [ RNPITPTGHV 0.3009 GLWASNIS -2-71 QTSLGAV .20 1= PLT _PT _ 465 LAGAFASFY 06.010 20 FQTSILGAYV 0.200 EAYGKPVKY 6. 671 LPIMRNPiTP 0.206 13 1i ITPTGHVFQT |0.100| Table XVIMILA.35meres. 333 RIRLAIALL 6.000 5 LPIMRNPITPTG 0.100 24P4C12 343 EASKAVGQM 6 F-5 -[ WLPIMRNPIT 0.100 Each peptide is a portion of SEQ 489 SAFIRTLRY 6.0 I0 NO: 3; each start position is 79 ENKDKPYLL 6.0 FT l YWiLMWRNPI 50.060 IO7 :ii WLIRNI .00 specified, the length of peptide is 379~ LATSGOPOY 6.0000 7 ][ PIMRNPITPT 10.045 9 a acds, and the end 15 1PTGHVFQTSI 0.4 position for each peptde is the I1 LNYWLPIMR 0.0101 start position plus eigt.63hLPLNY NYYWLPIMRN 0.003 start Subseuence (fie] 381 TSGQPQYVL 5.000 ii ] F OSLA 0.002 66 jj j GAY 20 .01 217 ISVKIFEF 5. 00 0 17 ][VFQTSILGAY 00 132 FSQVGEVF -171 GHVFQTSILG 0.0 A1 3 YYWLPiMRNP 10.001 683 RPYYMSKSL 40.00D 242 LSLLFILLL 15.000 12 PTPGVF O 0 406 TSCNPTAHL 5.000 12 i PITPTGHVFQ |0.001| -__ _____ 9 I MRNPITPTGH 0.001 15 KPVKYDPSF 0 572 V AFML 5.000 00_ 316 LAVLEAILL 4500 Table XIXV9HLA-B7-10mers- 34 ASKAVGQMM 0 5 K JJJF 4.0001 IC12 3 RVN0l 00 514 IARVLEYI I60 0 a noi n 287 GASISQLGF 3 161 Table XX-Vi.HLA-B35-9meres- Table XX-VI-HLA-835.9meres- Table XXV3-HLA-B35.9mers 24P4C12 ARM 2402 Each peptide is a portion of SEQ Each peptide isa portion of SEQ Each peptide Is a portion of SEQ iD NO: 3; each start position is 10 NO: 3; each start position is ID NO: 7; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 9 amino acids, and the end 9 amino acids, and the end 9 amino acids, and the end position for each peptide Is the position for each peptide position for each peptide Is the start position plus eight start position useht. start itio us ei t. F Subsequence Score tart Subse uence c 1311 |AALIVIAVL 3.000) 133 S EVFY 2775 YCWEEYRVL |3.000 251 1 RLVAGPLVL [2OWj 4 11 F 0.200 253 VAGPLVLVL 3.000 409 NP 2 1 RCFPWTNIT 0.200 651 IASGFFSVF 3.000 347 1 STM 2.000 I1[R~pwl 0.04 647 GAYVIASGF ]3.000 634 1 I 2.000 = 1 TNITPPALP 3.01 2 FAQSWYWL 3.000 6211 RIPGLGKDF 2.000 NITPPALPG 0.010 JZ. ISAPALGRCF 3.000 64i3J[ TSILAV 2.000 1 33]1 CFPWTNITP 0.00 I 234 VALGVALVL 3.000 482 IPTFPLISA 2.000 5 PWTNITPPA 0.001 369 IAYWAMTAL 3.00 110 CPTPQVCVS 2.000 1417 YTKNRNFCL 3.000 84131IMTSILGAY 2.000 Tl -HLA-B35-9mefs. 494 TLRYHTGSL |3.000 677( NNGSLDRPY 2.000 24PC12 L6_78 J NGSLDRPYY 3.000 421 31 0 Each peptide is a portion of SEQ 249 LLRLVAGPL 3.000 162 J '!QQ IhIS ID NO: 11; each start position is I____I___I_ specid, the length of peptide is 117 VSSCPEDPW 2.500 1 LPGVPWNMT 2.000 9 amino acids, and the end S2821 LGVLGVLAY 2.000 position for each peptide is the 28 I KNRSCDVI |2.400| 1167 CPSFLLPSA 2.000 start position plus eight. 317 AVLEAJllI 12.000 1 1 LPGVPWNM 2 SUM Subsuenco ore 266 LGVLAYGIY 2.000 571 H CVSAKNAFM 12.000 3 EAILLLV 1.200 33 VLLLICIAY 2.000 11121 TPQVCVSSC 2.000 ILLLVFL 1.000 267 GVLAYGlYY 2.000 L34 I QPQYVLWAS 2.000 41 AILLLVUF 1.o00 25 GPIKNRSCT [000] 500 GSLAFGALI 2.000 9 11 WIFLRQRI 0.4g 415 VNSSCPGLM 2.000 349 GQMMSTMFY 2.000 21 LEAIU.LVL -010 01 S50 VVGIVAWLY 2.0001 653 SGFFSVFGM 2.00 1 VLEAILLLV 0. 589 WLDKVTDL 2.000 4 KQRDEDDEA .80 [861 LLLVLIFLR 0.010 272 GIYYCWEEY 2.0001 660 GMCVDT1YL 15 0 7 LLVUFLRQ 10.010 188 TPPALPGIT 2.000] 301 -RSCTDVICC 1500 1 8 IfLVILIFILRQR 110.010 I432 KGUQRSVF 1r2.000 430 SSKGLIQRS [.5W 152 VPWNM1VIT 2.00 - Table XX-V6-HLA-B35-9niers 192 LPGITNDTT I2.000 Table -LA-35-9mers. 24P4C12 531 NPVARCIMC 2.000 24P4C12 Each peptide is a portion of SEQ 583 RNIVRVVL 2.00 Each peptide Is a portion of SEQ ID NO: 13; each start position Is IDN~ 7 echstrtposition is specified, the length of peptide is 366 LICIAYWAM 2.000 9 amino addsxand the end 1366~~~ UCAWM20 pecified, the length of peplide is 546 WCLEKFIKF 2.000 9 position eac 1 554 FLNRNAYIM 2000 position for each peptide sthe stat position Plus ei.t. 51 QIARVILEY 2.000 start position plus eight Star Subsen score 92 FSCILSSNI 2.000 530 I PVARCIM 200 11 jjrrEL-10G IJIE P 162 7 | LIPRSVFNL |1.000 Table XX-V8-HLA-B35-gmers- Table XXIV1HLAB35.10mers 8 || IPRSVFNL EN 24.C162 024P4C12 671 GLIPRSVFN 0.100 ach ide isa portion of SEQ Each pepbde Is a portion of SEQ __________ ID NO: 17; eachi start position is ID NO 3; each start position is S I YSSKGPR ed, the length of pepde is speed, the length of peptide is 4 L IPRSV 0.o20 amino acids, and the end 10 amino acids, and the end 91 PRSVFHL 0.04] position for each peptide Is the position for each ppkei h 9 |PRSVFNLQI pe0.004th I_.1 GYSSKGLIP 0.001 start onpeiht. start position plus nin. -- GISSubsequence Start If Subsequence JScore] Table XX-V7-HLA-B35-9mers- F-1 I VFQTSILGA 0.010 400 24P4C12 14_ G TS".00 Each peptide is a portion of SEQ 1711 HVFQTSILG 0.010 83 KPYLLYFNIF 0.00 ID NO: 15; each start position is 1 I 0.010 f 0 specified, the length of peptide is - i pMrp 5 1 683 R jMiKcL .0 9 amino acids, and the end f 0 position for each peptide is the j[ Y .001 start position plus eight 4 KORDEDDEAY StartI Subs uence j2oRe Ll j Nj MR0.00 8 || AVGQMMSTM F|2.0001 1 0 57| ILVAVGQMM I2.0 j Table XXV9.HLAB35mrs- 4 IPTFPLISAF2.00 4 I .WILVAVGQM 2.0001 24C12 0 7 VAVGQMMST 0.300 Each peptide is a portion of SEQ 1 320.00 6 1 ID NO: 19; each starposition is 0 1 |I SWYW1LVAV 9 m0o.cis02e0__ l g specified, the length of peptide Is 18.00 SYAVV 0009 amino acids, and the end213 NRIVF 0 0.001 I ositposition for each pepde is the 0 _ 1 ___ _10_01 start position plus eight. _StaL[Subse uence score] 10 34 NPTPTGHVM 24.000 TableXXWVLA35-9mers- 132346. E 24P4C12 FLSIL - 00 peptide is a portion of SEQ WAMTALYPL 3000 . ID NO: 17; each start position Is 8YPLPTQPAT 2000 r0.00 specified, Ile length of peptide is FT " PTQPATLGY I 0_ 200] 652 ASGFFSVFGM 0 9 amino aTds,and the en position for each peptide the t 488 start posi t ion plus eight 10 .AThG 0 .0 Start Subsunce ISoe 14 at132 FSTvGEVFY 10 fNPITPTGHV 4.000 15 &TL4YVLWA |0P100TH T 1000 1 ~ 1 |2 IIV0 oiIL 0.0P:(0RFW = 1 TPTGH . 2]2 . 00 1 MTALYPLPT 01 00THF 1751 AF0.0 19 1 TILGA ~ 2.000 r1671 TLGYVLWAS 0.1001 0 K"PLYW 00 51[ LPIMRNPITr 2.000 1I-78 1 LGYVLWASN 0.100 1 57 If TSI jffm] FI9 1 PLPMPATL 0.100 9 ITN I 8.000 4.f. jWLIMRNPI 0.4001 18j1 GYVI.WASNl 0.40 551! FIKFLNRNAY ' 6. 000 7 I IMRNPITPT 0.300 5E]1 TALYPILPTQ 0.0301 625 IfLGKDFKSPHL 6-000 200~~J 2001 7[ LYPLPTQPA 0.010 331][ RQlRtAAL 6.0001 11 JIPITPTGHVWF 0 I 7 ][ AMTALYPLP 0.010 343] EASKAVGQMM 6.000 F1611 GHVFQTS1L o0.10oo ALYPLPTQP 0.0 10 DPRQVLYPRN 6.000 - l X WA-YP . -AYC 6.000 _9 3n a0cids anAd nLY 6.000 163 Table )00~VI~ILA~I35-Imers Table XXI-VI.HLA.B35-10mors- TableXX-VI-HLAB35-i~mors 24P4C12 24P4C12 242C02 Each peptide is a portion of SEQ Each peptide Is a portion of SEQ Each peptide is a portion of SEQ ID Nr 3; each start position is ID NO: 3; each start position Is ID NO: 3; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 10 amino acids, and the end 10 amino adds, and the end 10 amino acds. and the end position for each peptide is the position for each peptide is the position for each peptide Is the start sition lus nine. start sition tus nine, start osiion lus nine. Start Subsequence [core startI Subseuence ore Score F57-2 II 5.0 396 SPGCEKVPIN 2.000 550M L 1.2 227 QSWYWILVAL |5.000 266 LGVLAYGIYY 2.000 4 RSVNLQI [20 500 I GSLAFGALIL 5.000 40I VPINTSCNPT 200 4171| SSCPGLMCVF | 5.000 378 YLATSGQPQY 2.000 Table M-V3HLA-B35-l mers 290 ISQLGFTTNL 5.000 365 ICIAYWAM 2.0001 24P4C12 76 GMGENKDKPY 4.000 293 LGF1-NLSAY 2.000 Each peptide is a portion of SEQ 68 ________ .00 26___VGVAY 2.0 ID NO:?7; each staut position is 8i RNTGAiYC(M | 4.00 262 I ILVLGVAY 2000 specified, the length of poplide is 317j AVLEALLLM 4.000 286 KGASISQLGF 2.000 10 amino acds, and the end 557 ||RNAYMIAlY | 4.000 529 ] VQNPVARCIM 2.000 pos1lon for each peptide is the 149 LPGVPWNMTV 4.000 6 2.000 s posiNQon plus ni. 676~67 || RNGSDRP 4000 66 RNNGSLD)RPY 4.0001 49 IVVGIVAWLY 2.000 StartI Subseqec Scorel 310 LAALIVLAVL 3.000 147 FCLPGVPWNM 2.000 5 FPW TNI 200 36 LAVLEAILLL W0i 25 VGLYI OO9 NTPLG . 320 IfEAIU.LMLIF 3.0 [04 SVQETWLAAL 2.00 ['0 ITPPALPGIT OA0 467 |GAFASFYWAF 3.000| 464 VIAGAFASFY 2f G 0 395 I SSPGCEKVPI 3.000| 20 20 DPSFRGPIKN 2.000 [ a 0 647 GAYVIASGFF 3.000 [61 MCVDTLFLCF 2000 8 0 677 NNGSLDRPYY 3.000 92 FSCILSSNII 2000 6 0 502 LAFGALILTL 3.000 512 VOIARVILEY 2.00 7 r 0.0101 430 SSKGUQRSV 3.000 182 FPWTNVTPPA 2.000 2 GFPWNrT 0.010 3811 TSGQPQYVLW 2.500 639 LPIMTSILGA 2000 362[ FVLLLICIAY 2.000 FCVSAINAFM 2.000 39~§) VLFLLFILGY 2.000 493 RTLRYHTGSL -. 000 Table XXI-VHLA-B3510mersI 188 TPPALPGITN 2.000 633 HLNYYV&PIM 2.000 24P4C12 152 VPWNMTVITS 2.000 531 NVCIMCC 2.000 Each peptide is a portion of SEQ 348 VGQMMSTMFY 2.000 I 2 ID N0. 11; each start position Is 31 SCTDVICCVL 2.000 485 1 IIRT 2.0 specified, the length of peptkle is 38410 amino acids, and the end 3114 If PTYAH N 2000 542_ KWLKD 2.00 position for each peptide Is the 409 NPTAHLVNSS 2000 rt posion lus nin. 613 LSFFFFSGRI 2000 517 VILEYIDHKL 2.000 iStrt Sub Score 220 KFEDFAQSW 2.000 414 LVNSSCPGLM 2.000 4 3 110JI CPTPQVCVSS 2.000 344 A VQMMI .500 5 AILLLVLIFL 1.0001 546] WCLEKFIKFL 2.000 465 LAGAFASEYW 1.500 9 LVIFLRQRI 0.400 271 YGIYYCWEEY 2.000 300 SAYOSVQE 1 .0 1 AVLEAILLLV 0.4001 30 RSCTDVICCV 2.000 659 FGMCVDTLFL ]1.5 2 ,_______ 11_300 172 LPSAPALGRC 2.000i 315]IAVLEAILL1.00 3401 16 f QECPSFL 2.000 118) SSCPEDPWTV 1.50DIo 164 Table XXI-VS-HLA-835-10mers- Table XXi.V7-HLA.535-10mers- Table XXI-Vg-HLAB35.l0mers1 24P4C12 24P4C12 24P4C12 Each peptide is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID NO: 11; each start position is ID NO: 15; each start position is ID NO 19; each start position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 10 amino acds, and the end 10 amino acids, and the end 10 amino acids, and the end position for each peptide is the position for each peptide is the on for each peptide is the str poiinpu ie tatggnpu ie start po*tion plus nine. I Sat Sbeuence Score Start HI Subsequence[ (~oe Start H Subsequence Score 6 ILLLVLIFLR 0.010 4 YWILVAVGQM 0.00 2 YWAMTALYPL 1.000 10 VLIFLRQRIR 0.010 6 LVAVGQMMS 0.100 13 TOPATIGYVI 1.000 7 LLLVLIFLRQ 0.010 7 LVAVGOMMST 0.100 9 YPLPTQPATL 1.000 8 LLVLIFLRQR ||0.010, IVAVG 18 LGYV.WASNI 1.000 3 WYW1LVAVGQ -0-001 14 ][ QP GYVLW 0.500 Table XX-V6-HLA-835-10mers- 11 LPTQPATLGY 0.2001 24P4C12 Table XXI-VO-HLA-B35-l mers- 1 AGYVLWAS 0.150 Each peptide is a portion of SEQ 24P4C12 111 GYVIWASNIS 0.100) ID NO: 13; each start position Is Each peptide isa portion of SEQ 1 4 AMTALYPLPT o.i0ol specified, the length of peptide is ID NO: 17; each start position Is 8 1 LYPLPTQPAT 0.100 10 amino acids, and the end specified, the length of peptides position for each peptide Is the 10 amino acids, and the end 17 TLGYVLWASN 0100J start position plus nine. position for each peptde is the 7 A TQPA 0 Start Subsequence Score start P ion lus nine. 3 0 9 IPRSVFNLQ 4.00 [art Subseuence Score 12 PTOPAThGYV 9M 11NL l NPITPTGHVF 0 16 1 LP O [0.010 4 |SSKGLIPRSV 3.000 01 7 |1 GUPRSVFNL |1.0 I0 TPTGHVFQTS 2. 15 00] 3]| YSSKGLIPRS 0.500| is][ TSIL 15 AYWAMTAYP[ 0 6| KGLPRSVFN 0.200 21] I GYV I ioM P A [0 5I SKGLIPRSVF 10.100 1 [ RNPITTGHV 0M Fi10| PRSVFNLQIY 0.020 6][ LPIMRNPITP 0200 8 LIPRSVFN 0.010 20 FQTSILGA 02 I | QGYSSKGUP 0.010 [19][ VFQTSILGAY 1.20o 2 GYSSKGLPR F. 0 [011 F7[ r HQ T0.100 ______ _____ [1811 I1 LG A D010 Table XX-V7-iLA-B35-10mers- 5 9 WLPIMRNPT- 0.100 24P4C12 15 PTGHVFQTSI 0.040 Each peptide Is a portion of SEQ 4 f YWLPIMRNPI 0.040 ID NO: 15; each start position Is 8 IMRNPITPTG 0.030 specified, the length of peptide is 10 amino acids, and the end 2 NYYWLPIMRN 0.010 position for each peptide Is the 7 PIMRNPITPT 0.010 start position plus nine. I LYYWLPIMR 0.010 Start i Subsequence Se 17 GHVF0 8 VAVGOMMSTM 1 0 . WWPIMRNP 0.001 5 [ wiV 2 1 1 PITPTGHVFQ 0.001 9 I AVGQMMSTMF 1.000 MRNPITPTGH 0.001 1 D :QSWYW;LVAV s 1.000tn 165 Tables XXIl-XLIX: TableXXIl-VI-HLA-A19mers 24P4C12 Each peptide is a portion of SEQ ID NO: 3: each start position is specfied, the length of peptide is 9 amino acids, and the end position for each peptide Is the start position plus eight. Pos 123456789 score 80 NKDKPYLY 34 58 YGDPRQyLY 33 222 FEDFAQSWY 26 5 QRDEDDEAY 25 77 MGENKDKPY 25 263 LVLGVLAY 24 489 SAFIRTLRY 23 513 OIARVILEY 23 628 DEKSPHLNY 22 40 LELLFILGY 21 267 GyLAYGIYY 21 363 VLLLICIAY 21 421 GLMCVFQGY 21 50 VyGIVAtY 20 318 VLEAILLL.M 20 629 FESPHL.NYY 20 133 SQTVGEyFY 19 437 RSVFNLgIY 19 662 C:DTLFLCF 19 11 EAYGKPyKY 18 370 AYWAMTALY 18 18 KYDPSFBGP 17 32 CIDVlCCVL 17 66 YERNSTGAY 17 277 WEEYRVLRD 17 379 LATSGQPQY 17 594 VUDLLLFFG 17 165 ELCPSFLLP 16 353 SIMFYPLVT 16 398 GCEKVPiNT 16 552 IKFLNRNAY 16 590 VLDKVTDLL 16 678 NGSLDRPYY 16 Table)UI-V3HLA-Ai-9mers 24P4C12 Each peptide is a portion of SEQ ID NO: 7; each start position Is specified, the length of peptide is 9 amino acids, and the end position for each peptide is the start position plus eight Pos 123456789 score 166 TableXXll-V3-HLA-AI-9mers 24P4C12 Each peptide is a portion of SEQ ID NO: 7; each start position is specified, the length of peptide is 9 amino adds, and the end position for each peptide is the start position plus eight Pos 123456789 score 8 NITPPALPG 11 9 ITPPALPGI 10 6 WINITPEAL 6 3 CFPWTNITP 5 6 LXAVGQMS 3 Table ll-VI-HLA-A201 TableXI-44LA--mers 1 SWYCW2LVAV 2 Omes-24P4C2 h pei 2 s iWILVoVG 2 Each peptide Is a portion of Each peptide Is a portion of SEQ ID NO: 3; each start SEQ ID NO: 11; each start Table)OUIMV8HLAAll.9mers- position is specified, the length position is specified, the length 24RC12 of pepbde Is 9 amino acids, and of peptide is 9 amino acids, and Each peptide is a portion of SEQ the end position for each the end position for each 10 NO: 17; each start position is peptide is the start position plus peptide is the start position plus specified, the length of pepfide is eight eight 9 amo acids, and the end Pos 123456789 score Pos 123456789 score position for each peptide is the 260 VULGYLGV 31 1 VLEAILL.V 20 star position plus eight 244 LLFILIIRL 29 7 LLVLIFLRQ 10 ,o 1256789 scor 580 LLMRNIVRV 29 e 95 ILSSNIISV 28 TableXXil-V6-HLA-A1-Omers- 19 FQTSILGAY 16 204 GISGLIDSL 28 24P4C12 14 PIGHVFgTS I1 261 LILGVLGVL 28 Each peptide is a portion of SEQ 12 IITGHMFQ 8 322 ILLLMLIFI 28 ID NO: 13; each start position is 18 VEQTSILGA 7 506 AULTLVQl 28 specified, the length of peptide is 20 QILGAW 7 170 FLLPSAPAL 27 9 amino acids, and the end 252 LVAGPLVLV 27 position for each peptide is the TableXXII.V94ILA-A19mers- 449 GLFWTLNWV 27 start position plus eight. 24P4C12 487 LSAFjRTL 27 Pos 123456789 score Each peptide is a portion of 604 LLWGGVGV 27 2 YSSKGLIPR 12 SEQ ID NO: 19; each start 45 ILGYIVGI 26 1 GySSKGLIP position is specified, the length 232 ILVALGVA. 26 3 S§KGUERS 7 of peptde is 9 amino acids, and 233 LVALGVALV 26 8 IPRSVFNLQ 7 the end position for each 315 VLAVLEAJL 26 9 PBSVFNjQI 7 peptide is the start position plus 501 SLAFLIL 26 6 GI4PRSVFN 5 eight 521 YIDIKLRGV 26 Pos 123456789 score 42 LLFILGYIV 25 TableXXil-V7-HLA-A1-9mers- 11 PIQPATLGY 31 107 GLQCPIPQV 25 2402 15 AILGYVLWA 16 200 4CQQGISGL 25 Each peptide is a portion of 211 9LNARDISV 25 SEQ ID NO: 15; each start Tabe0$V1lLA.A0201- 239 ALVLSLFI 25 position is specified, the length Smers-24P 2 257 LVLVL!LGV 25 of peptide Is 9 amino acids, and Each peptide Isa portion of 258 VLVLIIGVL 25 the end position for each SEQ ID NO: 3; each start 282 VLRDKGASI 25 peptide is the start position plus position Is specified, the length 317 AVLEAILLL 25 eight. of peptide Is 9 amino adds, and 457 VLALGCVL 25 Pos 123456789 score the end position for each 598 ULFFGKLLV 25 5 ILVAVGQMM 5 peptideis the start position plus 650 VIASGEFSV 25 3 YWILVAVGQ 4 eight 686 YMSKSLLKI 25 7 VVGQFMST 4 Pos 123456789 score 41 FLLFILGY 24 167 Table)IIl-VII-HLA-A0201- Table)OII-VIILA-A0201 TableXlI.VI-HLA-A0201 gmer-244C12 9mers.24P4C12 Smers-244C12 Each peptide is a portion of Each peptide is a portion of U6 peptide is a portion of SEQ ID NO: 3; each start SEQ ID NO: 3; each start SEQ ID NO: 3; each start position is specified, the length position is specified, the length position Is specified, the length of peptide is 9 amino acids, and of peptide is 9 amino acds, and of peptide is 9 amino acids, and the end position for each the end position for each the end position for each peptide is the start position plus peptide is the start position plus peptIde is the start position plus eight eight eight Pos 123456789 score Pus 123456789 score Pos 123456789 score 49 IWGIyAWL 24 34 DVICCVLFL 20 514 IARVILEY1 18 310 LAALIlLAV 24 38 CVLFLLFIL 20 517 VILEYjDHK 18 311 AALIVLAVL 24 44 FILGYIWG 20 583 RNIVRVWL 18 333 RIRIAIALL 24 207 GLIDSLNAR 20 602 GKLLVYGGV 18 434 LIQRSjFNL 24 228 SWYWILVAL 20 645 ILGAYVIAS 18 509 LTLVQ!ARV 24 234 VALGVALV. 20 46 LGYIWGIV 17 525 KLRGVQNPV 24 238 LGVALVLSL 20 128 GKNEFSQTV 17 564 AIYGKNFCV 24 242 LULLFILLL 20 154 WNIV!TSL 17 581 LMRNIVRVV 24 319 LEAILLLML 20 1 ALGRCEPWT 17 596 DLLLFEGKL 24 326 MLIFLORI 20 184 WTNVTEPAL 17 605 LWGGVGVL 24 339 AW(EASKA 20 213 NARDISVKI 17 35 VICCVLFLL 23 364 LLLIC[AYW 20 246 FILLL.LVA 17 56 WLYGDERQV 23 417 SSCPGLMCV 20 289 SISQLGF 17 240 LVLSLLFIL 23 503 AFGALILTL 20 300 SAYQSYQET 17 251 RLVAGPLVL 23 633 HLNYYWLPI 20 305 VQETWLAAL 17 253 VAGPLVLVL 23 644 SILGAYViA 20 312 ALIVLAVLE 17 309 WLAALIVLA 23 673 OLERNNGSL 20 325 LMLIFLRQR 17 340 LLKEASKAV 23 690 SW<ILGKK 20 335 RIAIALLKE 17 358 PLVTFYLLL 23 48 YIWG!VAW 19 354 TMFYPLVW 17 494 TLRYHIGSL 23 245 LFILLLRLV 19 359 LVTFVLLLI 17 518 ILEYLDHKL 23 255 GPLVLVLIL 19 453 TLNWVLALG 17 547 CLEKFIKFL 23 262 ILGVLGVLA 19 456 WVLALGQCV 17 589 WLDKyTDL 23 268 VLAYG!YYC 19 502 LAFGALILT 17 590 VLDKVIDLL 23 291 SQLGFTNL 19 504 FGAULWV 17 597 LLLFFdKLL 23 318 VLEAILLLM 19 513 QIARVILEY 17 100 IISVAENGL 22 323 LLLMLIFLR 19 554 FLNRNAYIM 17 241 VLSLLEILL 22 329 FLRQRIRIA 19 560 YIMIA!YGK 17 248 LLLRLVAGP 22 351 MMSTMEYPL 19 586 VRWVIDKV 17 249 LLRLVAGPL 22 365 WCIAYWA 19 642 MTSILGAYV 17 265 VLGVLAYGI 22 414 LVNSSCPGL 19 658 VFGMCVDTL 17 446 GVLGLEWTL 22 464 VLAGAEASF 19 31 SCTDVICCV 16 452 WTLNWVLAL 22 544 CLWCLggF 19 43 LFILGYIW 16 578 FMLLMBNIV 22 617 FFSGRIPGL 19 64 VLYPRNSTG 16 638 WLPIMISIL 22 686 LFLCFLEDL 19 90 NIFSCjLSS 16 660 GMCVDTLFL 22 86 LLYFNIFSC 18 119 SCPEDEWV 16 158 VITSLQQEL 21 231 WILVALGVA 18 144 NRNFCLPGV 16 187 VTPPALPGI 21 235 ALGVALVLS 18 148 CLPGVEWNM 16 191 ALPGIINDT 21 243 SLLFILLLR 18 161 SLQQELCPS 16 237 GVALVLSLL 21 336 IAIALLJEA 18 230 YWILVLGV 16 247 ILLLRLVAG 21 355 MFYPLVTFV 18 254 AGPLVLVLI 16 313 LIVLALEA 21 369 IAYWAMTAL 18 308 TWLAALIVL 16 314 MAVLEAI 21 380 ATSGQQYV 18 316 LAVLEAILL 16 442 LQIYGVIGL 21 394 ISSPGCEKV 18 320 EAILLLMLI 16 507 ULTLVQlA 21 439 VFNLQIYGV 18 357 YPLVTEVLL 16 537 IMCCFECCL 21 459 ALGQCVLAG 18 362 FVU.LICiA 16 599 LFFGKLLW 21 510 fLVQIARVI 18 373 AMTALXLAT 16 693 KILGKKNEA 21 511 LVQtABVIL 18 376 ALYLATSGQ 16 168 TableXXIl-V14iLAAO2F TabteXXIil-V5-HLA-A0201- Each peptide isa portion of 9mers-24P 2 9mers24P4C12 SEQ ID NO: 17; each start Each peptide is a portion of Each peptide isa portion of position is specified, the length SEQ ID NO: 3; each start SEQ ID NO: 11; each start of peptide is 9 amino acids, and position is specified, the length position is specified, the length the end position for each of peptide Is 9 amino acds, and of peptide is 9 amino acids, and peptide is the start position plus the end position for each the end position for each eiht peptide is the start position plus peptide is the start position plus Pos 123456789 score eight. eight 4 WLPIMLNI 19 Pos 123456789 score Pos 123456789 score 7 IMRNPITPT 19 407 SCNPTAHLV 16 1 VLEAILLV 25 20 QTSILGAYV 17 458 LALGQGVLA 16 9 VUFL RI 21 10 NPITPIGHV 15 637 YWLPIMTSI ' 16 2 LEAILLLVL 20 16 GHVFQJSIL 12 640 PIMTSILGA 16 6 LLLVLIFLR 19 15 TGHVFQTSI 11 52 GIVAWLYGD 15 3 EAILIIVU 18 18 VFQTSILGA 11 141 YTKNRNFCL 15 4 AILLLVUF 18 12 ITPTGtIVFQ 10 225 FAQSWXWIL 15 7 LLVLIFLRQ 13 5 LPIMRNPIT 9 250 LRLVAGPLV 15 8 LVUFLRQR 13 13 TPTGH FQT 9 264 GVLGVLAYG 15 275 YCWEEYRVL 15 TableXill-VHLA-A0201 366 LICIAYWAM 15 TableXaII-VB-HLA-A0201- 9mers.24P402 368 CIAYWAMTA 15 gmers-24PC12 Each peptide Is a portion of 371 YWAMTALYL 15 Each peptide Is a portion of SEQ ID NO: 19; each start 374 MTALYLATS 15 SEQ I0 NO: 13; each start position is specified, the length 406 TSCNPIAHL 15 position is specified, the length of peptide Is 9 amino ac 433 GLIQRSVFN 15 of peptide is 9 amino acids, and and the end position for each 443 QIYGVLGLF 15 the end position for each peptide is the start position plus 491 FIRTLRYHT 15 peptide Is the start position plus eight. 573 SAKNAEMLL 15 eight Pos 123456789 score 657 SVFGMCVDT 15 Pos 123456789 score 9 PLPTOEATL 21 663 VDTLFLCFL 15 2 YSSKGLIPR 12 2 WAMTALYPL 20 1 GYSSKGLIP 7 15 ATLGYVLWA 20 TableXXll-V3-HILA-A0201- 3 SSKGLIPRS 7 6 ALYPLPTQP 16 9mers-24P4C12 8 IRSVF7HLQ 7 12 TPATLGYV 14 Each peptide is a portion of SEQ 9 PESVFNLQI 7 13 QPATLGYVL 1 ID NO: 7; each start position is 6 GjPRSVFN 5 16 TLGYVLWAS 14 specified, the length of peptide is 5 TALYPLPTQ 13 9 amino acids, and the end TabeOI.VILA-A0201- 4 MTALYELPT 12 position for each peptide Is the 9mers-24PC12 8 YPLPTQPAT 12 start position plus eight. Each peptide is a portion of SEQ 3 AMTALYPIP 11 Pos 123456789 score ID NO: 15; each star position is 9 ITPPALPGI 22 specified, the length of peptide 6 WTNITPPAL 17 Is 9 amino acds, and the end TabIeXXIV-VI.HLAA0203 8 NITPPALPG 11 position for each peptide is the 9mers-2414C12 2 RCFPWINIT 10 start position plus eight. Pos 1234567890 soore Pos 123456789 score NoResultsFound. TableXXll-V5-HLA-A0201- 1 SWYWILVAV 20 9mers-24P4C12 4 VILVAGQM 18 TableXXN.V3-HLA.A0203 Each peplide is a portion of 5 ILVAVGQMM 16 9mers-24P4C12 SEQ ID NO'11; each start 7 VAVGWMST 13 Pos 1234567890 score position Is specified, the length 8 AVGQMMSTM 12 NoResultsFound. of peptide is 9 amino acids, and 6 LVAVGQMMS 10 the end position for eacd) TableXXIVV5-HLA-A0203 peptide is the start position plus TabIe l-HLA.A0201- 9mers.24P4C12 eight 9mers24P4C12 Pos 123456789 score Pos 123456789 score NoResultsFound. 5 ILLLVE;IFL 28 169 TabIeXXIV-V6HiLA-A0203- TableXOV-VI-HLA-A3-9mers- TableXXV-VI-HLA-A3-9mers 9mers-24P4C12 24P 24P Pos 1234567890 score Each peptide Is a portion of Each peptide is a portion of NoResultsFound. SEQ I0 NO: 3; each start SEQ ID NO: 3; each start position is specified, the length position is specified, the length TableXXIV-V7-HLA.A0203- of peptide is 9 amino acids, and of peptide is 9 amino acids, and 9mers-24P4C12 the end position for each the end position for each Pos 1234567890 score peptide is the start position plus peptide is the start position plus NoResultsFound. eight eight Pos 123456789 score Pos 123456789 scoe TableXXIV-VB-HLA.A0203- 393 NISSPGCEK 21 457 VLALGQVL 18 9mers-24P4C12 517 ViLEYIONK 21 564 AlYGKNFCV 18 Pos 1234567890 score 593 KVI.LLLFF 21 587 RWVDKV 18 NoResultsFound. 619 SGRIPGLGK 21 649 YVIASGFFS 18 621 RIFGL -DF 21 10 DEAYGI- VK 17 TableXXIV-V9-HLA-A0203- 44 FILGYJVG 20 63 QV1XP HST 17 9mers-24P4C12 56 WLYGDPROV 20 121 PEfPWVGK 17 Pos 1234567890 score 243 SLLFILLLR 20 177 ALaRCf-WT 17 NoResultsFound. 259 LVIILfYLG 20 211 SLyARDISV t7 347 AV GQJY TM 20 233 LVALGVALV 17 TableXXV-V1-HLA-A3-9mers- 363 VILLICIAY 20 235 ALGVALVLS 17 24P 463 CVLAGAEAS 20 239 ALSLLFI 17 Each peptide is a portion of 501 SLAFG6IL 20 252 LVAGPLVLV 17 SEQ ID NO: 3; each start 806 WGGVGVLS 20 309 WL6&LVLA 17 position is specified, the length 689 KSLLKILGK 20 335 R LE 17 of peptide is 9 amino acids, and 16 PVkYDPSFR 19 365 LCtAYWA 17 the end position for each 170 FU.PS6PAL 19 368 CI6YWAMTA 17 peptide is the start position plus 186 NVTPPALPG 19 401 KVEINISCN 17 eight 207 GLIDSUAR 19 421 GLMCVE9GY 17 Pos 123456789 score 246 FILLLSLVA 19 456 WVLALgQCV 17 585 IVEVVDK 29 249 LLELVfPL 19 459 ALGQCLAG 17 424 CVEQGyjSK 27 260 VLILGVLGV 19 510 TLVQlAV1 17 64 VLYPRNSTG 26 262 llVLLA 19 542 KCCLWCLEK 17 135 TVGEVFYTK 26 298 NLAYOSVQ 19 562 MIAIYGKNF 17 251 RLyAGE1VL 26 317 AVLEAILLL 19 580 LLMRNIVRV 17 50 LLLQI 24 333 RIBLJ1L 1 583 RN1VRLVL 17 506 ALILTLVi 24XL 1 513 O16RVILEY 24 433 GL1QRLfN 19 644 SILGAYVIA 17 603 KLLWGGVG 24 508 IILVQIAR 19 657 SVEGMCVDT 17 690 SLLKILGKK 24 525 KLRGVQNPV 19 662 CVPTLELCF 17 267 GVLAYiYY 23 560 YMLAlGK 19 26 PIKNRSCT 16 282 VLRDKGASI 23 588 WVLDKVTD 19 34 DVICCVFL 16 312 ALIVLAMLE 23 604 L VGV 19 45 ILGYIYGI 16 334 IR1AIALLK 23 605 LWGGW- 19 86 LLYFNIFSC 16 102 SVAENaLQC 22 681 LDEPYYMSK 19 157 T\1TSC9Q 16 232 ILVALGVAL 22 11 EAYGKPVKY 18 165 ELCPsLUP 16 247 ILLLRLVAG 22 49 lWGlWL 18 237 GVtLVLSLL 16 443 QIYGVLGLF 22 73 AYCGMGENK 18 258 VWIGVL 16 464 VLAGAEASF 22 220 KIEE0EAQS 18 289 SISMGFTT 16 516 RVILEYIDH 22 248 LLRLVAGP 18 304 SVEW 16 579 MLLMRNIVR 22 261 LILGVLGVL 18 323 LLLMLIELR 16 50 WIVAWLY 21 264 GLGVILYG 18 364 LLICAYW 16 212 LNARDISVK 21 272 GIYYCEY 18 470 ASE1WAFHK 16 281 RVLRDEGAS 21 278 EEXRVLRPK 18 494 TL9YHIGSL 16 321 AlLLLMLIF 21 314 IVLAVLAJ 18 511 LVQIRL 16 338 IALLKEASK 21 432 KGLI0-VF 18 554 FLNRNAYIM 16 339 ALLKXEAKA 21 441 NLQIYLG 18 571 CVSAKNAFM 16 376 ALYLATSGQ 21 446 GVLGLEffTL 18 584 NLVRWVLD 16 170 TabIeXXV-Vi-HLA-A3-9mers- TableXXV-VI HLA.A3-9meFS- Each peptide is a portion of SEQ 24P 24P 10 NO: 13; each start position is Each peptide is a portion of Each peptide Is a portion of specified, the length of peptide is SEQ ID NO 3; each start SEQ ID NO: 3; each start 9 amino adds, and the end position is specified, the length position is specified, the length position for each peptide is the of peptide is 9 amino acids, and of peptide Is 9 amino adds, and start position phus eight the end position for each the end position for each Pos 123456789 score peptide is the start position plus peptide is the start position plus 6 GUPRSVFN 22 eight. eight 5 KG!PESVF 18 Pos 123456789 score Pos 123458789 score 7 LIRSVFNL 11 673 DLERNYGSL 16 527 RGyQNEYAR 14 693 KILGKKNEA 16 528 GVNPyRC 14 TabIeXXV-VT-HLA-A3-Smers 698 KNEAPPDNK 16 534 ARCIMCCFK 14 24P4C12 20 DPSFRGPIK 15 558 NAYlMqY 14 Each peptide is a porton-of 48 YIVGIVAW 15 567 GKNFCVSAI 14 SEQ ID NO: 15; each start 58 YGQPRLY 15 596 DLLLFFGKL 14 position is specified, the length 99 NIISVAFNG 15 609 GVGVLFF 14 of peptide is 9 amino acids, and 151 GVPWNMTVI 15 638 WLPIMTSL 14 the end position for each 191 ALEGIIDT 15 647 GAjVVESGF 14 peptde is the start position plus 231 WILVALGVA 15 665 TLFLCFLED 14 eight 234 VALGVALVL 15 685 YYMSKSLLK 14 Pos 123456789 score 257 LVLVLILGV 15 694 ILGKKNEAP 14 8 AVGQMMSTM 20 318 VLEAILLLM 15 699 NEAPPDNKK 14 5 ILAVGQMM 19 322 ILLLMIFL 15 701 APPDNKKRK 14 6 L\AVGQMMS 15 327 LIELRQBIR 15 4 WiLVAVGQM 14 329 FLRQRIRIA 15 TableXXVV3-HLAA34mers. 3 YWILVAVGQ 12 532 PVARCIlMCC 15 24P4C12 1 SWjWLVAV 10 589 VVLDKVrDL 15 Each peptideisaportionof 597 LLLFFGKLL 15 SEQ ID NO: 7; each start TableXXVV8-HLAA39mers. 598 LLEFGL.LV 15 position is specified, the length 24P4C12 622 IPGLGKDFK 15 of peptide is 9 amino adds, and Each peptide is a portion of SEQ 645 ILGAYY!AS 15 the end position for each ID NO: 17; each start position is 651 IA§GFESVF 15 peptide Is the start position plus specified, the length of peptide is 680 SLDRPYYMS 15 eight 9 amino adds, ard the end 691 LLKILGKKN 15 Pos 123456789 score position for each peptide Is the 7 DERDEA GK 14 8 NIIPPALPG 17 start position plus eight 42 LLEILQXIV 14 Pos 123456789 score 53 IVAWLYGDP 14 TableXXV-V5-HLA-A3-9mers- 11 PITTGHVF 22 81 KDKPYLLYF 14 24P4C12 6 PIMRNEITP 16 95 ILSSNJISV 14 EachpeptideisaportionofSEQ 4 WIMWPl 12 148 CLEGVEWNM 14 N each start position is 171 LLPSAPALG 14 specified, the length of pepbde is 1 NYXWLEIMR 10 244 LLEILLLRL 14 9 amino acds, and the end 17 IVEQTSILG 10 311 AALIVLAVL 14 position foreach peptides the 315 VLAVLMIL 14 start position plus eight 324 LLMLIELRQ 14 Pos 123458789 score TabIeXXV.V9.HLA-A34niers* 326 MLIFLBQRI 14 4 AILLLAIF 21 24P4C12 337 AIAIIKEAS 14 8 LVLIFEQR 20 Each peptide isa portion of SEQ 359 LV1_-LLI 14 5 ILLLIFL 16 ID NO: 19; each st position is 370 AYWAMTALY 14 6 LLLVLIELR 16 specified, the length of peptide Is 378 YLATSGQPQ 14 1 VLEAILLLV 15 9 amino acds, and te end 388 VLWASUISS 14 7 LLIFLQ 14 position for each peptide is the 453 TLh!WVLALG 14 9 VLIFLRI 14 start position plus eight 465 LAGAFAEFY 14 Pos 123456789 score 487 LlAFJBTL 14 TableXV644LA.A3-mers. 6 ALYPLETOP 25 496 RYfTGSLAF 14 2402 9 PLTQPTL 18 523 DHLRIVON 14 11 PT-QPAILGY 12 171 16 TLG LWAS 12 TableXXVI-V1i-HLAAA26- Pos 123456789 score 9mers-249442 7 LIPRSVFNL 16 Table)OVI1LAA26- Each peptide is a portion of 5 KGLIPRSVF 9 9mers.24P4C12 SEQ ID NO: 3; each start Each peptide is a portion of position is specited, the length TableXXVI.V?-HLA-A26-9mers SEQ ID NO: 3; each start of peptide is 9 amino acids, and 24P4C12 position is specified, the length the end position for each Each peptide is a portion of SEQ ID of peptide is 9 amino adds, and peptide is the start position plus NO: 15; each start position is the end position for each eight specified, the length of peptide is 9 peptide is the start position plus Pos 123456789 score ammo adds, and the end position eight. 184 WTNVTPPAL 17 for each peptide is the start position Pos 123456789 score 216 DISVKIFED 17 plus eight. 34 DVICCVLFL 35 261 ULGVLGVL 17 Pos 123456789 score 49 IWGIVAWL 28 358 PLVTFVW. 17 8 AVGQMMSTM 12 483 PTFPLISAF 28 438 SVFNLQIYG 17 6 LVAVGCMMS 11 605 LWGGVGVL 27 442 LQIYGVLGL 17 4 WLVAVGQM 10 593 KVTDLLLFF 26 443 QIYGVLGLF 17 1 SWYWLVAV 8 317 AVLEAILLL 25 487 LISAFIRTI 17 5 ILVAVGQMM 6 592 DKVTDLLLF 25 608 GGVGVLSFF 17 2 WVYWILVAVG 5 138 EVFYTKNRN 24 664 DTIFLCFLE 17 7 VAVGQMMST 5 240 LVLSLLFIL 24 589 VVLDKVTDL 24 TableXXVI-V3-HLA-A26-9mers- TabIeXXVI-V8-HLA-A26-9mers 38 CVLFLLFIL 23 24P4C12 24P4C12 237 GVALVLSLL 23 Each peptide Is a portion of SEQ Each peptide Is a portion of SEQ ID 11 EAYGKPVKY 22 ID NO: 7; each start position is NO: 17; each start position is 267 GVLAYGIYY 22 specified, the length of peptide is 9 specified, the length of peptide is 9 285 DKGASISQL 22 amino acids, and the end position amino acds, and the end position 452 WTLNWVLAL 22 for each peptide Is the start for each peptide is the stat position 50 VVGIVAWLY 20 position plus eight. plus eight 79 ENKDKPYLL 20 Pos 123456789 score Pos 123456789 score 157 TVITSLQQE 20 6 WTNITPPAL 17 19 FQTSILGAY 20 263 LGVLGVLAY 20 9 ITPPALPGI 13 11 PITPTGHVF 15 446 GVLGLFWTL 20 17 HVFQTSILG 15 628 DFKSPHLNY 20 TabI*)OM-V5-HLA-A26-9mers- 16 GHVFQTSIL 13 641 IMTSILGAY 20 241402 20 QTSILGAYV 10 662 CVDTLFLCF 20 Each peptide is a portion of SEQ 14 PTGHVFQTS 9 236 LGVALVLSL 19 ID NO: 11; each start position is 258 VLVLILGVL 19 specified, the length of peptide is TableXXVI.V9-HLAA26-9mers 307 ETWLAALIV 19 9 amino acids, and the end 24P4C12 320 EAILLLMLI 19 position for each peptide Is the Each peptide is a portion of SEQ 414 LVNSSCPGL 19 start position plus eight ID NO: 19; each start position Is 437 RSVFNLQIY 19 sr specified, the length of peptide i89 513 QlARVILEY 19 P amino adds, and the end position 609 GVGVLSFFF 19 3 EAILLLVLI 19 for each peptide is the start 673 DLERNNGSL 19 4 AILILVUF 18 position plus eight 32 CTDVICCVL 18 8 IVUFIROR 15 Pos 123456789 score 198 DTTIQQGIS 18 2 LEAILLLVL 14 11 PTQPATLGY 20 200 TIQQGISGL 18 5 ILLLVUFL 13 15 ATLGYVLWA 13 204 GISGLIDSL 18 2 WAMTALYPL 12 244 LLFILLLRL 18 TableXX-V6-HLAA284mes. 13 QPATLGYVL 10 294 GFTTNLSAY 18 24P4C12 4 MTM..PLPT 9 354 TMFYPLVTF 18 EachpeptieisaportionofSEQtD 9 PLPTQPA11 9 360 . VTFVLLLIC 18 NO: 13;eachstartpositionis 400 EKVPINTSC 18 specified, the length of peptide is9 TableXXVt.V LA.B0702 511 LVQIARVIL 18 amino adds, and the end position for 9meR C12 596 DUILFFGKL 18 each pepide is the start position 102 SVAENGLQC 17 pluseight 172 Each peptide is a portion of SEQ TableXXVIIV1.HLAB0702- TableXXVII-VI-HLA-80702 ID NO: 3; each start position is 9mers-24P4C12 9mers-24PC12 specified, the length of peptide is 9 Each peplide is a portion of SEQ Each peptide is a portion of SEQ amino acids, and the end position ID NO: 3; each stat position is ID NO: 3; each start position Is for each peptide Is the start specified, the length of peptide is 9 specified, the length of pepbde is9 position plus eight amino acids, and the end position amino ads, and the end position Pos 123456789 score for each peptide is the start for each peptide is the start 255 GPLVLVLIL 23 position plu eight position plus eight 357 YPLVTFVLL 23 Pos 123458789 score Pos 123456789 score 683 RPYYMSKSL 21 170 FLIPSAPAL 13 104 AENGLOCPT 11 149 LPGVPWNMT 20 182 FPWrNVrPP 13 107 GLQCPTPQV 11 396 SPGCEKVPI 20 228 SWYWILVA. 13 109 QCPTPQVCV 11 482 IPTFPLISA 20 241 VLSLLFILL 13 112 TPQVCVSSC 11 631 SPHLNYYWL 20 249 LLRLVAGPL 13 123 OPWTVGKNE 11 15 KPVKYDPSF 19 261 LILGVLGVI 13 163 QQELCPSFL 11 152 VPWNMTVIT 19 302 YQSVQE1WL 13 169 SFLLPSAPA 11 167 CPSFLLPSA 19 319 LEAILLLtL 13 177 ALGRCFPWT 11 25 GPIKNRSCT 18 358 PLVTFVLU. 13 191 ALPGITNDT 11 172 LPSAPALGR 18 369 lAYWAMTAL 13 237 GVALV.SLL 11 83 KPYLLYFNI 17 371 YWAMTALYL 13 239 ALVLSLI 11 188 TPPALPGIT 17 409 NPTAHLVNS 13 258 VLVLILGVL 11 192 LPGITNDTT 17 442 LQIYGVLGL 13 262 ILGVLGVLA 11 57 LYGDPROVL 16 446 GVLGLEWTL 13 275 YCWEEYRVL 11 232 ILVALGVAL 16 478 KPODIPTFP 13 310 LMLIVLAV 11 253 VAGPLVLVL 16 487 LISAFIRTL 13 332 QRIRAdAL 11 479 PODIPTFPL 16 494 TLRYHTGSL 13 343 EASKAVGQM 11 503 AFGALILTL 16 501 SLAFGALIL 13 354 TMFYPLVTF 11 49 IVVGIVAWL 15 511 LVQIARVIL 13 384 QPQYVLWAS 1t 120 CPEDPWTVG 15 590 WDKVTDLL 13 414 LVNSSCPGL 11 175 APALGRCFP 15 622 IPGLGKDFK 13 426 FQGYSSKGL 11 189 PPALPGITN 15 651 IASGFFSVF 13 434 LIQRSVFNL I1 234 VALGVALVL 15 32 CTDVICCVL 12 440 FNLQIYGVL 11 251 RLVAGPLVL 15 78 GENKDKPYL 12 450 LFWTLNWVL 11 381 TSGQPQYVL 15 154 WNM1VITSL 12 464 VLAGAFASF 11 406 TSCNPTAHL 15 184 WTNVTPPAL 12 518 ILEYIDHKL 11 583 RNIVRVWL 15 242 LSLLFILLL 12 531 NPVARCIMC 11 617 FFSGRIPGL 15 244 LLFILLLRL 12 537 IMCCFKCCL 11 20 DPSFRGPIK 14 285 DKGASISQL 12 571 CVSAKNAFM 11 34 DVICCVLFL 14 305 VQETW.AAL 1 573 SAKNAFMLL 11 66 YPRNSTGAY 14 308 TWLAL1VL 12 574 AKNAFMLLM 11 204 GISGLIDSL 14 315 VLAVLEAIL 12 598 DLIIFFGKL 11 236 LGVALVLSL 14 322 ILLLMUFL 12 597 LLFFGKLL 11 252 LVAGPLVLV 14 358 FYPLVTFVL 12 599 LFFGKLLW Ii 291 SQLGFTTNL 14 373 AMTALYLAT 12 638 WLPIMTSIL I1 311 AALIVLAVL 14 380 ATSGQPQYV 12 663 VDTLFLCFL 11 317 AVLEAILLL 14 457 VLALGOCVL 12 686 YMSKSLLK I 1 333 RIRIAIALL 14 525 KLRGVQNPV 12 702 PPDNKKRKK 11 351 MMSTMFYPL 14 547 CLEKFIKFL 12 419 CPGLMCVFQ 14 572 VSAKNAFML 12 TableXXVil-V3HLA-60702 452 WTLNWVLAL 14 589 WLDKVrDL 12 9mers-24P4CIZ 499 TGSLAFGAL 14 591 LDKVTLLL 12 Each peptide isaportionof SEQ ID 605 LWGGVGVL 14 626 GKDFKSPHL 12 NO: 7; each start position is 660 GMCVDTLFL 14 658 VFGMCVDTL 12 specified, the length of peptide is9 60 DPRQVLYPR 13 701 APPDNKKRK 12 amio acds, and the end position 100 IISVAENGL 13 28 KNRSCTVI 11 for each peptide i the start position 110 CPTPQVCVS 13 45 ILGYIVVGI 11 plusight 164 QELCPSFUE 13 79 ENKKPYLL pti Pos 123456789 score 173 TabIeXVIl-V3-HLA-B0702- e TableXXVUI.VI -HILA-6084mers 9mers-24P4C12 1 SWYWILVAV 9 Each peptide Is a portion of SEQ Each peptide is a portion of SEQ ID 5 ILVAVG(MM 9 ID NO: 3; each start position is NO: 7; each start position is 8 AVGQMMSTM 9 specfied, the length of peptide is9 specified, the length of peptide is 9 7 VAVGQMMST 8 amnno acids, and the end position amino acids, and the end position 4 WILVAVGQM 7 for each peptide is the start for each peptide Is the start position position plus eight plus eight. Table)0(VI.8-HLA.B0702-Smers- Pos 123456789 score Pos 123456789 score 241402 589 WLDKVTDL 22 4 FPWTNITPP 12 EachpeptideisaportionofSEQID 333 RIRAIALL 21 6 WTNITPPAL 12 NO: 17; each start position is 583 RNIVRVVVL 21 1 GRCFPWTNI 10 specified, the length of peptide is 9 591 WKVTDLU. 21 2 RCFPWTNIT 9 amino acds, and the end position 626 GKDFKSPHL 21 5 PWTNITPPA 9 for each peptide is the start position 687 MSKSLU(IL 21 9 ITPPALPGI 9 plus eigt 340 LLKEASKAV 20 8 NITPPALPG 7 Pos 123456789 score 474 WAFHKPQDI 20 '19 FQTSILGAY 20 523 DHKLRGVQN 20 TabIeXXVI-VS-H-LA-B0702- 11 PITPTGHVF 15 540 CFKCCLWCL 20 gmers-24P4C12 17 HVFQTSILG 15 617 FFSGRIPGL 20 Each peplide is a portion of SEQ ID 16 GHVFQTSIL 13 2 GGKORDEDD 19 NO: 11; each start position Is 20 OTSILGAYV 10 232 ILVALGVAL 19 specified, the length of peptide is 9 14 PTGHVFQTS 9 255 GPLVLVLIL 19 amino acids, and the end position; 631 SPHLNYYWL 19 for each peptide Is the start position 694 ILGKKNEAP 19 plus eight. TabeOXXVII-A-B0702-9mers. 139 VFYTKNRNF 18 Pos 123456789 score 24P4C1 2 170 FLLPSAPAL 18 2 LEAILLLVL 14 EachpeptideIsaportionofSEQID 241 VLSLLFILL 18 5 ILLLVLIFL 12 NO:19; each start position is 247 ILLLRLVAG 18 4 AILLLVLIF 11 specfied,thelengthofpepldeis9 258 VLYLLGVL 18 1 VLEAILLLV 9 aminoacids, andithe end position 315 VLAVLEAIL 18 3 EAILLLVLI 9 for each peptide is the sart positon 322 ILLLMLIFL 18 9 VUFLRQRI 7 plus eight 357 YPLVTFVLL 18 Pos 123456789 score 457 VLALGQCVL 18 TableXXVII-V6-HLA-B0702. 13 PATLGYV1 23 501 SLAFGALIL 18 gmers-24P4C12 8 YPLPTQPAT 19 514 LARVILEYI 18 Each peptide Is a portion of SEQ ID 10 LPTQPATLG 14 518 ILEYIDHKL 18 NO: 13; each start position is 15 ATLGYVLWA 13 546 WCLEKFN(F 18 specified, the length of peptide Is9 2 WAMTALYPL 12 547 CLEKFIK. 18 amino acids, and the end position 7 LYPLPTQPA 11 683 RPYYMSKSL 18 for each peptide Is the start position 9 PLPTQPATL 1 11 EAYGKPVKY 17 plus eighL 213 NARDISVKI 17 Pos 123456789 score 7ableXXVI.VI-HLA-B0&.9mers 216 DISVKIFED 17 8 IPRSVFNLQ 14 EachpepldeIsaportionofSEQ 358 PLVTFVLLL 1 5 KGIPRSVF 12 ID NO: 3; each start position Is 533 VARCIMCCF 17 7 LIPRSVFNL 11 specified, the length of peptide is 9 590 VLDKVTDLL 17 9 PRSVFNLQI 10 amino adds, and the end position 596 DLLLFFGKL 17 4 SKGLIPRSV 7 for each peptide is the start 597 LLLFFGKLL 17 position plus eight. 673 DLERNNGSL 17 TableXXVil-V7-HLA-B0702. Pos 123456789 score 691 (ILGKKN 17 9mers-24P4C12 79 ENKDKPYLL 32 45 ILGYIWGI 16 Each peptideIs a portion of SEQ ID 1 YTKNRNFCL 29 64 VLYPRNSTG 16 NO: 15; each start position is 282 VLRDKGASI 29 81 KDKPYLLYF 16 specified, the length of peptideIs9 573 SAKNAFMLL 26 100 IISVAENGL 16 amino acids, and the end position 249 LLRLVAGPL 23 158 VITSLQQEL 16 for each peptide is the start position 494 TLRYHTGSL 23 204 GISGLIDSL 16 plus eight 26 PIKNRSCTD 22 211 SLNARDISV 16 Pos 123455789 scor 329 FLRORIRIA 22 244 LLFILLLRL 16 174 TableXXViII-Vi-HLA-808-9maIs TableXXVIII.V5-BD8-9M1r5 TableXVII.VMLA-809mers Each peptide is a portion of SEQ 24P4C12 24P4C12 ID NO: 3; each start position is Each peptide is a portion of SEQ ID Each peptide is a portion of SEO specified, the length of peptide is 9 NO: 11; each start position is ID NO: 17; each start position is amino acids, and the end position specified, the length of peptide is 9 specified, the length of peptide Is 9 for each peptide is the start amno acids. and the end position amino ecids, and the end position position plus eight. for each peptide Is the start position for each peptide is the start Pos 123456789 score plus eight. position plus eight 251 RLVAGPLVL 16 Pos 123456789 score Pos 123456789 score 253 VAGPLVLVL 16 2 LEAILLLVL 10 15 TGHVFQTSI 7 338 IALLKEASK 16 6 LLLVLIFLR 8 369 IAYWAMTAL 16 TableXXWfll.9-H-k6O& 433 GLIQRSVFN 16 TabIXXVII.V6-HLA-BOB-9m&5 fmers-24PC12 551 FIKFLNRNA 16 24PC12 Each peptide is a portion of SEQ 638 WLPIMTSIL 16 Each peptide is a portion of SEQ ID NO: 19; each start position is 702 PPDNKKRKK 16 ID NO: 13; each start position is specified, the length of peptide is 35 VICCVLFLL 15 specified, thelengthofpeptideis9 9aminoacds, andtheend 200 TIOQGISGL 15 amino acids, and the end position position for each peptide is the 225 FAQSWYWIL 15 for each peptide is the start start position plus eight 234 VALGVALVL 15 position plus eight Pos 123456789 score 316 LAVLEAILL 15 Pos 123456789 score 9 PtPTQPATL 16 331 RQRIRIAIA 15 6 GLIPRSVFN 16 13 QPATIGYVL 16 396 SPGCEKVPI 15 7 LIPRSVFNL 15 2 WAMTALYPL 14 434 LIQRSVFNL 15 3 SSKGLIPRS 13 16 TLGYVLWAS 8 487 LISAFIRTL 15 8 IPRSVFNLQ 13 18 GYVLWASNI 8 553 KFLNRNAYI 15 1 GYSSKGUP I1 8 YPLPTQPAT 7 564 AJYGKNFCV 15 9 PRSVFNLOI 8 579 MLLMRNIVR 15 TableXXIX-VI-HLA-B1 51O-9mers 693 KILGKKNEA 15 TableXOVIII-V7LA.BOB-mer 24P4C12 24P4C12 Each peptde is a portion of SEQ ID TabIeXXVlI.Y3-HLA-B08-9mers- Each peptide is a portion of SEQ NO: 3; each start position is 24P4C12 ID NO: 15; each start position is specified, the length of peptide Is 9 Each peptide is a portion of SEQ specified, the length of peptide is 9 amino acids, and the end position ID NO: 7; each start position is amino acids, and the end position for each peptide is the start position specified, the length of peptide is 9 for each peptide is the start plus eight. amino acids, end the end position position plus eight. Pos 123456789 score for each peptide is the start Pos 123456789 score 275 YCWEEYRVL 16 position plus eight. 5 ILVAVGQMM 7 583 RNIVRVL 16 Pos 123456789 score 4 WILVAVGQM 6 57 LYGDPRQVL 15 6 WTNITPPAL 11 7 VAVGQMMST 5 232 ILVALGVAL 15 4 FPWTNITPP 8 1 SWYWILVAV 4 253 VAGPLVLVL 15 1 GRCFPWTNI 7 381 TSGQPOYVL 15 9 ITPPALPGI 7 TabIeXXVIIIVM4LA.BO89rnrs- 487 USAFIRTL 15 242442 605 LWGGVGV 15 TableX iI.V5.BO-9msrs- Each peptide is a portion of SEQ 49 IWGIVAWL 14 24P4C12 ID NO: 17; each start position Is 78 GENKDKPYL 14 Each peptide is a portion of SEQ I) specified, the length of pepide is9 100 IISVAENGL NO: 11; each start position is amino acids, and the end position 170 FILLPSAPAL 14 specified, the length of peptide is 9 for each peptide is the start 184 WTNVrPPAL 14 amino acids, and the end position position plus eight 200 TIQQGISGL 14 for each peptide is the start position Pos 123456789 score 204 GISGUDSL 14 plus eight 5 LPIMRNPIT 15 251 RLVAGPLVL 14 Pos 123456789 score 4 WLPIMRNPI 12 357 YPLVTFVLL 14 5 ILLLVLIFL 18 16 GHVFQTSIL 11 389 tAYWAMTAL 14 3 EAILLLVLI 14 11 PITPTGHVF 10 457 VLALGQCVL 14 9 VLIFLRQRI 13 7 IMRNPiTPT 8 617 FFSGRIPGL 1 4 AILLLILUF 12 13 TPTGHVFQT 7 32 CTDVICCVL 13 175 TableXXIX-V1-HLA-B1 510-9mers- TableXXIX-V1.HLA.B1510-9mers. TableXXIX-Vi-HLA.Bi 510-Smers 24P4C12 24P4C12 24P4C12 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 acds, 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 Pos 123456789 score Pos 123456789 scre Pos 123456789 scre 79 ENKDKPYLL 13 236 LGVALVLSL 11 679 GSLDRPYYM 9 228 SWYWILVAL 13 241 VLSLLFILL 11 15 KPVKVDPSF 8 234 VALGVALVL 13 242 LSLLFILLL 11 81 KDKPYLLYF 8 255 GPLVLVLIL 13 285 DKGASISQL 11 132 FSQTVGEVF 8 261 LILGVLGVL 13 291 SQLGFTTNL 11 139 VFY1KNRNF 8 302 YQSVQETWL 13 319 LEAILLLIL 11 148 CLPGVPWNM 8 308 TWLAALIVL 13 332 QRIRIAIAL 11 162 LQQELCPSF 8 440 FNLQIYGVL 13 333 RIRIAIALL 11 174 SAPALGRCF 8 446 GVLGLFWTL 13 351 MMSTMFYPL 11 287 GASISOLGF 8 499 TGSLAFGAL 13 354 TMFYPLVTF 11 415 VNSSCPGLM 8 511 LVOIARVIL 13 358 PLVTFVLLL 11 464 VLAGAFASF 8 518 ILEYIDHKL 13 414 LVNSSCPGL 11 468 AFASFYWAF 8 537 IMCCFKCCL 13 434 LIQRSVFNL 11 496 RYHTGSLAF 8 547 CLEKFIKFL 13 479 PQOIPTFPL 11 53D QMPVARCIM 8 572 VSAKNAFML 13 494 TLRYHTGSL 11 570 FCVSAKNAF 8 163 QQELCPSFL 12 590 VLDKVTDLL 11 608 GGVGVLSFF 8 237 GVALVLSLL 12 591 LDKVTDLLL 11 609 GVGVLSFFF 8 244 LLFILLLRL 12 631 SPILNYYWL 11 647 GAYVIASGF 8 258 VLVLILGVL 12 684 PYYMSKSLL 11 48 IVAW 7 305 VQETWLAAL 12 35 V1CCVIFLL 10 69 NSTGAYCGM 7 311 AALIVLAVL 12 38 CVLFLLFIL 10 214 AROISVKIF 7 315 VLAVLEAIL 12 124 PWTVGKNEF 10 238 VALVLSLLF 7 317 AVLEAILLL 12 225 FAQSWYW1L 10 318 VLEAILM 7 322 ILLLMLIFL 12 240 LVLSUFIL 10 321 AILUJMLIF 7 356 FYPLVTFVL 12 249 LLRLVAGPL 10 366 UCIAYWAM 7 371 YWAMTALYL 12 316 .AVLEAILL 10 443 QIYGVLGLF 7 406 TSCNPTAHL 12 343 EASKAVGQM 10 533 VARCIMCCF 7 412 AHLVNSSCP 12 418 SCPGLMCVF 10 546 WCLEIFIKF 7 442 LQlYGVLGL 12 426 FQGYSSKGL 10 554 FLNRNAYIM 7 450 LFWTLNWVL 12 477 HKPQDIPTF 10 562 MAYGKNF 7 452 WTLNWVLAL 12 483 PTFPLISAF 10 571 CVSAKNAFM 7 476 FHKPQDIPT 12 540 CFKCCLWCL 10 574 AINAFMLLM 7 497 YHTGSLAFG 12 573 SAXNAFMLL 10 593 1VDLLLFF 7 501 SLAFGAUL 12 596 DLLLFFGKL 10 621 RIPGLGKDF 7 503 AFGALILTL 12 597 LLLFFGKLL 10 634 LNYYWLPIM 7 523 DHKLRGVQN 12 632 PHLNYYWLP 10 653 SGFFSVFGM 7 589 WLDKVTDL 12 638 WLPIMTSIL 10 626 GKDFKSPHL 12 663 VDTLFLCFL 10 Table)UX-V3.HLAB1510-9merr, 651 IASGFFSVF 12 666 LFLCFLEDL 10 24P4C12 658 VFGMCVDTL 12 683 RPYYMSKSL 10 Each peptide is a portion of SEQ ID 660 GMCVDTLFL 12 887 MSKSW(IL 10 NO: 7; each start position is 673 DLERNNGSL 12 33 TDVICCVLF 9 specified, the length of peptide is 9 34 DVICCVLFL 11 36 ICCVLFLLF 9 amino acids, and the end position 88 YFNIFSCIL 11 217 ISVKIFEDF 9 for each peptide is the start position 141 YTKNRNFCL 11 347 AVGQMMSTM 9 plus eight 154 WNMTVITSL 11 432 KGLIQRSVF 9 Pos 123456789 scre 158 VITSLQQEL 11 481 GQCVLAGAF 9 6 WTNITPPAL 13 1164 QELCPSFLL 11 607 VGGVGVLSF 9 176 TableXXIX-V5-B1510-9mers- TableXXXVg-81510-9mers-24P4C12 TabISXXX-VI4ILA.8270"mers 24P4C12 Each peptide Is a portion of SEQ ID NO: 24P4Ci2 Each peptide is a portion of SEQ 19; each start position is specified, the Each peptide is a portion of SEQ ID ID NO: 11; each start position is length of peptide is 9 amino acds, and NO: 3; each start position is specified, the length of peptide is 9 the end position for each peptide is the spcified, the length of peptide is9 amino acids, and the end position start position plus eight. amino adds, and the end position for each peptide is the start Pos 123456789 score for each peptide is the start position position plus eight 13 QPATLGY 13 plus eight Pos 123456789 score 9 PLPTQPATL 1 Pos 12345789 score 2 LEAILLLVL 13 2 WAMTALYPL 10 237 GVALVLSLL 17 5 ILLLVLIFL 12 242 LSLLFILLL 17 TableXTbXVXHLAVB2765-9mersB 261 LILGVLGVL 17 TablIeXXXV6-415109mers. 24P4C12 287 GASISQLGF 17 24P4C2 Eachpeptide is a portion of SEOD 311 LVLA 17 Each peptide is a portion of SEQ ID NO: 3; each start position is 338 IALKEASK 17 NO: 13; each start position is specified, the length of peptidle is 9 354 TMFYPLVTF. 17 specified, the length of peptide is 9 amino afds and the end position 381 TSGOYVL 17 ,:amino acids, and the end position for for each peptide is the start position 429 YSSKGLIOR 17 each peptide is the start position plus plus eight 477 HKPOIPTF 17 eight. Pos 123456789 score 503 AFGALILTL 17 Pos 123456789 score 334 IRIAIALLK 26 516 RVILEYIDH 17 7 LIPRSVFNL 11 332 ORIRIAIAI 25 546 WCLEKFIKF 7 5 KGLIPRSVF 10 675 ERNNGSLDR 24 549 EKFIKFLNR 17 3 SSKGUPRS 5 214 ARDISVKIF 23 605 LWGGVGVL 17 6 GLIPRSVFN 5 534 ARCIMCCFK 21 621 RIPGLGKDF 17 620 GRIPGLGKD 211 111 EAYGKPVKY 16 TableXXIXV1510-9mers- 5 QRDEDDEAY 20 23 FRGPIKNRS 16 24P4C12 204 GISGLIDSL 20 137 GEVFYTKNR 16 Each peptide is a portion of SEQ ID 446 GVLGLFWrL 20 139 VFYTKNRNF 16 NO: 15; each start position is specified, 689 KSIIKILGK 20 170 FLLPSAPAL 16 the length of peptide is 9 amino acids, 251 RLVAGPLVL 19 283 LRDKGASIS 16 and the end position for each peptide 424 CVFQGYSSK 19 285 DKGASISQL 16 is the start position plus eight. 436 QRSVFNLQI 19 321 AIWNUF 16 Pos 123456789 score 483 PTFPLISAF 19 322 ILLLMLIFL 16 8 AVGQMMSTM 9 583 RNIVRVWL 19 323 LLLMLIFLR 16 4 WILVAVGQM 8 608 GGVGWSFF 19 327 LIFLRRIR 16 5 ILVAVGQMM 8 15 KPVKYDPSF 18 432 KGUQRSVF 16 1 SWYWILVAV 3 22 SFRGPIKNR 1 440 FNLQIYGVL 16 . 2 WYWILVAVG 3 179 GRCFPWTNV 18 442 LQIYGVLGL 16 3 YWILVAVGQ 3 200 TIQOGISGL 18 443 QIYGVtGLF 16 6 LVAVGQMMS 3 207 GLIDSLNAR 18 457 VLALGQCVL 16 234 VALGVALVL 18 508 ILTIVOIAR 16 TableXXIX-V8B1510-9mers- 244 LLFIW.RL 18 517 VLEYIDHK 16 24P4C12 255 GPLVLVUL 18 589 WLDKVTL 16 Each peptide is a portion of SEQ ID 291 SQLGFTTNL 18 617 FFSGRPGL 16 NO: 17; each start position is 317 AVLEAILLL 18 626 GKDFKSPHL 16 specified, the length of peptide is 9 330 LRQRIRIAI 18 699 NEAPPDNKK 16 amino acids, and the end position 333. RRIAIALL 18 10 DEAYGKPVK 15 for each peptide is the start position 496 RYHTGSLAF 18 40 LFLLFILGY 15 plus eight. 527 RGVQNPVAR 18 60 DPRQVLYPR 15 Pos 123456789 score 847 GAYVIASGF 18 73 AYCGMGENK 15 16 GHVFQTSIL 21 688 LCFLEDLER 18 81 KDKPYLLYF 15 S 11 PITPTGHVF 10 683 RPYYMSKSL 18 124 PWIVGKNEF 15 13 QPATLGYVL 13 690 SLLKILGKK 18 212 LNARDISVK 15 9 PLPTOPATL 12 49 IVGiVAWL 17 217 ISVFEDF 15 2 WAMTALYPL 10 78 GENKDKPYL 17 228 SWYWLVAL 15 154 WNMVTSL 17 236 LGVALVLSL 15 177 Table)0(-Vi-HLA-82705-9mers- TableXXX-V1-HLA-B2705-9mers- Table)X-Vi-HLA-B2705-9mers. 24P4C12 24P4C12 24P4C12 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 adds, 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 Pos 123456789 score Pos 123456789 score Pos 123456789 score 238 VALVLSLLF 15 464 VLAGAFASF 14 582 MRNIVRV 13 243 SU.FILLLR 15 485 FPLISAFIR 14 590 VLDKVTDLL 13 253 VAGPLVLVL 15 487 LISAFIRTL 14 592 DKVTDLLLF 13 258 VLVLILGVL 15 488 ISAFIRTLR 14 610 VGVLSFFFF 13 308 TWLAALIVL 15 489 SAFIRTILRY 14 637 YWLPIMTSI 13 316 LAVLEAILL 15 501 SLAFGALIL 14 648 AYVIASGFF 13 369 IAYWAMTAL 15 513. QIARVILEY 14 653 SGFFSVFGM 13 461 GOCVLAGAF 15 515 ARVILEYID 14 666 LFLCFLEDL 13 470 ASFYWAFHK 15 552 IKFLNRNAY 14 681 LDRPYYMSIK 13 518 ILEYIDHKL 15 556 NRNAYIMIA 14 682 DRPYYMSKS 13 542 KCCLWCLEK 15 558 NAYIMlAIY 14 685 YYMSKSLLK 13 543 CCLWCLEKF 15 560 YIMIAIYGK 14 686 YMSKSLLKI 13 547 CLEKFIKFL 15 575 KNAFMLLMR 14 29 NRSCTDVIC 12 567 GKNFCVSAK 15 585 IVRVVVLDK 14 32 CTDVICCVL 12 579 MLLMRNIVR 15 595 TDLLLFFGK 14 33 TDVICCVLF 12 586 VRVVVLDKV 15 613 LSFFFFSGR 14 35 VICCVLFLL 12 593 KVrDLLLFF 15 643 TSILGAYVI 14 57 LYGDPRQVL 12 596 DLLLFFGKL 15 659 FGMCVDTLF 14 58 YGDPRQVLY 12 607 VGGVGVLSF 15 660 GMCVDTLFL 14 79 ENKDKPYLL 12 609 GVGVLSFFF 15 679 GSLDRPYYM 14 80 NKDKPYLLY 12 622 IPGLGKDFK 15 700 EAPPDNKKR 14 93 SCILSSNII 12 651 IASGFFSVF 15 701 APPDNKKRK 14 100 IISVAENGL 12 684 PYYMSKSLL 15 702 PPDNKKRKK 14 121 PEDPWTVGK 12 698 KNEAPPDNK 15 7 DEDDEAYGK 13 132 FSQTVGEVF 12 34 DVICCVLFL 14 36 ICCVLFLLF 13 144 NRNFCLPGV 12 38 CVLFLLFIL 14 172 LPSAPALGR 13 151 GVPWNMTVI 12 61 PRQVLYPRN 14 241 VLSLLFILL 13 163 QQELCPSFL 12 75 CGMGENKDK 14 249 LLRLVAGPL 13 190 PALPGITND 12 83 KPYLLYFNI 14 250 LRLVAGPLV 13 193 PGITNDTTI 12 84 PYLLYFNIF 14 273 IYYCWEEYR 13 239 ALVLSLLFI 12 135 TVGEVFYTK 14 275 YCWEEYRVL 13 276 CWEEYRVLR 12 148 CLPGVPWNM 14 280 YRVLRDKGA 13 302 YQSVQETWL 12 158 VITSLQQEL 14 294 GFTTNLSAY 13 305 VQETWLAAL 12 162 LQQELCPSF 14 319 LEAILLLML 13 315 VLAVLEAIL 12 164 QELCPSFLL 14 347 AVGQMMSTM 13 320 EAILLLMLI 12 232 ILVALGVAL 14 348 VGQMMSTMF 13 328 IFLRQRIRI 12 240 LVLSLLFIL 14 349 GQMMSTMFY 13 343 EASKAVGQM 12 263 LGVLGVLAY 14 356 FYPLVTFVL 13 371 YWAMTALYL 12 267 GVLAYGIYY 14 357 YPLVTFVLL 13 386 QYVLWASNI 12 272 GIYYCWEEY 14 358 PLVTFVLLL 13 393 NISSPGCEK 12 278 EEYRVLRDK 14 363 VLLLICIAY 13 406 TSCNPTAiL 12 325 LMLIFLRQR 14 492 IRTLRYHTG 13 414 LVNSSCPGL 12 379 LATSGQPQY 14 495 LRYHTGSLA 13 421 GLMCVFQGY 12 -418 SCPGLMCVF 14 506 AULTLVQI 13 426 FQGYSSKGL 12 434 UQRSVFNL 14 526 LRGVQNPVA 13 468 AFASFYWAF 12 437 RSVFNLQIY 14 545 LWCLEKFIK 13 490 AFIRTLRYH 12 450 LFWTLNWVL 14 570 FCVSAKNAF 13 500 GSLAFGALI 12 452 WTLNWVLAL 14 572 VSAKNAFML 13 510 TLVQtARVI 12 178 TableXXX.Vi-HLA-B2705-9mers- TableXX.V6-HLA-B2705-9m1s- Each peptide is a portion of SEQ 24P4C12 24P4C12 ID NO: 19; each start position is Each peptide is a portion of SEQ ID Each peptde Isa portion of SEQ specified, the length of peptide is9 NO: 3; each start position is ID NO: 13; each start position is amino acds, and the end position specified, the length of peptde is 9 specified, the length of peptide is 9 for each peptide is the start amino acids, and the end position amino acids, and the end position position plus eight. for each peptide is the start position for each peptide is the start Pos 123456789 score plus eight position plus eight 18 GYVIWASNI 15 Pos 123456789 score Pos 123456789 score 13 QPATLGYVL 13 519 LEYIDHKLR 12 9 PRSVFNLQI 19 2 WAMTALYPL 12 537 IMCCFKCCL 12 5 KGLIPRSVF 17 9 PLPTQPAT. 12 540 CFKCCLWCL 12 2 YSSKGLIPR 16 11 PTQPATLGY 10 553 KFLNRNAYI 12 7 LIPRSVFNL 14 6 ALYPLPTQP 8 557 RNAYIMIAI 12 3 SSKGUPRS 9 15 ATLGYVLWA 7 562 MIAIYGKNF 12 591 LDKVTDLLL 12 TableXXXV7.HLA-B2705- Tabe)OWJV1.HLA.B27O9. 597 LLLFFGKLL 12 9mers-24PC12 gmerse-24P4C12 614 SFFFFSGRI 12 Each peptide isa portion of SEQ Each peptide is a portion of SEQ 619 SGRIPGLGK 12 ID NO: 15; each start position is ID NO: 3; each start position is 628 DFKSPHLNY 12 specified, the length of peptide Is specified, the length of peptide Is 631 SPHLNYYWL 12 9 amino acids, end the end 9 amino acids, and the end 634 LNYYWLPIM 12 position for each peptide Is the position for each peptide is the 658 VFGMCVDTL 12 start position plus eight start position plus eight 662 CVDTLFLCF 12 Pos 123456789 score Pos 123458789 score 663 VDTLFLCFL 12 8 AVGQMMSTM 13 332 ORIRAIAL 23 673 DLERNNGSL 12 4 WILVAVGQM 12 179 GRCFPWTNV 22 687 MSKSLLKIL 12 5 ILVAVGQMM 11 250 LRLVAGPIN 21 3 YWILVAVGQ 6 214 ARDISVKIF 20 TableXXX-V3.HLA-B2705-9mers- 436 QRSVFNLQI 20 24P4C12 TableXXXVB-HLAB27054mers- 144 NRNFCLPGV 19 Each peptideIs a portion of SEQID 24P4C12 330 LRQRIRIAI 19 NO: 7; each start position is Each peptde i a portion of SEQ ID 582 MRNIVRVVV 19 specified, the length of peptide is9 NO:17;eachstartpositionis 586 VRWVLDKV 19 amino acids, and the end position for specified, the length of peptide Is 9 255 GPLVLVLIL 17 each peptide is the start position plus amio acds, and the end position 583 RNIVRVVVL 17 eight for each peptide is the start position 251 RLVAGPLVL 16 Pos 123456789 score plus eight 683 RPYYMSKSL 16 1 GRCFPWTNI 24 Pos 123456789 score 78 GENKDKPYL 15 6 WTNITPPAL 11 16 GHVFQTSIL 15 170 FLLPSAPAL 15 I NYYWLPIMR 14 334 IRIAIALLK 15 TableXXX-VS-HLA-B2705-9mors- 8 MRNPITPTG 1 446 GVLGLFWTL 15 24P4C12 9 RNPITPTGH 14 620 GRIPGLGKD 15 Each peptide is a portion of SEQ ID 11 PI GHVF 12 647 GAYVIASGF 15 NO: 11; each start position is 15 TGHVFQTSI 11 660 GMCVDTLFL 15 specified, the length of peptide is 9 19 FQTSILGAY 10 49 IWGIVAWL 14 amino acids, and the end position 2 YWLPIMRN 8 228 SWYWILVAL 14 for each peptide Is the start position 4 WLPIMRNPI 7 234 VALGVALVL 14 plus eight. 7 IMRNPITPT 7 244 LLFILLLRL 14 Pos 123456789 score 17 HVFQTSILG 7 317 AVLEAILLL 14 4 AILLLVLIF 17 333 RIRIAILL 14 5 ILLVLIFL 17 452 WLNWVLAL 14 6 LLLVLIFLR 16 TableXXXV9-HLA-B2705-9mers- 602 GKLLWGGV 14 2 LEALLLVL 14 24P4C12 626 GKDFKSPHL 14 8 LVUFLRQR 14 679 GSLDRPYYM 14 3 EAILLLVLI 12 23 FRGPIKNRS 13 9 VLIFLRQRI 11 34 DV1ICCVLFL 13 83 KPYLLYFNI 13 179 Table)000-V1-HLA-B2709- TableXXXI-V1 .HLA-B2709- TableX -VI-HLA-B2709 9merse-24P4C12 gmerse-24P4C12 gmers-24P412 Each peptide is a portion of SEQ Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID N0. 3; each start position is ID NO: 3; each start position is ID NO: 3; each stat position is specified, the length of peptide is specified, the length of peptide is specified, the length of peptide is 9 amino adds, and the end 9 amino adds, and the end 9 amino acids, and the end position for each peptide is the position for each peptde Is the position for each peptide Is the start position plus eight start posion plus eight. start position plus eighL Pos 123456789 score Pos 123456789 score Pos 123455789 score 107 GLQCPTPQV 13 518 ILEYIDHKL 12 509 LTLVQIARV 11 204 GISGLIDSL 13 553 KFLNRNAYI 12 510 TLVOIARVI 11 232 ILVALGVAL 13 593 KVTDLLLFF 12 511 LVQIARVIL 11 236 LGVALVLSL 13 596 DUIFFGKL 12 526 LRGVQNPVA 11 237 GVALVLSLL 13 597 LLIFFGKLL 12 534 ARCIMCCFK 11 240 LVLSLLFIL 13 605 LWGGVGVL 12 537 IMCCFKCCL 11 242 LSLLFILLL 13 608 GGVGVLSFF 12 564 AIYGKNFCV 11 253 VAGPLVLVL 13 621 RIPGLGKDF 12 572 VSAKNAFML 11 291 SQLGFTTNL 13 637 YWLPIMTSI 12 591 LDKVTDLLL 11 311 AALIVLAVL 13 666 LFLCFLEOL 12 592 DKVIDLLLF 11 322 ILLLMLIFL 13 684 PYYMSKSLL 12 598 LLFFGKLLV 11 357 YPLVTFVLL 13 5 QRDEDDEAY 11 599 LFFGKLLW 11 358 PLVTFVLLL 13 28 KNRSCTDVI 11 609 GVGVLSFFF 11 369 IAYWAMTAL 13 29 NRSCTDVIC 11 614 SFFFFSGRI 11 440 FNLQIYGVL 13 32 CTDVICCVL 11 617 FFSGRIPGL 11 442 LQIYGVLGL 13 41 FLLFILGYI 11 631 SPHU4YYWL 11 449 GLFWTLNWV 13 42 LLFILGYIV 11 634 LNYYWLPIM 11 496 RYHTGSLAF 13 46 LGYIWGIV 11 643 TSILGAYVI 11 500 GSLAFGALI 13 67 PRNSTGAYC 11 653 SGFFSVFGM 11 515 ARVILEYID 13 79 ENKDKPYLL 11 658 VFGMCVDTL 11 557 RNAYIMIAI 13 87 LYFNIFSCI 11 663 VDTtFLCFL 11 589 VVLDKVTDL 13 100 IISVAENGL 11 675 ERNNGSLDR 11 15 KPVKYDPSF 12 128 GKNEFSQTV 11 687 MSKSLLKL 11 38 CVLFLLFIL 12 139 VFYTKNRNF I1 45 ILGYIVVGI 12 151 GVPWNMTVI II Table)O-V3-HLk82709 56 WLYGDPRQV 12 184 WTNVTPPAL I Imers-24P4C12 61 PRQVLYPRN 12 217 ISVKIFEDF 11 Each peptide is a portion of SEQ 81 KDKPYLLYF 12 225 FAQSWYWIL 11 IDNO:7;eachstartpositim is 158 VITSLQQEL 12 230 YWILVALGV 11 specified, the length of peptide Is 164 QELCPSFLL 12 238 VALVLSLF 11 9 amino acds, and the end 258 VLVULGVL 12 239 ALVLSLLFI 11 position for each peptide is the 261 LILGVLGVL 12 249 LLRLVAGPL 11 start position plus eigh 287 GASISQLGF 12 257 LVLVLILGV I1 Pos 123456789 score 308 TWLAALIVL 12 260 VULGVLGV 11 1 GRCFPWTNI 22 316 - LAVLEAILL 12 280 YRVLRDKGA 11 6 WThITPPAL 11 321 AILLLMLIF 12 283 LRDKGASIS 11 9 ITPPALPGI 11 328 IFLRQRIRI 12 285 DKGASISQL 11 355 MFYPLVTFV 12 297 TNLSAYQSV 11 TableXXX-V5-82709.9mars 371 YWAMTALYL 12 310 LAAUVLAV 11 241402 414 LVNSSCPGL 12 314 IVLAVLEAI 11 EachpeptideIsaportionof 432 KGLIQRSVF 12 319 LEAILLLML 11 SEQIDNO:11;eachstart 434 UQRSVFNL 12 351 MNSTMFYPL 11 position Is specified, the length 461 GQCVLAGAF 12 354 TMFYPLVTF 11 of peptide is 9 amino acds, 492 IRTLRYHTG 12 381 TSGQPQWL 11 and the end position for each 495 LRYHTGSLA 12 386 QYVIWASNI 11 peptide Is the start position plus 501 SLAFGAUL 12 427. QGYSSKGU 11 eight 503 AFGALILTL 12 480 QPIPTFPL I I Pos 123456789 score 506 ALILTLVOI 12 483 PTFPLISAF 11 4 AILLLVLIF 13 180 5 ILLLVLIFL 13- Each peptide is a portion of TableXXXII-VILA-B4402. 2 LEAILLLVL 11 SEQ ID NO; 19; each start 9mers-24P4C12 1 VLEAILLLV 10 position is specified, the Each peptide Is a portion of SEQ 3 EAILLLVLI 10 length of peptde is9 amino ID NO: 3; each start position Is 9 VLIFLRQRI 10 acids, and the end position for specified, the length of peptide is each peptide is the start 9 amino acis and the end TableXXXl-V6-HLA-B2709- position plus eight position for each peptide is the 9mers-24P4C12 Pos 123456789 score start posibon plus eight Each peptide is a portion of SEQ 18 GYVLWASNI 14 Pos 123458789 score ID NO: 13; each start position Is 2 WAMTALYPL 11 629 FKSPHLNYY 16 specified, the length of peptide is 13 OPATLGYVL 11 699 NEAPPONKK 16 9 amino acids, and the end 9 PLPTQPATL 10 34 DVCCVLFL 15 position for each peptide is the 12 TQPATLGYV 8 79 ENKDKPYLL 15 start position plus eight. 130 NEFSQ GE 15 Pos 123456789 score TabloXXI-Vi-HLA.B4402. 154 WNMTVITSL 15 9 PRSVFNLQI 20 9mers-24PC12 204 GISGUDSL 15 5 KGLIPRSVF 12 Each peptide Is a portion of SEQ 234 VALGVALVL 15 7 LIPRSVFNL 12 ID NO: 3; each start position is 241 VtSUFILL 15 4 SKGLIPRSV 9 specified, the length of peptide is 263 LGVIGVLAY 15 9 amino adds, and the end 278 EEYRVLRDI( 15 TableXXX-V7-HLA-B2709- poiion for each peptide is the 294 GFTTNLSAY 15 9mers-24P4C12 start pion plus eight 354 TMFYPLVTF 15 Each peptide is a portion of SEQ Pos 123456789 score 370 AYWAMTALY 15 ID NO: 15; each start position is 164 QELCPSFLL 22 399 CEKVPINTS 15 specified, the length of peptide is 319 LEAILLLML 22 442 LQIYGVLGL 15 9 amino acids, and the end 222 FEDFAQSWY 21 488 AFASFYWAF 15 position for each peptide is the 78 GENIDKPYL 20 477 HKPQDIPTF 15 start position plus eight. 306 C1WLAALI 20 499 TGSLAFGAL 15 Pos 123456789 score 483 PTFPLISAF 20 513 QIARVILEY 15 I SWYWILVAV 12 317 AVLEALL 19 547 CLEKFIKFL 15 4 WILVAVGQM 12 332 QRIRAAL 19 66 YPRNSTGAY 14 5 ILVAVGQMM 10 503 AFGALILTL 18 80 NKDKPYLLY 14 8 AVGQMMSTM 9 506 ALILTLVQI 18 84 PYLLYFNIF 14 552 lKFLNRNAY 18 93 SCILSSNII 14 TableX)0-V8-HLA-B2709- 58 YGDPRQVLY 17 104 AENGLQCPT 14 9mers-24P4C12 170 FLLPSAPAL 17 193 PGITNDTT 14 Each peptide is a portion of 214 ARDISVKIF 17 223 EDFAOSWYW 14 SEQ ID NO: 17; each start 242 LSLLFILLL 17 239 ALVLSLLFI 14 position is specified, the length 583 RNIVRVL 17 244 LLFILLLRL 14 of peptide is 9 amino acids, 11 EAYGKPWY 16 258 VLVULGVL 14 and the end position for each 40 LFLLFILGY 16 261 LILGWGVL 14 peptide is the start position 48 YIWGIVAW 16 285 DKGASISOL 14 plus eight 81 KDKPYLYF 16 291 SQLGFTTNL 14 Pos 123456789 score 121 PEDPW1VGK 16 301 AYQSVQETW 14 16 GHVFQTSIL 14 228 SWYWILVAL 16 305 VOETWLML 14 8 MRNPITPTG 13 253 VAGPLVLVL 16 308 TWLAAUVL 14 11 PITPTGHVF 10 254 AGPLVLV 16 316 LAVLEAILL 14 10 NPITPTGHV 9 311 MLIVLAV. 16 322 ILLLMLIFL 14 4 WLPIMRNPI 8 320 EAILLLMLI 16 330 LRORIRIAl 14 15 TGHVFQTSI 8 321 A1LLLMLIF 16 333 RIRIAIALL 14 20 QTSILGAYV 8 383 VLUCIA 16 358 FYPLVTFVL 14 382 SGQPQYVLW 16 357 YPLVTFVLL 14 TableXXXI-V9-iLA-82709- 452 WTLNVMAL 16 358 PLVTFVLLL 14 9lmers-24P4C1 480. QDIPTFPLI 16 364 LWLCIAYW 14 487 LISAFIRTL 16 418 SCPGLMCVF 14 489 SAFIRTIRY 16 432 KGLIQRSVF 14 617 FFSGRIPGL 16 446 GVLGLFWTL 14 181 TableXXXII-V1-HLA-84402- TableXXXII-VI-HLA-64402- TableX=I-V1-HLA-B4402. 9mers-24P4C12 9mers-24PC12 9mors-24P4C12 Each peptide is a portion of SEQ Each pepte Is a portion of SEQ Each peptide isa portion of SEQ ID NO: 3; each start position is ID NO: 3; each start position is ID NO: 3; each start position is specified, the length of peptide is specified, the length of peptide is specified. the length of peptide is 9 amino adds, and the end 9 amino acids, and the end 9 amino acids, and the end position for each peptide is the position for each peptide is the position for each peptide is the start position plus eight start position plus efght start posItIon plus eight Pos 123458789 score Pos 123456789 score Pos 123456789 score 496 RYHTGSLAF 14 519 LEYIDHKLR 13 548 LEKFIKFLN 12 546 WCLEKFIKF 14 529 VQNPVARCI 13 553 KR.NRNAYI 12 558 NAYIMIAIY 14 543 CCLWCLEKF 13 557 RNAYIMIAI 12 573 SAKNAFMLL 14 570 FCVSAKNAF 13 562 MIYGKNF 12 577 AFMLLMRNI 14 589 WLDKVrOL 13 572 VSAKNAFML 12 592 DKVTDLLLF 14 590 VLDKVrDLL 13 591 LDKVTDLLL 12 593 KVTDLLLFF 14 605 LWGGVGVL 13 607 VGGVGVLSF 12 596 DLLLFFGKL 14 631 SPHLNYYWL 13 608 GGVGVLSFF 12 597 LLLFFGKLL 14 631 YWLPIMTSI 13 610 VGVLSFFFF 12 621 RIPGLGKDF 14 648 AYVLASGFF 13 630 KSPHLNYYW 12 641 IMTSILGAY 14 674 LERNNGSLD 13 638 WLPIMTSIL 12 643 TSILGAYVI 14 687 MSKSLLKIL 13 647 GAYASGF 12 651 IASGFFSVF 14 33 TDVICCVLF 12 658 VFGMCVDTL 12 662 CVDTLFLCF 14 35 V1CCVLFLL 12 659 FGMCVDTLF 12 671 LEDLERNNG 14 38 CVLFLLFIL 12 660 GMCVDTLFL 12 678 NGSLDRPYY 14 50 WGIVAWLY 12 663 VDTLFLCFL 12 5 QRDEDDEAY 13 100 IISVAENGL 12 666 LFLCFLEOL 12 7 DEDDEAYGK 13 132 FSQTVGEVF 12 673 DLERNNGSL 12 32 CTDVICCVL 13 133 SQ1VGEVFY 12 677 NNGSLDRPY 12 36 ICCVLFLLF 13 139 VFYTKNRNF 12 683 RPYYMSKSL 12 49 IWGIVAWL 13 41 YTKNRNFCL 12 686 YMSKSLLKI 12 57 LYGDPRQVL 13 163 QQELCPSFL 12 10 DEAYGKPVK 11 77 MGENKDKPY 13 217 ISVKIFEDF 12 15 KPVXYDPSF 11 87 LYFNIFSCI 13 221 IFEDFAQSW 12 28 KNRSCTVI 11 137 GEVFYTKNR 13 236 LGVALVLSL 12 37 CCVLFLLFI 11 146 NFCLPGVPW 13 240 LVLSLLFIL 12 41 FLLFILGYI 11 174 SAPALGRCF 13 249 LLRLVAGPL 12 45 ILGYIWGI 11 176 PALGRCFPW 13 267 GVLAYGIYY 12 117 VSSCPEOPW 11 184 WTNVTPPAL 13 269 LAYGIYYCW 12 124 PWTVGKNEF 11 187 VTPPALPGI 13 275 YCWEEYRVL 12 151 GVPWNMTV] 11 200 TIOQGISGL 13 287 GASISQLGF 12 197 NDTIIQQGI 11 209 IDSLNARDI 13 314 IVLAVIEAI 12 201 IQQISGLI 11 213 NARDISVKI 13 326 MUFLRQRI 12 266 LGVLAYGIY 11 232 ILVALGVAL 13 328 IFLRQRIRI 12 302 YQSVQE1WL 11 237 GVALVLSLL 13 349 GQMMSTMFY 12 359 LVTFVLLLI 11 238 VALVLSLLF 13 369 lAYWAMTAL 12 361 TFVLLLICI 11 251 RLVAGPLVL 13 371 YWAMTALYL 12 379 LATSGQPQY 11 255 GPLVLVLIL 13 406 TSCNPTAHL 12 381 TSGQPQYVL 11 277 WEEYRVLRD 13 421 GLNCVFQGY 12 436 QRSVFNLQI 11 342 KEASKAVGQ 13 426 FQGYSSKGL 12 444 IYGVLGLFW 11 351 MMSTMFYPL 13 434 UQRSVFNL 12 465 LAGAFASFY 11 440 FNLQIYGVL 13 437 RSVFNLQIY 12 474 WAFHKPQDl 11 443 QIYGVLGLF 13 450 FWTLNWVL 12 484 TFPLISAFI 11 448 LGLFWTLtW 13 457 VLALGQCVL 12 494 TLRYHTGSL 11 461 GQCVLAGAF 13 464 VLAGAFASF 12 533 VARCIMCCF 11 466 AGAFASFYW 13 479 PQDIPTFPL 12 53 MCCFKCCLW 11 501 SLAFGALIL 13 510 TLVCAARV1 12 540 CFKCCLWCL 11 518 ILEYIDHKL 13 511 IVOIARVIL 12 614 SFFFFSGRI 11 182 TableX0I0-V1-HLA-B4402. 2 LEALLLVL 23 Each peptide isa portion of SEQ ID 9mers-24P4C12 3 EAILLLVLI 17 NO: 19; each start position is Each peptide is a portion of SEQ 4 AILLLVLIF 17 specified, the length of peptide Is 9 ID NO: 3; each start position is 5 ILLLVLIFL 14 amino acids, and the end poston for specified, the length of peptide is 9 VLIFLRQRI 12 each peptde is the start position plus 9 amino acds, and the end eight. position for each peptide is the TableX0IlV8.HLA-B4402. Pos 123456789 score start position plus eight. 9mers-24P402 11 PTQPATLGY 15 Pos 123456789 score Each peptide is a portion of SEQ 9 PLPTQPATL 14 626 GKDFKSPHL 11 ID NO: 13; each start position is 2 WAMTALYPL 13 628 DFKSPHLNY 11 specified, the length of peptide is 14 PATLGYVLW 13 684 PYYMSKSLL 11 9 amino acids, and the end 13 PATLGYVL 12 19 YDPSFRGPI 10 position for each peptide is the 18 GYVLWASNI 10 83 KPYLLYFNI 10 start position plus eight 6 ALYPLPTOP 8 88 YFNIFSCIL 10 Pos 123456789 score 15 ATLGYVLWA 7 158 VfISLQQEL 10 5 KGLIPRSVF 14 162 LQQELCPSF 10 7 LIPRSVFNL 13 TabIX1I-VILA-B5101 225 FAQSWYWIL 10 9 PRSVFNLQI 1 Imers-24P4C12 272 GIYYCWEEY 10 6 GUPRSVFN 8 Each peptide isa portion of SEQ 315 VLAVLEAIL 10 ID NO 3; each start position is 348 VGQMMSTMF 10 TableXXYiI-V7-HLA-B4402. specified, the length of peptide is 9 386 QYVLWASNI 10 gmers-24P4CI2 amino acds, and the end position 396 SPGCEKVPI 10 Each peptide is a portion of SEQ for each peptide is the start 414 LVNSSCPGL 10 ID NO: 15; each start position is position pus eight. 500 GSLAFGALI 10 specified, the length of peptide Is Pos 123456789 score 514 IARVILEYI 10 9 amino acids, and the end 234 VALGVALVL 27 537 IMCCFKCCL 10 position for each peptide is the 213 NARDISVKI 25 544 CLWCLEKFI 10 start position pus eight. 46 LGYIVVGIV 24 555 LNRNAYIMI 10 Pos 123456789 score 83 KPYULYFNI 24 609 GVGVLSFFF 10 1 SWYWILVAV 6 311 MLIVLAVL 24 3 WV1LVAVGQ 6 253 VAGPLVLVL 23 TableX)OUI-V3-HLA-84402. 8 GQMMSTM 4 310 LAALIVLAV 23 9mers-24P4C12 4 WILVAVGM 3 357 YPLVTFVL 23 Each peptide is a portion of 2 WYMLVAVG 2 369 IAYWAMTAL 23 SEQ ID NO: 7; each start 474 WAFHKPQDI 23 position is specified, the length TableXXX-V8-HLA4MU- 514 IARVILEYI 23 of peptide is 9 amino acids, and 9mers-24P4C12 683 RPYYMSKSL 22 the end position for each Each peptide Is a portion of SEQ 254 AGPLVLVLI 21 peptide is the start position plus ID NO: 17; each start position is 255 GPLVLVUL 21 eight speed, the length of peptide is 9 320 EAIUJLvLI 21 Pos 123456789 score amino acids, and the end posIfon 396 SPGCEKVPI 21 6 WTNITPPAL 13 foreachpeptideisthestart 427 QGYSSKGLI 21 9 ITPPALPGI 13 position plus eight 11 EAYGKPVKY 20 1 GRCFPWTNI 8 Pos 123456789 score 193 PGITNDTI 20 2 RCFPWTNIT 7 11 PITPTGHVF 15 316 LAVLEAILL 20 7 TNITPPALP 6 19 FOTSILGAY 14 123 DPWTVGKNE 19 8 NITPPALPG 6 4 V&PIMRNPI 11 236 LGVALVLSL 18 16 GHVFQTSIL 11 314 IVLAVLEAI 18 TableXX001-VS-HLA-B4402- 15 TGHVFQTSI 8 599 LFFGKLLVV 18 9mers-24P4C12 686 YMSKSUKI 18 Each peptide Is a portion of SEQ TabteXXII9-HLAB4402.9mers- 60 DPRQVLYPR 17 ID NO: 11; each start position is 24P4C12 150 PGVPWNMTV 17 specfied, the length of peptide is 225 FAQSWYWL 17 9 amino adds, and the end 261 LILGVLGVL 17 position for each peptide is the 269 LAYGIYYCW 17 start position plus eight. 300 SAYOSVQET 17 POS 123456789 score 504 FGALILTLV 17 183 TableXXXIII-VI-HLA-B5101- TableX)0II-V1-HLA-B5101. Pos 123456789 score 9mers-24P4C12 9mers-24P4C12 4 FPWTNITPP 15 558 NAYIMIAIY 17 499 TGSLAFGAL 14 9 ITPPALPGI 14 573 SAKNAFMLL 17 509 LTLVQIARV 14 1 GRCFPWTNI 11 651 IASGFFSVF 17 576 NAFMLLMRN 14 6 WTNITPPAL 8 182 FPWTNVTPP 16 586 VRVVVLDKV 14 192 LPGITNQTT 16 589 VVWLDKVTDL 14 TableX00II-V5HLA-B5101-9mers 328 IFLRQRIRI 16 602 GKLLWGGV 14 24P4C12 355 MFYPLVTFV 16 605 LWGGVGVL 14 Each peptide is a portion of SEQ ID 359 LVTFVLLLI 16 639 LPIMTSILG 14 NO: 11: each start position Is 458 LALGQCVLA 16 701 APPDNKKRK 14 specified, the length of peptide is 9 502 LAFGALILT 16 702 PPDNKKRKK 14 amino acids, and the end position for 505 GALILTLVQ 16 19 YDPSFRGPI 13 each peptide Is the start position plus 510 TLVQIARVI 16 28 KNRSCTDVI 13 eight. 581 LMRNIVRW 16 34 DVICCVLFL 13 Pos 123456789 score 631 SPHLNYYWL 16 54 VAWLYGDPR 13 3 EAILLLVU 22 9 DDEAYGKPV 15 66 YPRNSTGAY 13 5 ILLLVUFL 14 45 ILGYIVVGI 15 112 TPQVCVSSC 13 2 LEAILLLVL 13 56 WLYGDPRQV 15 149 LPGVPWNMT 13 1 VLEAILLLV 12 110 CPTPQVCVS 15 174 SAPALGRCF 13 9 VLIFLRQRI 12 120 CPEDPWTVG 15 176 PALGRCFPW 13 151 GVPWNMTVI 15 187 VTPPALPGI 13 Table)0XII-V6.HLA-B5101 172 LPSAPALGR 15 189 PPALPGITN 13 9mers-24P4C12 224 DFAQSWYWI 15 201 IQQGISGLI 13 Each peptide Is a portion of SEQ 275 YCWEEYRVL 15 239 ALVLSLLFI 13 ID NO: 13; each start position is 308 TWLAALIVL 15 252 LVAGPLVLV 13 specified, the length of peptide is 9 336 IAIALLKEA 15 282 VLRDKGASI 13 amino adds, and the end position 338 IALLKEASK 15 285 DKGASISQL 13 for each peptide is the start 375 TALYLATSG 15 293 LGFTTNLSA 13 position plus eight. 485 FPLISAFIR 15 322 ILLLMLIFL 13 Pos 123456789 score 529 VQNPVARCI 15 330 LRQRIRAI 13 8 IPRSVFNLQ 16 564 AIYGKNFCV 15 340 LLKEASKAV 13 7 LIPRSVFNL 12 582 MRNIVRV 15 343 EASKAVGQM 13 9 PRSVFNLQI 12 596 DLLLFFGKL 15 356 FYPLVTFVL 13 5 KGUPRSVF 11 637 YWLPIMTSI 15 361 TFVLLUICI 13 4 SKGUPRSV 10 643 TSILGAYVI 15 384 QPQYVLWAS 13 647 GAYVIASGF 15 478 KPQDIPTFP 13 TableX)0II-V7-HLA-85101 700 EAPPDNKKR 15 487 USAFIRTL 13 9mers-24P4C12 20 DPSFRGPIK 14 489 SAFIRTLRY 13 Each peptide is a portion of SEQ 41 FLLFILGYI 14 500 GSLAFGALI 13 ID NO: 15; each start position is 43 LFILGYIW 14 506 ALILTLVQI 13 specified, the length of peptkde Is 9 72 GAYCGMGEN 14 521 YIDHKLRGV 13 amino acids, and the end position 87 LYFNIFSCI 14 531 NPVARCIMC 13 for each peptide Is the start 119 SCPEDPWTV 14 553 KFLNRNAYI 13 position plus elght 152 VPWNMTVIT 14 555 LNRNAYIMI 13 Pos 123456789 score 188 TPPALPGIT 14 563 IAlYGKNFC 13 1 SWYWILVAV 14 190 PALPGITND 14 578 FMLLMRNIV 13 7 VAVGQMMST 12 209 IDSLNARDI 14 580 LLMRNIVRV 13 2 WYWILVAVG 6 230 YWILVALGV 14 3 YWILVAVGQ 6 238 VALVLSLLF 14 TableX0I0-V3HLA45101 257 LVLVULGV 14 9mers-24P4C12 Table)00III-V8HILA-B5101-9mers. 409 NPTAHLVNS 14 Each peptide is a portion of SEQ 24P4C12 411 TAHLVNSSC 14 ID NO: 7; each start position is 450 LFWTLNWVL 14 specified, the length of peptide Is 9 465 LAGAFASFY 14 amino acids, and the end position 467 GAFASFYWA 14 for each peptide Is the start 482 IPTFPLISA 14 position plus eight 184 Each peptide is a portion of SEQ ID TableX=V.V1-HLA.A11Omers- rableXXXIV.V3-HLA-AIlOmers NO: 17; each start position is 24P4C12 24P4C12 specified, the length of peptide is 9 Each peptide is a portion of SEQ Each peptide is a portion of SEQ ID amino acids, and the end position for ID NO: 3; each start position Is NO: 7; each start position Is each peptide is the start position plus specified, the length of peptide is specified, the length of peptide is eight. 10 amino acds, and the end 10 amino acids, and the end Pos 123456789 score position for each peptide is the position for each pepdde Is the start 10 NPITPTGHV 21 start position plus rime, position plus nine. 15 TGHVFQTSI 18 Pus 1234567890 score Pos 1234567890 score 13 TPTGHVFQT 14 49 IYGIVAWLY 18 10 ITPPAEGIT 10 4 WLPIMRNPI 13 378 YfATSGgPQY 18 3 ROFPWTNITP 9 5 LPIMRNPIT 13 420 PGLMCVEQGY 18 7 WINITPfALP 8 464 VjTAGAF6SFY 18 8 TtAITPPALPG 6 TableXXXI-V9-HLA-85101- 10 DEAYGiEVKY 17 9 NITPPAGI 4 9mers-24P4C12 57 LYGDPRQVLY 17 Each peplide is a portion of SEQ 121 PEDPWTVGKN 17 TableXXXIV.V5.HLA.AI ID NO: 19; each start position is 265 VLGVLA GIY 17 10mers-24PC12 specified, the length of peptide Is9 271 YGIYYCWEEY 17 Each peptide is a portion of amino acids, and the end position 276 CWEEYR'LLRD 17 SEQ ID NO: 11; each start for each peptide is the start 369 1AYWAMIALY 17 poti is specified, the length position plus eight. 551 FIKFLNBNAY 17 of pepdde Is 10 amino acids, Pos 123456789 score 80 NKDKPYLLYF 16 and the end position for each 13 QPATLGYVL 20 348 V90MMSIMFY 16 peptide is the start positon plus 2 WAMTALYPL 18 676 RNNGSLDRPY 16 nine. 5 TALYPLPTQ 16 677 NNGSLDRPYY 16 Pos 1234567890 score 8 YPLPTOPAT 15 4 K2RDEDDEAY 15 2 VLEA1LVL 19 10 LPTQPATLG 14 18 KYDPSFEGPI 15 7 LLLVLIFLRQ 10 12 TQPATLGYV 13 65 LYPRNSIGAY 15 1 AVEAILLLV 9 17 LGYVLWASN 12 76 GMGENKDKPY 15 9 PLPTQPATL 11 214 ARDISVKIFE 15 TableMIV.VB.HLAA14lmevs 14 PATLGYVLW 11 293 LGMLSAY 15 24P4C12 18 GYVLWASNI 11 436 SVFNLQIY 15 Each peptde is a portion of SEQ 479 FPQDIPTEfPLI 15 ID NO: 13; each start position is TableXXXIV-V1I-HLA-Ai-10mers. 557 RtjAYIMIAIY 15 specified, the lengt of pepbde is 24P4C12 628 DEKSPHLNYY 15 10 amino adds, and the end Each peptide is a portion of SEQ 640 PIMTSILGAY 15 position for each peptide is the ID NO: 3; each start position Is 664 DILFLCELED 15 start position plus nine. specified, the length of peptide is 283 LRDKGASISQ 14 Pos 1234567890 score 10 amino acids, and the end 521 YIDHKLRGVQ 14 10 PRSVFNLQIY 15 position for each peptide Is the 673 DLERNNGSLD 14 1 QFYSSCGUP 7 start position plus nine. 141 YIKNRFCLP 13 4 SSKGUERSV 7 Pos 1234567890 score 305 VFETWLAALI 13 9 IERSVFNLQI 7 221 IFEDFAQSWY 25 382 SGQQYMLWA 13 488 IAFIRILRY 25 407 SNPTAHLVN 13 TabeXXV-V7HLA-AI1l1mers 39 VLFLLFILGY 23 518 IkYIDtiKLR 13 24P4C12 58 YGDPRQVLYP 23 547 CLEKFIKFLN 13 Each peptide Is a portion of SEQ, 79 EHKDKPYLLY 23 670 FIEDLERNNG 13 ID NO: 15; each start position is 262 ILGVLGVLAY 23 680 SLDRPYYMSK 13 specified, the length of peptide is 512 VLQARV!LEY 22 7 DEDDEAYGKP 12 10 amino acids, and Vie end 627 KFKSPjLNY 21 35 VICGWELLF 12 position foreach peptideisthe 132 FaQTVGEVFY 20 159 IfSLQQELCP 12 start position plus nine. 266 LGVLAYGIYY 20 163 QE PFLL 12 Pus 1234567890 score 362 FVLLLICIAY 20 242 L LLFILLLR 12 1 QVVLVAV 4 590 VLDKVTLLL 20 618 FSGRIPGLGK 12 2 SWYWILVAVG 4 594 VIDLLLEFGK 20 626 CLMFKSEHLN 12 4 YWILVAVGQM 3 318 VLEAILLLML 19 698 KbAEAPPDKK 12 5 VALVAVaQMM 2 32 CTDVICCVLF 18 6 iCVAVGIQMMS 2 185 8 VAVGQMMSTM 2 TableXXXV.V LA.A0201- TableXXXV.VI.HLA-A0201. 9 AVGMis-TMF 2 l0mers-24P4Cl2 mers-244C12 Each peptide is a portion of SEQ Each peptide is a portion of SEQ TabIXXV.V8MLA-A1 ID NO: 3; each start position is ID NO: 3; each start position is I Omers-24P412 specified, the length of peptide is specified, the length of peptide is Each peptides a portion of SEQ 10 amino acids, and the end 10 amino acids, and the end ID NO: 1l7; each start position Is position for each peplde Is the position for each peptide is the specified, the length of peptide is start position plus nine, start position plus nine. 10 amnino acids, and the end Pos 1234567890 score Pos 1234567890 score position for each peptide is the 441 NLQIYgVLGL 26 95 ILSSNIISVA 20 start position plus nine. 502 LAFGALILT 26 191 ALPGITNDTT 20 Pos 1234567890 score 517 VILEYIDHKL 26 238 VALVL,%LFI 20 19 VFQTSILGAY 16 603 KLLWGGVGV 26 261 LILGVLGVLA 20 4 YWLPIMRNPI 7 604 LLWGGVGVL 26 314 IVLAVLEAIL 20 13 IIPTGHVFQT 7 45 ILGYIWGIV 25 325 LMLIFLRQRI 20 21 QISILGAYVI 7 252 LVAGPLVLVL 25 329 FLRQRAI 20 304 SVQETWLAAL 25 350 QMMSTMFYPL 20 TableXXXIV-V9-HLA-A1-10mers- 312 ALIVLAVLEA 25 358 PLVV-L 20 24P4C12 318 VLEAILLLML 25 368 CIAYWAMTAL 20 Each peptide is a portion of SEQ ID 486 PUSAEIRT 25 393 NISSPGCEKV 20 NO: 19; each start position is 657 SVFGMCVDTL 25 55 FLNRiAYIMI 20 specified, the length of pepfde is 10 665 TLFLCELEDL 25 596 DLLLFFGKLL 20 amino acids, and the end position for 248 LLLRLyAGPL 24 645 ILGAYVIASG 20 each peptide is the start position plus 259 LVULGVLGV 24 649 YVIASGFFSV 20 nine. 310 LAALIVAVL 24 34 DV1CCMLVLL 19 Pos 1234567890 score 339 ALLKEASKAV 24 64 VLYPRNSTGA 19 11 LPTQPATLGY 21 597 LLLFFGKLLV 24 85 YLLYFNIFSC 19 12 PIQPATLGYV 10 41 FLLFILGYIV 23 186 NVTPPALPGI 19 42 LLFIL YI1W 23 233 LVALGVAILVIL 19 56 WL.YGDERQVL 23 264 GVLGVIAYGI 19 TableXXXV-VI-HLA-A0201- 231 WILVALGVAL 23 317 AVLEA!LLLM 19 10mers-24P4C12 249 LLRLVAGPLV 23 327 LIFLRQRIRI 19 Each peptide is a portion of SEQ 256 PLVLVLILGV 23 335 RIAA EA 19 ID NO: 3; each start position is 313 LIVLAVLEAI 23 351 MMSTMEYPLV 19 specified, the length of peptide is 315 VLAVLEAILL 23 357 YPLVTEVLLL 19 10 amino acids, and the end 438 SVFNLgIYGV 23 363 VILLICIAYW 19 position for each peptide is the 459 ALGQ AGA 23 364 LLLICIAWA 19 start position plus nine. 686 YMSKSLLKIL 23 365 LLICIAYWAM 19 Pos 1234567890 score 99 NIISVAENGL 22 380 ATSGQEQYVL 19 235 ALGVALVLSL 29 257 LVLVLILGVL 22 457 VLALGCVLA 19 44 FILGYJWGI 28 354 TMFYPLVTFV 22 536 CIMCCEKCCL 19 232 ILVALGVALV 28 413 HLVNSSCPGL 22 588 VVLDKVTDL 19 243 SLLFILLLRL 28 449 GLWrINWVL 22 633 HLNYYWLPIM 19 309 WLAAI4VLAV 28 506 ALILTLVQIA 22 644 SILGAYIAS 19 579 MLLMRNIVRV 28 510 TVQIARVIL 22 39 VLFLLFILGY 18 244 LLFILLLRLV 27 513 QIARVILEYI 22 157 TVTSLQQEL 18 260 VLILGVLGVL 27 581 LMRNIVRVW 22 203 QGISGILIDSL 18 433 GLIQRSVFNL 27 585 IVRVYLDKV 22 208 UDSLNARDI 18 508 ILTLVQIARV 27 590 VLDKVIDLLL 22 240 LVLSLLFILL 18 580 LLMRNIVRW 27 199 TTiQqisGL 21 246 FILLVAG 18 598 LLFFGELLW 27 247 ILLLRLVAGP 21 262 ILGVLQVLAY 18 48 YIWGIVAWL 26 253 VAGPL-LVLl 21 281 RVLRDKGASI 18 94 CILSShIlISV 26 316 LAVLEAILU 21 322 ILLLMIFLR 18 239 ALVLSLLFIL 26 501 SAFGALILT 21 332 MRIL 18 241 VLSU.EILLL 26 505 GALILTLVQI 21 360 VTFVLLLICI 18 251 RLVAGELVLV 26 641 IMTSILGAW 21 388 VLWASHISSP 18 321 AILLLMUFL 26 86 LLYFNIFSCI 20 448 LGLFWTNWMV 18 186 TableXXXV-VI-HLA-A0201- TableXXXV.VI.KLAA0201 Pos 1234567890 score 10mers-24P4C12 10mers.24P42 9 NITPPALPGI 23 Each peptide is a portion of SEQ Each peptide isa portion of SEQ 10 ITPPALPGIT 12 ID NO: 3; each start position is ID NO: 3; each start position is specfied, the length of peptide is specified, the length of peptide is Table)0OCV.VS-HLA.A0201 10 amino acds, and the end 10 amino acids, and the end 10mers.24P4C12 position for each peptide is the position for each peptide Is the Each peptde Isa portion of SEQ start position plus nine. start position plus nine. ID NO: 11; each start position is Pos 1234567890 score Pos 1234587890 score specfied, the length of peptide is 493 RTLRYjTGSL 18 323 LLLNIFLRQ 15 10 amino acids, and the end 525 KLRGV!PVA 18 340 LU(WKAVG 15 position for each peptide is the 589 VVLDKVFDLL 18 378 YLATSGQPQY 15 start position plus nine. 616 FFFSGRIPGL 18 379 LATSGQPQYV 15 Pos 1234567890 score 662 CVDTLFLCFL 18 430 SSKGL!QRSV 15 5 AILLLVUFL 26 685 YYMSKSLLKI 18 464 VLAGAFASFY 15 1 AVLEA!LLLV 25 130 NEFSQIVGEV 17 498 HTGSLAFGAL 15 2 VLEAILLLVI 25 143 KNRNFCLPGV 17 520 EYIDHIRGV 15 3 LEAILLLVLl 18 148 CLPGVPWNMT 17 539 CCFKCCLWCL 15 6 ILLLVLIFLR 18 170 FLLPSAPALG 17 601 FGKLL VGGV 15 8 LLVLIFLRQR 16 211 SLNARDISVK 17 690 SLLKIIGKKN 15 9 LVUFIRQRI 16 227 QSWYMLVAL 17 26 PIKNRSCTDV 14 7 LLL!FLRQ 15 254 AGPLVLVLIL 17 30 RSCTD%1CCV 1 10 VUFLBQRIR 12 296 TNLSAYQSV 17 37 CCVLFLLFIL 14 324 LLMLILROR 17 102 SVAENgLQCP 14 TableXXXV-V6-HLA.A0201 373 AMTALYLATS 17 149 LPGVPWNMTV 14 ltners-24PC12 481 DIPTFPLISA 17 153 PWNMTVITSL 1 Each peptide is a portion of SEQ 546 WCLEKEIKFL 17 162 LQQELCPSFL 14 ID NO: 13; each start position is 563 IAlYGKNFCV 17 165 ELCPSELLPS 14 specified, the length of peptide is 582 MRNIRVVVL 17 171 LPSAPALGR 14 10 amino acids, and the end 40 LFLLFILGYI 16 177 ALGRCFPWTN 14 position for each peptide is the 108 LQCPTEOVCV 16 220 KIFEDEAQSW 14 start position plus nine. 118 SSCPEDPWTV 16 273 IYYCWEYRV 14 Pos 1234567890 scre 169 SFLLPAPAL 16 338 IALLKEASKA 14 7 GUPRSVFNL 29 200 TIQQGISGLI 16 353 swhIYEvrF 14 4 SSKGUPRSV 15 207 GLIDSLNARD 16 370 AYWAMIALY. 14 212 LNARDISVKI 16 395 SSPGCEKVPI 14 TabeXXXV-VT.HLA.A0201. 236 LGVALVLSLL 16 416 NSSCPGLMCV 14 l0mers-24PC12 292 QLGFTINLSA 16 445 YGVLGLFWTL 14 Each peptide is a portion of SEQ 307 ETWLAAUVL 16 483 P1FPL!SAFI 14 ID NO: 15; each start position is 319 LEAILLLMLI 16 500 GSLAFGALIL 14 spedfled. the length of pepie is .337 AIALLKEASK 16 571 CVSAKNAFML 14 10 amino acids, and the end 366 LICIAYWAMT 16 577 AFMLLMRNIV 14 position for each peptide is the 405 NTSCNETAHL 16 595 TDLLLFFGKL 14 start position plus nine. 451 FWTLNWVLAL 16 606 WGGGVLSF 14 Pos 1234567890 score 456 WVLALGOCVL 16 639 LPIMTfiLGA 14 1 QWWILVAV 4 458 LALGQCVLAG 16 680 SLDRPYYMSK 14 2 SWYWILYAVG 4 503 AFGAULTLV 16 693 KILGKNEAP 14 4 Y71LVAVGQM 3 509 LTLVQiARVI 16 694 ILGK EAPP 14 5 WILVAVGQMM 2 637 YWLPIMTSIL 16 6 ILVAVGQMMS 2 33 TDVICCVLFL 15 Tab*X*(V-V3-HLA.A0201- 8 VAVGQMMSTM 2 36 ICCVLFLLFI 15 l1mem-24P4C2 9 AVGQMSTMF 2 90 NIFSC!LSSN 15 Each peptide is a portion of SEQ 161 SLQQELICPSF 15 ID NO: 7; each start position is TableXXXV.V8-HLA-A0201 225 FAQSWYWILV 15 specified, the length of peptide Is 110mers24PC12 234 VALGVLVLS 15 10aminoacids,andtheend 250 LRLVAGPLVL 15 position for each peptide Is the 284 RDKGANISQL 135 start position plus nine. 187 Each peptide is a portion of SEQ TabIeXXXVV -HLA.A0203. TableX)MIVI-HLA.A0203 ID NO: 17; each start position is l0mers-24P4C12 l0mers-24PC12 specified, the length of peptide Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID is 10 amino acids, and the end N. 3; each start position is NO: 3; each start position Is position for each peptide is the specified. the Length of peptide Is 10 specified, the length of peptide is 10 start position plus nine. amino adds, and the end position amino acis, and the end position Pos 1234567890 score for each peptide is the start position for each peptide is the start position 4 YWLPIMRNPI 15 plus nine, plus nine. 5 WLPIMRNPIT 15 Pos 1234567890 score Pos 1234567890 scoe 18 HVFOTI|LGA 15 46 LGYIVVGIVA 10 218 SVKIFEDFAQ 9 7 PIMRNEITPT 14 64 VjYPRNBTGA 10 227 QLWYWILVAL 9 13 ITPTGHVFQT 14 95 ILSSNIISVA 10 231 W!LVALGVAL 9 8 IMRNPITPTG 13 166 LCPSFLLPSA 10 246 FILLIRIVAG 9 21 QTSILGAYVI 13 182 FEWTNVPPA 10 262 ILGVLGMIAY 9 20 FQTSILGAYV 12 205 ISGLDSLNA 10 280 YRVLRDKGAS 9 15 PTGHVEQTSI 11 217 ISVKIFEDFA 1 293 LGFUFNLSAY 9 10 RNPITPTGHV 10 226 AQSWYWILVA 10 309 WLAALIYLAV 9 16 TGHVFQTSIL 10 230 YWILVALGVA 10 313 LjVLAVLEAI 9 12 PITPT.QHVFQ 8 245 LEILLLRLVA 10 329 FLRQRIRIAI 9 261 LILGVLGVLA 10 331 RQiRIAAL 9 TableXXXV-V9-HLA-A0201- 279 EYRVLRDKGA 10 336 kA1ALLSEAS 9 10mers-24P4C12 292 &LGF1LSA 10 339 ALLKEASKAV 9 Each peptide is a portion of SEQ 302 YgSVOE1YLA 10 362 FVLLLICIAY 9 ID NO:19; each start position is 308 TML!VLA 10 365 LCtAYWAM 9 specified, the length of peptide is 312 AWlVLAYLEA 10 368 C5AYAMTAL 9 10 amino acids, and the end 328 IELRQRIRIA 10 372 WANTALYLAT 9 position for each peptide is the 335 R1AIALLKEA 10 383 GqPYVLWAS 9 start position plus nine. 338 IALIKEASM 10 404 IHTSCNETAH 9 Pos 1234567890 score 361 TFVLLLICIA 10 451 FWTLNWA-AL 9 9 YPLPTQPATL 20 364 ILLICLAYWA 10 458 LALGOCVLAG 9 2 YWAMTALYPL 19 367 iYWv A 10 460 LGQCVLAGAF 9 7 ALYPLPTQPA 19 371 YWAMTALYLA 10 462 QCVLAGAFAS 9 12 PTQPAILGYV 17 382 SGQPQWLWA 10 467 GAJASFYWAF 9 16 ATLGYVLWAS 15 403 P!NTSCNPTA 10 482 ETFPLISAF 9 4 AMTALYPLPT 14 450 LEWlNV 10 495 LBYHTGaLAF 9 5 MTALYELPTO 13 457 VLALGQ9VLA 10 498 H{GSLAFGAL 9 17 TLGYVLWASN 13 466 AGAFASEYWA 10 507 LTLVdIAR 9 13 TQPATLGYVL 11 481 D!PTFPLISA 10 526 LRGVQNPVAR 9 18 LGYVLWASNI 11 494 TIRYHTGSLA 10 551 FIKFLNRNAY 9 15 PATLGVVLWA 9 497 YHTG&LAFGA 10 556 NRNAYIMIAI 9 506 ALILTL.VQIA 10 566 Y.GKNFCMSAK 9 TableXOXV-V1-HLA-A0203- 525 KLRGVQNPVA 10 569 NfCVSAKNAF 9 10mers-24P4C12 550 KIFL_1RNA 10 640 PIMTSILGAY 9 Each peptide is a portion of SEQ ID 555 WNAYIMIA 10 644 S!LGAYYIAS 9 NO: 3; each start position is 565 IYGKNFVSA 10 693 K!LG"EAP 9 specified, the length of peptide is 10 568 KNFCVSANA 10 amino acids, and the end position 639 LEIMISILGA 10 for each peptide is the start position 643 TILGAYVL 10 TabteXXXVI-V3-HLA-A0203-10mer plus nine. 692 LEILGKNEA 10 24P4C12 Pos 1234567890 score 4 KRDEDPEAY 9 Each peptide is a portion of SEQ ID 303 QSVQETWLAA 19 47 GYIVVGIVAW 9 NO: 7; each start position Is specfied, 168 PZFLLPSAPA 18 65 LYPRSIGAY 9 thelengthofpeplideis10aino 330 L.QRIRIAIA 18 96 LSSNIIaVAE 9 adds, and the end poston for each 459 ALGQCVLAGA 18 167 CESFLLPSAP 9 peptide is the start position plus nine. 461 GQCVL4.AGAFA 18 169 SELIPSAPAL 9 Pos 1234567890 score 304 SYQETWLAAL 17 183 PWENVTEPAL 9 5 FEMIIPPA 10 3 1G!KQ E5DEA 10 206 SGLIDSLNAR 9 6 PARNInEPAL 9 188 TableXXXVI-V3-HLA-A0203l1mers- 16 ATLGYVLWAS 9 Tab1eX0meVIrsHLA.A310mem 24P4C12 9 YPLPTQEATL 8 24P4C12 Each peptide is a portion of SEQ ID 17 TLGYVLWASN 8 Each peptide is a portion of SEQ ID NO: 7; each start position is specified, M. 3; each start position Is specfied, the length of peptie is 10 amino TableXXXViHLA-A3-l0mers- the length of peptide is 10 amino acids, and the end position for each 24P4C12 adds, and the end position for each peptide is the start position plus nine. Each peptide is a portion of SEQ ID peptide Is the start posltlor) plus nine. Pos 1234567890 score NO: 3; each start position is specfied, Pos 1234567890 score 7 WINITPEALP 8 the length of peptide is 10 amino 340 LIEAZAVG 19 acids. and the end position for each 347 AV GQMMSTMF 19 TableXXXVI-V5-HLA-A0203- peptide is the start positon plus nine. 494 TLRYHTGSLA 19 10mers-24P4C12 Pos 1234567890 score 605 LVjGGVGVLS 19 Pos 1234567890 score 333 RIFLAWJJ( 32 618 FSGRIPGLGK 19 NoResuttsFound. 211 SLjiAR2SVK 30 645 ILGAWASG 19 .337 AIALLKEASK 28 673 DLERNNGSLD 19 TableXXXVI-V6-HLA-A0203- 516 Rq[LETDHK 28 6 RDFDDEAYGK 18 10mers-24P4C12 281 RVLRDDASI 27 64 VL.PROTGA 18 Pos 1234567890 score 680 SLDRPYYSK 27 134 QTVGEYYTK 18 NoResultsFound. 464 VIAGAFASFY 25 231 WIALGVAL 18 584 NIYRV~LDK. 24 235 ALGVA LVLSL 18 621 RIPGLGKDFK 24 247 IL[LRLVAGP 18 TableXXXVI-V7-HLA-A0203-10mers- 49 IWGIVAWLY 23 258 VLVLGVLG 18 24P4C12 463 CVLAGAFASF 23 324 LLMUFIROR 18 Each peptide is a portion of SEQ ID 233 LVALGVALVL 22 456 WVLgQCVL 18 NO: 15; each start position is specified, 262 ILGVLGVLAY 22 532 PVARCIMCCF 18 the length of peptide is 10 amino acids, 376 AI. GQP 22 72 GAYCGMfENK 17 and the end position for each peptide is 443 QIYGWGLFW 22 86 LLXFNIFSCI 17 the start position plus nine. 525 KLEGVQUPVA 22 161 SLQELCPSF 17 Pos 1234567890 score 587 RVYVLaKWD 22 207 GLIDSUbjARD 17 1 QSWYWLVAV 9 603 KLLWGGVGV 22 220 KIFEDEAQSW 17 2 SWYWILVAVG 8 56 WLYGDFRQVt 21 232 ILVALGVALV 17 63 QVLYPRNSTG 21 249 LLBLVF6PLV 17 TableXXXVI-V8-HLA-A0203-10mers- 177 ALGRC2 24P4C12 58 AIIGKNECVS 21 264 GV!GVLAYGI 17 Each peptide is a portion of SEQ ID 606 VGVLSF 21 265 VAGVAYGIY 17 NO: 17; each start position Is 39 VlFLLFILGY 20 292 QLG1HLSA 17 specified, the length of peptide isl1 53 IVAWLYGDPR 20 309 WLALVLAV 17 amino acids, and the end position for 171 LLPSAPALGR 20 326 ML!FLBQRIR 1 each peptide is the start position plus 251 RLYAGPVLV 20 364 LLLICIAYWA 17 nine. 252 LV6GP1,YLVL 20 388 W.ASJSSP 17 Pos 1234567890 score 282 VLPKSlS 20 392 SNISSGCEK 17 18 HVFQTSILGA 10 362 FVLLLIQIAY 20 488 PL!SAFIRTL 17 19 VFQTSILGAY 9 378 YLATSGQPQY 20 506 AL1LTLYOIA 17 20 FQTSILGAYV 8 544 CLWCLEKFIK 20 551 FINFLNANAY 17 650 VIASGEESVF 20 580 LLMRNIVRW 17 TableXXXVI-V9.HLA-A0203-10mers- 95 ILSSNASVA 19 598 LLFFGIL 17 24P4C12 170 FLPSAALG 19 612 VLSFFFFSGR 17 Each peptide is a portion of SEQ ID 191 ALPGITNDTT 19 624 GLQKDEKSPH 17 .NO: 19; each start position is 237 GVALVSLLF 19 649 YV1ASGEFSV 17 specified, the length of peptide Is 10 248 LLLRLYAGPL 19 657 SVFGMCVDTL 17 amino adds, and the end position for 260 VL1LGVLGVI 19 667 FLCFLEDLER 17 each peptide is the start position plus 261 LILGVLQVLA 19 684 PYVMSKSW( 17 nine. 298 NL_ AY0SVQE 19 689 KS LLKkK 17 Pos 1234567890 score 32 ALIVLAVLEA 19 9 DDE-AYGKPVK 16 7 ALYPLPTQPA 10 314 IVLjVILAIL 19 44 FLLGYIYYGI 16 15 PATLGYYLWA 10 317 AVLEAL 19 126 TVGKNf SQT 16 8 LPLPT'QPAT 9 322 IYP LMLIFLR 19 165 ELCPsLPS 16 189 Table)0(VI-V-HLA-A3-10mers. Each peptide Isa portion of SEQ ID Pos 1234567890 score 24P4C12 NO: 7; each start position is 9 AVQMNLSTMF 19 Each peptide is a portion of SEQ ID specified, the length of peptide is 10 6 ILVAVggMMS 16 NO: 3; each start position is specified, amino acids, and the end position for 5 WILVAVGQMM 14 the length of peptide is 10 amino each peptide is the start position pius 7 LVAVGQ!MST 14 acids, and the end position for each nine. 2 SWVILVAVG 12 peptide is the start position plus nine. Pos 1234567890 score 8 VAVGQMMSTM 9 Pos 1234567890 score 3 RCEPWIWTP 11 243 SLLFILLLRL 16 9 NIIPPALPGl 11 TableXXXVIIV8ILAA3-lmers 246 FILLL.LVAG 16 8 TN!TPPALPG 9 24P4C12 259 LVLILGVLGV 16 10 ITPPALPGIT 7 Each peptide is a portion of SEQ ID 272 GIlYCWEEYR 16 7 wTWTEeALP 5 NQ 17; each start position is 304 SVQETWLAAL 16 specified, the length of peptide Is 10 318 VLEAILLLML 16 amino acids, and the end position for 339 ALLKEASKAV 16 TableXXXVII-V5-HLA-A3-l0mers each peptide is the start position plus 363 VLLLICIAYW 16 2412402 nine. 453 TLgWVLALGQ 16 EachpeptideisaportionofSEQlD Pos 1234567890 score 457 VLALGQVLA 16 NO: 11; each start position is specified, 12 PIIPT Q 15 459 ALGQCVLAGA 16 the length of peptide is 10 amino acids, 11 NPITPTGHVF 14 487 LIAFIBTLR 16 and the end position for each peptide Is 18 HVEQTSILGA 13 508 ILILVQ!ARV 16 the start position plus nine. 7 PIMRNEITPT 12 518 ILEYIDHKLR 16 Pos 1234567890 score 5 WLPIMRNPIT 11 559 AYIMIAIYGK 16 1 AVLEALLLV 19 1 LNYYWPIMR 10 566 YGNFQVSAK 16 2 VLEAILLLVL 19 8 IMRNPITPTG 10 571 CVSAKNAFML 16 6 LLLVUFLR 19 2 QTSlGAYVI 10 579 MLLMRNIVRV 16 8 LLYLIELRQR 18 9 MRIAPIITGH 9 596 DLLLFEQKLL 16 10 VL!FLRgRIR 17 6 LPIMRNPITP 8 640 PIMTSILGAY 16 7 LIFLRQ 15 19 VF-TSILGAY 8 690 SLLKILGKKN 16 5 AILLLLIFL 14 693 KILGK-MEAP 16 9 LVUFLRQRI 14 TableX*MI.V9-HLA.A3-10mers 35 VIrCVLELLF 15 4 EAILILYLIF 11 24P4C12 41 FLLFILGYIV 15 Each peptide is a portion of SEQ ID 42 LLEILEYIW 15 7able)(VII-VS-HLA.A3-l0mers. NO: 19; each start position is 107 GLQCPIEQVC 15 241402 specified, the length of peptide is 10 120 CPEDPWTVGK 15 Each peptide Is a portion of SEQ ID amino acids, and the end position for 180 RCEPWIfNVTP 15 NO: 13; each start position is each peptide is t start position pius 323 LLLMLIELRQ 15 specified, the length of peptide is 10 nine. 329 FLQIRIAI 15 amino acids, and the end position for Pos 1234567890 score 367 ICIAYWAMTA 15 each peptide is the start position pius 7 ALYPLPIQPA 20 369 IAYWAMTALY 15 nine. 17 TLGYVLWASN 15 423 MCYFQQYSSK 15 Pos 1234567890 score 10 PLPTQPATLG 14 446 GVLGLETU 15 7 GLIPRYfNL 16 9 YPLPTCPATL 13 491 FIRTLRYHTG 15 5 SKGLISVF 14 1 AYWAMIALYP 11 507 LILTLQlAR 15 1 QGXSSKGLIP 12 18 LGXVLW6SNI 10 510 TLYQIABVIL 15 8 LIRRSfENLQ 11 4 AMTALYELP 9 585 IVBVWYLDKV 15 9 IPRSVFNLOI 11 11 LPIQ GY 9 597 LLLFFGKLLV 15 6 KGLIPLSVFN 10 13 IQPATIGYVI 9 604 LLVVGGVGVL 15 4 SSKGUERSV 7 688 SKSLLI!LGK 15 TableXXXVUI-VI-HLA-A2B-1 Omers 694 ILjKK1EAPP 15 TabIeX VU.V7HLA-A3-l0mers- 24PC12 697 KKNEAPPDNK 15 2402 Each peptide is a portion of SEQ ID 698 *IjgEAP7EDNKK 15 Each peptide is a portion of SEQ ID NO: 3; each start position Is NO: 15; each start position is specified, the length of peptide is 10 TableXJO(VIV3-HLA-A3-10mers- specified, the length of peptide is 10 amino acids, and te end position for 24P4C12 amino acids, and the end position for each peptide is the start position each peptide is the start position plus plus nine. nine. Pos 1234567890 score 190 TableXXXVIII-VI.HLA.A26-10mers- 7ableXXXVIII.VI-HLA.A26-10mers- 10 ITPPALPGIT 10 24P4C12 2402 7 wTNITPPALP 8 Each peptide is a portion of SEQ ID Each peptide is a portion of SEQ ID 3 RCFPWTNITP 7 NO: 3; each start position is NQ 3: each start position is 8 TNITPPALPG 6 specified, te length of peptide is 10 specfied, the length of peptide is 10 4 CFPWTNITPP 4 amino acids, and the end position for ammo adds, and the end position for each peptide Is the start position each peptide is the start position TabeX)MIIVS.HLA-A26 plus nine. pus nine. l0mers-24C2 Pos 1234567890 score Pos 1234567890 score Each peptde isa portion of 34 DVICCVLFLL 34 532 PVARCIMCCF 18 SEQ ID NO: 11; each start 138 EVFYTKNRNF 32 549 EKFIKFLNRN 18 position is specified, the length 307 ETWLAALIVL 31 609 GVGVLSFFFF 18 of peptide is 10 amino acids, 657 SVFGMCVDTL 28 99 NIISVAENGL 17 and the end position for each 199 TTIQQGISGL 26 102 SVAENGLQCP 17 peptideisthestartpostionplus 304 SVQETWLAAL 26 156 MTVITSLQQE 17 nine. 588 WVLDKVTDL 26 236 LGVALVLSLL 17 Pos 1234567890 soore 592 DKVTDLLLFF 25 260 VLILGVLGVL 17 4 EAILLLVUF 27 49 IWGIVAWLY 24 316 LAVIEAILLL 17 1 AVLEAILLLV 17 606 WGGVGVLSF 24 317 AVLEAIUJJJ 17 5 ALLLVUFL 17 157 TVITSLQQEL 23 321 AILLLMLIFL 17 2 VLEAILLLVI 13 252 LVAGPLVLVL 23 360 VTFVLLUC1 17 257 LVLVLILGVL 23 442 LQIYGVLGLF 17 TableXXXVIII-V64ILA.A26 320 EAULllIvLIF 23 596 DLLLFFGKLL 17 10mers-244 2 628 DFKSPHLNYY 23 604 LLWGGVGVL 17 Each peptide Is a portion of 79 ENKDKPYLLY 22 616 FFFSGRIPGL 17 SEQ ID NO: 13; each start 353 STMFYPLVTF 22 664 DTLFLCFLED 17 position is specified, the length 362 FVLLLICIAY 22 665 TLFLCFLEOL 17 of peptide is 10amio acids, 662 CVDTLFLCFL 22 682 DRPYYMSKSL 17 and the end position for each 672 EDLERNNGSL 22 32 CTDVICCVLF 16 peptide is the start poon plus 48 YIWGIVAWL 20 37 CCVLFLLFIL 16 nine. 198 DTTIQQGISG 20 123 DPWTGKNEF 16 Pos 1234 890 sce 216 DISVKIFEDF 20 165 ELCPSFLLPS 16 7 GLIPRSVFNL 17 240 LVLSLLFLL 20 186 NVTPPALPGI 16 10 PRSVFNLQIY 14 293 LGFTTNLSAY 20 224 DFAQSvYWIL 16 5 SKGLIPRSVF 10 640 PIMTSILGAY 20 239 ALVISILFIL 16 10 DEAYGKPVKY 19 262 ILGVLGVLAY 16 TabIeXXXVIII-HLA.A26 39 VLFLLFILGY 19 266 LGVLAYGIYY 16 l1mers-24P4C2 131 EFSQTVGEVF 19 332 ORIRIAIALL 16 Each peptide isa portion of SEQ 233 LVALGVALVL 19 359 LVTFVLLLIC 16 IDNO:15;eachstartpositionis 237 GVALVLSLLF 19 380 ATSGQPQYVL 16 specified, the length of peptide is 347 AVGQMMSTMF 19 400 EKVPINTSCN 16 10 amino acids, and the end 438 SVFNLQIYGV 19 405 NTSCNPTAHL 16 position for each peptde is the 463 CVLAGAFASF 19 424 CVFQGYSSKG 16 start position plus ine. 498 HTGSLAFGAL 19 433 GLIQRSVFNL 16 Pos 1234567890 score 512 VQIARVILEY 19 539 CCFKCCLWCL 16 9 AVGQMMSTMF 19 520 EY1DHKLRGV 19 593 KVTDLLLFFG 16 7 LVAVGQMMST 11 571 CVSAKNAFML 19 4 YWLVAVGQM 10 589 WLDKVTDLL 19 TableX)OMII-V3-HLA.A26. Omors 33 TDVICCVLFL 18 24P4C12 TableXXXV11M8HLA-A26. 203 QGISGLIDSL 18 Each peptide is a portion of SEQ ID NO: 10mers-24PC12 314 IVLAVLEAL 18 7; each start position Is specified, the Each peptide is a portion of SEQ ID 456 WVLALGQCVL 18 length of peptide Is 10 amlno acds, and NO: 17; each start position is 481 DIPTFPLISA 18 the end position for each peptide is the specified, the length of peptide Is 10 486 PLSAFIRTL 18 start position plus nine, amino acds, and the end position 493 RTLRYHTGSL 18 Pos 1234567890 sor for each peptide is the start position 502 LAFGAULTL 18 6 PWrNITPPAL 10 plus nine. 516 RVILEYIDHK 18 9 NITPPALPGI - 10 Pos 1234567890 score 191 18 HVFQTSILGA 19 TabIOXXXIX.VI.HLABO702- TableXXV1-HLA-B0702 19 VFQTSILGAY 16 l0mers-24PC12 10mers-24PC12 11 NPITPTGHVF 13 Each peptide is a portion of SEQ Each peptide is a portion of SEQ 13 ITPTGHVFQT 13 ID NO: 3; each start position Is ID NO: 3; each start position is 16 TGHVFQTSIL 10 specified, the length of peptide Is specified, the length of pepbde is 15 PTGHVFQTSI 9 10 amino acids, and the end 10 amino acids, and the end position for each peptie is the position for each peptide is the TableXXXVII-V9-HLA-A26-10mors- start position pus nine, start position plus nine. 24P4C12 Pos 1234567890 score Pos 1234567890 score Each peptide is a portion of SEQ ID 331 RQRIRAIAL 14 316 LAWEAILL 12 NO: 19; each start position is 405 NTSCNPTAHL 14 409 NPTAHLVNSS 12 specified, the length of peptide is 10 451 FWTLNWVLAL 14 419 CPGLMCVFQG 12 amino acids, and the end position for 502 LAFGAULTL 14 425 VFQGYSSKGL 12 each peptide is the start position plus 582 MRNIVRVWL 14 456 WVLALGQCVL 12 nine. 590 VLDKVTLLL 14 493 RTIRYHTGSL 12 Pos 1234567890 score 15 KPVKYDPSFR 13 581 LMRNIVRV 12 12 PTQPATLGYV 14 60 DPRQVLYPRN 13 588 WVLDKVTDL 12 5 MTALYPLPTQ 13 66 YPRNSTGAYC 13 604 LLWGGVGVL 12 16 ATLGYVLWAS 13 110 CPTPQVCVSS 13 606 WGGVGVLSF 12 2 YWAMTALYPL 12 120 CPEDPWrVGK 13 622 IPGLGKDFKS 12 11 LPTQPATLGY 12 167 CPSFLLPSAP 13 837 YWLPIMTSIL 12 9 YPLPTQPATL 10 172 LPSAPALGRC 13 662 CVDTLFLCFL 12 13 TQPATLGYVL 10 226 AQSWYWILVA 13 701 APPDNKKRKK 12 15 PATLGYVLWA 6 227 QSWYWILVAL 13 18 KYOPSFRGPI 11 231 WILVALGVAL 13 25 GPIKNRSCTD 11 TableXXXIX-V1-HLA-B0702- 250 LRLVAGPLVL 13 31 SOTDVICOV I 1 10mers-24P4C12 284 RDKGASISQL 13 44 FILGYIWGI 11 Each peptide is a portion of SEQ 290 ISQLGMNL 13 77 MGENKDKPYL I1 ID NO: 3; each start position is 301 AYQSVQEIWL 13 78 GENKDKPYLL 11 specified, the length of peptide is 310 LAALIVLAVL 13 140 FKNRNFCL I1 10 amino acids, and the end 314 IVLAVLEAIL 13 152 VPWNMTVITS 1i position for each peptide Is the 318 VLEAIUIML 13 153 PWNMTVITSL 11 start position plus nine. 321 AILLLMLIFL 13 162 LOQELCPSFL II Pos 1234567890 score 350 QMMSTMFYPL 13 188 TPPALPGITN 11 357 YPLVTFVLLL 23 355 MFYPLVTFVL 13 224 DFAQSWYWIL I1 478 KPQDIPTFPL 23 356 FYPLVTFVU. 13 236 LGVALVLSI± 11 683 RPYYMSKSLL 21 368 CIAYWAMTAL 13 240 LVLSLLFILL 11 182 FPWTNVTPPA 19 396 SPGCEKVPIN 13 248 LLLRLVAGPL 11 83 KPYLLYFNIF 18 441 NLQIYGVLGL 13 257 LVLVULGVL 11 192 LPGITNDTTI 18 498 HTGSLAFGAL 13 260 VLILGVLGVL 11 482 IPTFPLISAF 18 500 GSLAFGALIL 13 274 YYCWEEYRVL 11 639 LPIMTSILGA 18 510 TIVOIARVIL 13 312 AUVLAVLEA 11 149 LPGVPWNMTV 17 525 KLRGVONPVA 13 315 VLAVLEAILL 11 252 LVAGPLVLVL 17 571 CVSAKNAFML 13 332 QRIRIAIALL 11 380 ATSGQPOYVL 17 572 VSAKNAFMLL 13 384 QPQWLWASN 11 402 VPINTSCNPT 17 657 SVFGMCVDTL 13 395 SSPGCEKVPI 11 485 FPLISAFIRT 17 686 YMSKSLLKIL 13 413 HLVNSSCPGL 11 123 DPWTVGKNEF 16 20 DPSFRGPIK 12 433 GUQRSVFNL 11 235 ALGVALVLSL 16 48 YIWGIVAWL 12 435 IQRSVFNLQI 11 254 AGPLVLVLIL 15 169 SFLLPSAPAL 12 439 VFNLQIYGVL 11 370 AYWAMTALYL 15 183 PWTNVTPPAL 12 445 YGVLGLFWFL 11 659 FGMCVDTLFL 15 189 PPALPGITND 12 449 GLFWTLNWVL 11 33 TDVICCVLFL 14 239 ALVLSLLFIL 12 503 AFGALILTLV 11 56 WLYGDPRQVL 14 243 SLLFILIIRL 12 531 NPVARCIMCC 11 175 APALGRCFPW 14 304 SVQEVWLAAL 12 536 CIMCCFKCCL 11 233 LVALGVALVL 14 307 ETWLAALIVL 12 539 CCFKCCLWCL 11 241 VLSLLFILLL 14 309 WLAALIVLAV 12 546 WCLEKFIKFL 11 192 TableXXXIX-VI-HLA-B0702- 24P4C12 10mers-24P4C12 Pos 1234567890 score Each peptide is a portion of SEQ TabIeXx.V7-HLkBO702 NoResultsFound. ID NO: 3; each start position Is iomers.24PCl2 specified, the length of peptide Is Each peptide is a portion of SEQ ID TableXLV3-HLA-B08.l1mers 10 amino acids, and the end NO: 15; each statposition is 24P4C12 position for each peptide is the specified, the length of peptide Is 10 Pos 1234567890 score start position plus nine. amino acds, and the end position for NoResubFound. Pos 1234567890 score each peptide is the start position plus 565 IYGKNFCVSA 11 nine. TableXL.V5-HLA.B08.l1mers 589 VVLDKVTDLL 11 Pos 1234567890 score 24P4C12 595 TDLLLFFGKL 11 9 AVGQMMSTMF 10 Pos 1234567890 score 616 FFFSGRIPGL 11 1 QSWYWILVAV 9 NoResuttsFound. 625 LGKDFKSPHL 11 8 VAVGQMMSTM 8 630 KSPHLNYYWL 11 4 YWILVAVGQM 7 TableXLV6HLA.08-l0mers 672 EDLERNNGSL 11 7 LVAVGQMMST 7 24P4C12 5 WILVAVGQMM 6 Pos 1234567890 score TableXXXJX-V3-HLA-B0702- NoResutsFound. 10mers-24P4C12 TableX)VJX.VS-HLA-BO7O2 Each peptide is a portion of SEQ ID l0mers.24P4C2 TableXL.W.HLA.B08.l0mers NO: 7; each start position is Each peptide is a portion of SEQ . ARM specified, the length of peptide is 10 ID NO: 17; each start position is Poe 1234567890 score amino adds, and the end position specified, the length of peptide is NoResultsFound. for each peptide is the start position 10 amino acids, and the end plus nine. position for each peptide is the TableXL.VO-HLA.B08-10mers* Pos 1234567890 score start position pus nine. 2412402 5 FPWTNITPPA 19 Pos 1234567890 score Pos 1234567890 score 6 PWTNITPPAL 12 11 NPITPTGHVF 17 NoResuttsFound. 1 LGRCFPWTNI 9 14 TPTGHVFQTS 13 16 TGI4VFQTSIL 11 TableXL-ILA-B08 TabIeXXXJX-V5-HLA-B0702- 6 LPIMRNPITP 10 lmers-24P4C12 10mers-24P4C12 4 YWLPIMRNPI 9 Pos 1234567890 score Each peptide is a portion of SEQ 7 PIMRNPITPT 9 NoResultsFound. ID NO- 11; each start position is 21 QTSILGAYVI 9 specified, the length of peptide is 10 RNPITPTGHV 8 TableXL-VI-HLA-81510-l0mes 10 amino acids, and the end 13 ITPTGHVFQT 8 24P4C12 position for each peptide is the 15 PTGHVFQTSI 8 Pos 1234567890 score start position plus nine. 18 HVFQTSILGA 8 NoResultsFound. Pos 1234567890 score 2 VLEAILLLVL 14 TabIXXXX.V9-HLA-B0702- TableXU-V-HLA-B15104 mers 5 AILLLVLIFL 13 10mem-24P4C12 24P4C12 1 AVLEAILLLV 10 Each peptide Isa portion of SEQ Pos 1234567890 Score 4 EAILLLVUF 10 ID N0 19; each start position is NoResultsFound. 3 LEAILLLVLI 9 specified, the length of pepte is 9 LVLIFLRQRI 7 10 amino acds, and the end TblsXU-V5.HLA-B1510-10mem position for each peptide Is the 24P4C12 TableX)0X.V6-HLA-B0702- start position plus nine. Pos 1234567890 score 10mers-24P4C12 Pos 1234567890 score NoResulFound. Each peptide is a portion of SEQ ID 9 YPIPTQPATL 22 NO: 13; each start position is 11 LPTQPATLGY 13 TableXLIV.HLA.B1510 specified, the length of peptide is 10 14 OPATIGYVIW 13 lomers-2412C12 amino acids, and the end position 2 YWAMTALYPL 12 Pos 1234567890 score 'for each peptide Is the start position 4 AMTALYPLPT 12 NoResultsFound. plus nine. 13 TQPATLGYVL 12 Pos 1234567890 score 7 ALYPLPTQPA 11 TableXU.VT.HLA81510-10mers 9 IPRSVFNLQI 21 24P4C12 7 GLIPRSVFNL 12 TabIeXL-VILA-078-0mers 193 Pos 1234567890 score TableXll-V3-HLA-B2709-10mers- TabteXLIV.Vi-HLA-B4402 NoResultsFound. 24P4C12 10mem-24P4C12 Pos 1234567890 score Each peptide is a portion of SEQ ID TabIeXLI-V8-HLA-B151 0 -10mers- NoResultsFound. NO: 3; each start position is 2402 specified, the length of peptide Is 10 Pos 1234567890 score TableXLIII.VS-HLA-82709-i0mers- amino acds, and the end position NoResultsFound. 24P4C12 for each peptide is the start position Pos 1234567890 sore plus nine. TableXLI-V9-HLA-B1510-10mers- NoResultsFound. Pos 1234567890 score 24P4C12 199 TTIQQGISGL 16 Pos 1234567890 score TableXLIlIl-V6-HLA-B2709-10mers- 203 QGISGUDSL 16 NoResultsFound. 24P4C12 260 VULGVLGVL 16 Pos 1234567890 score 293 LGFNLSAY 16 NoResultsFound. 307 ETWLAALIVL 16 TableXLIl.VI.HLA-B2705-10mers- 316 LAVLEAILLL 16 24P4C12 TableXLIll-V7-HLA-B2709-o1mers-24P4C12 38 ATSGOPQYVL 16 Pos 1234567890 score Pos 1234567890 score 546 WCLEKFIKFL 16 NoResultsFound. NoResultsFound. 657 SVFGMCVDTL 16 34 DVICCVLFLL 15 TabteXLII-V3-HLA-B2705-10mers-2 4

P

4 C1 2 TabilII-HLA-B2709-110mers 65 LYPRNSTGAY 15 Pos 1234567890 score 24P4C12 79 ENKDKPYLLY 15 NoResuttsFound. Pos 1234567890 score 99 NIISVAENGL 15 NoResultFound. 104 AENGLQCPTP 15 TableXL.-V5-HLA-B2705-10mers- 138 EVFYTKRNF 15 24P4C12 TablXLIII-V9-HLA-B2709-10mers- 213 NARDISVKIF 15 Pos 1234567890 score 241402 235 ALGVALVLSL 15 NoResultFounkd. Pos 1234567890 score 239 ALVLSLLFIL 15 NoResuttFound. 278 EEYRVLRDKG 15 TableXLIl-V6-HLA-82705-10mers- 284 RDKGASISQL 15 24P4C12 TableXLIV-Vi-HLA-B4402- 353 STMFYPLVTF 15 Pos 1234567890 score l0mers-24PC12 355 MFYPLVTFVL 15 NoResultsFound. Each peptide Isa portion of SEQ I) 356 FYPLVTFVLL 15 NO: 3; each start position Is 362 FVLLLUCIAY 15 TableXLI-V7-HLA-B270510mers- specified, the length of peptide is 10 383 VLWCIAYW 15 24P4C12 amino acds, and the end position 370 AYWAMTALYL 15 Pos 1234567890 score for each peptide is the start position 417 SSCPGLMCVF 15 NoResultsFound. plus nine. 442 LQIYGVLGLF 15 Pos 1234567890 score 451 FWTLNWVL.AL 15 TableXLII-V8-HLA-92705-10mers- 10 DEAYGKPVKY 23 482 IPTFPLISAF 15 24P4C12 78 GENKDKPYLL 22 561 IMIAIYGKNF 15 Pos 1234567890 score 222 FEDFAQSWYW 21 596 DLLLFFGKLL 15 NoResultsFound. 319 LEAILLLMLI 20 616 FFFSGRJPGL 15 47 GYIWGIVAW 19 637 YWVLPIMTSIL 15 TabteXUl-V9.HLA-B2705-1Omers- 332 QRIRIAIALL 18 840 PIMTSILGAY 15 24P4C12 486 PUSAFIRTI 18 4 KQRDEDDEAY 14. Pos 1234567890 score 502 LAFGALILTL 18 18 KYDPSFRGPI 14 NoResultsFound. 620 GRIPGLGKDF 18 80 NKDKPYLLYF 14 39 VLFLLFILGY 17 83 KPYLLYFNIF 14 TableXLIlIl-VI.HLA-B2709.10mers- 241 VLSLILLL 17 130 NEFSQTVGEV 14 24P4C12 254 AGPLVLVUL 17 131 EFSQTVGEVF 14 Pos 1234567890 score 320 EAILLLMLIF 17 157 WITSLQQEL 14 NoResultsFound. 321 AILU.MLIFL 17 164 OELCPSFLLP 14 476 FHKPODIPTF 17 173 PSAPALGRCF 14 TableXIll-V3-HLA-B2709-10mers- 512 VQIARVILEY 17 175 APALGRCFPW 14 24P4C12 699 NEAPPDNKKR 17 183 PWThVTPPAL 14 Pos 1234567890 score 121 PEDPW VGKN 16 220 KIFEDFAQSW 14 169 SFLL.PSAPAL 16 227 QSWYWILVAL 14 194 TableXLIV.VI-HLA-84402- TableXLIV.VI-HLA-B4402. TabIeXLIV-V1-HLA-B4402 10mers-24P4C12 10mers-24P4C12 10mers-24P4C12 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 peplide Is 10 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 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 nine. plus nine. plus nine. Pos 1234567890 score Pos 1234567890 score Pos 1234567890 score 231 WILVALGVAL 14 445 YGVLGLFWTL 13 368 CIAYWAMTAL 12 233 LVALGVALVL 14 447 VLGLWTLNW 13 369 IAYWAMTALY 12 240 LVLSLLFILL 14 449 GLFWTLNWVL 13 378 YLATSGQPQY 12 243 SLLFILLLRL 14 460 LGQCVLAGAF 13 381 TSGQPQYVLW 12 250 LRLVAGPLVL 14 478 KPQDIPTFPL 13 395 SSPGCEKVPI 12 252 LVAGPLVLVL 14 483 PTFPLISAFI 13 420 PGLMCVFQGY 12 253 VAGPLVLVLI 14 493 RTLRYHTGSL 13 436 QRSVFNLQIY 12 262 ILGVLGVLAY 14 495 LRYHTGSLAF 13 439 VFNLQIYGVL 12 304 SVQETWLAAL 14 498 HTGSLAFGAL 13 443 QIYGVLGLFW 12 331 RQRIRIAIAL 14 500 GSLAFGALIL 13 456 WVLALGQCVL 12 357 YPLVTFVLLL 14 517 V1LEYlDHKL 13 463 CVLAGAFASF 12 431 SKGLIORSVF 14 539 CCFKCCLWCL 13 464 VLAGAFASFY 12 433 GLIQRSVFNL 14 557 RNAYIMIAJY 13 488 ISAFIRTLRY 12 467 GAFASFYWAF 14 582 MRNIVRVWL 13 505 GALILTLVQI 12 542 KCCLWCLEKF 14 590 VLDKVTDLLL 13 509 LTLVQIARVI 12 545 LWCLEKFIKF 14 591 LDKVTDLLLF 13 510 TLVQIARVIL 12 551 FIKFLNRNAY 14 592 DKVTDLLLFF 13 548 LEKFIKFLNR 12 569 HFCVSAKNAF 14 606 WGGVGVLSF 13 556 NRNAYIMIAI 12 589 VVLDKVTDLL 14 659 FGMCVDTLFL 13 571 CVSAKNAFML 12 595 TDLLLFFGKL 14 661 MCVDTLFLCF 13 572 VSAKNAFMLL 12 627 KDFKSPHLNY 14 662 CVDTLFLCFL 13 576 NAFMLLMRNI 12 629 FKSPHLNYYW 14 671 LEDLERNNGS 13 588 WVLDKVTDL 12 665 TLFLCFLEDL 14 672 EDLERNNGSL 13 604 LLWGGVGVL 12 686 YMSKSLLKIL 14 682 DRPYYMSKSL 13 628 DFKSPHLNYY 12 7 DEDDEAYGKP 13 33 TDVICCVLFL 12 630 KSPHLNYYWL 12 31 SCTDVICCVL 13 37 CCVLFLLFIL 12 650 VIASGFFSVF 12 32 CTDVICCVLF 13 44 FILGYIWGI 12 674 LERNNGSLDR 12 35 VICCVLFLLF 13 76 GMGENKDKPY 12 676 RNNGSLDRPY 12 49 IWGIVAWLY 13 123 DPWTVGKNEF 12 677 NNGSLDRPYY 12 56 WLYGDPRQVL 13 132 FSQTVGEVFY 12 685 YYMSKSLLKI 12 57 LYGDPRQVLY 13 150 PGVPWNMTVI 12 14 GKPVKYDPSF 11 87 LYFNIFSCIL 13 163 QQELCPSFLL 12 27 IKNRSCTDVI 11 145 RNFCLPGVPW 13 216 DISVKIFEDF 12 40 LFLLFILGYI 11 153 PWNMTVITSL 13 223 EDFAQSWYWI 12 48 YIWGIVAWL 11 186 NVTPPALPGI 13 236 LGVALVLSLL 12 77 MGENKDKPYL 11 237 GVALVLSLLF 13 266 LGVLAYGIYY 12 116 CVSSCPEDPW 11 248 LLLRLVAGPL 13 274 YYCWEEYRVL 12 137 GEVFYTKNRN 11 257 LVLVLILGVL 13 277 WEEYRVLRDK 12 161 SLQQELCPSF 11 271 YGIYYCWEEY 13 286 KGASISQLGF 12 162 LQQELCPSFL 11 301 AYQSVQETWL 13 290 ISQLGFTTNL 12 208 LIDSLNARDI 11 310 LAAIUVLAVL 13 300 SAYQSVQETW 12 212 LNARDISVKI 11 315 VLAVLEAILL 13 306 QETWLAALIV 12 221 IFEDFAQSWY 11 327 LIFLRQRIRI 13 313 LIVLAVLEAI 12 238 VALVLSLLFI 11 342 KEASKAVGQM 13 318 VLEAILLLML 12 264 GVLGVLAYGI 11 347 AVGQMMSTMF 13 329 FLRQRIRIAI 12 305 VQETWLAALI 11 405 NTSCNPTAHL 13 350 QMMSTMFYPL 12 314 IVLAVLEAIL 11 425 VFQGYSSKGL 13 358 PLVTFVLLLI 12 348 VGQMMSTMFY 11 441 NLQIYGVLGL 13 360 VTFVLLUCI 12 413 HLVNSSCPGL 11 195 TableXLIV.V1I-HLA-B4402- 18 LGYVLWASNI 9 10mers-24P4C12 TableXUV.VG-HLA4402. 16 AILGYVIWAS 8 Each peptide Is a portion of SEQ ID l0mers-24PC12 7 ALYPIPTOPA 7 NO: 3; each start position is Each peptide is a portion of SEQ ID specified, the length of peptide is 10 NCY. 13; each start position is amino acids, and the end position spcified, the length of peptide is 10 TabaXLV.VI.HLA-B5101-10merS for each peptide is the start position amino adds, and the end position 24P4C12 plus nine. for each peptide is the start position Pos 1234567890 score Pos 1234567890 score plus nine. NoResultsFound. 479 PQODIPTFPLI 11 Pos 1234567890 score 499 TGSLAFGALI 11 7 GLIPRSVFNL 17 TableXLVVHLA85101-l0mers 519 LEYIDHKLRG I1 5 SKGUPRSVF 14 24C12 528 GVQNPVARCI I1 10 PRSVFNLIY 12 Pos 1234567890 sore 532 PVARCIMCCF 11 9 IPRSVFNLQI 10 NoResultsFound. 536 CIMCCFKCCL 11 537 IMCCFKCCLW 11 TableXLIV.VT-HLA.B4402. TableXLV5LAB5101-l1mers 543 CCLWCLEKFI I I1mers-24P4C12 24P412 552 IKFLNRNAYI 11 Each peptie is a portion of SEQ ID Pos 1234567890 score 607 VGGVGVLSFF II NO: 15; each start position is NoResultsFound. 608 GGVGVLSFFF 11 specified, the length of peptide Is 10 609 GVGVLSFFFF 11 amino acids, and the end position TableXLV.V6-HLA-B5101-10meTs 625 LGKDFKSPHL 11 for each peptde is the start position 24P4012 632 PHLNYYWLPI 11 plus nine. Pos 1234567890 score 642 MITSILGAYVI 11 Pos 1234567890 score NoResultsFound. 646 LGAYVIASGF 11 9 AVGOMMSTMF 13 658 VFGMCVDTLF 11 4 WILVAVG(M 6 Tabl.XLV.7-HLA.B510't-l1mers 683 RPYYMSKSLL 11 24P4Ci2 TabIeXLIV.V8-KLA.4402- Pos 1234567890 score TableXLIV-V3-HLA-B4402-10mers- imers-24P4C12 NoResultound. 24P4C12 Each peptide is a portion of SEQ Each peptide Is a portion of SEQ ID ID NO: 17; each start position Is TabIeXLV-VB.HLA.B51014lfllers NO: 7; each start position is specified, the length of peptide is 24PC12 specified, the length of peptide is 10 10 amino acids, and the end Pos 1234567890 score amino acids, and the end position position for each people Is the NoResultsFound. for each peptide is the start position start position plus nine. plus nine. Pos 1234567890 score TableXLV-V LA-B5101.l0mers Pos 1234567890 score 11 NPITPTGHVF 17 24P4C12 6 PWTNITPPAL 14 4 YWLPIMRNPI 14 Pos 1234567890 score 9 NITPPALPGI 13 19 VFQTSILGAY 14 NoResultsFound. 1 LGRCFPWTNI 8 16 TGHVFQTSL 11 3 RCFPWTNITP 7 21 QISILGAYVI 11 8 TNITPPALPG 6 15 PTGHVFQTSI a TableXUV-V5-HLA.6M02-10mers TabeXLIV-V95HLA-444 m2 24P4C12 l1mers-24PC12 Each peptide is a portion of SEQID Eachpeptideisapotion ofSEQ NO: 11; each start position is IDNC.19;eachstartpositionIs specified, the length of peptide is 10 specified, the length of peptide is amino acids, and the end position for 10 amino ads, and the end each peptide is the start position position for each peptide Is the plus nine. start position plus nine. Pos 1234567890 score Pos 1234567890 score 3 LEAILLLVL 21 9 YPLPTQPATL 16 4 EAILLLVLIF 18 14 QPATLGYVIW 13 5 AILLLVLIFL 17 11 LPTQPATLGY 12 2 .VLEAILLLVL 13 13 TQPATLGYVL 12 9 LVUFLRQR 10 2 YWAMTALYPL 1 196 TableXLVt-V1-HLA-DRB1-0101- TableXLVI-VI-HLA-DRBi-0101 15mers-24P4C12 15mers-24P4C12 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 specified, the length of peptide is 15 specified, the length of peptide is 15 amino acids, and the end position for amino adds, and the end position for each peptide is the start position plus each peptide is the start position plus fourteen. fourteen. Pos 123456789012345 Pos 123456789012345 so . e e 227 QSWYWILVALGVALV 39 231 WILVALGVALVLSLL 25 206 SGLIDSLNARDISVK 33 239 ALVLSLLFILLLRLV 25 247 ILLLRLVAGPLVLVL 33 293 LGFTNLSAYQSVQE 25 313 LIVLAVLEA1LLLML 33 299 LSAYQSVQETWLAAL 25 601 FGKLLWGGVGVLSF 33 304 SVQETWLAAUVLAV 25 246 FILLLRLVAGPLVLV 32 319 LEAILLLMIFLRQR 25 262 ILGVLGVLAYGIYYC 32 326 MUFLRQRIRIAIAL 25 353 STMFYPLVTFVLLLI 32 337 AIALLKEASKAVGQM 25 368 CIAYWAMTALYLATS 32 354 TMFYPLVTFVLLUC 25 652 ASGFFSVFGMCVDTL 32 371 YWAMTALYLATSGQP 25 39 VLFU.FILGYIWGI 31 399 CEKVPINTSCNPTAH 25 181 CFPWTNVTPPALPGI 31 451 FWTLNWVLALGQCVL 25 277 WEEYRVLRDKGASIS 31 454 LNWVLALGQCVLAGA 25 559 AYIMIAIYGKNFCVS 31 471 SFYWAFHKPQDIPTF 25 639 LPIMTSILGAYVIAS 31 482 IPTE1PUSAFIRTLR 25 85 YLLYFNIFSCILSSN 30 526 LRGVQNPVARCIMCC 25 89 FNIFSCILSSNIISV 30 683 RNIVRWVLDKVTDL 25 257 LVLVLILGVLGVLAY 30 603 KLLWGGVGVLSFFF 25 259 LVLILGVLGVLAYGI 30 51 VGIVAWLYGDPRQVL 24 635 NYYWLPIMTSILGAY 30 97 SSNIISVAENGLQCP 24 646 LGAYVIASGFFSVFG 30 229 WYWILVALGVALVLS 24 235 ALGVALVLSLLFILL 29 238 VALVLSLLFILLLRL 24 345 SKAVGQMMSTMFYPL 29 255 GPLVLVULGVLGVL 24 40 LFLLFILGYIWGIV 28 256 PLVLVLILGVLGVLA 24 242 LSLLFILLLRLVAGP 28 279 EYRVLRDKGASISOL 24 359 LVTFVLLLICIAYWA 28 307 ETWLAALIVLAVLEA 24 453 TLNWVLALGQCVLAG 28 310 LAALIVLAVLEAILL 24 612 VLSFFFFSGRIPGLG 28 383 GQPQYVLWASNISSP 24 640 PIMTSILGAYVIASG 28 420 PGLMCVFQGYSSKGL 24 167 CPSFLLPSAPALGRC 27 459 ALGQCVLAGAFASFY 24 243 SLLFILLLRLVAGPL 27 506 AULTLVQIARVILE 24 280 YRVLRDKGASISQLG 27 523 DHKLRGVQNPVARCI 24 362 FVLLICIAYWAMTA 27 569 NFCVSAKNAFMLLMR 24 423 MCVFQGYSSKGUQR 27 579 MLLMRNIVRVWLDK 24 501 SLAFGALILTLVOIA 27 588 WVLDKVTDLLLFFG 24 575 KNAFMLLMRNIVRW 27 607 VGGVGVLSFFFFSGR 24 129 KNEFSQTVGEVFYTK 26 644 SILGAYVIASGFFSV 24 230 YWILVALGVALVLSL 26 660 GMCVDTLFLCFLEDL 24 254 AGPLVLVLILGVLGV 26 47 GYIWGIVAWLYGDP 23 384 QPQYVLWASNISSPG 26 59 GDPRQVLYPRNSTGA 23 436 ORSVFNLQYGVLGL 26 165 ELCPSFLLPSAPALG 23 437 RSVFNLQIYGVLGLF 26 166 LCPSFLLPSAPALGR 23 448 LGLFWTLNWVLALGQ 26 241 VLSLLFILLLRLVAG 23 492 IRTLRYHTGSLAFGA 26 374 MTALYLATSGQPQYV 23 551 FIKFLNRNAYIMIAI 26 412 AHLVNSSCPGLMCVF 23 594 VTDilLFFGKLLWG 26 507 ULTLVQtARVILEY 23 633 HLNYYWLPIMTSILG 26 508 ILTLVQIARVILEYI 23 688 SKSLLKILGKKNEAP 26 566 YGKNFCVSAKNAFML 23 44 FILGYIWGIVAWLY 25 604 LLWGGVGVLSFFFF 23 53 IVAWLYGDPRQVLYP 25 636 YYWLPIMTSILGAYV 23 62 RQVLYPRNSTGAYCG 25 33 TDVICCVLFLLFILG 22 90 NIFSCILSSNIISVA 25 43 LFILGYIWGIVAWL 22 228 SWYWILVALGVALVL 25 86 LLYFNIFSCILSSNI 22 197 TableXLVI-VHLA-DRBI-0101- TableXLVI-Vi-HLA-DRB1-0101. 15mers-24P4C12 15mers-24P4C12 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 specified, the length of peptide is 15 specified, the length of peptide is 15 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 fourteen. fourteen. Pos 123456789012345 scor Pos 123456789012345 e e 160 TSLOQELCPSFLLPS 22 411 TAHLVNSSCPGLMCV 19 198 DTTIQQGISGLIDSL 22 442 LQlYGVLGLFWTLNW 19 312 ALIVLAVLEALLLM 22 450 LGQCVLAGAFASFYW 19 316 LAVLEAILLLMLIFL 22 495 LRYHTGSLAFGALIL 19 349 GQMMSTMFYPLVTEV 22 503 AFGALILTLVQIARV 19 363 VLLLICIAYWAMTAL 22 557 RNAYIMIAIYGKNFC 19 419 CPGLMCVFQGYSSKG 22 586 VRWVLDKVTDLLLF 19 439 VFNLQIYGVLGLFWT 22 683 RPYYMSKSLLKILGK 19 441 NLQIYGVLGLFWTLN 22 684 PYYMSKSLLKILGKK 19 458 LALGOCVLAGAFASF 22 481 DIPTFPLISAFIRTL 22 TableXLVI-V3-HLA-DRB1-0101 511 LVQJARVILEYIDHK 22 15mers-24P4C12 587 RWVLDKVTDLLLFF 22 Each peptide is a portion of SEQ ID NO: 598 LLFFGKLLWGGVGV 22 7; each start position is specified, the 655 FFSVFGMCVDTLFLC 22 length of peptide is 15 amino acids, and 689 KSLLKILGKKNEAPP 22 the end position for each peptide is the 138 EVFYTKNRNFCLPGV 21 start position plus fourteen. 151 GVPWNMTVITSLQQE 21 Pos 123456789012345 score 153 PWNMTVITSLQQELC 21 9 CFPWTNITPPALPGI 31 203 QGISGLIDSLNARDI 21 7 GRCFPWTNITPPALP 19 300 SAYQSVOETWLAALI 21 12 WTNITPPALPGITND 19 329 FLRORIRAIALLKE 21 10 FPWTNITPPALPGIT 18 331 RQRIRIAIALLKEAS 21 14 NITPPALPGITNDTT 16 409 NPTAHLVNSSCPGLM 21 518 ILEYIDHKLRGVQNP 21 TableXLVI-V5-HLA-DRBI-0101 548 LEKFIKFLNRNAYIM 21 15mers-24P4C12 606 WGGVGVLSFFFFSG 21 Each peplide is a portion of SEQ ID NO: 10 DEAYGKPVKYDPSFR 20 11; each start position is specified, the 20 DPSFRGPIKNRSCTD 20 length of peptide is 15 amino acids, and 272 GIYYCWEEYRVLRDK 20 the end position for each peptide is the 333 RIRIAIALLKEASKA 20 start position plus fourteen. 449 GLFWTLNWVLALGQC 20 Pos 123456789012345 score 476 FHKPQDIPTFPUSA 20 2 UVLAVLEAILLLVL 33 543 CCLWCLEKFIKFLNR 20 8 LEAILLLVUFLRQR 25 563 IAIYGKNFCVSAKNA 20 15 VLIFLRQRIRIAIAL 25 599 LFFGKLLWGGVGVL 20 1 ALVLAVLEAILLLV 22 614 SFFFFSGRIPGLGKD 20 5 LAVLEAILLLVLFL 22 634 LNYYWLPIMTSILGA 20 6 AVLEAILLLVLIFLR 19 645 ILGAWIASGFFSVF 20 12 LLLVUFLRQRIRIA 19 656 FSVFGMCVDTLFLCF 20 13 LLVLIFLRQRIRIA 18 657 SVFGMCVDTLFLCFL 20 7 VLEAILVLIFLRO 17 37 CCVLFLFILGYW 19 11 ILLLVUFLRQRIRI 17 38 CVLFLLFILGYIWG 19 14 LVLIFLRQRIRIAA 17 82 DKPYLLYFNIFSCIL 19 4 VLAVLEAILLLVLIF 16 122 EDPWTVGKNEFSQTV 19 10 AILLLVUFLRQRIR 16 179 GRCFPWTNVTPPALP 19 184 WTNVTPPALPGITND 19 TableXLVI-V6-HLA-DR81-O101 245 LFILU.RLVAGPLVL 19 15mers-24P4C12 271 YGIYYCWEEYRVLRD 19 317 AVLEAILLLMUFLR 19 323 LLLMLIFLRQRIRIA 19 336 IAIALLKEASKAVGQ 19 369 IAYWAMTALYLATSG 19 198 Each peptide is a portion of SEQ ID Each peptide Is a portion of SEQ ID NO: NO: 13; each start position is 19; each start position is specified, the specified, the length of peptide is 15 length of peptide is 15 amino acids, and amino acids, and the end position for the end position for each peptide is the each peptide is the start position plus start position plus fourteen. fourteen. Pos 123456789012345 score Pos 123456789012345 score 4 CIAYWAMTALYPLPT 32 2 MCVFQGYSSKGLIPR 27 10 MTALYPLPTOPATLG 30 15 PRSVFNLQIYGVLGL 26 22 TLGYVLWASNISSPG 26 7 GYSSKGLIPRSVFNL 24 21 ATLGYVLWASNISSP 24 4 VFOGYSSKGLIPRSV 16 7 YWAMTALYPLPTQPA 23 10 SKGLIPRSVFNLOIY 16 13 LYPLPTQPATLGYVL 23 12 GLIPRSVFNLQIYGV 16 5 IAYWAMTALYPLPTQ 19 1 LMCVFQGYSSKGLIP 15 2 LICIAYWAMTALYPL 17 8 YSSKGLIPRSVFNLQ 15 1 LLICIAYWAMTALYP 16 16 LPTOPATLGYVLWAS 16 TabeXLVI-V7-HLA-DRB1-0101- 23 LGYVLWASNISSPGC 16 15mers-24P4C12 24 GYVLWASNISSPGCE 16 Each peptide is a portion of SEQ ID 9 AMTALYPLPTQPATL 15 NO- 15; each start position is specified, the length of peptide is 15 amino adds, TableXLVI-Vi-HILA-DRB1-0301 and the end position for each peptide Is 15mers-24P4C12 the start position plus fourteen. Each peptide is a portion of SEQ ID NO: Pos 123456789012345 score 3; each start position Is specified, the 6 QSWYWILVAVGQMMS 31 length of peptide is 15 amino acids, and 12 LVAVGQMMSTMFYPL 29 the end position for each peptide is the 7 SWYWILVAVGQMMST 25 start position plus fourteen. 8 WYWILVAVGQMMSTM 24 Pos 123456789012345 score 9 YWILVAVGQMMSTMF 24 54 VAWLYGDPRQVLYPR 36 1 FEDFAQSWYWILVAV 18 586 VRWVLDKVTDLLLF 31 5 AQSWYWILVAVGQMM 16 667 FLCFLEDLERNNGSL 29 11 ILVAVGQMMSTMFYP 15 312 ALIVLAVLEAILLLM 28 97 SSNIISVAENGLQCP 27 TabIeXLVI-V8-HLA-DRB1-0101- 155 NMTVITSLQQELCPS 27 15mers-24P4C12 454 LNWVLALGQCVLAGA 27 Each peptide is a portion of SEQ ID NO: 549 EKFIKFLNRNAYIMI 27 17; each start position is specified, the 136 VGEVFYTKNRNFCLP 26 length of peptide is 15 amino acids, and 508 ILTLVQIARVILEYI 26 the end position for each peptide Is the 622 IPGLGKDFKSPHLNY 26 start position plus fourteen. 376 ALYLATSGQPQYVLW 25 Pos 123456789012345 score 447 VGLFWTLNWVLALG 25 24 VFQTSILGAYVIASG 28 279 EYRVLRDKGASISQL 24 7 NYYWLPIMRNPITPT 24 534 ARCIMCCFKCCLWCL 24 23 HVFQTSILGAYVIAS 23 567 GKNFCVSAKNAFMLL 24 6 LNYYWLPIMRNPITP 20 229 WYWILVALGVALVLS 23 5 HLNYYWLPIMRNPIT 18 238 VALVLSLLFILRL 23 21 TGHVFOTSILGAYVI 18 14 GKPVKYDPSFRGPIK 22 3 SPHLNYYWLPIMRNP 17 218 SVKIFEDFAQSWYWI 22 8 YYWLPIMRNPITPTG 17 219 VKIFEDFAQSWYWIL 22 13 IMRNPITPTGHVFQT 17 235 ALGVALVLSLLFILL 22 11 LPIMRNPITPTGHVF 16 241 VLSLLFILLLRLVAG 22 12 PIMRNPITPTGHVFO 16 360 VTFVLLLICIAYWAM 22 14 MRNPITPTGHVFQTS 16 515 ARVILEYIDHKLRGV 22 26 QTSILGAYVIASGFF 16 594 VTDLLLFFGKLLWG 22 9 YWLPIMRNPITPTGH 15 33 TDVICCVLFLLFILG 21 18 ITPTGHVFQTSILGA 15 167 CPSFLLPSAPALGRC 21 19 TPTGHVFQTSILGAY 14 192 LPGITNDTTIQQGIS 21 20 PTGHVFQTSILGAYV 14 237 GVALVLSLLFILLLR 21 239 ALVLSLLFILLLRLV 21 TableXLVI-V9-HLA-DRBI-0101- 260 VULGVLGVLAYGIY 21 15mers-24P4C12 302 YQSVQETWLAALIVL 21 319 LEAILLLMUFLRQR 21 431 SKGLIQRSVFNLQIY 21 199 TableXLVIl-Vi -HLA-DRB1-0301- TabIeXLVII-V1 -HLA-DRB1-0301 15mers-24P4C12 15mers-24P4C12 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 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 start position plus fourteen. start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score 461 GQCVLAGAFASFYWA 21 462 QCVLAGAFASFYWAF 18 587 RWVLDKVTDLLLFF 21 530 QNPVARCIMCCFKCC 18 590 VLDKVTDLLLFFGKL 21 560 YIMIAYGKNFCVSA 18 595 TDLLLFFGKLLWGG 21 569 NFCVSAKNAFMLLMR 18 658 VFGMCVDTLFLCFLE 21 579 MLLMRNIVRVWLDK 18 32 CTDVICCVLFLLFIL 20 585 IVRVVVLDKVTDLLL 18 37 CCVLFLLFILGYlW 20 655 FFSVFGMCVDTLFLC 18 46 LGYIWGIVAWLYGD 20 656 FSVFGMCVDTLFLCF 18 47 GYIWGIVAWLYGDP 20 660 GMCVDTLFLCFLEDL 18 74 YCGMGENKDKPYLLY 20 664 DTLFLCFLEDLERNN 18 76 GMGENKDKPYLLYFN 20 284 RDKGASISQLGFTTN 17 231 WILVALGVALVLSLL 20 290 ISQLGFTTNLSAYOS 17 233 LVALGVALVLSLLFI 20 324 LLMLIFLRQRIRIAI 17 246 FILLLRLVAGPLVLV 20 325 LMLIFLRQRIRIAIA 17 250 LRLVAGPLVLVULG 20 353 STMFYPLVTFVLLLI 17 255 GPLVLVLILGVLGVL 20 423 MCVFOGYSSKGLIQR 17 258 VLVLILGVLGVLAYG 20 437 RSVFNLQIYGVLGLF 17 313 LIVLAVLEAILLLML 20 485 FPLISAFIRTLRYHT 17 316 LAVLEAILLLMLIFL 20 517 VILEYIDHKLRGVQN 17 323 LLLMLIFLRQRIRIA 20 519 LEYIDHKLRGVQNPV 17 338 IALLKEASKAVGQMM 20 523 DHKLRGVQNPVARCI 17 411 TAHLVNSSCPGLMCV 20 542 KCCLWCLEKFIKFLN 17 439 VFNLQIYGVLGLFWT 20 545 LWCLEKFIKFLNRNA 17 484 TFPLISAFIRTLRYH 20 548 LEKFIKFLNRNAYIM 17 559 AYIMIAIYGKNFCVS 20 614 SFFFFSGRIPGLGKD 17 588 WVLDKVTDLLLFFG 20 619 SGRIPGLGKDFKSPH 17 602 GKLLWGGVGVLSFF 20 670 FLEDLERNNGSLDRP 17 604 LLWGGVGVLSFFFF 20 692 LKILGKKNEAPPDNK 17 691 LLKILGKKNEAPPDN 20 156 MTVITSLQQELCPSF 19 TableXLVII-V3-HLA-DRB1-0301-15mers 159 ITSLQQELCPSFLLP 19 24P4C12 205 ISGUDSLNARDISV 19 Each peptide is a portion of SEQ ID NO: 335 RIAIALLKEASKAVG 19 7; each start position is specified, the 348 VGQMMSTMFYPLVTF 19 length of peptide is 15 amino acids, and 366 LICIAYWAMTALYLA 19 the end position for each peptide is the 385 PQYVLWASNISSPGC 19 start position plus fourteen. 505 GALLTLVQIARVIL 19 Pos 123456789012345 score 576 NAFMLLMRNIVRWV 19 12 WTNITPPALPGITND 12 607 VGGVGVLSFFFFSGR 19 3 APALGRCFPWTNITP 10 626 GKDFKSPHLNYYWLP 19 9 CFPWTNITPPALPGI 10 638 WLPIMTSILGAYVIA 19 7 GRCFPWTNITPPALP 8 648 AYVIASGFFSVFGMC 19 6 LGRCFPWTNITPPAL 7 663 VDTLFLCFLEDLERN 19 668 LCFLEDLERNNGSLD 19 684 PYYMSKSLLKILGKK 19 TableXLVI-V5-HLA-DRBI-0301 689 KSLLKILGKKNEAPP 19 15mers-24P4C12 3 GKQRDEDDEAYGKPV 18 Each peptide Is a portion of SEQ ID NO: 61 PRQVLYPRNSTGAYC 18 11; each start position is specified, the 98 SNIISVAENGLQCPT 18 length of peptide is 15 amino acids, and 114 QVCVSSCPEDPWTVG 18 the end position for each peptide Is the 214 ARDISVKIFEDFAQS 18 start position plus fourteen. 243 SLLFILLLRLVAGPL 18 Pos 123456789012345 score 263 LGVLGVLAYGIYYCW 18 1 ALVLAVLEAILLLV 28 327 UFLRQRIRIAALL 18 8 LEAJLLLVLIFLRQR 21 345 SKAVGQMMSTMFYPL 18 2 UVLAVLEAILLLVL 20 200 TableXLVII-VS-HLA-DRBIO3O1- 14 MRNPITPTGHVFQTS 9 15mers-24P4C12 19 rPTGHvFQTSILGAY 8 Each peptide is a portion of SEQ ID NO: 11; each start position is specified, the TableXLVI.V9HLADR81-0301-15mors length of peptide is 15 amino acids, and 24P4C12 the end position for each peptide is the EachpopideisaportionofSEQIDNO: start position plus fourteen. 19; each start position is specified, the Pos 123456789012345 score length of peptde is 15 amino adds, and the 5 LAVLEAILLLVLIFL 20 end position for each peptide is the star 12 LLLVLIFLRQRIRIA 20 position plus fourteen. 13 LLVUFLRQRIRIAI 17 Pos 123456789012345 score 14 LVLIFLRQRIRIAIA 17 2 LICIAYWAMTALYPL 19 4 VLAVLEAILLLVLIF 15 23 LGYVLWASNISSPGC 19 9 EAILLLVLIFLRQRI 15 10 MTALYPLPTQPATLG 13 10 AILLLVLIFLRQRIR 13 7 YWAMTALYPLPTQPA 12 112 ALYPLPTQPAT1.GYV 12 TabteXLVII-V6-HLA-DRB1-0301- 13 LYPLPTQPATLGYVL 12 15mers-24P4C12 20 PATLGYVLWASNISS 12 Each peptide Is a portion of SEQ ID NO: 3 ICIAYWAMTALYPLP 10 13; each start position is specified, the 14 YPLPTQPATLGYVIW 10 length of peptide Is 15 amino acids, and 24 GYVIWASNISSPGCE 10 the end position for each peptide Is the 5 IAYWAMTALYPLPTQ 9 start position plus fourteen. 16 LPTOPATLGYVLWAS 9 Pos 123456789012345 score 10 SKGLIPRSVFNLQIY 22 TableXLVII-DRI -0401-15mers. 2 'MCVFQGYSSKGLIPR 17 24P4C12 8 YSSKGLIPRSVFNLQ 16 Each peptide isa portion of SEQ ID NO: 11 KGLIPRSVFNLQIYG 12 3; each start position is specified, the 1 LMCVFQGYSSKGLIP 11 length of peptide is 15 amino acids, and 15 PRSVFNLQIYGVLGL 10 the end position for each peptide is the start position plus fourteen. TableXLVI-V7-HLA-DRBI-0301-15mers- Pos 123456789012345 score 24P4C12 85 YLLYFNFSCILSSN 28 Each peptide is a portion of SEQ ID NO: 89 FNIFSCILSSNIISV 28 15; each start position is specified, the 243 SLLFILLLRLVAGPL 28 length of peptide is 15 amino adds, and 353 STMFYPLVTFVLLLI 28 the end position for each peptide is the 469 FASFYWAFHKPOIP 28 start position plus fourteen. 548 LEKFIKFLNRNAY1M 28 Pos 123456789012345 score 575 KNAFMLLMRNIVRW 28 9 YWILVAVGQMMSTMF- 18 635 NYYWLPIMTSILGAY 28 12 LVAVGQMMSTMFYPL 18 54 VAWLYGDPRQVLYPR 26 1 FEDFAQSWYWILVAV 16 98 SNIISVAENGLOCPT 26 8 WYWILVAVGQMMSTM 13 153 PWNMTVITSLQQELC 26 10 WILVAVGQMMSTMFY 10 189 PPALPGrrNDTTIQQ 26 13 VAVGQMMSTMFYPLV 10 192 LPGITNDT1QQGIS 26 323 LLLMLIFLRQRIRIA 26 TableXLVI-V8-HLA-DRBI-0301-15mers. 337 AJAW(EASKAVGQM 26 24P4C12 385 PQYVLWASNISSPGC 26 Each peptide is a portion of SEQ ID NO: 419 CPGLMCVFQGYSSKG 26 17; each start position is specified, the 454 LNWVLALGQCVLAGA 26 length of peptide is 15 amino acids, and 508 ILTLVQIARVILEYI 26 the end position for each peptide Is the 523 DHKLRGVQNPVARCI 26 start position plus fourteen. 579 MLLMRNIVRVWLDK 26 Pos 123456789012345 score 16 PVKYDPSFRGPIKNR 22 22 GHVFQTSILGAYVIA 17 38 CVLFLLFILGYIWG 22 8 YYWLPIMRNPITPTG 16 82 DIPYIJYFNIFSCIL 22 15 RNPITPTGHVFQTSI 14 86 LLYFNIFSCILSSNI 22 26 QTSILGAYVIASGFF 13 122 EDPWrVGKNEFSQTV 22 21 TGHVFQTSILGAYVI 12 138 EVFYTKNRNFCLPGV 22 10 WLPIMRNPITPTGHV 11 181 CFPWTNVTPPALPGI 22 11 LPIMRNPITPTGHVF 11 219 VVIFEDFAQSWYIL 22 3 SPHLNYYWLPIMRNP 10 227 QSWYWILVALGVALV 22 7 NYYWLPIMRNPI1PT 10 228 SWYWILVALGVALVL 22 201 TableXLVIll-V1-DR1 -0401 -15mers- TableXLVII-VI-DRI-0401-1 5mers 24P4C12 24P4C12 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 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 start position plus fourteen. start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 sore 272 GIYYCWEEYRVLRDK 22 312 ALIVLAVLEAILLLM 20 277 WEEYRVLRDKGASIS 22 313 UVLAVLEAILLLML 20 292 OLGFTTNLSAYOSVQ 22 315 VLAVLEAILLLMLIF 20 299 LSAYOSVQETWLAAL 22 316 LAVLEAILLLMLIFL 20 306 QETWLAALIVLAVLE 22 319 LEAILLLMLIFLRQR 20 354 TMFYPLVrFVLLLIC 22 321 AJLLLMUFLRQRIR 20 359 LVTFVLLLICIAYWA 22 324 LLMLIFLRQRIRIAI 20 384 QPQYVLWASNISSPG 22 331 RQRIRIAIALLKEAS 20 423 MCVFQGYSSKGLIQR 22 333 RIRIAIALLKEASKA 20 442 LQIYGVLGLFWTLNW 22 335 RIAJALLKEASKAVG 20 448 LGLFWTLNWVLALGQ 22 356 FYPLVTFVLLUCIA 20 453 TLNWVLALGQCVLAG 22 363 VLLUCIAYWAMTAL 20 488 ISAFIRTLRYHTGSL 22 364 LLLCIAYWAMTALY 20 501 SLAFGALILTLVQIA 22 371 YWAMTALYLATSGOP 20 557 RNAYIMIAIYGKNFC 22 374 MTALYLATSGQPQYV 20 633 HLNYYWLPIMTSILG 22 401 KVPINTSCNPTAHLV 20 646 LGAYVIASGFFSVFG 22 420 PGLMCVFQGYSSKGL 20 652 ASGFFSVFGMCVDTL 22 436 QRSVFNLQIYGVLGL 20 667 FLCFLEDLERNNGSL 22 444 IYGVLGLFWTLNWVL 20 682 DRPYYMSKSLLKILG 22 445 YGVLGLFWTLNWVLA 20 14 GKPVKYDPSFRGPK 20 447 VLGLFWTLNWVLALG 20 39 VLFLLFILGYIWGI 20 451 FWTLNWVLALGQCVL 20 40 LFLLFILGYIWGIV 20 479 PQDIPTFPLISAFIR 20 43 LFILGYIWGIVAWL 20 484 TFPUSAFIRTLRYH 20 97 SSNIISVAENGLOCP 20 485 FPLISAFIRTLRYHT 20 133 SQTVGEVFYTKNRNF 20 505 GALILTLVQARVIL 20 146 NFCLPGVPWNMTVIT 20 506 AULTLVQIARVILE 20 149 LPGVPWNMTVITSLQ 20 511 LVQIARVILEYIDHK 20 155 NMTVITSLOQELCPS 20 514 IARVILEYIDHKLRG 20 156 MTVITSLQQELCPSF 20 516 RVILEYIDHKLRGVQ 20 198 DTTIQQGISGLIDSL 20 542 KCCLWCLEKFIKFLN 20 202 QQGISGUDSLNARD 20 545 LWCLEKFIKFLNRNA 20 206 SGLIDSLNARDISVK 20 549 EKFIKFLNRNAYIMI 20 216 DISVKIFEDFAQSWY 20 558 NAYiMIAlYGKNFCV 20 229 WYWILVALGVALVLS 20 582 MRNIVRVVVLDKVTD 20 230 YWILVALGVALVLSL 20 583 RNIVRWVLDKVTDL 20 233 LVALGVALVLSLLFI 20 586 VRVWLDKVrDLLLF 20 235 ALGVALVLSLLFILL .20 588 WVLDKVTDLLLFFG 20 238 VALVLSIlFILLLRL 20 594 VTDLLLFFGKLLWG 20 239 ALVLSLLFILLLRLV 20 595 TDLLLFFGKLLVVGG 20 241 VLSLLFillLRLVAG 20 601 FGKLLWGGVGVLSF 20 242 LSLLFILLLRLVAGP 20 619 SGRIPGLGKDFKSPH 20 246 FILLLRLVAGPLVLV 20 639 . LPIMTSILGAYVIAS 20 247 ILLLRLVAGPLVLVL 20 642 MTSILGAYVIASGFF 20 254 AGPLVLVLLGVLGV 20 660 GMCVDTLFLCFLEDL 20 255 GPLVLVULGVLGVL 20 668 LCFLEDLERNNGSLD 20 257 LVLVLILGVLGVLAY 20 688 SKSLLKILGKKNEAP 20 259 LVLILGVLGVLAYGI 20 90 NIFSCILSSNIISVA 18 262 ILGVLGVLAYGIYYC 20 125 WTVGKNEFSQTVGEV 18 279 EYRVLRDKGASISQL 20 152 VPWNMTVITSLQQEL 18 287 GASISCLGFTTNLSA 20 166 LCPSFLLPSAPALGR 18 290 ISQLGFTTNLSAYQS 20 195 ITNDTTIQQGISGU 18 307 ETWLAALIVLAVLEA 20 203 QGISGUDSLNARDI 18 310 LAALIVLAVLEAILL 20 210 DSLNARDISVKIFED 18 311 AAUVLAVLEAILLL 20 289 SISQLGFTTNLSAYQ 18 202 TableXLVIII-Vi-DRi -0401-1 Smers. TabteXLVIII-VI-DR1-0401-15mers 24P4C12 24P4C12 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 length of peptide is 15 amino acids, and length of peptide is 15 amino adds, and the end position for each peptide is the the end position for each peptide is the start position plus fourteen. start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score 295 FTTNLSAYQSVQETW 18 36' ICCVLFLLFILGYIV 14 342 KEASKAVGQMMSTMF 18 37 CCVLFLLFILGYIVV 14 373 AMTALYLATSGQPOY 18 42 LLFILGYVGIVAW 14 398 GCEKVPINTSCNPTA 18 46LGYIV VGIVAWLYGD 14 428 GYSSKGLIQRSVFNL 18 47 GYIWGIVAWLYGDP 14 433 GUQRSVFNLQIYGV 18 48 YIWGIVAWLYGDPR 14 476 FHKPQDIPTFPLISA 18 51 VGIVAWLYGDPRQVL 14 481 DIPTFPLISAFIRTL 18 61 PRQVLYPRNSTGAYC 14 502 LAFGALILTLVQIAR 18 83 KPYLLYFNIFSCILS 14 527 RGVQNPVARCIMCCF 18 84 PYLLYFNIFSCILSS 14 568 KNFCVSAKNAFMLLM 18 88 YFNIFSCILSSNIIS 14 611 GVLSFFFFSGRIPGL 18 92 FSCILSSNIISVAEN 14 623 PGLGKDFKSPHLNYY 18 93 SCILSSNIISVAENG 14 657 SVFGMCVDTLFLCFL 18 124 PWTVGKNEFSQTVGE 14 669 CFLEDLERNNGSLOR 18 136 VGEVFYTKNRNFCLP 14 20 DPSFRGPIKNRSCTD 16 159 ITSLOQELCPSFLLP 14 45 ILGYIWGIVAWLYG 16 163 QQELCPSFLLPSAPA 14 53 IVAWLYGDPRQVLYP 16 169 SFLLPSAPALGRCFP 14 55 AWLYGDPRQVLYPRN 16 175 APALGRCFPWTNV'P 14 63 QVLYPRNSTGAYCGM 16 184 WTNVTPPALPGITND 14 144 NRNFCLPGVPWNMTV 16 205 ISGLIDSLNARDISV 14 151 GVPWNMTVITSLQQE 16 218 SVKIFEDFAQSWYW 14 167 CPSFLLPSAPALGRC 16 231 WILVALGVALVLSLL 14 222 FEDFAQSWYWILVAL 16 237 GVALVLSLLFLU.R 14 226 AQSWYWILVALGVAL 16 244 LLFILLLRLVAGPLV 14 271 YGIYYCWEEYRVLRD 16 249 LLRLVAGPLVLVLIL 14 326 MUFLRQRIRIAIAL 16 250 LRLVAGPLVLVULG 14 368 CIAYWAMTALYLATS 16 256 PLVLVLILGVLGVLA 14 369 IAYWAMTALYLATSG 16 258 VLVULGVLGVLAYG 14 375 TALYLATSGQPQYVL 16 260 VULGVLGVLAYGIY 14 387 YVLWASNISSPGCEK 16 263 LGVLGVLAYGYYCW 14 437 RSVFNLQIYGVLGLF 16 296 TTNLSAYOSVQETWL 14 449 GLFWTLNWVLALGQC 16 302 YQSVQETWLAALIVL 14 466 AGAFASFYWAFHKPQ 16 322 ILLLMLIFLRQRIRI 14 470 ASFYWAFHKPQDIPT 16 338 IALLKEASKAVGQMM 14 471 SFYWAFHKPQDIPTF 16 345 SKAVGQMMSTMFYPL 14 473 YWAFHKPQDIPTFPL 16 348 VGOMMSTMFYPLVTF 14 482 IPTFPLISAFIRTLR 16 349 GQMMSTMFYPLVTFV 14 518 ILEYIDHKLRGVQNP 16 352 MSTMFYPLVTFVLLL 14 543 CCLWCLEKFIKFLNR 16 357 YPLVTFVL.CIAY 14 563 IAYGKNFCVSAKNA 16 360 VTFVLLUCIAYWAM 14 598 LLFFGKLLVVGGVGV 16 361 TFVLLLICIAYWAMT 14 612 VLSFFFFSGRIPGLG 16 362 FVLLUCIAYWAMTA 14 613 LSFFFFSGRIPGLGK . 16 366 UCIAYWAMTALYLA 14 614 SFFFFSGRIPGLGKD 16 376 ALYLATSGQPQYVLW 14 634 LNYYWLPIMTSILGA 16 391 ASNISSPGCEKVPIN 14 653 SGFFSVFGMCVDTLF 16 399 CEKVPINTSCNPTAH 14 664 DTLFLCFLEDLERNN 16 411 TAHLVNSSCPGMCV 14 62 RQVLYPRNSTGAYCG 15 412 AHLVNSSCPGLMCVF 14 325 LMUFLRQRIRIAIA 15 422 LMCVFQGYSSKGLIQ 14 327 UFLRQRIRIAIALL 15 432 KGUQRSVFNLQIYG 14 519 LEYIDHKLRGVONPV 15 439 VFNLQIYGVLGLFWT 14 587 RWVLDKVTDLLLFF 15 441 NLQIYGVLGLFWTLN 14 32 CTDVICCVLFLLFIL 14 455 NWVLALGQCVLAGAF 14 33 TDVICCVLFLLFILG 14 457 VLALGQOCVLAGAFAS 14 203 TabIeXLVIII-V1-DR-0401-15mers- Each peptide is a portion of SEQ ID NO: 24P4C12 11; each start position is specified, the Each peptide is a portion of SEQ ID NO: length of peptide Is 15 amino acids, and 3; each start position is specified, the the end position for each peptide is the length of peplde is 15 amino acids, and start position plus fourteen. the end position for each peptide is the Pos 123456789012345 score start position plus fourteen. 12 LLLVLIFLRQRIRIA 26 Pos 123456789012345 score I AlVLAVLEAILLLV 20 462 QCVLAGAFASFYWAF 14 2 LIVLAVLEAILLLVL 20 489 SAFIRTLRYHTGSLA 14 4 VLAVLEAILLLVLIF 20 492 IRTLRYHTGSLAFGA 14- 5 LAVLEAILLLVLIFL 20 499 TGSLAFGALILTLVQ 14 8 LEAILLLVLIFLROR 20 504 FGALILTLVQIARVI 14 10 AJLLLVLIFLRQRIR 20 509 LTLVQIARVILEYID 14 13 LLVIJFLRQRIRIAI 20 515 ARVILEYIDHKLRGV 14 15 VLIFLRQRIRIAIAL 16 526 LRGVQNPVARCIMCC 14 14 LVUFLRQRIRIAIA 15 534 ARCIMCCFKCCLWCL 14 9 EAILLLVLIFLRORI 14 535 RCIMCCFKCCLWCLE 14 11 ILLLVLIFLRQRIRI 14 552 IKFLNRNAYMIAJY 14 3 IVLAVLEAILLLVLI 12 559 AYIMIAlYGKNFCVS 14 6 AVLEAILLLVLIFLR 12 576 NAFMLLMRNIVRVW 14 578 FMLLMRNIVRWVVD 14 TableXLVI-V6-HLA-DRi0401-15mers 585 IVRVVVLDKVTOLLL 14 24P4C12 591 LDKVTDLLLFFGKLL 14 Each peptide is a portion of SEQ ID NO: 596 DLLLFFGKLLWGGV 14 13; ead start position is specified, the 602 GKLLWGGVGVLSFF 14 length of peptide Is 15 amino acids, and 603 KLLWGGVGVLSFFF 14 the end position for each peptide Is the 604 LLWGGVGVLSFFFF 14 start position plus fourteen. 607 VGGVGVLSFFFFSGR 14 Pos 123456789012345 score 609 GVGVLSFFFFSGRIP 14 2 MCVFQGYSSKGLIPR 22 610 VGVLSFFFFSGRIPG 14 15 PRSVFNLQYGVLGL 20 622 IPGLGKDFKSPHLNY 14 12 GLIPRSVFNLQIYGV 18 631 SPHLNYYWLPIMTSI 14 1 - LMCVFQGYSSKGLIP 14 636 YYWLPIMTSILGAYV 14 11 KGLIPRSVFNLQYG 14 647 GAYVIASGFFSVFGM 14 7 GYSSKGLIPRSVFNL 12 655 FFSVFGMCVDTLFLC 14 8 YSSKGLIPRSVFNLQ 12 658 VFGMCVDTLFLCFLE 14 9 SSKGLIPRSVFNLQI 12 663 VDTLFLCFLEDLERN 14 665 TLFLCFLEDLERNNG 14 TableXLVIII-V7-HLA-DRI-0401-15mers 678 NGSLDRPYYMSKSLL 14 24P4C12 684 PYYMSKSLLKILGKK 14 Each peptide is a portion of SEQ ID NO: 689 KSLLKILGKKNEAPP 14 15; each start position is specified, the length of peptide Is 15 amino acids, and TableXLVIll-V3-HLA-DR1-0401- the end position for each peptide Is tho 15mers-24P4C12 start position plus fourteen. Each peptide is a portion of SEQ ID NO- Pos 123456789012345 score 7; each start position Is specified, the 9 YWILVAVGQMMSTMF 26 length of peptide is 15 amino acids, and 6 QSWYWILVAVGQMMS 22 the end position for each peptide Is the 7 SWYWILVAVGQMMST 22 start position plus fourteen. 8 WYWILVAVGQMMSTM 20 Pos 123456789012345 score 1 FEDFAQSWYWLVAV 16 9 CFPWTNITPPALPGI 22 5 AQSWYWILVAVGQMM 16 3 APALGRCFPWTNITP 14 10 WILVAVGOMMSTMFY 14 12 WTNITPPALPGITND 14 12 LVAVGQMMSTMFYPL 14 4 PALGRCFPWTNITPP 12 5 ALGRCFPWTNITPPA 12 TableXLVIII-V8-HLA-DR1-0401-15mers 8 RCFPWTNITPPALPG 12 24P4C12 13 TNITPPALPGITNDT 12 Each peptide is a portion of SEQ ID NO: 3; 14 NITPPALPGITNDTT 12 each start position is specified, the length of 7 GRCFPWTNITPPALP 10 peptide is 17 amino acids, and the end position for each peptide is the start TableXLVll-V5-DR1-0401-15mers- position plus fourteen. 24P4C12 Pos 123456789012345 score 204 TableXLVIII-V8-HLA-DR1-0401-15mers- TabIeXUX-Vi-DRB1-101-1 5mers 24P4C12 24P4C12 Each peptde is a portion of SEQ ID NO: 3; Each peptide is a portion of SEQ ID NO: each start position is specified, the length of 3; each start position Is specified, the peptide is 17 amino acids, and the end length of peptide Is 15 amino adds, and position for each peptide is the start the end position for each peptide is the position plus fourteen. start position plus fourteen. Pos 123456789012345 score Pos 123456789012345 score 7 NYYWLPIMRNPITPT 28 276 CWEEYRVLRDKGASI 21 5 HLNYYWLPIMRNPIT 22 338 IAKEASKAVGQMM 21 8 YYWLPIMRNPITPTG 20 508 ILTLVQIARVILEYI 21 15 RNPITPTGHVFQTSI 20 516 RVILEYIDHKLRGVQ 21 26 QTSILGAYVIASGFF 20 542 KCCLWCLEKFIKFLN 21 18 ITPTGHVFQTSILGA 18 585 IVRVWLDKVTDLLL 21 19 TPTGHVFQTSILGAY 18 685 YYMSKSLLKILGKKN 21 3 SPHLNYYWLPIMRNP 14 172 LPSAPALGRCFPWTN 20 10 WLPIMRNPITPTGHV 14 334 IRIAIALLKEASKAV 20 11 LPIMRNPITPTGHVF 14 371 YWAMTALYLATSGQP 20 21 TGHVFQTSILGAYVI 14 549 EKFIKFLNRNAYIMI 20 591 LDKVTDLLLFFGKLL 20 TableXLVIIl-V9-HLA-DRI-0401- 619 SGRIPGLGKDFKSPH 20 15mers-24P4C12 689 KSLLKILGKKNEAPP 20 Each peptide Is a portion of SEQ ID 36 ICCVLFLLFILGYIV 19 NO: 19; each start position is 122 EDPWTVGKNEFSQTV 19 specified, the length of peptide s 15 256 PLVLVLILGVLGVLA 19 amino acids, and the end position for 259 LVLILGVLGVLAYGI 19 each peptide is the start position plus 310 LAAIJVLAVLEAILL 19 fourteen. 353 STMFYPLVTFVLLLI 19 Pos 123456789012345 score 523 DHKLRGVQNPVARCI 19 10 MTALYPLPTQPATLG 26 567 GKNFCVSAKNAFMLL 19 23 LGYVLWASNISSPGC 26 612 VLSFFFFSGRIPGLG 19 11 TALYPLPTQPATLGY 22 636 YYWLPIMTSILGAYV 19 22 TLGYVLWASNISSPG 22 16 -PVKYOPSFRGPIKNR 18 7 YWAMTALYPLPTOPA 20 48 YIWGIVAWLYGDPR 18 20 PATLGYVLWASNISS 20 85 YLLYFNIFSCILSSN 18 5 IAYWAMTALYPLPTQ 16 137 GEVFYTKNRNFCLPG 18 2 UCIAYWAMTALYPL 14 181 CFPWTNVTPPALPGI 18 3 ICIAYWAMTALYPLP 12 227 QSWYWILVALGVALV 18 15 PLPTQPATLGYVLWA 12 244 LLFILLLRLVAGPLV 18 21 ATLGYVLWASNISSP 12 326 MLIFLRQRIRIAAL 18 419 CPGLMCVFQGYSSKG 18 TableXLIX-VI-DRBI1101-15mers- 469 FASFYWAFHKPQDIP 18 24P4C12 470 ASFYWAFHKPQDIPT 18 Each peptide is a portion of SEQ ID NO: 488 ISAFIRTLRYHTGSL 18 3; each start position is specified, the 489 .SAFIRTLRYHTGSLA 18 length of peptide is 15 amino acids, and 597 LLLFFGKLLWGGVG 18 the end position for each peptide Is the 41 FLLFILGYIWGIVA 17 start position plus fourteen. 45 ILGYIWGIVAWLYG 17 Pos 123456789012345 score .71 TGAYCGMGENKDKPY 17 243 SLLFILU.LRLVAGPL 31 86 LLYFNIFSCILSSNI 17 10 DEAYGKPVKYDPSFR 26 306 QETWLAAUVLAVLE 17 20 DPSFRGPIKNRSCTD 26 325 LMUFLRQRIRIAIA 17 668 LCFLEDLERNNGSLD 26 354 TMFYPLVTFVLLUC 17 575 KNAFMLLMRNIVRW 25 369 IAYWAMTALYLATSG 17 613 LSFFFFSGRIPGLGK 25 384 QPQYVLWASNISSPG 17 226 AQSWYWILVALGVAL 23 442 LQIYGVLGLFWTLNW 17 228 SWYWILVALGVALVL 23 482 IPTFPUSAFIRTLR 17 277 WEEYRVLRDKGASIS 23 501 SLAFGALILTLVQA 17 359 LVTFVLLICIAYWA 23 548 LEKFIKFLNRNAYM 17 448 LGLFWTLNWVLALGO 23 615 FFFFSGRIPGLGKDF 17 579 MLLMRNIVRVVVLDK 23 635 NYYWLPIMTSILGAY 17 598 LLFFGKLLWGGVGV 22 652 ASGFFSVFGMCVDTL 17 633 HLNYYWLPIMTSILG 22 82 DKPYLLYFNIFSCIL 16 205 TableXLX-V1-DRB1-1101-1 5mers- Pos 123456789012345 score 24P4C12 15 VLIFLRQRIRIAIAL 18 Each peptide is a portion of SEQ ID NO: 14 LVLIFLRQRIRIAIA 17 3; each start position is specified, the 12 LLLVUFLRQRIRIA 16 length of peptide is 15 amino acids, and 10 AILLLVLIFLRQRIR 15 the end position for each peptide is the 2 LIVLAVLEAILLLVL 14 start position plus fourteen. 8 LEAILLLVLIFLRQR 14 Pos 123456789012345 score 13 LLVLIFLRQRIRIAI 14 89 FNIFSCILSSNIISV 16 1 ALIVLAVLEAILLLV 13 179 GRCFPWTNVTPPALP 16 5 LAVLEAILLLVLIFL 13 253 VAGPLVLVLILGVLG 16 9 EAILLLVLIFLRQRI 13 299 LSAYQSVQETWLAAL 16 11 ILLLVUFLRQRIRI 13 323 LLLMLIFLRQRIRIA 16 368 CIAYWAMTALYLATS 16 TableXUX-V6-HLA-DRBI-1101 387 YVLWASNISSPGCEK 16 15mers-24P4C12 490 AFIRTLRYHTGSLAF 16 Each peptide is a portion of SEQ ID NO: 494 TLRYHTGSLAFGALI 16 13; each start position is specified, the 506 ALILTLVQIARVILE 16 length of peptde is 15 amino acids, and 517 VILEYIDHKLRGVQN 16 the end position for each peptide is the 557 RNAYIMIAIYGKNFC 16 start position plus fourteen. 563 IAIYGKNFCVSAKNA 16 Pos 123456789012345 score 583 RNIVRVVVLDKVTOL 16 8 YSSKGLIPRSVFNLO 15 646 LGAYVIASGFFSVFG 16 1 LMCVFQGYSSKGLIP 14 43 LFILGYIVVGIVAWL 15 15 PRSVFNLQIYGVLGL 13 44 FILGYIVVGIVAWLY 15 2 MCVFOGYSSKGLIPR 10 47 GYlVGIVAWLYGDP 15 5 FQGYSSKGLIPRSVF 10 54 VAWLYGDPRQVLYPR 15 3 CVFQGYSSKGLIPRS 9 73 AYCGMGENKDKPYLL 15 11 KGLIPRSVFNLQIYG 9 153 PWNMTVITSLQQELC 15 6 QGYSSKGLIPRSVFN 8 156 MTVITSLOQELCPSF 15 4 VFQGYSSKGUPRSV 7 195 ITNDTTIQQGISGLI 15 7 GYSSKGLIPRSVFNL 7 207 GLIDSLNARDISVKI 15 242 LSLLFILLLRLVAGP 15 TableXLIX-V7-HLA-DRB1-1101-15mers 357 YPLVTFVLLICIAY 15 24P4C12 429 YSSKGLIQRSVFNLQ 15 Each peptide is a portion of SEQ ID NO: 485 FPUSAFIRTLRYHT 15 15; each start position Is specified, the 519 LEYIDHKLRGVQNPV 15 length of peptide is15 amino adds, and the 527 RGVQNPVARCIMCCF 15 end position for each peptide is the start 545 LWCLEKFIKFLNRNA 15 position plus fourteen. 595 TDLLLFFGKLWGG 15 Pos 123456789012345 score 600 FFGKLLWGGVGVLS 15 5 AQSWYWILVAVGQMM 23 603 KLLVVGGVGVLSFFF 15 6 QSWYWILVAVGQMMS 18 681 LDRPYYMSKSLLKIL 15 9 YWILVAVGQMMSTMF 18 7 SWYWILVAVGQMMST 16 TableXLIX-V3-HLA-DRBi-1101-15mers- 12 LVAVGQMMSTMFYPL 12 24P4C12 1 FEDFAQSWYWLVAV 11 Each peptide is a portion of SEQ ID NO: 7; each start position is specified, the length of TableXLIXV8-HiLA-DRBI-1101-1Smers peptide Is 15 amino acids, and the end 24P4C12 position for each peptide is the start position Each peptide Is a portion of SEQ ID NO: plus fourteen. 17; each start position is specified, the Pos 123456789012345 score length of peptide is 15 amino acids, and the 9 CFPWTNITPPALPGI 18 end position for each peptide is the start 7 GRCFPWrNITPPALP 16 position plus fourteen. 12 WTNITPPALPGITND 8 Pos 123456789012345 score 7 . NYYWLPIMRNPITPT 24 TableXLIX-V5-HLA-DRBI-110115mers. 5 HLNYYWLPIMRNPIT 18 24P4C12 6 LNYYWLPIMRNPITP 17 Each peptide is a portion of SEQ ID NO: 15 RNPITPTGHVFQTSI 16 11; each start position Is specified, the 8 YYWLPIMRNPITPTG 13 length of peptide is 15 amino acids, and the 21 TGHVFQTSLGAYVI 13 end position for each peptide is the start position plus fourteen. TabIeXLIX-V9-HLA-DRB1-1101-15mers 206 24P4C12 Each peptide is a portion of SEQ ID NO: 19; each start position is specified, the length of peptide is 15 amino acids, and the end positon for each peptide is the start position plus fourteen. Pos 123456789012345 score 4 CIAYWAMTALYPLPT 22 10 MTALYPLPTQPATLG 18 22 TLGYVLWASNISSPG 17 7 YWAMTALYPLPTQPA 14 13 LYPLPTQPATLGYVL 13 20 PATLGYVLWASNISS 12 23 LGYVLWASNISSPGC 12 24 GYVLWASNISSPGCE 12 5 IAYWAMTALYPLPTQ 10 11 TALYPLPTOPATLGY 10 207 Table L: Properties of 24P4C12 Bioinformajic URL Outcome Program ORF ORF finder 6 to 2138 Protein length 710aa Tansmcmbrane region TM Prod http/www.ch.anbnet.org/ I I TM, 39-59, 86-104, 231-250,252-273, 309 330, 360-380, 457-474, 497-515. 559-581, 604 626, 641-663 HMMTop http://www.enzim.hu/hmmtop/ 1 ITM, 35-59 84-104 231 250 257-277 308-330 355 377 456-475 500-519 550 572 597-618 649-671 Sosui httpJ/www.genome.ad.jp/SOSui/ 13TM, 34-65, 86-108, 145 167, 225-247, 307-329, 357-379,414-436,447-469, 501-523, 564-586, 600-622, 644-666 TMHMM http:/www.cbs.dtu.dk/scvioesflMHMM 10IN, 36-58,228-250, 252 274, 308-330, 356-378, 454-476,497-519, 559-58), 597-619 Signal Pqptide Signal P http://www.cbs.dtu.dk/servicesSignalP/ no p1 p1/MW tool http://www.expasy.ch/tools/ 8.9 pi Molecular weight p1/MW tool http://www.expasy.ch/tools/ 79.3 kD Localization PSORT http:/psortnibb.ac.jp/ 80% Plasma Membrane, 40/o Golgi PSORT If http://psortnibb.acjp/ 65% Plasma Membrane, 38% endoplasmic reticulum Motifs Pfan http://www.sanger.ac.uk/Pfam/ DUF580, uknown function Prints httpJ/www.biochem.ucl.ac.uk/ Blocks http-//www.blocks.fhcrc.org/ Anion exchanger family 313-359 Prosite http://www.prosite.org/ CYS-RICH 536 - 547 Table LI. Exon coapositions of 24P4C12 v.1 Exon number Start End Length I 1 45 45 2 46 94 49 3 95 16B 74 4 169 247 79 5 248 347 100 6 348 473 126 7 474 534 61 8 535 622 88 9 623 706 84 10 707 942 236 11 943 1042 100 12 1043 1135 93 13 1136 1238 103 14 1239 1492 254 15 1493 1587 95 16 1588 1691 104 17 1692 1765 24 18 1766 1836 71 19 1837 1931 95 20 1932 2016 85 21 2017 2573 557 208 Table LII. Nucleotid4 sequence of transcript variant 24P4C12 v.7 (SEQ ID NO: 94) gagccatggg gggaaagcag cgggacgagg atgacgaggc ctacgggaag ccagtcaaat 60 acgacccctc ctttcgaggc cccatcaaga acagaagctg cacagatgtc atctgctgcg 120 tcctcttcct gctcttcatt ctaggttaca tcgtggtggg gattgtggcc tggttgtatg 180 gagacccccg gcaagtcctc taccccagga actctactgg ggcctactgt ggcatggggg 240 agaacaaaga taagccgtat ctcctgtact tcaacatctt cagctgcatc ctgtccagca 300 acatcatctc agttgctgag aacggcctac agtgccccac accccaggtg tgtgtgtcct 360 cctgcccgga ggacccatgg actgtgggaa aaaacgagtt ctcacagact gttggggaag 420 tcttctatac aaaaaacagg aacttttgtc tgccaggggt accctggaat atgacqgtga 480 tcacaagcct gcaacaggaa ctctgcccca gtttcctcct cccctctgct ccagctctgg 540 ggcgctgctt tccatggacc aacgttactc caccggcgct cccagggatc accaatgaca 600 ccaccataca gcaggggatc agcggtctta ttgacagcct caatgcccga gacatcagtg 660 ttaagatctt tgaagattit gcccagtcct ggtattggat tcttgtggct gtggacaga 720 tgatgtctac catgttctac ccaciggtca cctttgtcct cctcctcatc tgcattgcct 780 actgggccat gactgctctg tacctqgcta catcggca accccagtat gtgctctggg 640 catccaacat cagctccccc ggctgtgaga aaqtgccaat aaatacatca tgcaacccca 900 cggcccacct tgtgaactcc tcgtgcccag ggctgatgtg cgtcttccag ggctactcat 960 ccaaaggcct aatccaacgt tctgtcttca atctgcaaat ctatggqqtc ctgggqctct 1020 tctggaccct taactgggta ctggccctgg gccaatgcgt cctcgctgga gcctttgcct 1080 ccttctactg ggccttccac aagccccagg acatccctac cttcccctta atctctgcct 1140 tcatccgcac actccgttac cacactgggt cattgqcatt tggagccctc atcctgaccc 1200 ttgtgcagat agcccgggtc atcttggagt atattgacca caagctcaga ggagtgcaga 1260 accctgtagc ccgctgcatc atgtgctgtt tcaagtgctg cctctggtgt ctggaaaaat 1320 ttatcaagtt cctaaaccgc aatgcataca tcatgatcgc catctacqgg aaqaatttct 1380 gtgtctcagc caaaaatgcg ttcatgctac tcatqcgaaa cattgtcagg gtggtcgtcc 1440 tggacaaagt cacagacctg ctgctgttct ttgggaagct gctggtggtc ggaggcgtgg 1500 gggtcctgtc cttctttttt ttctccggtc gcatcccqgg gctgggtaaa gactttaaga 1560 gcccccacct caactattac tggctgccca tcatgacctc catcctgggg gcctatgtca 1620 tcgccagcgg cttcttcagc gttttcggca tgtgtgtgga cacgctcttc ctctqcttcc 1680 tggaagacct ggagcggaac aacggctccc tggaccggcc ctactacatg tccaagagcc 1740 ttctaaagat tctgggcaag aagaacgagg cgcccccgga caecaagaag aggaagaagt 1900 gacagctccg gccctgatcc aggactgcac cccaccccca ccgtccagcc atccaacctc 1860 acttcgcctt acaggtctcc attttgtggt aaaaaaaggt tttaggccag gcgccgtggc 1920 tcacgcctgt aatccaacac tttgagaggc tgaggcgggc ggatcacctg agtcaggagt 1980 tcgagaccag cctggccaac atggtgaaac ctccgtctct attaaaaata caaaaattag 2040 ccgagagtgg tggcatgcac ctgtcatccc agctactcgg gaggctgagg caggagaatc 2100 gcttgaaccc gggaggcaga ggttgcagtg agccgagatc gcgccactgc actccaacct 2160 gggtgacaga ctctgtctcc anacaaaac aaacaaacaa aaaqatttta ttaaagatat 2220 tttgttaact cagtaaaaaa aaaaaaaaaa a 2251 Table LIII. Nucleotide sequence alignment of 24P4C12v.1 v.1 (SEQ ID NO: 95) and 24P4C12 v.7 (SEQ ID NO: 96). Score =1358 bits (706), Expect =0.Oldentities = 706/706 (100%) Strand - Plus/ Plus 24P4C12v. 1: 1 gagccatgggggaaagcagcgggacgaggatgacgaggcctacgggaagccagtcaaat 60 24 P4Cl2v.7: 1 gagccatggggggaaagcagcgggacgaggatgacgaggcctacgggaagccagtcaaat 60 24P4Cl2v.1: 61 acgacccctcctttcgaggccccatcaaaacagaagctgcacagatgtcatctgctgcg 120 24 P4C12v.7: 61 acgacccctcctttcgaggccccatcaaqaacagaegctgcacagatgtcatctgctgcg 2.20 24P4C12v.1: 121 tcctcttcctgctcttcattctagttacatcgtggtggggattgtggcctggttgtatg 180 24P4C12v.7: 121 tcctcttcctgctcttcattctaggttacatcgtggtggggattgtggcctggttgtatg 180 24P4Cl2v.1: 181 gagacccccqgcaagtcctctaccccaggaactctactggggcctactgtggcatggggg 240 24P4C12v.7: 191 gagacccccqgcaagtcctctaccccagqaactctactqgggcctactgtggcatggggg 240 2424C12v.e: 241 agaacaaagataagccgtatctcctgtacttcaacatttcagctgcatcctgtccagca 300 209 liII 1I I llllllIllIllIll lllllillil||1|1|||11|||||1||1||| 24P4C12v.7: 241 agaacaaagataagccgtatctcctgtacttcaacatcttcagctgcatcctgtccagca 300 24P4C12v.1: 301 acatcatctcagttgctgagaacggcctacagtgccccacaccccaggtgtgtgtgtcct 360 1lilili11 1 lli11111111111 II ill lli lIII|||||I||I||I 1|| I|I|||||I| 24P4C12v.7: 301 acatcatctcagttgctgagaacggcctacagtgccccacaccccagggtqtgtgtcct 360 24P4C12v.1: 361 cctgcccggaggacccatggactgtgggaaaaaacgagttctcacagactgttggggaag 420 24P4C12v.7: 361 cctgcccggaggacccatggactgtgggaaaaaacgagttctcacagactgttggggaag 420 24P4C12v.1: 421 tcttctatacaaaaaacaggaacttttgtctgccaggggtaccctggaatatgacggtga 480 24P4C12v.7: 421 tcttctatacaaaaaacaggaacttttgtctgccaggggtaccctggaatatgacggtga 490 24P4C12v.1: 481 tcacaagcctgcaacaggaactctgccccagtttcctcctcccctctgctccagctctgg 540 24P4C12v.7: 481 tcacaagcctgcaacaggaactctgccccagtttcctcctcccctctgctccagctctgg 540 24P4C12v.1: 541 ggcgctgctttccatggaccaacgttactccaccggcgctcccagggatcaccaatgaca 600 24P4C12v.7: 541 ggcgctgctttccatggaccaacgttactccaccggcgctcccagggatcaccaatgaca 600 24P4C12v.1: 601 ccaccatacagcaggggatcagcggtcttattgacagcctcaatgcccgagacatcagtg 660 24P4C12v.7: 601 ccaccatacagcaggggatcagcggtcttattgacagcctcaatgcccgagacatcagtg 660 24P4C12v.1: 661 ttaagatctttgaagattttqcccagtcctggtattggattcttgt 706 24P4C12v.7: 661 ttaagatctttgaagattttgcccagtcctggtattggattcttgt 706 Score - 2971 bits (1545), Expect - 0,0Identities - 1545/1545 (100%) Strand - Plus / Plus 24P4C12v.1: 1043 ggctgtgggacagatgatgtctaccatgttctacccactggtcacctttgtcctcctcct 1102 |Ii 111111 111 |||||l ll l|||||11 |111 il lillilllll 1111 || 24P4Cl2v.7: 707 ggctgtgggacagatgatgtctaccatgttctacccactggtcacctttgtcctcctcct 766 24P4C12v.1: 1103 catctgcattgcctactgggccatgactgctctgtacctggctacatcggggcaacccca 1162 1111111111111111111 111111111111111111111 1 11111 111111111 11 24P4C12v.7: 767 catctgcattgcctactgggccatgact.gctctgtacctggctacatcggggcaacccca 826 24P4C12v.1: 1163 gtatgtgctctgggcatccaacatcagctcccccggctgtgagaaagtgccaataaatac 1222 1l1lilll1ill1ill111lll1lil1llllllililllli11111illll11llll1lIli 24P4C12v.7: 827 gtatgtgctctgggcatccaacatcagctcccccggctgtgagaaagtgccaataaatac 886 24P4C12v.1: 1223 atcatgcaaccccacggcccaccttgtgaactcctcgtgcccagggctgatgtgcgtctt 1282 lillllll1111 lillilll illl1111ll 1111111 lil illlli l t lillliiii 24P4C12v.7: 887 atcatgcaaccccacggcccaccttgtgaactcctcgtgcccagggctgatgtgcgtctt 946 24P4C12v.1: 1283 ccagggctactcatccaaaggcctaatccaacgttctgtcttcaatctgcaaatctatgg 1342 lill11IIlI l i11 1 II I li1111 Il IllI I 111 ll1111 24P4C12v.7: 947 ccagggctactcatccaaaggcctaatccaacgttctgtcttcaatctgcaaetctatgg 1006 24P4C12v.1: 1343 ggtcctggggctcttctggacccttaactgggtactggccctgggccaatgcgtcctcgc 1402 24P4C12v.7: 1007 ggtcctggggctcttctggacccttaactgggtactggccctgggccaatgcgtcctcgc 1066 210 24P4C12v.1: 1403 tgqaqcctttgcctccttctactgggccttccacaagccccaggacatccctaccttccc 1462 till iliti il i l ll l l l li 11111111111111111111litt 24P4C12v.7. 1067 tggagcctttgcctccttctactgggccttccacaagccccaggacatccctaccttccc 1126 24P4C12v.1: 1463 cttaatctctgccttcatccgcacactccgttaccacactgggtcattggcatttggagc 1522 illI I I ll ll l i 111111111llltli11111111 11111111ill 11111111 24P4Cl2v.7: 1127 cttaatctctgccttcatccgcacactccgttaccacactgggtcattggcatttggagc 1186 24P4C12v.1: 1523 cctcatcctgacccttgtgcagatagcccgggtcatcttggagtatattgaccacaagct 1582 lil 1|1||l111111llilillill11lillt111111111 1i111 111li 24P4Cl2v.7: 1187 cctcatcctgacccttgtgcagatagcccgggtcatcttggagtatattgaccacaagct 1246 24P4Cl2v.1: 1583 cagaggagtgcagaaccctgtagcccgetgcatcatgtgctgtttcaagtgctgcctctg 1642 I ilil IltltIl I 111111111111111111111 111111lil lIiil 24P4C12v.7: 1247 cagaggagtgcagaaccctgtagcccgctgcatcatgtgctgtttcaagtgctgcctctg 1306 24P4C12v.1: 1643 gtgtctggaaaaatttatcaagttcctaaaccgcaatgcatacatcatgatcgccatcta 1702 li l i i l llliltI tt tl l i ll I ill i l111 i il tl illtIiltt ill 1111 i litlIl 24P4C12v.7: 1307 gtgtctggaaaaatttatcaagttcctaaaccgcaatgcatacatcatgatcgccatcta 1366 24P4Cl2v.1: 1703 cgggaagaatttctgtgtctcagccaaaaatgcgttcatgctactcatgcgaaacattgt 1762 tilill lit 11111 il liii Illtilll lllilt t ill l i ll 11litliltil 24P4C12v.7: 1367 cgggaagaatttctgtgtctcagccaaaaatgcgttcatgctactcatgcgaaacattgt 1426 24P4C12v.1: 1763 cagggtggtcgtcctggacaaagtcacagacctgctgctgttctttgggaagctgctggt 1822 |lil liltliltllill lil111 t il i ll t Ilt Illlil I|lt||| t il l| 1||Ill 24P4C12v.7: 1427 cagggtggtcgtcctggacaaagtcacagacctgctgctgttctttgggaagctgctggt 1486 24P4C12v.1: 1823 ggtcggaggcgtgggggtcctgtccttcttttttttctccggtcgcatcccqgqctggg 1882 24P4Cl2v.7: 1487 ggtcgqaggcgtgggggtcctgtccttcttttttttctccggtcgcatcccggggctggg 1546 24P4C12v.1: 1883 taaagactttaagagcccccacctcaactattactggctgcccatcatgacctccatcct 1942 ili tllilll11 111I tllil 11111 illlltl il 1111 it111111lili 24P4C12v.7: 1547 taaagactttaagagcccccacctcaactattactggctgcccatcatgacctccatcct 1606 24P4C12v.1: 1943 gggggcctatgtcatcgccagcggcttcttcagcgttttcggcatgtgtgtggacacgct 2002 litt lit iIt lllllItlt lll1 l llliltllt l I lll1 1 1 li i lllliltlIl 24P4C12v.7: 1607 gggggcctatgtcatcgccagcggcttcttcagcgttttcggcatgtgtgtggacacgct 1666 24P4C12v.1: 2003 cttcctctgcttcctggaagacctggagcggaacaacggctccctggaccggccctacta 2062 lilllt lltl l l ll l l lllilt t111 tl 11 il 1 1 1 1 i iil llt itillllllltt itlitl 24P4Cl2v. 7: 1667 cttcctctgcttcctggaagacctggagcggaacaacggctccctggaccggccctacta 1726 24P4C12v.1: 2063 catgtccaagagccttctaaagattctgggcaagaagaacgaggcgcccccggacaacaa 2122 il l l l i l lllilt ~ l111111 i11 l tl lilllil1liliil t till 1 lll1 ll1 ll 24P4C12v.7: 1727 catgtccaagagccttctaaagattctgggcaagaagaacgaggcgcccccggacaacea 1786 24P4C12v.1: 2123 gaagaggaagaagtgacagctccggccctgatccaggactgcaccccacccccaccgtcc 2182 24P4C12v.7: 1787 gaagaggaagaagtgacagctccggccctgatccaggactgcaccccacccccaccgtcc 1846 24P4C12v.1: 2183 agccatccaacctcacttcgccttacaggtctccattttgtggtaaaaaaaggttttagg 2242 24P4C12v.7: 1847 agccatccaacctcacttcgccttacaggtctccattttgtggtaaaaaaaggttttagg 1906 211 24P4C12v. 1: 2243 ccaggcgccgtggctcacgcctgtaatccaacactttgagaggctgaggcgggcggatca 2302 24P4C12v.7: 1907 ccaggcgccgtggctcacgcctgtaatccaacactttgagaggctgaggcgggcggatca 1966 24P4C12v.1: 2303 cctgagtcaggagttcgagaccagcctggccaacatggtgaaacctccgtctctattaaa 2362 24P4C12v.7: 1967 cctgagtcaggagttcgagaccagcctggccaacatggtgaaacctccgtctctattaaa 2026 24P4C12v.1: 2363 aatacaaaaattagccgagagtggtggcatgcacctgtcatcccagctactcgggaggct 2422 1|1 ll11111l1111|1l1il 11ll 11il il l ll illl111 Il 11111 I ilill l i l IlI l 24P4C12v.7: 2027 aatacaaaaattagccgagagtggtggcatgcacctgtcatcccagctactcgggaggct 2086 24P4C12v.1: 2423 gaggcaggagaatcgcttgaacccgggaggcagaggttgcagtgagccgagatcgcgcca 2402 1 11| lilllli lil 11111 lll 1 li ll 111 1 11 1111111 i lIi 11111 1 I 24P4C12v.7: 2087 gaggcaggagaatcgcttgaacccgggaggcagaggttgcagtgagccgagatcgcgcca 2146 24P4C12v.1: 2483 ctgcactccaacctgggtgacagactctgtctccaaaacaaaacaaacaaacaaaaagat 2542 lillliI lllill111111111ill Ill llii|1ilII I liiilliilillt 24P4C12v.7: 2147 ctgcactccaacctgggtgacagactctgtctccaaaacaaaacaaacaaacaaaaagat 2206 24P4C12v.1: 2543 tttattaaagatattttgttaactcagtaaaaaaaaaaaaaaaaa 2587 , 24P4C12v.7: 2207 tttattaaagatattttgttaactcagtaaaaaaaaaaaaaaaaa 2251 Table LIV. Peptide sequences of protein coded by 24P4Cl2 v.7 (SEQ ID NO: 97) .MGGKQRDEDD EAYGRPVKYD PSFRGPIKNR SCTDVICCVL FLLFILGYIV VGIVAWLYGD 60 PROVLYPRNS TGAYCGMGEN KDKPYLLYFN IFSCILSSNI ISVAENGLQC PTPQVCVSSC 120 PEDPWTVGKN EFSQTVGEVF YTKNRNFCLP GVPWNMTVIT SLQQELCPSF LLPSAPALGR 180 CFPWTNVTPP ALPGITNDTT IQQGISGLID SLNARDISVK IFEDFAQSWY WILVAVGQMM 240 STMFYPLVTF VLLLICIAYW AMTALYLATS GQPQYVLWAS NISSPGCEKV PINTSCNPTA 300 HLVNSSCPGL MCVFQGYSSK GLIQRSVFNL QIYGVLGLEW TLNWVLALGQ CVLAGAFASF 360 YWAFHKPQDI PTFPLISAFI RTLRYHTGSL AFGALILTLV QIARVILEYI DHKLRGVQNP 420 VARCIMCCFK CCLWCLEKFI KFLNRNAYIM IAIYGKNFCV SAKNAFMLLM RNIVRVVVLD 480 KVTDLLLFFG KLLVVGGVGV LSFFFFSGRI PGLGKDFKSP HLNYYWLPIM TSIIGAYVIA 540 SGFFSVFGMC VDTLFLCFLE DLERNNGSLD RPYYMSKSLL KILGKKNEAP PDNKKRKK 598 Table LV. Amino acid sequence alignment of 24P4C12v.1 v.1 (SEQ ID NO: 98) and 24P4Cl2 v.7 (SEQ ID NO: 99). Score = 1195 bits (3091), Expect - 0.OIdentities = 598/710 (84%), Positives 598/710 (84%). Gaps - 112/710 (15%) 24P4C12v.1: 1 MGGKORDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLLLFILGYIVVGIVAWLYGD 60 MGGKORDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 24P4C12v.7: 1 MGGKQRDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 60 24P4C12v.1: 61 PRQVLYPPNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPQVCVSSC 120 PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPQVCVSSC 24P4C12v.7: 61 PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLOCPTPQVCVSSC 120 24P4C12v.1: 121 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNNTVITSLOQELCPSFLLPSAPALGR 180 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLOQELCPSFLLPSAPALGR 24P4C12v.7: 121 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLOQELCPSFLLPSAPAIGR 180 24P4C12v.1: 181 CFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFAQSWYWILVALGVAL 240 CFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFAQSWYWILVA 24P4Cl2v.7: 181 CFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFAQSWYWILVA----- 235 24P4C12v.1: 241 VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFTTNLS 300 212 24P4C12v.7: 235 ------------------------------------------------------------ 235 24P4Cl2v.1: 301 AYQSVQETWLAALIVLAVLEAILLLMLIFLRQRIRIAIALLKEASKAVGQMMSTMFYPLV 360 VGOMMSTMFYPLV 24P4C12v.7: 236 ------------------------------------------------ VGQMMSTMFYPLV 248 24P4Cl2v.1: 361 TFVLLLICIAYWAMTALYLATSGOPQYVLWASISSPGCEKVPINTSCNPTAHLVNSSCP 420 TFVLLLICIAYWAMTALYLATSGOPQYVLWASNISSPGCEKVPINTSCNPTAHLVNSSCP 24P4C12v.7: 249 TFVLLLICIAYWANTALYLATSGOPQYVLWASNISSPGCEKVPINTSCNPTAHLVNSSCP 308 24P4C12v.1: 421 GLMCVFQGYSSXGLIORSVFNLQIYGVLGLFWTLNWVLALGQCVLAGAFASFYWAFHKPQ 480 GLMCVFGYSSKGLIORSVFNLQIYGVLGLFWTLNWVLALGQCVLAGAFASEYWAFHKPO 24P4C12v.7: 309 GIMCVFOGYSSKGLIQRSVFNLQIYGVLGLWTLNWVLALGQCVLAGAFASFYWAFHKPQ 368 24P4C12v.1: 481 DIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVONPVARCIMCC 540 DIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVQNPVARCIMCC 24P4C12v.7: 369 DIPTFPLISAFIRTLRYHTGSLAFGALILTLVOIARVILEYIDHKLRGVQNPVARCIMCC 428 24P4C12v.1: 541 FKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAFWLLMRNIVRVVVLDKVTDLLLF 600 FKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNA1!MLLMRNIVRVVVLDKVTDLLLF 24P4C12v.7: 429 FKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAELLMRNIVRVVVLDKVTDLLLF 488 24P4C12v.1: 601 FGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMTSILGAYVIASGFFSVFG 660 FGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPiLNYYWLPIlTSILGAYVIASGFFSVG 24P4C12v.7: 489 FGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMTSILGAYVIASGFFSVFG 548 24P4C12v.1: 661 MCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKRKK 710 MCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKRKK 24P4C12v.7: 549 MCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKRKKl 598 Table LVI. Nucleotide sequence of transcript variant 24P4C12 v.8 (SEQ ID NO: 100) gagccatggg gggaaagcag cgggacqagg atgacgaggc ctacgggaag ccagtcaaat 60 acgacccctc ctttcgaggc cccatcaaga acagaagctg cacagatgtc atctgctgcg 120 tcctcttcct gctcttcatt ctaggttaca tcgtggtggg gattgtggcc tggttgtatg 180 gagacccccg gcaagtcctc tacccagga actctactgg ggcctactgt ggcatgggqg 240 agaacaaaga taagccgtat ctcctgtact tcaacatctt cagctgcatc ctgtccagca 300 acatcatctc agttgctqag aacggcctac agtgccccac accccaggt tgtgtgtcct 360 cctgcccgga ggacccatgg actgtgggaa aaaacgagtt ctcacagact gttggggaag 420 tcttctatac aaaaaacagg aacttttgtc tgccaggggt accctggaat atgacggtga 480 tcacaagcct gcaacaggaa ctctgcccc& gtttcctcct cccctctgct ccagctctgg 540 ggcgctgctt tccatggacc aacgttactc caccggcgct cccagggatc accaatgaca 600 ccaccataca gcaggggatc agcggtctta ttgacagcct caatgcccga gacatcagtg 660 ttaagatctt tgaagatttt gcccagtcct ggtattggat tcttgttgcc ctqggggtgg 720 ctctggtctt gagcctactg tttatcttgc ttctgcgcct ggtggctggg cccctggtgc 760 tggtgctgat cctgggagtg ctgggcgtgc tggcatacgg catctactac tgctgggagg 840 agtaccgagt gctgcgggac aagggcgcct ccatctccca gctgggtttc accaccaacc 900 tcagtgccta ccagagcgtg caggagacct qgctggccqc cctgatcgtg ttqqcggtgc 960 ttgaagccat cctgctgctg atgctcatct tcctgcggca gcggattcgt attgccatcg 1020 ccctcctgaa ggaggccagc aaggctgtgg gacagatgat gtctaccatg ttctacccac 1080 tggtcacctt tgtcctcctc ctcatctgca ttgcctactg ggccatgact gctctgtacc 1140 tggctacatc ggggcaaccc cagtatgtgc tctgggcatc caacatcagc tCCCCCggct 1200 gtgagaaagt gccaataaat acatcatgca accccacggc ccaccttgtg aactcctcgt 1260 gcccagggct gatgtgcgte ttccagggct actcatccaa aggcctaatc caacgttctg 1320 tcttcaatct gcaaatctat ggggtcctgg ggctcttctg gacccttaac tgggtactgg 1380 ccctgggcca atgcgtcctc gctggagcct ttgcctcctt ctactgggcc ttccacaagc 1440 cccaggacat ccctaccttc cccttaatct ctqccttCat ccgcacactc cgttaccaca 1500 ctgggtcatt ggcatttgga gccctcatcc tgacccttgt gcagatagcc cgggtcatct 1560 tggagtatat tgaccacaag ctcagaggag tgcagaaccc tgtagcccgc tgcatcatgt 1620 gctgtttcaa gtgctgcctc tggtgtctgg aaaaatttat caagttccta aaccgcaatg 1680 catacatcat gatcgccatc tacgggaaga atttctgtgt cteagccaaa aatgcgttca 1740 tgctactcat gcgaaacatt gtcagggtqg tcgtcctgga caaagtcaca gacctgctgc 1800 tgttctttgg gaagctgctg gtggtcggag gcgtgggggt cctgtccttc ttttttttct 1860 ccggtcgcat cccggggctg ggtaaagact ttaagagccc ccacctcaac tattactggc 1920 tgcccatcat gaggaaccca ataaccccaa cgggteatgt CttcCagacc tccatcctgg 1980 gggcctatgt catcgccagc ggcttcttca gcgttttcgg catgtgtgtg gacacgctct 2040 tcctctgctt cctggaagac ctggagcgga acaacggctc cctggaccgg ccctactaca 2100 tgtccaagag ccttctaaag attctgggca agaaqaacga ggcgcccccg gacaacaaga 2160 agaggaagaa gtgacagctc cggccctgat ccaggactgC aCCCCaCccc caccgtccaq 2220 213 ccatccoacc tcacttcgcc ttacaggtct ccattttgtg gtaaaaaaag gttttaggcc 2280 aggcgccgtg gctcacgcct-gtaatccaac actttgagag gctgaggcgg gcggatcacc 2340 tgagtcagga gttcgagacc agcctggcca acatggtgaa acctccgtct ctattaaaaa 2400 tacaaaaatt agccgagagt ggtggcatgc acctgtcatc ccagctactc gggaggctga 2460 ggcaggagaa tcgcttgaac ccgggaggca gaggttgcag tgagccgaga tcgcgccact 2520 gcactccaac ctgggtgaca gactctgtct ccaaaacaaa acaaacaaac aaaaagattt 2580 tattaaagat attttgttaa ctcagtaaaa aaaaaaaaaa aaa 2623 Table LV!. Nuclectide sequence alignment of 24P4C2v.1 v.1 (SEQ ID NO 101) and 24P4C12 v.8 (SEQ ID NO; 102) Score = 3715 bits (1932), Expect = 0.OIdentities = 1932/1932 (100%) Strand - Plus / Plus 24P4Cl2v.1: 1 gagccatggggggaaagcagcgggacgaggatgacgaggcctacgggaagccagtcaaat 60 24P4Cl2v.8: 1 gagccatggggggaaagcagcgggacgaggatgacgaggcctacgggaagccagtcaaat 60 24P4Cl2v.1: 61 acgacccctcctttcgaggccccatcaagaacagaagctgcacagatgtcatctgctgcg 120 111lIIilIlI lIIII I lI Ill illIll i I 11lll IIi I Iliil||lilii 24P4C12v.8: 61 acgacccctcctttcgaggccccatcaagaacagaagctgcacagaLgtcatctgctgcg 120 24P4Cl2v.1: 121 tcctcttcctgctcttcattctaggttacatcgtggtggggattgtggcctggttgtatg 180 24P4Cl2v.8: 121 tcctcttcctgctcttcattctaggttacatcgtggtggggattgtggcctggttgtatg 180 24P4Cl2v.1: 181 gagacccccggcaagtcctctaccccaggaactctactggggcctactgtgcatggggg 240 111ill1ll11lll1lll1lllilll1lli11ll1l1ll1l11l111lil111ll1l Ilill 24P4C12v.8: 181 gagacccccggcaagtcctctaccccaggaactctactggggcctactgtggcatggggg 240 24P4C12v.1: 241 agaacaaagataagccgtatctcctgtacttcaacatcttcagctgcatcctgtccagca 300 iIiIIIII|IIIllilI I Ili||l I liiil1111||1I11II1I1illli 24P4Cl2v.8: 241 agaacaaagataagccgtatctcctgtacttcaacatcttcagctgcatcctgtccagca 300 24P4C12v.1: 301 acatcatctcagttgctgagaacggcctacagtgccccacaccccaggtgtgtgtgtcct 360 24P4C12v.8: 301 acatcatctcagttgctgagaacggcctacagtgccccacaccccaggtgtgtgtgtcct 360 24P4Cl2v.1: 361 cctgcccggaggacccatggactgtgggaaaaaacgagttctcacagactgttggggaag 420 24P4C12v.8: 361 cctgcccggaggacccatggactgtgggaaaaaacgagttctcacagactgttggggaag 420 24P4Cl2v.1: 421 tcttctatacaaaaaacaggaacttttgtctgccagggqtaccctggaatatgacggtga 480 11111l 111 11 1|II ll 11i 111l11lil lill 11111illl ll lilii 24P4C12v.8: 421 tcttctataaaaaaacaggaacttttgttgccaggggtaccctggaatatgacggtga 480 24P4C12v.1: 481 tcacaagcctgcaacaggaactctgccccagtttcctcctcccctctgctccagctctgg 540 lilli 1 1 |111 111 lill ll11 lli lilill 1 l 1i 11i I l 24P4C12v.8: 481 tcacaagcctgcaacaggaactctgccccagtttctcctcccctctgCtccagctctgg 540 24P4C12v.1: 541 ggcgctgctttccatggaccaacgttactccaccggcgctcccagggatcaccaatgaca 600 11ill Ill11lil lIl II i I lllllil 11 i1111 l lill lillill ll1 l iIll 24P4C12v.8: 541 ggcgctgctttccatggaccaacgttactccaccggcgctcccagggatcaccaatgaca 600 24P4Cl2v.1: 601 ccaccatacagcaggggetcagcggtcttattgacagcctcaatgccgagacatcagtg 660 111 1111111IIIIIIIIIIII lil1ll ll lli li lll1ll1ll1l1il1lil ill 1l lili 24P4C12v.8: 601 ccaccatacagcaggggatcagcggtcttattgacagcctcaatgcccgagacatcogtg 660 214 24P4C12v.1: 661 ttaagatctttgaagattttgcccagtcctggtattggattcttgttgccctgggggtgg 720 li l l l i l l l l l ll lll11 11 11 llll111 11 11 1 11 ill 1||||| 1||||1| 24P4C12v.8: 661 ttaagatctttgaagattttgcccagtcctggtattggattcttgttgccctgggggtgg 720 24P4C12v.1: 721 ctctggtcttgagcctactgtttatcttgcttctgcgcCtggtggctgggcccctggtgc 780 111l ll 1lil l llll ll llllll I Ill I l111 1liillll11l1111 24P4C12v.8: 721 ctctggtcttgagcctactgtttatcttgcttctgcgcctggtggctgggcccctggtgc 780 24P4C12v.1: 781 tggtgctgatcctgggagtgctgggcgtgctggcatacggcatctactactgctgggagg 840 11ill 11l111l1l1IllI I l ll1ll1 11li illi li lill ll lllll l 24P4C12v.8: 781 tggtgctgatcctgggagtgctgggcgtgctggcatacggcatctactactgctgggagg 840 24P4C12v.1: 841 agtaccgagtgctgcgggacaagggcgcctccatctcccagctgggtttcaccaccaacc 900 11ll1111l1ll1111l11l11i11ll1lll1l11ll11ll1111l11illl1ll11l||1 24P4C12v.8: 841 agtaccgagtgctgcgggacaagggcgcctccatctcccagctgggtttcaccaccaacc 900 24P4C12v.1: 901 tcagtgcctaccagagcgtgcaggagacctggctggccgccctgatcgtgttggcggtgc 960 1il1l1l11ililill 1l 11l 111111l1l lill li llillillill11 il1 llill 24P4C12v.8: 901 tcagtgcctaccagagcgtgcaggagacctggctggccgccctgatcgtgttggcgggc 960 24P4C12v.1: 961 ttgaagccatcctgctgctgatgctcatcttcctgcggcagcggattcgtattgccatcg 1020 11i ll 111 11 11 11 Ill i l lllllilll llil 1illilllillli 24P4C12v.8: 961 ttgaagccatcctgctgctgatgctcatcttcctgcggcagcggattcgtattgccatcg 1020 24P4C12v.1: 1021 ccctcctgaaggaggccagcaaggctgtgggacagatgatgtctaccatgttctacccac 1080 24P4C12v.8: 1021 ccctcctgaaggaggccagcaaggctgtgggacagatgatgtctaccatgttctacccac 1080 24P4C12v.1: 1081 tggtcacctttgtcctcctcctcatctgcattgcctactgggccatgactgctctgtacc 1140 1il1lll1l1111ll11ill1ll11l1ll1lil11111111l111l11l lilll11ilil 24P4C12v.8: 1081 tggtcacctttgtcctcctcctcatctgcattgcctactgggccatgactgctctgtacc 1140 24P4C12v.1: 1141 tggctacatcggggcaaccccagtatgtgctctgggcatccaacatcagctcccccggct 1200 lll1 iilll1ll111l1llll11l11ll111ll11l1lll11l1il111l11l1lillil 24P4C12v.8: 1141 tggctacatcggggcaaccccagtatgtgctctgggcatccaacatcagctcccccggct 1200 24P4C12v.1: 1201 gtgagaaagtgccaataaatacatcatgcaaccccacggcccaccttgtgaactcctcgt 1260 lill,,li lillIlilI llililillilillilllilil11111 l1i1l1illil11 ll 24P4C12v.8: 1201 gtgagaaagtgccaataaatacatcatgcaaccccacggcccaccttgtgaactcctcgt 1260 24P4C12v.1: 1261 gcccagggctgatgtgcgtcttccagggctactcatccaaaggcctaatccaacgttctg 1320 24P4C12v.8: 1261 gcccagggctgatgtgcgtcttccagggctactcatccaaaggcctaatccaacgttctg 1320 24P4C12v.1: 1321 tcttcaatctgcaaatctatggggtcctggggctcttctggacccttaactgggtactgg 1380 lit l lilIIIllll 1i11l1111111111ll1llil11ill1111illli lili 11il11 24P4C12v.8: 1321 tcttcaatctgcaaatctatggggtcctggggctcttctggacccttaactgggtactgg 1380 24P4C12v.1: 1381 ccctgggccaatgcgtcctcgctggagcctttgcctccttctactgggccttccacaagc 1440 111|11111|||1|111l111l1llillilliiillil11l11111111 I11 illillill 24P4C12v.8: 1381 ccctgggccaatgcgtcctcgctggagcctttgcctccttctactgggccttccacaagc 1440 24P4C12v.1: 1441 cccaggacatccctaccttccccttaatctctgccttcatccgcacactccgttaccaca 1500 liII 11 ll l l |111ll ll lll l llill 11ili1l111 1 11Illi 1illi 24P4C12v.8: 1441 cccaggacatccctaccttccccttaatctctgccttcatccgcacactccgttaccaca 1500 215 24P4C12v.1: 1501 ctgggtcattggcatttggagccctcatcctgacccttgtgcagatagcccgggtcatct 1560 1||111111111lil11||11Il1lliiIll ili l ii 111ill1 ilIi111111111illilllii 24P4C12v.8: 1501 ctgggtcattggcatttggagccctcatcctgacccttgtgcagatagcccgggtcatct 1560 24P4C12v.1: 1561 tggagtatattgaccacaagctcagaggagtgcagaaccctgtagcccgctgcatcatgt 1620 24P4C12v.8: 1561 tggagtatattgaccacaagctcagaggagtgcagaaccctgtagcccgctgcatcatgt 1620 24P4C12v.1: 1621 gctgtttcaagtgctgcctctggtgtctggaaaaatttatcaagttcctaaaccgcaatg 1680 111 11lll IIlll1l1l1l11ll1111 lllili Ililli 1 l11liili lill11 i 24P4C12v.8: 1621 gctgtttcaagtgctgcctctggtgtctggaaaaatttatcaagttcctaaaccgcaatg 1680 24P4C12v.1: 1681 catacatcatgatcgccatctacgggaagaatttctgtgtctcagccaaaaatgcgttca 1740 111Il1111111 lI1i111 ll1ll liiiill11l1||lil111l111111 l111 liiil|1||||| 24P4C12v.8: 1681 catacatcatgatcgccatctacgggaagaatttctgtgtctcagccaaaaatgcgttca 1740 24P4C12v.1: 1741 tgctactcatgcgaaacattgtcagggtggtcgtcctggacaaagtcacagacctgctgc 1800 11illll1l11li 1l1ll li illi l i 111 111 11 ll lill11 ll1ill 24P4C12v.8: 1741 tgctactcatgcgaaacattgtcagggtggtcgtcctggacaaagtcacagacctgctgc 1800 24P4C12v.1: 1801 tgttctttgggaagctgctggtggtcggaggcgtgggggtcctgtccttcttttttttct 1860 24P4C12v.8: 1801 tgttctttgggaagctgctggtggtcggaggcgtgggggtcctgtccttcttttttttct 1860 24P4C12v.1: 1861 ccggtcgcatcccggggctgggtaaagactttaagagcccccacctcaactattactggc 1920 li i l li lll I l l llllli11 11 11 11 lIl ll lll 1ll 1lill1ll1ill 24P4C12v.8: 1861 ccggtcgcatcccggggctgggtaaagactttaagagcccccacctcaactattactggc 1920 24P4C12v.1: 1921 tgcccatcatga 1932 24P4C12v.e: 1921 tgcccatcatga 1932 Score = 1263 bits (657), Expect = 0.OIdentities - 657/657 (100%) Strand - Plus / Plus 24P4C12v.1: 1931 gacctccatcctgggggcctatgtcatcgccagcggcttcttcagcgttttcggcatgtg 1990 24P4C12v.8: 1967 gacctccatcctgggggcctatgtcatcgccagcggcttcttcagcgttttcggcatgtg 2026 24P4C12v.1: 1991 tgtggacacgctcttcctctgcttcctggaagacctggagcggaacaacggctccctgga 2050 24P4C12v.8: 2027 tgtggacacgctcttcctctgcttcctggaagacctggagcggaacaacggctccctgga 2086 24P4C12v.1: 2051 ccggccctactacatgtccaagagccttctaaagattctgggcaagaagaacgaggcgcc 2110 24P4C12v.8: 2087 ccggccctactacatgtccaagagccttctaaagattctgggcaagaagaacgaggcgcc 2146 24P4C12v.1: 2111 cccggacaacaagaagaggaagaagtgacagctccggccctgatccaggactgcacccca 2170 11 1 11| 1 1| 1 I||l ll ill l|| I llIllIll 11111i llilI lill 11i i l11 24P4C12v.8: 2147 cccggacaacaagaagaggaagaagtgacagctccggccctgatccaggactgcacccca 2206 24P4C12v.1: 2171 cccccaccgtccagccatccaacctcacttcgccttacaggtctccattttgtggtaaaa 2230 1111ll1llil1ll1ll1ll11il1ll1ll1ll1lll1llilllilIll11llill1111li 24P4C12v.8: 2207 cccccaccgtccagccatccaacctcacttcgccttacaggtctccattttgtggtaaaa 2266 24P4C12v.1: 2231 aaaggttttaggccaggcgccgtggctcacgcctgtaatccaacactttgagaggctgag 2290 216 24P4C12v.8: 2267 aaaggttttaggccaggcgccgtggctcacgcctgtaatccaacactttgagaggctgag 2326 24P4C12v.1: 2291 gcgggcggatcacctgagtcaggagttcgagaccagcctggccaacatggtgaaacctcc 2350 24P4C12v.8: 2327 gcgggcggatcacctgagtcaggagttcgagaccagcctggccaacatggtgaaacctcc 2386 24P4C12v.1: 2351 gtctctattaaaaatacaaaaattagccgagagtggtggcatgcacctgtcatcccagct 2410 |11||11!lliiililililll lll lli|li lli | lilll1 ill1111 ~ill 24P4C12v.8: 2387 gtctctattaaaaatacaaaaattagccgagagtggtggcatgcacctgtcatcccagct 2446 24P4C12v.1: 2411 actcgggaggctgaggcaggagaatcgcttgaacccgggaggcagaggttgcagtgagcc 2470 24P4C12v.8: 2447 actcgggaggctgaggcaggagaatcgcttgaacccgggaggcagaggttgcagtgagcc 2506 24P4C12v.1: 2471 gagatcgcgccactgcactccaacctgggtgacagactctgtctccaaaacaaaacaaac 2530 I1lilllllllilill1lllll11l1illlllili1l11ill11lll1llilllllillil 24P4C12v.8: 2507 gagatcgcgccactgcactccaacctgggtgacagactctgtctccaaaacaaaacaaac 2566 24P4C12v.1: 2531 aaacaaaaagattttattaaagatattttgttaactcagtaaaaaaaaaaaaaaaaa 2587 lI lI l 1 11llll ll llI lll ll llli11 lll lll ll ll111 || 24P4C12v.8: 2567 aaacaaaaagattttattaaagatattttgttaactcagtaaaaaaaaaaaaaaaaa 2623 Table LVIII. Peptide sequences of protein coded by 24P4C12 v.6 (SEQ ID NO: 103) MGGKQRDEDD EAYGKPVKYD PSFRGPIKNR SCTDVICCVL FLLFILGYIV VGIVAWLYGD 60 PRQVLYPRNS TGAYCGMGEN KDKPYLLYFN IFSCILSSNI ISVAENGLOC PTPOVCVSSC 120 PEDPWTVGKN EFSQTVGEVF YTKNRNFCLP GVPWNMTVIT SLQQELCPSF LLPSAPALGR 180 CFPWTNVTPP ALPGITNDTT IQQGISGLID SLNARDISVK IFEDFAQSWY WILVALGVAL 240 VLSLLFILLL RLVAGPLVLV LILGVLGVLA YGIYYCWEEY RVLRDKGASI SQLGFTTNLS 300 AYQSVQETWL AALIVLAVLE AILLIALIFL RQRIRIAIAL LKEASKAVGQ MMSTMFYPLV 360 TFVLLLICIA YWAMTALYLA TSGOPQYVLW ASNISSPGCE KVPINTSCNP TAHLVNSSCP 420 GLMCVFQGYS SKGLIQRSVF NLQIYGVLGL FWTLNWVLAL GQCVLAGAFA SFYWAFHKPQ 480 DIPTFPLISA FIRTLRYHTG SLAFGALILT LVQIARVILE YIDHKLRGVQ NPVARCIMCC 540 FKCCLWCLEK FIKFLNRNAY IMIAIYGKNF CVSAKNAFHL LMRNIVRVVV LDKVTDLLLF 600 FGKLLVVGGV GVLSFFFFSG RIPGrI(KDFK SPHLNYYWLP IMRNPITPTG HVFQTSILGA 660 YVIASGFFSV FGMCVDTLFL CFLEDLERNN GSLDRPYYMS KSLLKILGKK NEAPPDNKKR 720 KK 722 Table LIX. Amino acid sequence alignment of 24P4C12v.1 v.1 (SEQ ID NO: 104) and 24P4C12 v.8 (SEQIDNO: 105) Score - 1438 bits (3722), Expect = 0.OIdentities = 710/722 (98%); Positives 710/722 (98%), Gaps = 12/722 (1%) 24P4C12v.1: 1 MGGKORDEDDEAYGKPVKYDPSFRGPIENRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 60 MGGKQRDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 24P4Cl2v.8: 1 NGGKORDEDDEAYGKPVYDPSFRGPI1NRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 60 24P4C12v.1: 61 PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLX)CPTPQVCVSSC 120 PRQVLYPRNSTGAYCGMGENKDKPYLLYNIFSCILSSNIISVAENGLQCPTPQVCVSSC 24P4C12v.8: 61 PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPQVCVSSC 120 24P4C12v.1: 121 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGR 180 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGR 24P4Cl2v.8: 121 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGR 180 24P4C12v.1: 181 CFPWTNVTPPALPGITNDTTIOOGISGLIDSLNARDISVKIFEDFAQSWYWILVALGVAL 240 CFPWTNVTPPALPGITNDTTIOQGISGLIDSLNARDISVKIFEDFASWYWILVALGVAL 24P4C12v.8: 181 CFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFASWYWILVALGVAL 240 24P4C12v.1: 241 VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFPTNLS 300 VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFTTNLS 217 24P4C12v.8: 241 VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFTTNLS 300 24P4C12v.1: 301 AYQSVOETWLAALIVLAVLEAILLLMLIFLRRIRIAIALLKEASKAVGQMMSTMFYPLV 360 AYQSVQETWLAALIVLAVLEAILLLMLIFLRQRIRIAIALLKEASKAVGQMMSTMFYPLV 24P4C12v.8: 301 AYQSVQETWLAALIVLAVLEAILLLMLIFLRQRIRIAIALLKEASKAVGQMMSTMFYPLV 360 24P4Cl2v.1: 361 TFVLLLICIAYWAMTALYLATSGQPQYVLWASNISSPGCEKVPINTSCNPTAHLVNSSCP 420 TFVLLLICIAYWAMTALYLATSGQPQYVLWASNISSPGCEKVPINTSCNPTAHLVNSSCP 24P4C12v.8: 361 TFVLLLICIAYWAMTALYLATSGQPQYVLWASNISSPGCEKVPINTSCNPTAHLVNSSCP 420 24P4C12v.1: 421 GLMCVFQGYSSKGLIQRSVFNLQIYGVLGLFWTLNWVLALGQCVLAGAFASFYWAFHKPQ 480 GLMCVFQGYSSKGLIQRSVFNLQIYGVLGLFWTLNWVLALGQCVLAGAFASFYWAFHKPO 24P4C12v.8: 421 GLMCVFQGYSSKGLIQRSVFNLQIYGVLGLFWTLNWVLALGOCVLAGAFASFYWAFHKPQ 480 24P4C12v.1: 481 DIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVQNPVARCIMCC 540 DIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVQNPVARCIMCC 24P4C12v.8: 481 DIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVQNPVARCINCC 540 24P4C12v.1: 541 FKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAEMLLMRNIVRVVVLDKVTDLLLF 600 FKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAFLIMRNIVRVVVLDKVTDLLLF 24P4C12v.8: 541 FKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAFKLIMRNIVRVVVLDKVTDLLLF 600 24P4C12v.1: 601 FGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIM------------TSILGA 648 FGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIM TSILGA 24P4C12v.8: 601 FGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMRNPITPTGHVFQTSILGA 660 24P4C12v.1: 649 YVIASGFFSVFMCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKR 708 YVIASGFFSVFGMCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKR 24P4C12v.8: 661 YVIASGFFSVFGMCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKR 720 24P4C12v.1: 709 KK 710 KK 24P4C12v.8: 721 KK 722 Table LX. Nucleotide sequence of transcript variant 24P4C12 v.9 (SEQ M NO: 106) gagccatggg gggaaagcag cgggacgagg atgacgaggc ctacgggaag ccagtcaaat 60 acgacccctc ctttcgaggc cccatcaaga acagaagctg cacagatgtc atctgctgcg 120 tcctcttcct gctcttcatt ctaggttaca tcgtggtggg gattgtggcc tqgttgtatg 180 gagacccccg gcaagtcctc taccccagga actctactgg ggcctactgt ggcatggggg 240 agaacaaaga taagccgtat ctcctgtact tcaacatctt cagctgcatc ctgtccagca 300 acatcatctc agttgctgag aacggcctac agtgccccac accccaggtg ttgtgtcct 360 cctgcccgga ggacccatgg actgtgggaa aaaacgagtt ctcacagact gttggggaag 420 tcttctatac aaaaaaaagg aacttttgtc tgccaggggt accctggaat atgacggtga 480 tcacaagcct gcaacaggaa ctctgcccca gtttcctcct cCtctgct ccagctctgg 540 ggcgctqctt tccatggacc aacgttactc caccggcgct ccagggatc accaatgaca 600 ccaccataca gcaggggatc aqcggtctta ttgacagcct caatgcccga gacatcagtg 660 ttaagatctt tgaagatttt gcccagtcct ggtattggat tcttgttgcc ctgggggtgg 720 ctctggtctt gagcctactg tttatcttgc ttctgcgcct ggtggctggg cccctggtgc 780 tggtgctgat cctgggagtg ctgggcgtgc tggcatacgg catctactac tgctgggagg 640 agtaccgagt gctgcgggac aagggcgcct ccatctccca gctgggtttc accaccaacc 900 tcagtgccta ccagagcgtg caggagacct ggctggccgc cctgatcgtg ttggcggtgc 960 ttgaagccat cctgctgctg atgctcatct tcctgcggca gcggattcgt attgccatcg 1020 ccctcctgaa ggaggccagc aaggctgtgg gacagatgat gtctaccatg ttctacccac 1080 tggtcacctt tgtcctcctc ctcatctgca ttgcctactg ggccatgact gctctgtatc 1140 ctctgcccac gcagccagcc actcttggat atgtgctctg ggcatccaac atcagctccc 1200 ccggctgtga gaaagtgcca ataaatacat catgcaaccc cacggcccac cttgtgaact 1260 cctcgtgccc agggctgatg tgcgtcttcc agggctactc atccaaaggc ctaatccaac 1320 gttctgtctt caatctgcaa atctatgggg tcctggggct cttctggacc cttaactggg 1380 tactggccct gggccaatgc gtcctcgctg gagcctttgc ctccttctac tgggccttcc 1440 acaagcccca ggacatccct accttcccct taatctctgc cttcatccgc acactccgtt 1500 accacactgg gtcattggca tttggagccc tcatcctgac ccttgtgcag atagcccggg 1560 tcatcttgga gtatattgac cacaagctca gaggagtgca gaaccctgta gcccgctgca 1620 tcatgtgctg tttcaagtgc tgcctctggt gtctggaaaa atttatcaag ttcctaaacc 1680 gcaatgcata catcatgatc gccatctacg ggaagaattt ctgtgtctca gccaaaaatg 1740 cgttcatgct actcatgcga aacattgtca gggtggtcgt cctggacaaa gtcacagacc 1800 tgctgctgtt ctttgggaag ctgctggtgg tcggaggcgt gggggtcctg tCcttctttt 1860 ttttctccgg tcgcatcccg gggctggta aaactttaa gagcccccac ctcaactatt 1920 actggctgcc catcatgacc tccatcctgg gggcctatgt catcgccagc ggcttcttca 1980 gcgttttcgg catgtgtgtg gacacgctct tcctctgctt cctgaagaaCatggagcgga 2040 218 acaacggctc cctggaccgg ccctactaca tgtccaagag ccttctaaag attctgggca 2100 agaagaacga ggcgcccccg gacaacaaga agaggaagaa gtgacagctc cggccctgat 2160 ccaggactgc accccacccc caccgtccag ccatccaacc tcacttcgcc ttacaggtct 2220 ccattttgtg gtaaaaaaag gttttaggcc aggcgccgtg gctcacgcct gtaatccaac 2280 actttgagag gctgaggcgg gcggatcacc tgagtcagga gttcgagacc agcctggcca 2340 acatggtgaa acctccgtct ctattaaaaa tacaaaaatt agccgagagt ggtggcatgc 2400 acctgtcatc ccagctactc gggaggctga ggcaggagaa tcgcttgaac ccgggaggca 2460 gaggttgcag tgagccgaga tcgcgccact gcactccaac ctgggtgaca gactctgtct 2520 ccaaaacaaa acaaaceaac aaaaagattt tattaaagat attttgttaa ctcagtaaaa 2580 aaaaaaaaaa aaa 2593 Table LXI. Nucleotide sequence alignment of 24P4C12v.1 v.1 (SEQ ID NO: 107) and 24P4Cl2 v.9 (SEQ ID NO: 108) Score = 2188 bits (1138), Expect - 0.OIdentities = 1138/1138 (100%) Strand - Plus / Plus 24P4Cl2v.1: I gagccatggggggaaagcagcgggacgaggatgacgaggcctacgggaagccagtcaaat 60 111 I lll illllllli lli lll11 lill lll li lI11 il I li ll111 24P4Cl2v.9; 1 gagccatggggggaaagcagcgggacgaggatgacgaggcctacgggaagccagtcaaat 60 24P4C12v.1: 61 acgacccctcctttcgaggccccatcaagaacagaagctgcacagatgtcatctgctgcg 120 lillllllllillilllllililllllllilllllillllllllilli1111i1ll1lili 24P4C12v.9: 61 acgacccctcctttcgaggccccatcaagaacagaagctgcacagatgtcatctgctgcg 120 24P4C12v.1: 121 tcctcttcctgctcttcattctaggttacatcgtggtggggattgtggcctggttgtatg 180 24P4C12v.9: 121 tcctcttcctgctcttcattctagqttacatcgtggtggggattgtggcctggttgtatg 180 24P4C12v.1: 181 gagacccccggcaagtcctctaccccaggaactctactggggcctactgtggcatggggg 240 111ll1lll1lll1ll|1lill1iliill11l1llilllillll1llililll1illli 24P4Cl2v.9: 181 gagacccccggcaagtcctctaccccaggaactctactggggcctactgtggcategggg 240 24P4Cl2v.1: 241 agaacaaagataagccgtatctcctgtacttcaacatcttcagctgcatcctgtccagca 300 24P4Cl2v.9: 241 agaacaaagataagccgtatctcctgtacttcaacatcttcagctgcatcctgtccagca 300 24P4Cl2v.1: 301 acatcatctcagttgctgagaacggcctacagtgccccacaccccaggtgtgtgtgtcct 360 tIll 1llillll lli 1111 111 IlIlI 11111 i ililli11l1l11lli1 l 24P4Cl2v.9: 301 acatcatctcagttgctgagaacggcctacagtgccccacaccccaggtgtgtgtgtcct 360 24P4C12v.1: 361 cctgcccggaggacccatggactgtgggaaaaaacgagttctcacagactgttggggaag 420 111111lIllllllllilllllllilllillillllllllllill lillllilli I lll 24P4C12v.9: 361 cctgcccggaggacccatggactgtgggaaaaaacgagttctcacagactgttggggaag 420 24P4Cl2v.1: 421 tcttctatacaaaaaacaggaacttttgtctgccaggggtaccctggaatatgacggtga 480 1ill1lll1111ilillllllill1lllillll1ill1lll1llillll11l11lllllll 24P4Cl2v.9: 421 tcttctatacaaaaaacaggaacttttgtctgccaggggtaccctggaatatgacggtga 480 24P4Cl2v.1: 481 tcacaagcctgcaacaggaactctgccccagtttcctcctcccctctgctccagctctgg 540 111l1l111l1111l1lillil11illlll1llil11lll1ll11llll1il11il11illi1 24P4Cl2v.9: 481 tcacaagcctgcaacaggaactctgccccagtttcctcctcccctctgctccagctctgg 540 24P4C12v.1: 541 ggcgctgctttccatggaccaacgttactccaccggcgctcccagggatcaccaatgaca 600 24P4C12v.9: 541 ggcgctgctttccatggaccaacgttactccaccggcgctcccagggatcaccaatgaca 600 24P4C12v.1: 601 ccaccatacagcaggggatcagcggtcttattgacagcctcaatgcccgagacatcagtg 660 lill ll ll l l llllilit l l ll2lil9i til ti illl iltli 219 24P4C12v.9: 601 ccaccatacagcaggggatcagcggtcttattgacagcctcaatgcccgagacatcagtg 660 24P4C12v.1: 661 ttaagatctttgaagattttgccCagtcctggtattggattcttgttgccctgggggtgg 720 i 11 1i Ii1I1 iI 11 1 I I |li I I ill ||11111 |1 |||||||||||||11 |||1|1|1 24P4C12v.9: 661 ttaagatctttgangattttgcccagtcctggtattggattcttgttgccctgggggtgg 720 24P4C12v.1: 721 ctctggtcttgagcctactgtttatcttgcttctgcgcctggtggctgggcccctggtgc 780 24P4C12v.9: 721 ctctggtcttgagcctactgtttatcttgcttctgcgcctggtggctgggcccctggtgc 780 24P4C12v.1: 781 tggtgctgatcctgggagtgctgggcgtgctggcatacggcatctactactgctgggagg 840 24P4C12v.9: 781 tggtgctgatcctgggagtgctgggcgtgctggcatacggcatctactactgctgggagg 840 24P4C12v.1: 841 agtaccgagtgctgcgggacaagggcgcctccatctcccagctgggtttcaccaccaacc 900 111111 l|||i i 11|1 111|||| 11111|l111111|1111|11|1 24P4C12v.9: 841 agtaccgagtgctgcgggacaagggcgcctccatctcccagctgggtttcaccaccaacc 900 24P4C12v.1: 901 tcagtgcctaccagagcgtgcaggagacctggctggccgccctgatcgtgttggcggtgc 960 24P4C12v.9: 901 tcagtgcctaccagagcgtgcaggagacctggetggccgccetgategtgttggcggtge 960 24P4C12v.1: 961 ttgaagccatcctgctgctgatgctcatcttcctgcggcagcggattcgtattgccatcg 1020 24P4C12v.9: 961 ttgaagccatcctgctgctgatgctcatcttcctgcggcagcggattcgtattgccatcg 1020 24P4C12v.1: 1021 ccctcctgaaggaggccagcaaggetgtgggacagatgatgtctaccatgttctacccac 1080 24P4C12v.9: 1021 ccctcctgaaggaggccagcaaggetgtgggacagatgatgtctaccatgttctacccac 1080 24P4C12v.1: 1081 tggtcacctttgtcctcCtcctcatctgcattgcctactgggccatgactgctctgta 1138 111|111|1111|11111||l||11 1111111111111111111111111 24P4C12v.9: 1081 tggtcacctttgtcctcctcctcatctgcattgcctactgggccatgactgctctgta 1138 Score - 2738 bits (1424), Expect - 0.OIdentities - 1424/1424 (100%) Strand - Plus / Plus 24P4C12v.1: 1164 tatgtgctctgggcatccaacatcagctcccccggctgtgagaaagtgccaataaataca 1223 24P4C12v.9: 1170 tatgtgctctgggcatccaacatcagctcccccggctgtgagaaagtgccaataaataca 1229 24P4C12v.1: 1224 tcatgcaaccccacggcccaccttgtgaactcctcgtgcccagggctgatgtgcgtcttc 1283 ||1111||1|11111111111|1111l11111l11111l||11l1111||ii11 24P4C12v.9: 1230 teatgcaaccccacggcccaccttgtgaactcctcgtgcccagggctgatgtgcgtcttc 1289 24P4C12v.1: 1284 cagggctactcatccaaaggcctaatccaacgttctgtcttcaatctgcaaatctatggg 1343 lillilllill111illilll1il1111lilill1l111lil111i11illil11lliil 24P4C12v.9: 1290 cagggctactcatccaaaggcctaatccascgttctgtcttcaatctgcaaatctatggg 1349 24P4C12v. 1: 1344 gtcctggggctcttctggaccettaactgggtactggccctgggccaatgcgtcctcgct 1403 iii 11111111111111111111111111111111111111111111111111111111 24P4C12v.9: 1350 gtcctggggctcttctggacccttaactgggtactggccctgggccaatgcgtcctcgct 1409 24P4C12v.1: 1404 ggagcctttgcctccttctactgggccttccacaagccccaggacatccctaccttcccc 1463 1li1l1 IllIllll Ilillilll 1il1llIllIllllllilli11111111111lilI 24P4C12v.9: 1410 ggagcctttgcctccttctactgggccttccacaagccccaggacatccctaccttcccc 1469 220 24P4C12v.1: 1464 ttaatctctgccttcatccgcacactccgttaccacactgggtcattggcatttggagcc 1523 l ll l illi lill llilll lllll111 lli lill ll l ll llll lli ll ||1 24P4C12v.9: 1470 ttaatctctgccttcatccgcacactccgttaccacactgggtcattggcatttggagcc 1529 24P4C12v.1: 1524 ctcatcctgacccttgtgcagatagcccgggtcatcttggagtatattgaccacaagctc 1583 Il I I liIi llilt 11 111Ill1 11 1 11 11 ill 11 I I l l lI 1i l i l l i 1 1 24P4C12v.9: 1530 ctcatcctgacccttgtgcagatagcccgggtcatcttggagtatattgaccacaagctc 1589 24P4C12v.1: 1584 agaggagtgcagaaccctgtagcccgctgcatcatgtgctgtttcaagtgctgcctctgg 1643 24P4C12v.9: 1590 agaggagtgcagaaccctgtagcccgctgcatcatgtgctgtttcaagtgctgcctctgg 1649 24P4C12v.1: 1644 tgtctggaaaaatttatcaagttcctaaaccgcaatgcatacatcatgatcgccatctac 1703 1 1 1 1 1 1 11 1 111111li | l llI1Il l i l l l li1l1I1Ill1I1Ill 1111Il 1lil 1I i l |iii 24P4C12v.9: 1650 tgtctggaaaaatttatcaagttcctaaaccgcaatgcatacatcatgatcgccatctac 1709 24P4C12v.1: 1704 gggaagaatttctgtgtctcagccaaaaatgcgttcatgctactcatgcgaaacattgtc 1763 24P4C12v.9: 1710 gggaagaatttctgtgtctcagccaaaaatgcgttcatgctactcatgcgaaacattgtc 1769 24P4C12v.1: 1764 agggtggtcgtcctggacaaagtcacagacctgctgctgttctttgggaagctgctggtg 1823 11i 1l1I 11l 111ll 1li 11111llill lil li i ll lillllll ll11 l ill1 24P4C12v.9: 1770 agggtggtcgtcctggacaaagtcacagacctgctgctgttctttgggaagctgctggtg 1829 24P4C12v.1: 1824 gtcggaggcgtgggggtcctgtccttcttttttttctccggtcgcatcccggggctgggt 1883 llil illII l l i i i | | lI l l l l illil I lil111 11Ilitlill1ilil111 11 1 11111 24P4C12v.9: 1830 gtcggaggcgtgggggtcctgtccttcttttttttctccggtcgcatcccggggctgggt 1889 24P4C12v.1: 1884 aaagactttaagagcccccacctcaactattactggctgcccatcatgacctccatcctg 1943 Ill I||| 11| Ill 11 li l I|1lill1 Il111l Il Illilli1 11i l l Illill l1 24P4C12v.9: 1890 aaagactttaagagcccccacctcaactattactggctgcccatcatgacctccatcctg 1949 24P4C12v.1: 1944 ggggcctatgtcatcgccagcggcttcttcagcgttttcggcatgtgtgtggacacgctc 2003 111l11ill111l1ll1111l1111|1111|| l l111 ll1lil lillI 1lil111 IlII 24P4C12v.9: 1950 ggggcctatgtcatcgccagcggcttcttcagcgttttcggcatgtgtgtggacacgctc 2009 24P4C12v.1: 2004 ttcctctgcttcctggaagacctggagcggaacaacggctccctggaccggccctactac 2063 111111lilllliilllliIllillillli11llilil111l11ll1lill 24P4C12v.9: 2010 ttcctctgcttcctggaagacctggagcg'gaacaacggctccctggaccggccctactac 2069 24P4C12v.1: 2064 atgtccaagagccttctaaagattctgggcaagaagaacgaggcgcccccggacaacaag 2123 111l 11ll I Illlili llll11 lll1l111 l11 lll11l1l1ll111l1illitl1illl1i 24P4C12v. 9: 2070 atgtccaagagccttctaaagattctgggcaagaagaacgaggcgcccccggacaacaag 2129 24P4C12v.1: 2124 aagaggaagaagtgacagctccggccctgatccaggactgcaccccacccccaccgtcca 2183 11111lt 1i11l11 ill11l1ll ll1|1||1il1Ill1l lI ill ll1ll1l|1||1lil1 24P4C12v.9: 2130 aagaggaagaagtgacagctccggccctgatccaggactgcaccccacccccaccgtcca 2189 24P4C12v.1: 2184 gccatccaacctcacttcgccttacaggtctccattttgtggtaaaaaaaggttttaggc 2243 24P4C12v.9: 2190 gccatccaacctcacttcgccttacaggtctccattttgtggtaaaaaaaggttttaggc 2249 24P4C12v.1: 2244 caggcgccgtggctcacgcctgtaatccaacactttgagaggctgaggcgggcggatcac 2303 1i11I1l11I11il11lll11l11 I iIlIllilIlliliIllilIIl1111i 24P4C12v.9: 2250 caggcgccgtggctcacgcctgtaatccaacactttgagaggctgaggcgggcggatcac 2309 221 24P4C12v.1: 2304 ctgagtcaggagttcgagaccagcctggccaacatggtgaaacctccgtctctattaaaa 2363 |||Illil Ii11 I li 11lil1Il11111111 IliI|Il I|il|1||1|||I111ll1 24P4C12v.9: 2310 ctgagtcaggagttcgagaccagcctggccaacatggtgaaacctccgtctctattaaaa 2369 24P4C12v.1: 2364 atacaaaaattagccgagagtggtggcatgcacctgtcatcccagctactcgggaggctg 2423 1| ||1|111 1 Il li i l| | ||i 1 1 1 1 I||||||lill|1|||||1 l iIlI 24P4C12v.9: 2370 atacaaaaattagccgagagtggtggcatgcacctgtcatcccagctactcgggaggctg 2429 24P4C12v.1: 2424 aggcaggagaatcgcttgaacccgggaggcagaggttgcagtgagccgagatcgcgccac 2483 1111ll11 I I1111li||||||||||||||||i1ll I1I|1|1||1l1I liil 1ll11|| 24P4C12v.9: 2430 aggcaggagaatcgcttgaacccgggaggcagaggttgcagtgagccgagatcgcgccac 2489 24P4C12v.1: 2464 tgcactccaacctgggtgacagactctgtctccaaaacaaaacaaacaaacaaaaagatt 2543 1ill1ll1lll1ll1llll1l111l1lll111l1llill1l1l11il11l1llll1illl1 24P4C12v. 9: 2490 tgcactccaacctgggtgacagactctgtctccaaaacaaaacaaacaaacaaaaagatt 2549 24P4C12v.1: 2544 ttattaaagatattttgttaactcagtaaaaaaaaaaaaaaaaa 2587 111111 IIII iii I 1111111111 I 11||||11 11111111111I I 24P4C12v.9; 2550 ttattaaagatattttgttaactcagtaaaaaaaaaaaaaaaaa 2593 Table LXII. Peptide sequences of protein coded by 24P4C12 v.9 (SEQ ID NO: 109) MGGKQRDEDD EAYGKPVKYD PSFRGPIKNR SCTDVICCVL FLLFILGYIV VGIVAWLYGD 60 PRQVLYPRNS TGAYCGMGEN KDKPYLLYFN IFSCILSSNI ISVAENGLQC PTPQVCVSSC 120 PEDPWTVGKN EFSQTVGEVF YTKNRNFCLP GVPWNMTVIT SLQQELCPSF LLPSAPALGR 180 CFPWTNVTPP ALPGITNDTT IQQGISGLID SLNARDISVK IFEDFAQSWY WILVALGVAL 240 VLSLLFILLL RLVAGPLVLV LILGVLGVLA YGIYYCWEEY RVLRDKGASI SQLGErTNLS 300 AYQSVQETWL AALIVLAVLE AILLLMLIFL RORIRIAIAL LKEASKAVGQ MNSTMFYPLV 360 TFVLLLICIA YWAMTALYPL PTQPATLGYV LWASNISSPG CEKVPINTSC NPTAHLVNSS 420 CPGLMCVFQG YSSKGLIQRS VFNLOIYGVL GLEWTLNWVL ALGQCVLAGA FASFYWAFHK 480 PQDIPTFPLI SAFIRTLRYH TGSLAFGALI LTLVQIARVI LEYIDHKLRG VQNPVARCIM 540 CCFKCCLWCL EKFIKFLNRN AYIMIAIYGK NFCVSAKNAF MLLMRNIVRV VVLDKVTDLL 600 LFFGKLLVVG GVGVLSFFFF SGRIPGLGKD FKSPHLNYYW LPIMTSILGA YVIASGFFSV 660 FGMCVDTLFL CFLEDLERNN GSLDRPYYMS KSLLKILGKK NEAPPDNKKR KK 712 Table LXIII. Amino acid sequence alignment of 24P4C12v. 1 v.1 (SEQ ID NO: 110) and 24P4C12 v. 9 (SEQ ID NO: 111) Score - 1424 bits (3686), Expect - 0.OIdentities = 704/713 (98%), Positives = 705/713 (98%), Gaps - 4/713 (0%) 24P4C12v.1: 1 MGGKORDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 60 MGGKQRDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 24P4C12v.9: 1 MGGKQRDEDDEAYGKPVKYDPSFRGPIKNRSCTDVICCVLFLLFILGYIVVGIVAWLYGD 60 24P4C12v.1: 61 PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPOVCVSSC 120 PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLQCPTPQVCVSSC 24P4C12v.9: 61 PRQVLYPRNSTGAYCGMGENKDKPYLLYFNIFSCILSSNIISVAENGLOCPTPQVCVSSC 120 24P4C12v.1: 121 PEDPWTVGKNEFSQTVGEVFYTONRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGR, 180 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGR 24P4C12v.9: 121 PEDPWTVGKNEFSQTVGEVFYTKNRNFCLPGVPWNMTVITSLQQELCPSFLLPSAPALGR 180 24P4C12v.1: 181 CFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFASWYWILVALGVAL 240 CFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIEDFAQSWYWILVALGVAL 24P4C12v.9: 181 CFPWTNVTPPALPGITNDTTIQQGISGLIDSLNARDISVKIFEDFAQSWYWILVALGVAL 240 24P4C12v.1: 241 VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQMGFTTNLS 300 VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFrTNLS 24P4C12v.9: 241 VLSLLFILLLRLVAGPLVLVLILGVLGVLAYGIYYCWEEYRVLRDKGASISQLGFTTNLS 300 24P4C12v.1: 301 AYQSVQETWLAALIVLAVLEAILLLMLIFLRQRIRIAIALLKEASKAVGQMSTMFYPLV 360 AYQSVOETWLAALIVLAVLEAILLLMLIFLRQRIRIAIALLKEASKAVGQMSTMFYPLV 24P4C12v.9: 301 AYQSVOETWLAALIVLAVLEAILLIMLIFLRQRIRIAIALLKEASKAVGQMSTMFYPLV 360 222 24P4C12v.1: 361 TFVLLLICIAYWAMTALYLATSGQPQ---YVLWASNISSPGCBKVPINTSCNPTAHLVNS 417 TFVLLLICIAYWANTALY + QP. YVLWASNISSPGCEKVPINTSCNPTAHLVNS 24P4C12v.9: 361 TEVLLLICIAYWAMTALYPLPT-QPATLGYVLWASNISSPGCEKVPINTSCNPTAHLVNS 419 24P4C12v.1: 418 SCPGLMCVFQGYSSKGLIQRSVFNLQIYGVLGLWTLNWVLALGQCVLAGAFASFYWAFH 477 SCPGLMCVFQGYSSKGLIQRSVFNLQIYGVLGLEWTLNWVLALGOCVLAGAFASFYWAFH 24P4Cl2v.9: 420 SCPGLMCVFQGYSSKGLIQRSVFNLQIYGVLGLEWTLNWVLALGQCVLAGAFASFYWAFH 479 24P4C12v.1: 478 KPQDIPTFPLISAFIRTLRYHTGSLAGALILTLVIARVILEYIDHKLRGVNPVARCI 537 KPQDIPTFPLISAFIRTLRYHTGSLAEGALILTLVQIARVILEYIDHKLRGVQNPVARCI 24P4C12v.9: 480 KPQDIPTFPLISAFIRTLRYHTGSLAFGALILTLVQIARVILEYIDHKLRGVQNPVARCI 539 24P4Cl2v.1: 538 MCCFKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAFMLLMRNIVRVVVLDKVTDL 597 MCCFKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAKNAFMLL24RNIVRVVVLDKVTDL 24P4C12v.9: 540 MCCFKCCLWCLEKFIKFLNRNAYIMIAIYGKNFCVSAkNAEMLLMRNIVRVVVLDKVTDL 599 24P4Cl2v.1: 598 LLFFGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMTSILGAYVIASGFFS 657 LLFEGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMTSILGAYVIASGFFS 24P4Cl2v.9: 600 LLFFGKLLVVGGVGVLSFFFFSGRIPGLGKDFKSPHLNYYWLPIMTSILGAYVIASGFFS 659 24P4C12v.1: 658 VFGMCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKRKK 710 -VFGMCVDTLFLCFLEDLERNNGSLDRPYYMSKSLLKILGKKNEAPPDNKKRKK 24P4Cl2v.9: 660 VFGMCVDTLFLCFLEDLERNGSLDRPYYMSKSLLKILGKKNEAPPDNKKRKK 712 223

Claims (20)

1. A method of identifying or isolating a peptide useful as a vaccine to elicit an immune response in a population of subjects to a protein comprising an amino acid sequence as set forth in SEQ ID NO:20, SEQ ID NO:21, SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, SEQ ID NO:25 or SEQ ID NO:26, said method comprises identifying an HLA supertype as being characteristic of said population and for which binding of epitopes of said vaccine is desired wherein said HLA supertype comprises two or more alleles of HLA types selected from the group consisting of A3, A2, B7, Al, B35 and A24; selecting from the peptides listed in Tables VIII-XLIX any epitopes of SEQ ID NO:20, SEQ ID NO:21, SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, SEQ ID NO:25 or SEQ ID NO:26 disclosed to bind alleles of said identified HLA supertype; experimentally assessing the ability of said peptides to bind to at least one allele of said HLA supertype and identifying or isolating a peptide that binds with an IC 50 equal to, or less than, 500 nanomolar to said HLA supertype allele, wherein said isolated peptide is useful as said vaccine.

2. The method according to claim 1, wherein peptides are selected that bind within IC 50 equal to, or less than, 500 nanomolar to three alleles of said HLA supertype.

3. A peptide isolated by performing the method of claim 1 or 2.

4. Use of the peptide according to claim 3 for the preparation of a vaccine to elicit an immune response in a population of subjects to a protein comprising an amino acid sequence of SEQ ID NO:20, SEQ ID NO:21, SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, SEQ ID NO:25 or SEQ ID NO:26.

5. The use of claim 4, wherein said immune response is a CTL response.

6. The use of claim 4, wherein the immune response is a humoral response. 224

7. A vaccine that comprises 3 or more peptides isolated by performing the method of claim 1 or 2.

8. Use of the vaccine according to claim 7 for the treatment of cancer in a subject.

9. A method to treat cancer in a subject, wherein said method comprises administering to said subject an effective amount of the vaccine of claim 7.

10. A recombinant expression vector comprising at least one nucleotide sequence encoding at least one peptide isolated by performing the method of claim 1 or 2, wherein said nucleotide sequence is operably linked to control sequences for its expression.

11. A recombinant expression vector comprising at least two nucleotide sequences encoding at least two peptides isolated by performing the method of claim 1 or 2, wherein said nucleotide sequences are operably linked to control sequences for their expression.

12. A recombinant expression vector comprising at least three nucleotide sequences encoding at least three peptides isolated by performing the method of claim 1 or 2, wherein said nucleotide sequences are operably linked to control sequences for their expression.

13. A method to treat cancer in a subject comprising administering to said subject an effective amount of the expression vector according to any one of claims 10 to 12.

14. Use of the recombinant expression vector according to any one of claims 10 to 12 for the treatment of cancer in a subject.

15. Use of the recombinant expression vector according to any one of claims 10 to 12 in the manufacture of a medicament for the treatment of cancer in a subject.

16. A pharmaceutical composition for the treatment of cancer comprising an antisense polynucleotide complementary to an mRNA encoding a protein of SEQ 225 ID NO:20, SEQ ID NO:21, SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, SEQ ID NO:25 or SEQ ID NO:26, and a physiologically acceptable carrier.

17. A pharmaceutical composition for the treatment of cancer comprising a ribozyme capable of cleaving an mRNA encoding a protein of SEQ ID NO:20, SEQ ID NO:21, SEQ ID NO:22, SEQ ID NO:23, SEQ ID NO:24, SEQ ID NO:25 or SEQ ID NO:26, and a physiologically acceptable carrier.

18. A method to treat cancer in a subject comprising administering to said subject an effective amount of pharmaceutical composition according to claim 16 or 17.

19. Use of the pharmaceutical composition according to claim 16 or 17 for the treatment of cancer.

20. The method according to any one of claims 1, 2, 9, 13 or 18, or the peptide of claim 3, or the use according to any one of claims 4 to 6, 8, 14, 15 or 19, or the vaccine of claim 7, or the recombinant expression vector according to any one of claims 10 to 12, or the pharmaceutical composition according the claims 16 or 17 substantially as described herein with reference to any one or more of the examples and/or drawings. DATED this TWENTY-THIRD day of DECEMBER 2008 Agensys, Inc. Patent Attorneys for the Applicant: F.B. RICE & CO. 226