CN1286973C - 一种组蛋白甲基转移酶及其制备方法 - Google Patents
一种组蛋白甲基转移酶及其制备方法 Download PDFInfo
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- CN1286973C CN1286973C CN 200410017613 CN200410017613A CN1286973C CN 1286973 C CN1286973 C CN 1286973C CN 200410017613 CN200410017613 CN 200410017613 CN 200410017613 A CN200410017613 A CN 200410017613A CN 1286973 C CN1286973 C CN 1286973C
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Abstract
本发明提供了一种新的组蛋白甲基转移酶-HSPC069SET蛋白,编码HSPC069SET蛋白的多核苷酸和经重组技术产生这种HSPC069SET蛋白的方法。本发明还公开了编码这种HSPC069SET蛋白的多核苷酸的用途。HSPC069SET蛋白具有组蛋白甲基转移功能。
Description
技术领域
本发明属于分子生物学领域,具体地说,本发明涉及新的编码人组蛋白甲基转移酶HSPC069SET的多核苷酸,以及此多核苷酸编码的多肽。本发明还涉及此多核苷酸和多肽的用途和制备。
背景技术
组蛋白的翻译后修饰对于染色体结构和基因转录活性的调控有重要意义。这些修饰主要包括乙酰化、磷酸化、甲基化、ADP核糖基化和泛素化。
近两年来,组蛋白甲基化的功能研究取得了很大的突破,特别是对于组蛋白H3的甲基化的研究。例如,组蛋白H3第9位赖氨酸的甲基化与基因的失活相关连(
Science.2001,293:1150-5);而组蛋白H3第4位赖氨酸的甲基化与基因的激活相关连(
Science.2001,293:2453-5)。在组成型异染色质区域,K9甲基化的组蛋白H3可以募集异染色质蛋白HP1(
Nature.2001,410:116-20):而H3-K4的甲基化广泛分布在常染色质(
Nat Genet.2002,30:73-6),它可以阻止NuRD复合体结合组蛋白H3的氨基端,还可以抑制H3-K9的甲基化,从而保持基因的转录活性(
Genes Dev.2002,16:479-89)。
组蛋白的甲基化都是由组蛋白甲基转移酶完成的。目前从酵母到人的多个物种当中已经分离到了十几个组蛋白H3甲基转移酶。他们的共同特点是都含有SET结构域,而且具有组蛋白甲基化位点的选择性。它们都可以调控基因的转录活性:一方面,是通过被修饰的组蛋白来起作用;另一方面,它们本身往往是包含在一个蛋白复合体中,这样可以使它们精确地定位在染色体的某些区段,而且可以在一个信号传导的网络中行使功能。例如,Rb蛋白可以募集H3-K9特异性的组蛋白甲基转移酶Suv39h1和HP1到细胞周期蛋白E基因的启动子区域,甲基化此处的组蛋白H3,从而抑制细胞周期蛋白E基因的转录。如果SUV39基因突变,则Rb蛋白不能抑制细胞周期蛋白E基因的转录(
Nature.2001,412:561-5)。
最近的一些研究证实,组蛋白甲基转移酶的突变会导致生物体功能的某些缺陷。Suv39h缺失的小鼠染色体不稳定,细胞内染色体个数不规则,发生肿瘤的几率升高,生存能力严重降低(
Cell.2001,107:323-37);另一个组蛋白H3甲基转移酶G9a缺失的小鼠胚胎发育迟缓而且早期致死(
Genes Dev.2002,16:1779-91)。这都表明组蛋白甲基转移酶对生物体的发育有重要的调控作用。
另外,组蛋白甲基转移酶还与人类疾病有关。位于染色体11q23的MLL基因的异位常见于多种急性白血病患者,该基因3′端含有SET结构域,具有H3-K4甲基转移酶活性,可以激活Hox a9基因的表达,异位后表达的融合蛋白丢失了SET结构域,从而失去了甲基转移酶活性,这种机制可能与白血病的发病有关(
Mol Cell.2002,10:1107-17)。
目前发现的组蛋白甲基转移酶在功能上并不是重叠的。首先,它们可以特异性地修饰组蛋白的不同位点,已知组蛋白H3上可以被甲基化的赖氨酸有K4、K9、K27、K36、K79,其中K27、K36甲基化的功能尚不清楚。其次,甲基化相同位点的甲基转移酶往往在亚细胞定位上有所差异,而且处于不同的蛋白复合体中,提示它们具有不同的功能。
综上所述,鉴于组蛋白甲基转移酶在重要作用,因此,本领域迫切需要开发新的组蛋白甲基转移酶。
发明内容
本发明的目的是提供一种新的人组蛋白甲基转移酶(HSPC069SET蛋白)以及其片段、类似物和衍生物。
本发明的另一目的是提供编码这些多肽的多核苷酸。
本发明的另一目的是提供生产这些多肽的方法以及该多肽和编码序列的用途。
在本发明的第一方面,提供新颖的分离出的HSPC069SET多肽,它包括:具有SEQID NO:2氨基酸序列的多肽、或其保守性变异多肽、或其活性片段、或其活性衍生物,附加条件是所述的多肽不具有SEQ ID NO:6所示的氨基酸序列。
较佳地,该多肽选自下组:
(a)具有SEQ ID NO:2氨基酸序列的多肽;
(b)将SEQ ID NO:2氨基酸序列经过一个或多个氨基酸残基的取代、缺失或添加而形成的,且具有组蛋白甲基转移功能的由(a)衍生的多肽。
更佳地,该多肽是具有SEQ ID NO:2或4氨基酸序列的多肽。
在本发明的第二方面,提供编码分离的这些多肽的多核苷酸,该多核苷酸包含一核苷酸序列,该核苷酸序列与选自下组的一种核苷酸序列有至少70%相同性:(a)编码上述人HSPC069SET多肽的多核苷酸;和(b)与多核苷酸(a)互补的多核苷酸。较佳地,该多核苷酸编码具有SEQ ID NO:2或4所示氨基酸序列的多肽。更佳地,该多核苷酸的序列是选自下组的一种:(a)具有SEQ ID NO:1中72-3704位的序列;(b)具有SEQ ID NO:1中1-6731位的序列;或(c)具有SEQ ID NO:3中1-1614位的序列。
在本发明的第三方面,提供了含有上述多核苷酸的载体,以及被该载体转化或转导的宿主细胞或者被上述多核苷酸直接转化或转导的宿主细胞。
在本发明的第四方面,提供了制备具有人HSPC069SET蛋白活性的多肽的方法,该方法包含:(a)在适合表达人HSPC069SET蛋白的条件下,培养上述被转化或转导的宿主细胞;(b)从培养物中分离出具有人HSPC069SET蛋白活性的多肽。
在本发明的第五方面,提供了与上述的人HSPC069SET多肽特异性结合的抗体。
在本发明的第六方面,提供了模拟、促进、拮抗人HSPC069SET多肽活性的化合物,以及抑制人HSPC069SET多肽的表达的化合物。还提供了筛选和/或制备这些化合物的方法。较佳地,该化合物是人HSPC069SET多肽的编码序列或其片段的反义序列。
在本发明的第七方面,提供了检测样品中是否存在HSPC069SET蛋白的方法,它包括:将样品与HSPC069SET蛋白的特异性抗体接触,观察是否形成抗体复合物,形成了抗体复合物就表示样品中存在HSPC069SET蛋白。
在本发明的第八方面,提供了一种检测与人HSPC069SET多肽异常表达相关的疾病或疾病易感性的方法,该方法包括:检测编码所述多肽的核酸序列中是否存在突变。
在本发明的第九方面,提供了本发明多肽和编码序列的用途。例如本发明多肽可被用于筛选促进人HSPC069SET多肽活性的激动剂,或者筛选抑制人HSPC069SET多肽活性的拮抗剂、或者被用于肽指纹图谱鉴定。本发明的人HSPC069SET蛋白的编码序列或其片段,可被作为引物用于PCR扩增反应,或者作为探针用于杂交反应,或者用于制造基因芯片或微阵列。
在本发明的第十方面,提供了一种具有组蛋白甲基转移酶组合物,它含有安全有效量的本发明的人HSPC069SET或HSPC069多肽以及可接受的载体。
本发明的其它方面由于本文的技术的公开,对本领域的技术人员而言是显而易见的。
附图说明
下列附图用于说明本发明的具体实施方案,而不用于限定由权利要求书所界定的本发明范围。
图1显示了HSPC069SET及其突变体蛋白的酶活性。图中的HSPC069为GST-HSPC069SET融合蛋白。
图2显示了HSPC069SET修饰组蛋白的位点特异性。
具体实施方式
本发明人经过广泛而深入的研究,先从CD34+造血干/祖细胞中克隆出的一种功能未知的蛋白HSPC069(SEQ ID NO:5和6,ORF位于72-6254位),然后又首次分离获得了一种新的组蛋白甲基转移酶HSPC069SET(SEQ ID NO:1和2),该酶具有组蛋白甲基转移的活性,不仅可以特异地甲基化组蛋白H3第36位的赖氨酸,还可使其自身甲基化。在此基础上完成了本发明。
在本发明中,术语“HSPC069SET蛋白”、“HSPC069SET多肽”或“组蛋白甲基转移酶HSPC069SET”可互换使用,都指具有人组蛋白甲基转移酶HSPC069SET氨基酸序列(SEQ ID NO:2)的蛋白或多肽。它们包括含有或不含起始甲硫氨酸的组蛋白甲基转移酶HSPC069SET。还包括具有组蛋白甲基转移酶活性且含有衍生自SEQ ID NO:2的SET结构域的活性片段和融合蛋白。
如本文所用,“分离的”是指物质从其原始环境中分离出来(如果是天然的物质,原始环境即是天然环境)。如活体细胞内的天然状态下的多聚核苷酸和多肽是没有分离纯化的,但同样的多聚核苷酸或多肽如从天然状态中同存在的其他物质中分开,则为分离纯化的。
如本文所用,“分离的HSPC069SET蛋白或多肽”是指HSPC069SET多肽基本上不含天然与其相关的其它蛋白、脂类、糖类或其它物质。本领域的技术人员能用标准的蛋白质纯化技术纯化HSPC069SET蛋白。基本上纯的多肽在非还原聚丙烯酰胺凝胶上能产生单一的主带。HSPC069SET多肽的纯度能用氨基酸序列分析。
本发明的多肽可以是重组多肽、天然多肽、合成多肽,优选重组多肽。本发明的多肽可以是天然纯化的产物,或是化学合成的产物,或使用重组技术从原核或真核宿主(例如,细菌、酵母、高等植物、昆虫和哺乳动物细胞)中产生。根据重组生产方案所用的宿主,本发明的多肽可以是糖基化的,或可以是非糖基化的。本发明的多肽还可包括或不包括起始的甲硫氨酸残基。
本发明还包括人HSPC069SET蛋白的片段、衍生物和类似物。如本文所用,术语“片段”、“衍生物”和“类似物”是指基本上保持本发明的天然人HSPC069SET蛋白相同的生物学功能或活性的多肽。本发明的多肽片段、衍生物或类似物可以是(i)有一个或多个保守或非保守性氨基酸残基(优选保守性氨基酸残基)被取代的多肽,而这样的取代的氨基酸残基可以是也可以不是由遗传密码编码的,或(ii)在一个或多个氨基酸残基中具有取代基团的多肽,或(iii)成熟多肽与另一个化合物(比如延长多肽半衰期的化合物,例如聚乙二醇)融合所形成的多肽,或(iv)附加的氨基酸序列融合到此多肽序列而形成的多肽(如前导序列或分泌序列或用来纯化此多肽的序列或蛋白原序列,或与抗原IgG片段的形成的融合蛋白)。根据本文的教导,这些片段、衍生物和类似物属于本领域熟练技术人员公知的范围。
在本发明中,术语“人HSPC069SET多肽”指具有人HSPC069SET蛋白活性的SEQID NO:2序列的多肽。该术语还包括具有与人HSPC069SET蛋白相同功能的、SEQ IDNO:2序列的变异形式。这些变异形式包括(但并不限于):一个或多个(通常为1-50个,较佳地1-30个,更佳地1-20个,最佳地1-10个)氨基酸的缺失、插入和/或取代,以及在C末端和/或N末端添加一个或数个(通常为20个以内,较佳地为10个以内,更佳地为5个以内)氨基酸。例如,在本领域中,用性能相近或相似的氨基酸进行取代时,通常不会改变蛋白质的功能。又比如,在C末端和/或N末端添加一个或数个氨基酸通常也不会改变蛋白质的功能。该术语还包括人HSPC069SET蛋白的活性片段和活性衍生物。
该多肽的变异形式包括:同源序列、保守性变异体、等位变异体、天然突变体、诱导突变体、在高或低的严紧度条件下能与人HSPC069SET DNA杂交的DNA所编码的蛋白、以及利用抗人HSPC069SET多肽的抗血清获得的多肽或蛋白。本发明还提供了其他多肽,如包含人HSPC069SET多肽或其片段的融合蛋白(如SEQ ID NO:4所示的融合蛋白)。除了几乎全长的多肽外,本发明还包括了人HSPC069SET多肽的可溶性片段。通常,该片段具有人HSPC069SET多肽序列的至少约10个连续氨基酸,通常至少约30个连续氨基酸,较佳地至少约50个连续氨基酸,更佳地至少约80个连续氨基酸,最佳地至少约100个连续氨基酸。
发明还提供人HSPC069SET蛋白或多肽的类似物。这些类似物与天然人HSPC069SET多肽的差别可以是氨基酸序列上的差异,也可以是不影响序列的修饰形式上的差异,或者兼而有之。这些多肽包括天然或诱导的遗传变异体。诱导变异体可以通过各种技术得到,如通过辐射或暴露于诱变剂而产生随机诱变,还可通过定点诱变法或其他已知分子生物学的技术。类似物还包括具有不同于天然L-氨基酸的残基(如D-氨基酸)的类似物,以及具有非天然存在的或合成的氨基酸(如β、γ-氨基酸)的类似物。应理解,本发明的多肽并不限于上述例举的代表性的多肽。
修饰(通常不改变一级结构)形式包括:体内或体外的多肽的化学衍生形式如乙酰化或羧基化。修饰还包括糖基化,如那些在多肽的合成和加工中或进一步加工步骤中进行糖基化修饰而产生的多肽。这种修饰可以通过将多肽暴露于进行糖基化的酶(如哺乳动物的糖基化酶或去糖基化酶)而完成。修饰形式还包括具有磷酸化氨基酸残基(如磷酸酪氨酸,磷酸丝氨酸,磷酸苏氨酸)的序列。还包括被修饰从而提高了其抗蛋白水解性能或优化了溶解性能的多肽。
在本发明中,“人HSPC069SET蛋白保守性变异多肽”指与SEQ ID NO:2的氨基酸序列相比,有至多10个,较佳地至多8个,更佳地至多5个,最佳地至多3个氨基酸被性质相似或相近的氨基酸所替换而形成多肽。这些保守性变异多肽最好根据表1进行氨基酸替换而产生。
表1
最初的残基 | 代表性的取代 | 优选的取代 |
Ala(A) | Val;Leu;Ile | Val |
Arg(R) | Lys;Gln;Asn | Lys |
Asn(N) | Gln;His;Lys;Arg | Gln |
Asp(D) | Glu | Glu |
Cys(C) | Ser | Ser |
Gln(Q) | Asn | Asn |
Glu(E) | Asp | Asp |
Gly(G) | Pro;Ala | Ala |
His(H) | Asn;Gln;Lys;Arg | Arg |
Ile(I) | Leu;Val;Met;Ala;Phe | Leu |
Leu(L) | Ile;Val;Met;Ala;Phe | Ile |
Lys(K) | Arg;Gln;Asn | Arg |
Met(M) | Leu;Phe;Ile | Leu |
Phe(F) | Leu;Val;Ile;Ala;Tyr | Leu |
Pro(P) | Ala | Ala |
Ser(S) | Thr | Thr |
Thr(T) | Ser | Ser |
Trp(W) | Tyr;Phe | Tyr |
Tyr(Y) | Trp;Phe;Thr;Ser | Phe |
Val(V) | Ile;Leu;Met;Phe;Ala | Leu |
本发明的多核苷酸可以是DNA形式或RNA形式。DNA形式包括cDNA、基因组DNA或人工合成的DNA。DNA可以是单链的或是双链的。DNA可以是编码链或非编码链。编码成熟多肽的编码区序列可以与SEQ ID NO:1所示的编码区序列相同或者是简并的变异体。如本文所用,“简并的变异体”在本发明中是指编码具有SEQ ID NO:2的蛋白质,但与SEQ ID NO:1所示的编码区序列有差别的核酸序列。
编码SEQ ID NO:2的成熟多肽的多核苷酸包括:只编码成熟多肽的编码序列;成熟多肽的编码序列和各种附加编码序列;成熟多肽的编码序列(和任选的附加编码序列)以及非编码序列。
术语“编码多肽的多核苷酸”可以是包括编码此多肽的多核苷酸,也可以是还包括附加编码和/或非编码序列的多核苷酸。
本发明还涉及上述多核苷酸的变异体,其编码与本发明有相同的氨基酸序列的多肽或多肽的片段、类似物和衍生物。此多核苷酸的变异体可以是天然发生的等位变异体或非天然发生的变异体。这些核苷酸变异体包括取代变异体、缺失变异体和插入变异体。如本领域所知的,等位变异体是一个多核苷酸的替换形式,它可能是一个或多个核苷酸的取代、缺失或插入,但不会从实质上改变其编码的多肽的功能。
本发明还涉及与上述的序列杂交且两个序列之间具有至少50%,较佳地至少70%,更佳地至少80%相同性的多核苷酸。本发明特别涉及在严格条件下与本发明所述多核苷酸可杂交的多核苷酸。在本发明中,“严格条件”是指:(1)在较低离子强度和较高温度下的杂交和洗脱,如0.2×SSC,0.1%SDS,60℃;或(2)杂交时加有变性剂,如50%(v/v)甲酰胺,0.1%小牛血清/0.1% Ficoll,42℃等;或(3)仅在两条序列之间的相同性至少在90%以上,更好是95%以上时才发生杂交。并且,可杂交的多核苷酸编码的多肽与SEQ ID NO:2所示的成熟多肽有相同的生物学功能和活性。
本发明还涉及与上述的序列杂交的核酸片段。如本文所用,“核酸片段”的长度至少含15个核苷酸,较好是至少30个核苷酸,更好是至少50个核苷酸,最好是至少100个核苷酸以上。核酸片段可用于核酸的扩增技术(如PCR)以确定和/或分离编码HSPC069SET蛋白的多聚核苷酸。
本发明中的多肽和多核苷酸优选以分离的形式提供,更佳地被纯化至均质。
本发明的人HSPC069SET核苷酸全长序列或其片段通常可以用PCR扩增法、重组法或人工合成的方法获得。对于PCR扩增法,可根据本发明所公开的有关核苷酸序列,尤其是开放阅读框序列来设计引物,并用市售的cDNA库或按本领域技术人员已知的常规方法所制备的cDNA库作为模板,扩增而得有关序列。当序列较长时,常常需要进行两次或多次PCR扩增,然后再将各次扩增出的片段按正确次序拼接在一起。
一旦获得了有关的序列,就可以用重组法来大批量地获得有关序列。这通常是将其克隆入载体,再转入细胞,然后通过常规方法从增殖后的宿主细胞中分离得到有关序列。
此外,还可用人工合成的方法来合成有关序列,尤其是片段长度较短时。通常,通过先合成多个小片段,然后再进行连接可获得序列很长的片段。
目前,已经可以完全通过化学合成来得到编码本发明蛋白(或其片段,或其衍生物)的DNA序列。然后可将该DNA序列引入本领域中已知的各种现有的DNA分子(或如载体)和细胞中。此外,还可通过化学合成将突变引入本发明蛋白序列中。
应用PCR技术扩增DNA/RNA的方法(Saiki,et al.Science 1985;230:1350-1354)被优选用于获得本发明的基因。特别是很难从文库中得到全长的cDNA时,可优选使用RACE法(RACE-cDNA末端快速扩增法),用于PCR的引物可根据本文所公开的本发明的序列信息适当地选择,并可用常规方法合成。可用常规方法如通过凝胶电泳分离和纯化扩增的DNA/RNA片段。
本发明也涉及包含本发明的多核苷酸的载体,以及用本发明的载体或HSPC069SET蛋白编码序列经基因工程产生的宿主细胞,以及经重组技术产生本发明所述多肽的方法。
通过常规的重组DNA技术(Science,1984;224:1431),可利用本发明的多聚核苷酸序列可用来表达或生产重组的HSPC069SET多肽。一般来说有以下步骤:
(1).用本发明的编码人HSPC069SET多肽的多核苷酸(或变异体),或用含有该多核苷酸的重组表达载体转化或转导合适的宿主细胞;
(2).在合适的培养基中培养的宿主细胞;
(3).从培养基或细胞中分离、纯化蛋白质。
本发明中,人HSPC069SET多核苷酸序列可插入到重组表达载体中。术语“重组表达载体”指本领域熟知的细菌质粒、噬菌体、酵母质粒、植物细胞病毒、哺乳动物细胞病毒如腺病毒、逆转录病毒或其他载体。在本发明中适用的载体包括但不限于:在细菌中表达的基于T7的表达载体(Rosenberg,et al.Gene,1987,56:125);在哺乳动物细胞中表达的pMSXND表达载体(Lee and Nathans,J Bio Chem.263:3521,1988)和在昆虫细胞中表达的来源于杆状病毒的载体。总之,只要能在宿主体内复制和稳定,任何质粒和载体都可以用。表达载体的一个重要特征是通常含有复制起点、启动子、标记基因和翻译控制元件。
本领域的技术人员熟知的方法能用于构建含人HSPC069SET编码DNA序列和合适的转录/翻译控制信号的表达载体。这些方法包括体外重组DNA技术、DNA合成技术、体内重组技术等(Sambroook,et al.Molecular Cloning,a Laboratory Manual,coldSpring Harbor Laboratory.New York,1989)。所述的DNA序列可有效连接到表达载体中的适当启动子上,以指导mRNA合成。这些启动子的代表性例子有:大肠杆菌的lac或trp启动子;λ噬菌体PL启动子;真核启动子包括CMV立即早期启动子、HSV胸苷激酶启动子、早期和晚期SV40启动子、反转录病毒的LTRs和其他一些已知的可控制基因在原核或真核细胞或其病毒中表达的启动子。表达载体还包括翻译起始用的核糖体结合位点和转录终止子。
此外,表达载体优选地包含一个或多个选择性标记基因,以提供用于选择转化的宿主细胞的表型性状,如真核细胞培养用的二氢叶酸还原酶、新霉素抗性以及绿色荧光蛋白(GFP),或用于大肠杆菌的四环素或氨苄青霉素抗性。
包含上述的适当DNA序列以及适当启动子或者控制序列的载体,可以用于转化适当的宿主细胞,以使其能够表达蛋白质。
宿主细胞可以是原核细胞,如细菌细胞;或是低等真核细胞,如酵母细胞;或是高等真核细胞,如哺乳动物细胞。代表性例子有:大肠杆菌,链霉菌属;鼠伤寒沙门氏菌的细菌细胞;真菌细胞如酵母;植物细胞;果蝇S2或Sf9的昆虫细胞;CHO、COS、293细胞、或Bowes黑素瘤细胞的动物细胞等。
本发明的多核苷酸在高等真核细胞中表达时,如果在载体中插入增强子序列时将会使转录得到增强。增强子是DNA的顺式作用因子,通常大约有10到300个碱基对,作用于启动子以增强基因的转录。可举的例子包括在复制起始点晚期一侧的100到270个碱基对的SV40增强子、在复制起始点晚期一侧的多瘤增强子以及腺病毒增强子等。
本领域一般技术人员都清楚如何选择适当的载体、启动子、增强子和宿主细胞。
用重组DNA转化宿主细胞可用本领域技术人员熟知的常规技术进行。当宿主为原核生物如大肠杆菌时,能吸收DNA的感受态细胞可在指数生长期后收获,用CaCl2法处理,所用的步骤在本领域众所周知。另一种方法是使用MgCl2。如果需要,转化也可用电穿孔的方法进行。当宿主是真核生物,可选用如下的DNA转染方法:磷酸钙共沉淀法,常规机械方法如显微注射、电穿孔、脂质体包装等。
获得的转化子可以用常规方法培养,表达本发明的基因所编码的多肽。根据所用的宿主细胞,培养中所用的培养基可选自各种常规培养基。在适于宿主细胞生长的条件下进行培养。当宿主细胞生长到适当的细胞密度后,用合适的方法(如温度转换或化学诱导)诱导选择的启动子,将细胞再培养一段时间。
在上面的方法中的重组多肽可在细胞内、或在细胞膜上表达、或分泌到细胞外。如果需要,可利用其物理的、化学的和其它特性通过各种分离方法分离和纯化重组的蛋白。这些方法是本领域技术人员所熟知的。这些方法的例子包括但并不限于:常规的复性处理、用蛋白沉淀剂处理(盐析方法)、离心、渗透破菌、超处理、超离心、分子筛层析(凝胶过滤)、吸附层析、离子交换层析、高效液相层析(HPLC)和其它各种液相层析技术及这些方法的结合。
重组的人HSPC069SET蛋白或多肽有多方面的用途。这些用途包括(但不限于):直接做为药物治疗HSPC069SET蛋白功能低下或丧失所致的疾病,和用于筛选促进或对抗HSPC069SET蛋白功能的抗体、多肽或其它配体。用表达的重组人HSPC069SET蛋白筛选多肽库可用于寻找有治疗价值的能抑制或刺激人HSPC069SET蛋白功能的多肽分子。
另一方面,本发明还包括对人HSPC069SET DNA或是其片段编码的多肽具有特异性的多克隆抗体和单克隆抗体,尤其是单克隆抗体。这里,“特异性”是指抗体能结合于人HSPC069SET基因产物或片段。较佳地,指那些能与人HSPC069SET基因产物或片段结合但不识别和结合于其它非相关抗原分子的抗体。本发明中抗体包括那些能够结合并抑制人HSPC069SET蛋白的分子,也包括那些并不影响人HSPC069SET蛋白功能的抗体。本发明还包括那些能与修饰或未经修饰形式的人HSPC069SET基因产物结合的抗体。
本发明不仅包括完整的单克隆或多克隆抗体,而且还包括具有免疫活性的抗体片段,如Fab’或(Fab)2片段;抗体重链;抗体轻链;遗传工程改造的单链Fv分子(Ladner等人,美国专利No.4,946,778);或嵌合抗体,如具有鼠抗体结合特异性但仍保留来自人的抗体部分的抗体。
本发明的抗体可以通过本领域内技术人员已知的各种技术进行制备。例如,纯化的人HSPC069SET基因产物或者其具有抗原性的片段,可被施用于动物以诱导多克隆抗体的产生。与之相似的,表达人HSPC069SET蛋白或其具有抗原性的片段的细胞可用来免疫动物来生产抗体。本发明的抗体也可以是单克隆抗体。此类单克隆抗体可以利用杂交瘤技术来制备(见Kohler等人,
Nature 256;495,1975;Kohler等人,Eur.J.Immunol.6:511,1976;Kohler等人,
Eur.J.Immunol.6:292,1976;Hammerling等人,
In Monoclonal Antibodies and T Cell Hybridomas,Elsevier,N.Y.,1981)。本发明的抗体包括能阻断人HSPC069SET蛋白功能的抗体以及不影响人HSPC069SET蛋白功能的抗体。本发明的各类抗体可以利用人HSPC069SET基因产物的片段或功能区,通过常规免疫技术获得。这些片段或功能区可以利用重组方法制备或利用多肽合成仪合成。与人HSPC069SET基因产物的未修饰形式结合的抗体可以用原核细胞(例如E.Coli)中生产的基因产物来免疫动物而产生;与翻译后修饰形式结合的抗体(如糖基化或磷酸化的蛋白或多肽),可以用真核细胞(例如酵母或昆虫细胞)中产生的基因产物来免疫动物而获得。
抗人HSPC069SET蛋白的抗体可用于免疫组织化学技术中,检测活检标本中的人HSPC069SET蛋白。
本发明中的抗体可用于治疗或预防与人HSPC069SET蛋白相关的疾病。给予适当剂量的抗体可以刺激或阻断人HSPC069SET蛋白的产生或活性。
抗体也可用于设计成针对体内某一特殊部位的免疫毒素。如人HSPC069SET蛋白高亲和性的单克隆抗体可与细菌或植物毒素(如白喉毒素,蓖麻蛋白,红豆碱等)共价结合。一种通常的方法是用巯基交联剂如SPDP,攻击抗体的氨基,通过二硫键的交换,将毒素结合于抗体上,这种杂交抗体可用于杀灭人HSPC069SET蛋白阳性的细胞。
多克隆抗体的生产可用人HSPC069SET蛋白或多肽免疫动物,如家兔,小鼠,大鼠等。多种佐剂可用于增强免疫反应,包括但不限于弗氏佐剂等。
利用本发明蛋白,通过各种常规筛选方法,可筛选出与HSPC069SET蛋白发生相互作用的物质,如受体、抑制剂、激动剂或拮抗剂等。
本发明蛋白及其抗体、抑制剂、激动剂、拮抗剂或受体等,当在治疗上进行施用(给药)时,可提供不同的效果。通常,可将这些物质配制于无毒的、惰性的和药学上可接受的水性载体介质中,其中pH通常约为5-8,较佳地pH约为6-8,尽管pH值可随被配制物质的性质以及待治疗的病症而有所变化。配制好的药物组合物可以通过常规途径进行给药,其中包括(但并不限于):肌内、腹膜内、静脉内、皮下、皮内、或局部给药。
本发明的多肽可直接用于疾病治疗,例如,用于治疗组蛋白H3甲基转移酶活性低下所导致的疾病。
本发明还提供了一种药物组合物,它含有安全有效量的本发明HSPC069SET多肽以及药学上可接受的载体或赋形剂。这类载体包括(但并不限于):盐水、缓冲液、葡萄糖、水、甘油、乙醇、及其组合。药物制剂应与给药方式相匹配。本发明的药物组合物可以被制成针剂形式,例如用生理盐水或含有葡萄糖和其他辅剂的水溶液通过常规方法进行制备。诸如片剂和胶囊之类的药物组合物,可通过常规方法进行制备。药物组合物如针剂、溶液、片剂和胶囊宜在无菌条件下制造。活性成分的给药量是治疗有效量,例如每天约1微克/千克体重-约5毫克/千克体重。此外,本发明的多肽还可与其他治疗剂一起使用。
使用药物组合物时,是将安全有效量的HSPC069SET蛋白施用于哺乳动物,其中该安全有效量通常至少约10微克/千克体重,而且在大多数情况下不超过约8毫克/千克体重,较佳地该剂量是约10微克/千克体重-约1毫克/千克体重。当然,具体剂量还应考虑给药途径、病人健康状况等因素,这些都是熟练医师技能范围之内的。
人HSPC069SET蛋白的多聚核苷酸也可用于多种治疗目的。基因治疗技术可用于治疗由于HSPC069SET蛋白的无表达或异常/无活性的HSPC069SET蛋白的表达所致的细胞增殖、发育或代谢异常。重组的基因治疗载体(如病毒载体)可设计成表达变异的HSPC069SET蛋白,以抑制内源性的HSPC069SET蛋白活性。来源于病毒的表达载体如逆转录病毒、腺病毒、腺病毒相关病毒、单纯疱疹病毒、细小病毒等可用于将HSPC069SET基因转移至细胞内。构建携带HSPC069SET基因的重组病毒载体的方法可见于已有文献(Sambrook,et al.)。另外重组人HSPC069SET基因可包装到脂质体中,然后再转移至细胞内。
抑制人HSPC069SET mRNA的寡聚核苷酸(包括反义RNA和DNA)以及核酶也在本发明的范围之内。核酶是一种能特异性分解特定RNA的酶样RNA分子,其作用机制是核酶分子与互补的靶RNA特异性杂交后进行核酸内切作用。反义的RNA和DNA及核酶可用已有的任何RNA或DNA合成技术获得,如固相磷酸酰胺化学合成法合成寡核苷酸的技术已广泛应用。反义RNA分子可通过编码该RNA的DNA序列在体外或体内转录获得。这种DNA序列已整合到载体的RNA聚合酶启动子的下游。为了增加核酸分子的稳定性,可用多种方法对其进行修饰,如增加两侧的序列长度,核糖核苷之间的连接应用磷酸硫酯键或肽键而非磷酸二酯键。
多聚核苷酸导入组织或细胞内的方法包括:将多聚核苷酸直接注入到体内组织中;或在体外通过载体(如病毒、噬菌体或质粒等)先将多聚核苷酸导入细胞中,再将细胞移植到体内等。
能与人HSPC069SET蛋白结合的多肽分子可通过筛选由各种可能组合的氨基酸结合于固相物组成的随机多肽库而获得。筛选时,必须对人HSPC069SET蛋白分子进行标记。
本发明还涉及定量和定位检测人HSPC069SET蛋白水平的诊断试验方法。这些试验是本领域所熟知的,且包括FISH测定和放射免疫测定。试验中所检测的人HSPC069SET蛋白水平,可以用作解释人HSPC069SET蛋白在各种疾病中的重要性和用于诊断HSPC069SET蛋白起作用的疾病。
一种检测检测样品中是否存在HSPC069SET蛋白的方法是利用HSPC069SET蛋白的特异性抗体进行检测,它包括:将样品与HSPC069SET蛋白特异性抗体接触;观察是否形成抗体复合物,形成了抗体复合物就表示样品中存在HSPC069SET蛋白。
HSPC069SET蛋白的多聚核苷酸可用于HSPC069SET蛋白相关疾病的诊断和治疗。在诊断方面,HSPC069SET蛋白的多聚核苷酸可用于检测HSPC069SET蛋白的表达与否或在疾病状态下HSPC069SET蛋白的异常表达。如HSPC069SET DNA序列可用于对活检标本的杂交以判断HSPC069SET蛋白的表达异常。杂交技术包括Southern印迹法,Northern印迹法、原位杂交等。这些技术方法都是公开的成熟技术,相关的试剂盒都可从商业途径得到。本发明的多核苷酸的一部分或全部可作为探针固定在微阵列(microarray)或DNA芯片(又称为“基因芯片”)上,用于分析组织中基因的差异表达分析和基因诊断。用HSPC069SET蛋白特异的引物进行RNA-聚合酶链反应(RT-PCR)体外扩增也可检测HSPC069SET蛋白的转录产物。
检测HSPC069SET基因的突变也可用于诊断HSPC069SET蛋白相关的疾病。HSPC069SET蛋白突变的形式包括与正常野生型HSPC069SET DNA序列相比的点突变、易位、缺失、重组和其它任何异常等。可用已有的技术如Southern印迹法、DNA序列分析、PCR和原位杂交检测突变。另外,突变有可能影响蛋白的表达,因此用Northern印迹法、Western印迹法可间接判断基因有无突变。
本发明的序列对染色体鉴定也是有价值的。简而言之,根据本发明HSPC069SET蛋白的cDNA制备PCR引物(优选15-35bp),可以将序列定位于染色体上。然后,将这些引物用于PCR筛选含各条人染色体的体细胞杂合细胞。只有那些含有相应于引物的人基因的杂合细胞会产生扩增的片段。
一旦序列被定位到准确的染色体位置,此序列在染色体上的物理位置就可以与基因图数据相关联。这些数据可见于例如,V.Mckusick,Mendelian Inheritance inMan(可通过与Johns Hopkins University Welch Medical Library联机获得)。然后可通过连锁分析,确定基因与业已定位到染色体区域上的疾病之间的关系。
在本发明的一个实例中,提供了一种分离的多核苷酸,它编码具有SEQ ID NO:2所示氨基酸序列的多肽。本发明的多核苷酸是从人造血干细胞cDNA文库中分离出的。其序列如SEQ ID NO:1所示,它包含的多核苷酸序列全长为6731个碱基,其开放读框位于72-3704位,编码全长为1211个氨基酸的人HSPC069SET蛋白(SEQ ID NO:2)。HSPC069SET蛋白具有组蛋白甲基转移酶的活性,它可以特异地甲基化组蛋白H3的第36位的赖氨酸。在本发明之前,尚未在人体中发现甲基化该位点的酶。另外,该酶还可以甲基化自身,目前所有的组蛋白甲基转移酶都不具备该性质。鉴于组蛋白甲基转移酶在生物体发育调控以及人类疾病发生中的重要意义,HSPC069SET组蛋白甲基转移酶可能被应用于治疗人类疾病。
下面结合具体实施例,进一步阐述本发明。应理解,这些实施例仅用于说明本发明而不用于限制本发明的范围。下列实施例中未注明具体条件的实验方法,通常按照常规条件如Sambrook等人,分子克隆:实验室手册(New York:Cold Spring HarborLaboratory Press,1989)中所述的条件,或按照制造厂商所建议的条件。
实施例1:HSPC069SET蛋白cDNA的克隆
HSPC069SET的cDNA片段来自于用常规方法构建的CD34阳性的造血干/祖细胞cDNA文库(方法参见Zhang et al.,
Genome Res.2000,10:1546-6)。以cDNA文库为模板,用一对寡核苷酸为引物-上游:ctcagatctaacagggacctaaggacatcatc(SEQ IDNO:7)和下游:cgcggtaccttattttcaatatattcacatatacatta(SEQ ID NO:8),进行PCR。扩增出的片段用BglII/KpnI酶切,连入pEGFP载体(Clontech公司),获得HPC069SET-pEGFP质粒,测序鉴定获得的HSPC069SET的核苷酸序列。
HSPC069SET cDNA全长为6731bp(SEQ ID NO:1),含有完整的开放性读框(72-3704位),编码含1211氨基酸残基的多肽(SEQ ID NO:2)。同源比较显示该段氨基酸序列中含有一个如下所示的进化上保守的SET结构域:
FQRKQHADVE VILTEKKGWG LRAAKDLPSN TFVLEYCGEV LDHKEFKARV 50
KEYARNKNIH YYFMALKNDE IIDATQKGNC SRFMNHSCEP NCETQKWTVN 100
GQLRVGFFTT KLVPSGSELT FDYQFQRYGK 130
(即SEQ ID NO:2中第1041-1170位)。
实施例2
HSPC069SET蛋白在大肠杆菌中的表达和纯化
以抽提的造血干细胞mRNA为模板,经反转录后,用一对寡核苷酸为引物-A:gcgtcgacgtgatggtgagcttcaggacaga(SEQ ID NO:9)和B:aactgcagatgtgaggcagacaagtcattcca(SEQ ID NO:10),进行PCR。扩增出的片段用限制性内内切酶SalI/PstI酶切,产物连入pGBKT7(购自Clontech公司),获得HPC069SET-pGBKT7质粒,测序鉴定获得的cDNA。
然后,对HPC069SET-pGBKT7用限制性内切酶EcoRI酶切后,连入pGEX-5X1载体(Amersham Biosciences),获得HSPC069SET-pGEX-5X1质粒。测序鉴定HSPC069SET的cDNA片段正确插入载体。用该质粒转化大肠杆菌BL21菌株。阳性转化子在含有Amp的LB培养基中培养过夜,然后以1∶100的比例转接到大体积的培养基中,培养至600纳米光密度达到0.6-1.0,加入IPTG至终浓度0.5mM,28摄氏度诱导表达3小时。收集细胞并用超声裂解细胞。上清液中加入谷胱甘肽Sepharose 4B珠子,旋转混匀1小时,离心收集珠子并用PBS缓冲液洗3次,最后将珠子上的蛋白保存在-80度备用。用12%的SDS-PAGE凝胶电泳鉴定获得蛋白的分子量。
测定结果表明,融合蛋白的分子量为62Kda,与预期相符。(表达的蛋白为GST-HSPC069SET融合蛋白,其编码序列和氨基酸序列如SEQ ID NO:3和4所示。)
实施例3
突变体的构建和突变体蛋白的获得
用常规的桥式PCR的方法,在实施例2制备的HSPC069SET-pGEX-5X1质粒的基础上,把HSPC069SET蛋白的SET结构域内的第1122位精氨酸突变为组氨酸(即SEQ ID NO:4中第449位)。通过与实施例2相同方法,用该突变体质粒获得突变的HSPC069SETMp蛋白,
实施例4
HSPC069SET蛋白酶活性的检测
采用GST-融合蛋白来检测酶活性是目前通用的方法。用已知的组蛋白甲基转移酶的GST-融合蛋白GST-mG9a(氨基酸621-1000),GST-SUV39H1(氨基酸82-412)和GST-MLL(氨基酸3745-3699)作为阳性对照,用组蛋白混合物作为底物。把GST-HSPC069SET蛋白或阳性对照蛋白与底物混合,加入碳14标记的甲基供体S-腺苷-[甲基-14C]-L-甲硫氨酸(PerkinElmer Life Sciences公司)和反应缓冲液(50mM Tris pH8.5,20mM KCl,10mM MgCl2,1%β-巯基乙醇,250mM蔗糖),37℃孵育1小时,反应产物用NuPAGE Novex Bis-Tris凝胶(Invitrogen公司)电泳,用考马斯亮蓝染色后把凝胶抽干,用Molecular Imager FX(Bio-Rad公司)检测同位素自显影。
结果显示,GST-HSPC069SET蛋白具有明显的酶活性,可以修饰组蛋白H3(图1A。注:HSPC069=GST-HSPC069SET融合蛋白)。如果用突变体GST-HSPC069SETMp蛋白替代GST-HSPC069SET蛋白,则酶活性消失(图1C),说明该活性依赖于SET结构域。
为了确定HSPC069SET蛋白修饰组蛋白H3的位点特异性,采用重组的组蛋白H3的各种突变体GST-H3N,N4,N9,N27和K36R作为底物(图2A),结果表明GST-HSPC069SET蛋白可以特异地修饰组蛋白H3的第36位的赖氨酸(图2B)。
除了可以修饰组蛋白之外,HSPC069SET蛋白还可以甲基化自身。不管底物组蛋白是否存在,GST-HSPC069SET均可被甲基化,说明HSPC069SET的这种自身甲基化的活性并不依赖组蛋白的存在(图1A,B,C,星号表示自身甲基化的信号)。目前已报道的所有组蛋白甲基转移酶均未发现具有该种活性。
实施例5抗HSPC069SET蛋白抗体的产生
将实施例2中获得的重组人HSPC069SET蛋白用来免疫动物以产生抗体,具体方法如下。重组分子用层析法进行分离后备用。也可用SDS-PAGE凝胶电泳法进行分离,将电泳条带从凝胶中切下,并用等体积的完全Freund’s佐剂乳化。用50-100μg/0.2ml乳化过的蛋白,对小鼠进行腹膜内注射。14天后,用非完全Freund’s佐剂乳化的同样抗原,对小鼠以50-100μg/0.2ml的剂量进行腹膜内注射以加强免疫。每隔14天进行一次加强免疫,至少进行三次。获得的抗血清的特异反应活性用它在体外沉淀人HSPC069SET蛋白基因翻译产物的能力加以评估。结果发现,抗体可特异性地与本发明蛋白发生结合。
在本发明提及的所有文献都在本申请中引用作为参考,就如同每一篇文献被单独引用作为参考那样。此外应理解,在阅读了本发明的上述讲授内容之后,本领域技术人员可以对本发明作各种改动或修改,这些等价形式同样落于本申请所附权利要求书所限定的范围。
序列表
<110>上海第二医科大学附属瑞金医院
<120>一种组蛋白甲基转移酶及其制备方法
<130>041666
<160>10
<170>PatentIn version 3.1
<210>1
<211>6731
<212>DNA
<213>智人(Homo sapiens)
<220>
<221>CDS
<222>(72)..(3704)
<223>
<400>1
acagggacct aaggacatca tcctattcta aatctgatcg ggactgtaaa actgagacct 60
cttacttaga g atg gaa aga aga ggc aag tat tct tca aaa cta gaa aga 110
Met Glu Arg Arg Gly Lys Tyr Ser Ser Lys Leu Glu Arg
1 5 10
gaa tct aaa agg act tca gaa aat gaa gca att aaa aga tgt tgt tct 158
Glu Ser Lys Arg Thr Ser Glu Asn Glu Ala Ile Lys Arg Cys Cys Ser
15 20 25
ccc cct aat gaa ctg gga ttc cga cga ggg tca tca tat tct aag cat 206
Pro Pro Asn Glu Leu Gly Phe Arg Arg Gly Ser Ser Tyr Ser Lys His
30 35 40 45
gac agt agt gct tcc cgt tat aaa tct acc ctt tca aaa cct ata ccc 254
Asp Ser Ser Ala Ser Arg Tyr Lys Ser Thr Leu Ser Lys Pro Ile Pro
50 55 60
aag tct gat aaa ttt aaa aat tct ttc tgt tgt aca gaa tta aat gaa 302
Lys Ser Asp Lys Phe Lys Asn Ser Phe Cys Cys Thr Glu Leu Asn Glu
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gaa atc aaa caa tct cat tct ttt agt tta cag aca cct tgt tca aaa 350
Glu Ile Lys Gln Ser His Ser Phe Ser Leu Gln Thr Pro Cys Ser Lys
80 85 90
ggt agt gaa tta aga atg att aat aaa aat cct gaa aga gaa aag gct 398
Gly Ser Glu Leu Arg Met Ile Asn Lys Asn Pro Glu Arg Glu Lys Ala
95 100 105
ggg tct cca gct cca tca aat cga tta aat gat tca cct act tta aaa 446
Gly Ser Pro Ala Pro Ser Asn Arg Leu Asn Asp Ser Pro Thr Leu Lys
110 115 120 125
aag cta gat gaa ttg cct att ttt aag tcc gaa ttt ata aca cat gat 494
Lys Leu Asp Glu Leu Pro Ile Phe Lys Ser Glu Phe Ile Thr His Asp
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agc cat gat agt att aag gaa tta gac tct tta tct aaa gtg aag aat 542
Ser His Asp Ser Ile Lys Glu Leu Asp Ser Leu Ser Lys Val Lys Asn
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gat caa tta aga agt ttt tgt ccc ata gaa tta aat ata aat gga tct 590
Asp Gln Leu Arg Ser Phe Cys Pro Ile Glu Leu Asn Ile Asn Gly Ser
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cct ggg gca gaa tct gat ttg gca aca ttt tgc act tct aaa act gat 638
Pro Gly Ala Glu Ser Asp Leu Ala Thr Phe Cys Thr Ser Lys Thr Asp
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gct gtt tta atg act tct gat gat agt gtg act gga tcg gaa tta tcc 686
Ala Val Leu Met Thr Ser Asp Asp Ser Val Thr Gly Ser Glu Leu Ser
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cct ttg gtc aaa gca tgc atg ctt tca tca aat gga ttt cag aat att 734
Pro Leu Val Lys Ala Cys Met Leu Ser Ser Asn Gly Phe Gln Asn Ile
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agt agg tgc aaa gaa aaa gac ttg gat gat acc tgc atg ctg cat aag 782
Ser Arg Cys Lys Glu Lys Asp Leu Asp Asp Thr Cys Met Leu His Lys
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aag tca gaa agc cca ttt aga gaa aca gaa cct ctg gtg tca cca cac 830
Lys Ser Glu Ser Pro Phe Arg Glu Thr Glu Pro Leu Val Ser Pro His
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caa gat aaa ctc atg tct atg cca gtt atg act gtg gat tat tcc aaa 878
Gln Asp Lys Leu Met Ser Met Pro Val Met Thr Val Asp Tyr Ser Lys
255 260 265
aca gta gtt aaa gaa cca gtt gat acg agg gtt tct tgc tgc aaa acc 926
Thr Val Val Lys Glu Pro Val Asp Thr Arg Val Ser Cys Cys Lys Thr
270 275 280 285
aaa gat tca gac ata tac tgt act ttg aac gat agc aac cct tct ttg 974
Lys Asp Ser Asp Ile Tyr Cys Thr Leu Asn Asp Ser Asn Pro Ser Leu
290 295 300
tgt aac tct gaa gct gaa aat att gag cct tca gtt atg aag att tct 1022
Cys Asn Ser Glu Ala Glu Asn Ile Glu Pro Ser Val Met Lys Ile Ser
305 310 315
tca aat agc ttt atg aat gtg cat ttg gaa tca aaa cca gtt ata tgt 1070
Ser Asn Ser Phe Met Asn Val His Leu Glu Ser Lys Pro Val Ile Cys
320 325 330
gat agt aga aat ttg aca gat cac tca aaa ttt gca tgt gaa gaa tat 1118
Asp Ser Arg Asn Leu Thr Asp His Ser Lys Phe Ala Cys Glu Glu Tyr
335 340 345
aag cag agc atc ggt agc act agt tca gct tct gtt aat cat ttt gat 1166
Lys Gln Ser Ile Gly Ser Thr Ser Ser Ala Ser Val Asn His Phe Asp
350 355 360 365
gat tta tat caa cct att ggg agt tca ggt att gct tca tct ctt cag 1214
Asp Leu Tyr Gln Pro Ile Gly Ser Ser Gly Ile Ala Ser Ser Leu Gln
370 375 380
agt ctt cca cca gga ata aag gtg gac agt cta act ctc ttg aaa tgc 1262
Ser Leu Pro Pro Gly Ile Lys Val Asp Ser Leu Thr Leu Leu Lys Cys
385 390 395
gga gag aac aca tct cca gtt ctg gat gca gtg cta aag agt aaa aaa 1310
Gly Glu Asn Thr Ser Pro Val Leu Asp Ala Val Leu Lys Ser Lys Lys
400 405 410
agt tca gag ttt tta aag cat gca ggg aaa gaa aca ata gta gaa gta 1358
Ser Ser Glu Phe Leu Lys His Ala Gly Lys Glu Thr Ile Val Glu Val
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ggt agt gac ctt cct gat tca gga aag gga ttt gct tcc agg gag aac 1406
Gly Ser Asp Leu Pro Asp Ser Gly Lys Gly Phe Ala Ser Arg Glu Asn
430 435 440 445
agg cgt aat aat ggg tta tct ggg aaa tgt ttg caa gag gct caa aaa 1454
Arg Arg Asn Asn Gly Leu Ser Gly Lys Cys Leu Gln Glu Ala Gln Lys
450 455 460
gaa ggg aat tcc ata ttg cct gaa aga aga gga aga cca gaa atc tct 1502
Glu Gly Asn Ser Ile Leu Pro Glu Arg Arg Gly Arg Pro Glu Ile Ser
465 470 475
tta gat gaa aga gga gaa gga gga cat gtg cat act tct gat gac tca 1550
Leu Asp Glu Arg Gly Glu Gly Gly His Val His Thr Ser Asp Asp Ser
480 485 490
gaa gtt gta ttt tct tct tgt gat ttg aat tta acc atg gaa gac agt 1598
Glu Val Val Phe Ser Ser Cys Asp Leu Asn Leu Thr Met Glu Asp Ser
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gat ggt gta act tat gca tta aag tgt gac agt agt ggt cat gcc cca 1646
Asp Gly Val Thr Tyr Ala Leu Lys Cys Asp Ser Ser Gly His Ala Pro
510 515 520 525
gaa att gtg tct aca gtt cat gaa gat tat tct ggc tct tct gaa agt 1694
Glu Ile Val Ser Thr Val His Glu Asp Tyr Ser Gly Ser Ser Glu Ser
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tca aat gat gaa agt gat tca gaa gat acg gat tcg gat gat agc agt 1742
Ser Asn Asp Glu Ser Asp Ser Glu Asp Thr Asp Ser Asp Asp Ser Ser
545 550 555
att cca asa aac cgt ctc cag tct gtt gtg gtt gtg cca aag aat tct 1790
Ile Pro Arg Asn Arg Leu Gln Ser Val Val Val Val Pro Lys Asn Ser
560 565 570
act ttg ccc atg gaa gaa aca agt cct tgt tct tct cgg agc agt caa 1838
Thr Leu Pro Met Glu Glu Thr Ser Pro Cys Ser Ser Arg Ser Ser Gln
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agt tat aga cac tat tct gac cat tgg gaa gat gag aga ttg gag tca 1886
Ser Tyr Arg His Tyr Ser Asp His Trp Glu Asp Glu Arg Leu Glu Ser
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agg aga cat ttg tat gag gaa aaa ttt gaa agt ata gca agt aaa gcc 1934
Arg Arg His Leu Tyr Glu Glu Lys Phe Glu Ser Ile Ala Ser Lys Ala
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tgt cct caa act gat aag ttt ttc ctt cat aaa gga aca gag aag aat 1982
Cys Pro Gln Thr Asp Lys Phe Phe Leu His Lys Gly Thr Glu Lys Asn
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ccg gaa att tct ttt aca cag tcc agt aga aaa caa ata gat aac cgc 2030
Pro Glu Ile Ser Phe Thr Gln Ser Ser Arg Lys Gln Ile Asp Asn Arg
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ctg cct gaa ctt tct cat cct cag agt gat ggg gtt gat agt aca agt 2078
Leu Pro Glu Leu Ser His Pro Gln Ser Asp Gly Val Asp Ser Thr Ser
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cat aca gat gtg aaa tct gac cct ctg ggt cac cca aat tca gag gaa 2126
His Thr Asp Val Lys Ser Asp Pro Leu Gly His Pro Asn Ser Glu Glu
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acc gtg aaa gcc aaa ata cct tct agg cag caa gaa gag ctg cca att 2174
Thr Val Lys Ala Lys Ile Pro Ser Arg Gln Gln Glu Glu Leu Pro Ile
690 695 700
tat tct tct gat ttt gaa gat gtc cca aat aag tct tgg caa cag acc 2222
Tyr Ser Ser Asp Phe Glu Asp Val Pro Asn Lys Ser Trp Gln Gln Thr
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act ttc caa aac agg cca gat agt aga ctg gga aaa aca gaa ttg agt 2270
Thr Phe Gln Asn Arg Pro Asp Ser Arg Leu Gly Lys Thr Glu Leu Ser
720 725 730
ttt tct tcc tct tgt gag ata cca cat gtg gat ggc ttg cac tca tca 2318
Phe Ser Ser Ser Cys Glu Ile Pro His Val Asp Gly Leu His Ser Ser
735 740 745
gaa gag ctc aga aac tta ggt tgg gac ttc tct caa gaa aag cct tct 2366
Glu Glu Leu Arg Asn Leu Gly Trp Asp Phe Ser Gln Glu Lys Pro Ser
750 755 760 765
gcc acg tat cag caa cct gac agt agc tat gga gct tgt ggt gga cac 2414
Ala Thr Tyr Gln Gln Pro Asp Ser Ser Tyr Gly Ala Cys Gly Gly His
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aag tat cag caa aat gca gaa cag tat ggt ggg aca cgt gat tac tgg 2462
Lys Tyr Gln Gln Asn Ala Glu Gln Tyr Gly Gly Thr Arg Asp Tyr Trp
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Gln Gly Asn Gly Tyr Trp Asp Pro Arg Ser Gly Arg Pro Pro Gly Thr
800 805 810
ggg gtt gtg tat gat cga act caa gga caa gta cca gat tcc cta aca 2558
Gly Val Val Tyr Asp Arg Thr Gln Gly Gln Val Pro Asp Ser Leu Thr
815 820 825
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Asp Asp Arg Glu Glu Glu Glu Asn Trp Asp Gln Gln Asp Gly Ser His
830 835 840 845
ttt tca gac cag tcc gat aaa ttt ctt cta tcc ctt cag aaa gac aag 2654
Phe Ser Asp Gln Ser Asp Lys Phe Leu Leu Ser Leu Gln Lys Asp Lys
850 855 860
ggg tca gtg caa gca cct gaa ata agc agc aat tcc att aag gac act 2702
Gly Ser Val Gln Ala Pro Glu Ile Ser Ser Asn Ser Ile Lys Asp Thr
865 870 875
tta gct gtg aat gaa aag aaa gat ttt tca aaa aac tta gaa aaa aat 2750
Leu Ala Val Asn Glu Lys Lys Asp Phe Ser Lys Asn Leu Glu Lys Asn
880 885 890
gat atc aaa gat aga ggg cct ctt aaa aaa agg agg cag gaa ata gag 2798
Asp Ile Lys Asp Arg Gly Pro Leu Lys Lys Arg Arg Gln Glu Ile Glu
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agt gat tct gaa agt gat ggt gag ctt cag gac aga aag aaa gtt aga 2846
Ser Asp Ser Glu Ser Asp Gly Glu Leu Gln Asp Arg Lys Lys Val Arg
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gtg gag gta gag cag gga gag aca tca gtg ccc cca ggt tca gca ctg 2894
Val Glu Val Glu Gln Gly Glu Thr Ser Val Pro Pro Gly Ser Ala Leu
930 935 940
gtt ggg ccc tcc tgt gtc atg gat gac ttc agg gac cca cag cga tgg 2942
Val Gly Pro Ser Cys Val Met Asp Asp Phe Arg Asp Pro Gln Arg Trp
945 950 955
aag gaa tgt gcc aag caa ggg aaa atg cca tgt tac ttt gat ctt att 2990
Lys Glu Cys Ala Lys Gln Gly Lys Met Pro Cys Tyr Phe Asp Leu Ile
960 965 970
gaa gaa aat gtt tat tta aca gaa aga aag aag aat aaa tct cat cga 3038
Glu Glu Asn Val Tyr Leu Thr Glu Arg Lys Lys Asn Lys Ser His Arg
975 980 985
gat att aag cga atg cag tgt gag tgt aca cct ctt tct aaa gat gaa 3086
Asp Ile Lys Arg Met Gln Cys Glu Cys Thr Pro Leu Ser Lys Asp Glu
990 995 1000 1005
aga gct caa ggt gaa ata gca tgt ggg gaa gat tgt ctt aat cgt 3131
Arg Ala Gln Gly Glu Ile Ala Cys Gly Glu Asp Cys Leu Asn Arg
1010 1015 1020
ctt ctc atg att gaa tgt tct tct cgg tgt cca aat ggg gat tat 3176
Leu Leu Met Ile Glu Cys Ser Ser Arg Cys Pro Asn Gly Asp Tyr
1025 1030 1035
tgt tcc aat aga cgg ttt cag aga aaa cag cat gca gat gtg gaa 3221
Cys Ser Asn Arg Arg Phe Gln Arg Lys Gln His Ala Asp Val Glu
1040 1045 1050
gtc ata ctc aca gaa aag aaa ggc tgg ggc ttg aga gct gcc aaa 3266
Val Ile Leu Thr Glu Lys Lys Gly Trp Gly Leu Arg Ala Ala Lys
1055 1060 1065
gac ctt cct tcg aac acc ttt gtc cta gaa tat tgt gga gag gta 3311
Asp Leu Pro Ser Asn Thr Phe Val Leu Glu Tyr Cys Gly Glu Val
1070 1075 1080
ctc gat cat aaa gag ttt aaa gct cga gtg aag gag tat gca cga 3356
Leu Asp His Lys Glu Phe Lys Ala Arg Val Lys Glu Tyr Ala Arg
1085 1090 1095
aac aaa aac atc cat tac tat ttc atg gcc ctg aag aat gat gag 3401
Asn Lys Asn Ile His Tyr Tyr Phe Met Ala Leu Lys Asn Asp Glu
1100 1105 1110
ata ata gat gcc act caa aaa gga aat tgc tct cgt ttc atg aat 3446
Ile Ile Asp Ala Thr Gln Lys Gly Asn Cys Ser Arg Phe Met Asn
1115 1120 1125
cac agc tgt gaa cca aat tgt gaa acc caa aaa tgg act gtg aac 3491
His Ser Cys Glu Pro Asn Cys Glu Thr Gln Lys Trp Thr Val Asn
1130 1135 1140
gga caa ctg agg gtt ggg ttt ttt acc acc aaa ctg gtt cct tca 3536
Gly Gln Leu Arg Val Gly Phe Phe Thr Thr Lys Leu Val Pro Ser
1145 1150 1155
ggc tca gag tta acg ttt gac tat cag ttc cag aga tat gga aaa 3581
Gly Ser Glu Leu Thr Phe Asp Tyr Gln Phe Gln Arg Tyr Gly Lys
1160 1165 1170
gaa gcc cag aaa tgt ttc tgc gga tca gcc aat tgc cgg ggt tac 3626
Glu Ala Gln Lys Cys Phe Cys Gly Ser Ala Asn Cys Arg Gly Tyr
1175 1180 1185
ctg gga gga gaa aac aga gtc agc att aga gca gca gga ggg aaa 3671
Leu Gly Gly Glu Asn Arg Val Ser Ile Arg Ala Ala Gly Gly Lys
1190 1195 1200
atg aag aag gaa cga tct cgt aag aag gat tca taggtggatg 3714
Met Lys Lys Glu Arg Ser Arg Lys Lys Asp Ser
1205 1210
gagagctaga agctctgatg gaaaatggtg agggtctctc tgataaaaac caggtgccca 3774
gcttatcccg gctaatggtt agaattgaaa ctttggagca gaaacttacc tgtctggaac 3834
tcatacagaa cacacactca cagtcctgcc tgaagtcctt tctggaacgt catgggctgt 3894
ctttgttgtg gatctggatg gcagagctag gtgacggccg ggaaagtaac cagaagcttc 3954
aggaagagat tataaagact ttggaacact tgcccattcc tactaaaaat atgttggagg 4014
aaagcaaagt acttccaatt attcaacgct ggtctcagac taagactgct gtccctccgt 4074
tgagtgaagg agatgggtat tctagtgaga atacatcgcg tgctcataca ccactcaaca 4134
cacctgatcc ttccaccaag ctgagcacag aagctgacac agacactccc aagaaactaa 4194
tgtttcgcag actgaaaatt ataagtgaaa atagcatgga cagtgcaatc tctgatgcaa 4254
ccagtgagct agaaggcaag gatggcaaag aggatcttga tcaattagaa aatgtccctg 4314
tagaggaaga ggaagaattg cagtcacaac agctactccc acaacagctg cctgaatgca 4374
aagttgatag tgaaaccaac atagaagcta gtaagctacc tacatctgaa ccagaagctg 4434
acgctgaaat agagcccaaa gagagcaacg gcacaaaact agaagaacct attaatgaag 4494
aaacaccatc ccaagatgaa gaggagggtg tgtctgatgt ggagagtgaa aggagccaag 4554
aacagccaga taaaacagtg gatataagtg atttggccac caaactcctg gacagttgga 4614
aagacctaaa ggaggtatat cgaattccaa agaaaagtca aactgaaaag gaaaacacaa 4674
gaaatcagcc tgaataaatg gaatgacttg tctgcctcac atattctaag gtgcagagtc 4734
agaatatgaa ctgttgcaac tgaacgagga agggatgctg ttggcttcag agatcaaaca 4794
cctgccccga agactcctaa taggtcaaga gagagagacc cagacaagca aactcaaaat 4854
aaagagaaaa ggaaacgaag aagctccctc tcaccaccct cttctgccta tgagcgggga 4914
acaaaaaggc cagatgacag atatgataca ccaacttcta aaaagaaagt acgaattaaa 4974
gaccgcaata aactttctac agaggaacgc cggaagttgt ttgagcaaga ggtggctcaa 5034
cgggaggctc agaaacaaca gcaacagatg cagaacctgg gaatgacatc accactgccc 5094
tatgactctc ttggttataa tgccccgcat catccctttg ctggttaccc accaggttat 5154
cccatgcagg cctatgtgga tcccagcaac cctaatgctg gaaaggtgct cctgcccaca 5214
cccagcatgg acccagtgtg ttctcctgct ccttatgatc atgctcagcc cttggtggga 5274
cattctacag aacccctttc tgcccctcca ccagtaccag tggtgccaca tgtggcagct 5334
cctgtggaag tttccagttc ccagtatgtg gcccagagtg atggtgtagt acaccaagac 5394
tccagcgttg ctgtcttgcc agtgccggcc cccggcccag ttcagggaca gaattatagt 5454
gtttgggatt caaaccaaca gtctgtcagt gtacagcagc agtactctcc tgcacagtct 5514
caagcaacca tatattatca aggacagaca tgtccaacag tctatggtgt gacatcacct 5574
tattcacaga caactccacc aattgtacag agttatgccc agccaagtct tcagtatatc 5634
caggggcaac agattttcac agctcatcca caaggagtgg tggtacagcc agccgcagca 5694
gtgactacaa tagttgcacc agggcagcct cagcccttgc agccatctga aatggttgtg 5754
acaaataatc tcttggatct gccgcccccc tctcctccca aaccaaaaac cattgtctta 5814
cctcccaact ggaagacagc tcgagatcca gaagggaaga tttattacta ccatgtgatc 5874
acaaggcaga ctcagtggga tcctcctact tgggaaagcc caggagatga tgccagcctt 5934
gagcatgaag ctgagatgga cctgggaact ccaacatatg atgaaaaccc catgaaggcc 5994
tcgaaaaagc ccaagacagc agaagcagac acctccagtg aactagcaaa gaaaagcaaa 6054
gaagtattca gaaaagagat gtcccagttc atcgtccagt gcctgaaccc ttaccggaaa 6114
cctgactgca aagtgggaag aattaccaca actgaagact ttaaacatct ggctcgcaag 6174
ctgactcacg gtgttatgaa taaggagctg aagtactgta agaatcctga ggacctggag 6234
tgcaatgaga atgtgaaaca caaaaccaag gagtacatta agaagtacat gcagaagttt 6294
ggggctgttt acaaacccaa agaggacact gaattagagt gactgttggg ccagggtggg 6354
aggatgggtg gtcaggtaag acagactcta gggagaggaa atcctgtggg cctttctgtc 6414
ccacccctgt cagcactgtg ctactgatga tacatcaccc tggggaattc aaccctgcag 6474
atgtcaactg aaggccacaa aaatgaactc catctacaag tgattaccta gttgtgagct 6534
gttggcatgt ggttagaagc catcagaggt gcaagggctt agaaaagacc ctggccagac 6594
ctgactccac tcttaaacct gggtcttctc cttggcggtg ctgtcagcgc acagacccat 6654
gcgcatcccc acccacaacc ctttaccctg atgatctgta ttatatttta atgtatatgt 6714
gaatatattg aaaataa 6731
<210>2
<211>1211
<212>PRT
<213>智人(Homo sapiens)
<400>2
Met Glu Arg Arg Gly Lys Tyr Ser Ser Lys Leu Glu Arg Glu Ser Lys
1 5 10 15
Arg Thr Ser Glu Asn Glu Ala Ile Lys Arg Cys Cys Ser Pro Pro Asn
20 25 30
Glu Leu Gly Phe Arg Arg Gly Ser Ser Tyr Ser Lys His Asp Ser Ser
35 40 45
Ala Ser Arg Tyr Lys Ser Thr Leu Ser Lys Pro Ile Pro Lys Ser Asp
50 55 60
Lys Phe Lys Asn Ser Phe Cys Cys Thr Glu Leu Asn Glu Glu Ile Lys
65 70 75 80
Gln Ser His Ser Phe Ser Leu Gln Thr Pro Cys Ser Lys Gly Ser Glu
85 90 95
Leu Arg Met Ile Asn Lys Asn Pro Glu Arg Glu Lys Ala Gly Ser Pro
100 105 110
Ala Pro Ser Asn Arg Leu Asn Asp Ser Pro Thr Leu Lys Lys Leu Asp
115 120 125
Glu Leu Pro Ile Phe Lys Ser Glu Phe Ile Thr His Asp Ser His Asp
130 135 140
Ser Ile Lys Glu Leu Asp Ser Leu Ser Lys Val Lys Asn Asp Gln Leu
145 150 155 160
Arg Ser Phe Cys Pro Ile Glu Leu Asn Ile Asn Gly Ser Pro Gly Ala
165 170 175
Glu Ser Asp Leu Ala Thr Phe Cys Thr Ser Lys Thr Asp Ala Val Leu
180 185 190
Met Thr Ser Asp Asp Ser Val Thr Gly Ser Glu Leu Ser Pro Leu Val
195 200 205
Lys Ala Cys Met Leu Ser Ser Asn Gly Phe Gln Asn Ile Ser Arg Cys
210 215 220
Lys Glu Lys Asp Leu Asp Asp Thr Cys Met Leu His Lys Lys Ser Glu
225 230 235 240
Ser Pro Phe Arg Glu Thr Glu Pro Leu Val Ser Pro His Gln Asp Lys
245 250 255
Leu Met Ser Met Pro Val Met Thr Val Asp Tyr Ser Lys Thr Val Val
260 265 270
Lys Glu Pro Val Asp Thr Arg Val Ser Cys Cys Lys Thr Lys Asp Ser
275 280 285
Asp Ile Tyr Cys Thr Leu Asn Asp Ser Asn Pro Ser Leu Cys Asn Ser
290 295 300
Glu Ala Glu Asn Ile Glu Pro Ser Val Met Lys Ile Ser Ser Asn Ser
305 310 315 320
Phe Met Asn Val His Leu Glu Ser Lys Pro Val Ile Cys Asp Ser Arg
325 330 335
Asn Leu Thr Asp His Ser Lys Phe Ala Cys Glu Glu Tyr Lys Gln Ser
340 345 350
Ile Gly Ser Thr Ser Ser Ala Ser Val Asn His Phe Asp Asp Leu Tyr
355 360 365
Gln Pro Ile Gly Ser Ser Gly Ile Ala Ser Ser Leu Gln Ser Leu Pro
370 375 380
Pro Gly Ile Lys Val Asp Ser Leu Thr Leu Leu Lys Cys Gly Glu Asn
385 390 395 400
Thr Ser Pro Val Leu Asp Ala Val Leu Lys Ser Lys Lys Ser Ser Glu
405 410 415
Phe Leu Lys His Ala Gly Lys Glu Thr Ile Val Glu Val Gly Ser Asp
420 425 430
Leu Pro Asp Ser Gly Lys Gly Phe Ala Ser Arg Glu Asn Arg Arg Asn
435 440 445
Asn Gly Leu Ser Gly Lys Cys Leu Gln Glu Ala Gln Lys Glu Gly Asn
450 455 460
Ser Ile Leu Pro Glu Arg Arg Gly Arg Pro Glu Ile Ser Leu Asp Glu
465 470 475 480
Arg Gly Glu Gly Gly His Val His Thr Ser Asp Asp Ser Glu Val Val
485 490 495
Phe Ser Ser Cys Asp Leu Asn Leu Thr Met Glu Asp Ser Asp Gly Val
500 505 510
Thr Tyr Ala Leu Lys Cys Asp Ser Ser Gly His Ala Pro Glu Ile Val
515 520 525
Ser Thr Val His Glu Asp Tyr Ser Gly Ser Ser Glu Ser Ser Asn Asp
530 535 540
Glu Ser Asp Ser Glu Asp Thr Asp Ser Asp Asp Ser Ser Ile Pro Arg
545 550 555 560
Asn Arg Leu Gln Ser Val Val Val Val Pro Lys Asn Ser Thr Leu Pro
565 570 575
Met Glu Glu Thr Ser Pro Cys Ser Ser Arg Ser Ser Gln Ser Tyr Arg
580 585 590
His Tyr Ser Asp His Trp Glu Asp Glu Arg Leu Glu Ser Arg Arg His
595 600 605
Leu Tyr Glu Glu Lys Phe Glu Ser Ile Ala Ser Lys Ala Cys Pro Gln
610 615 620
Thr Asp Lys Phe Phe Leu His Lys Gly Thr Glu Lys Asn Pro Glu Ile
625 630 635 640
Ser Phe Thr Gln Ser Ser Arg Lys Gln Ile Asp Asn Arg Leu Pro Glu
645 650 655
Leu Ser His Pro Gln Ser Asp Gly Val Asp Ser Thr Ser His Thr Asp
660 665 670
Val Lys Ser Asp Pro Leu Gly His Pro Asn Ser Glu Glu Thr Val Lys
675 680 685
Ala Lys Ile Pro Ser Arg Gln Gln Glu Glu Leu Pro Ile Tyr Ser Ser
690 695 700
Asp Phe Glu Asp Val Pro Asn Lys Ser Trp Gln Gln Thr Thr Phe Gln
705 710 715 720
Asn Arg Pro Asp Ser Arg Leu Gly Lys Thr Glu Leu Ser Phe Ser Ser
725 730 735
Ser Cys Glu Ile Pro His Val Asp Gly Leu His Ser Ser Glu Glu Leu
740 745 750
Arg Asn Leu Gly Trp Asp Phe Ser Gln Glu Lys Pro Ser Ala Thr Tyr
755 760 765
Gln Gln Pro Asp Ser Ser Tyr Gly Ala Cys Gly Gly His Lys Tyr Gln
770 775 780
Gln Asn Ala Glu Gln Tyr Gly Gly Thr Arg Asp Tyr Trp Gln Gly Asn
785 790 795 800
Gly Tyr Trp Asp Pro Arg Ser Gly Arg Pro Pro Gly Thr Gly Val Val
805 810 815
Tyr Asp Arg Thr Gln Gly Gln Val Pro Asp Ser Leu Thr Asp Asp Arg
820 825 830
Glu Glu Glu Glu Asn Trp Asp Gln Gln Asp Gly Ser His Phe Ser Asp
835 840 845
Gln Ser Asp Lys Phe Leu Leu Ser Leu Gln Lys Asp Lys Gly Ser Val
850 855 860
Gln Ala Pro Glu Ile Ser Ser Asn Ser Ile Lys Asp Thr Leu Ala Val
865 870 875 880
Asn Glu Lys Lys Asp Phe Ser Lys Asn Leu Glu Lys Asn Asp Ile Lys
885 890 895
Asp Arg Gly Pro Leu Lys Lys Arg Arg Gln Glu Ile Glu Ser Asp Ser
900 905 910
Glu Ser Asp Gly Glu Leu Gln Asp Arg Lys Lys Val Arg Val Glu Val
915 920 925
Glu Gln Gly Glu Thr Ser Val Pro Pro Gly Ser Ala Leu Val Gly Pro
930 935 940
Ser Cys Val Met Asp Asp Phe Arg Asp Pro Gln Arg Trp Lys Glu Cys
945 950 955 960
Ala Lys Gln Gly Lys Met Pro Cys Tyr Phe Asp Leu Ile Glu Glu Asn
965 970 975
Val Tyr Leu Thr Glu Arg Lys Lys Asn Lys Ser His Arg Asp Ile Lys
980 985 990
Arg Met Gln Cys Glu Cys Thr Pro Leu Ser Lys Asp Glu Arg Ala Gln
995 1000 1005
Gly Glu Ile Ala Cys Gly Glu Asp Cys Leu Asn Arg Leu Leu Met
1010 1015 1020
Ile Glu Cys Ser Ser Arg Cys Pro Asn Gly Asp Tyr Cys Ser Asn
1025 1030 1035
Arg Arg Phe Gln Arg Lys Gln His Ala Asp Val Glu Val Ile Leu
1040 1045 1050
Thr Glu Lys Lys Gly Trp Gly Leu Arg Ala Ala Lys Asp Leu Pro
1055 1060 1065
Ser Asn Thr Phe Val Leu Glu Tyr Cys Gly Glu Val Leu Asp His
1070 1075 1080
Lys Glu Phe Lys Ala Arg Val Lys Glu Tyr Ala Arg Asn Lys Asn
1085 1090 1095
Ile His Tyr Tyr Phe Met Ala Leu Lys Asn Asp Glu Ile Ile Asp
1100 1105 1110
Ala Thr Gln Lys Gly Asn Cys Ser Arg Phe Met Asn His Ser Cys
1115 1120 1125
Glu Pro Asn Cys Glu Thr Gln Lys Trp Thr Val Asn Gly Gln Leu
1130 1135 1140
Arg Val Gly Phe Phe Thr Thr Lys Leu Val Pro Ser Gly Ser Glu
1145 1150 1155
Leu Thr Phe Asp Tyr Gln Phe Gln Arg Tyr Gly Lys Glu Ala Gln
1160 1165 1170
Lys Cys Phe Cys Gly Ser Ala Asn Cys Arg Gly Tyr Leu Gly Gly
1175 1180 1185
Glu Asn Arg Val Ser Ile Arg Ala Ala Gly Gly Lys Met Lys Lys
1190 1195 1200
Glu Arg Ser Arg Lys Lys Asp Ser
1205 1210
<210>3
<211>1617
<212>DNA
<213>智人(Homo sapiens)
<400>3
atgtccccta tactaggtta ttggaaaatt aagggccttg tgcaacccac tcgacttctt 60
ttggaatatc ttgaagaaaa atatgaagag catttgtatg agcgcgatga aggtgataaa 120
tggcgaaaca aaaagtttga attgggtttg gagtttccca atcttcctta ttatattgat 180
ggtgatgtta aattaacaca gtctatggcc atcatacgtt atatagctga caagcacaac 240
atgttgggtg gttgtccaaa agagcgtgca gagatttcaa tgcttgaagg agcggttttg 300
gatattagat acggtgtttc gagaattgca tatagtaaag actttgaaac tctcaaagtt 360
gattttctta gcaagctacc tgaaatgctg aaaatgttcg aagatcgttt atgtcataaa 420
acatatttaa atggtgatca tgtaacccat cctgacttca tgttgtatga cgctcttgat 480
gttgttttat acatggaccc aatgtgcctg gatgcgttcc caaaattagt ttgttttaaa 540
aaacgtattg aagctatccc acaaattgat aagtacttga aatccagcaa gtatatagca 600
tggcctttgc agggctggca agccacgttt ggtggtggcg accatcctcc aaaatcggat 660
ctgatcgaag gtcgtgggat ccccgaattc ccggggatcc ccatggcccg ggcgacgtcg 720
actgatggtg agcttcagga cagaaagaaa gttagagtgg aggtagagca gggagagaca 780
tcagtgcccc caggttcagc actggttggg ccctcctgtg tcatggatga cttcagggac 840
ccacagcgat ggaaggaatg tgccaagcaa gggaaaatgc catgttactt tgatcttatt 900
gaagaaaatg tttatttaac agaaagaaag aagaataaat ctcatcgaga tattaagcga 960
atgcagtgtg agtgtacacc tctttctaaa gatgaaagag ctcaaggtga aatagcatgt 1020
ggggaagatt gtcttaatcg tcttctcatg attgaatgtt cttctcggtg tccaaatggg 1080
gattattgtt ccaatagacg gtttcagaga aaacagcatg cagatgtgga agtcatactc 1140
acagaaaaga aaggctgggg cttgagagct gccaaagacc ttccttcgaa cacctttgtc 1200
ctagaatatt gtggagaggt actcgatcat aaagagttta aagctcgagt gaaggagtat 1260
gcacgaaaca aaaacatcca ttactatttc atggccctga agaatgatga gataatagat 1320
gccactcaaa aaggaaattg ctctcgtttc atgaatcaca gctgtgaacc aaattgtgaa 1380
acccaaaaat ggactgtgaa cggacaactg agggttgggt tttttaccac caaactggtt 1440
ccttcaggct cagagttaac gtttgactat cagttccaga gatatggaaa agaagcccag 1500
aaatgtttct gcggatcagc caattgccgg ggttacctgg gaggagaaaa cagagtcagc 1560
attagagcag caggagggaa aatgaagaag gaacgatctc gtaagaagga ttcatag 1617
<210>4
<211>538
<212>PRT
<213>智人(Homo sapiens)
<400>4
Met Ser Pro Ile Leu Gly Tyr Trp Lys Ile Lys Gly Leu Val Gln Pro
1 5 10 15
Thr Arg Leu Leu Leu Glu Tyr Leu Glu Glu Lys Tyr Glu Glu His Leu
20 25 30
Tyr Glu Arg Asp Glu Gly Asp Lys Trp Arg Asn Lys Lys Phe Glu Leu
35 40 45
Gly Leu Glu Phe Pro Asn Leu Pro Tyr Tyr Ile Asp Gly Asp Val Lys
50 55 60
Leu Thr Gln Ser Met Ala Ile Ile Arg Tyr Ile Ala Asp Lys His Asn
65 70 75 80
Met Leu Gly Gly Cys Pro Lys Glu Arg Ala Glu Ile Ser Met Leu Glu
85 90 95
Gly Ala Val Leu Asp Ile Arg Tyr Gly Val Ser Arg Ile Ala Tyr Ser
100 105 110
Lys Asp Phe Glu Thr Leu Lys Val Asp Phe Leu Ser Lys Leu Pro Glu
115 120 125
Met Leu Lys Met Phe Glu Asp Arg Leu Cys His Lys Thr Tyr Leu Asn
130 135 140
Gly Asp His Val Thr His Pro Asp Phe Met Leu Tyr Asp Ala Leu Asp
145 150 155 160
Val Val Leu Tyr Met Asp Pro Met Cys Leu Asp Ala Phe Pro Lys Leu
165 170 175
Val Cys Phe Lys Lys Arg Ile Glu Ala Ile Pro Gln Ile Asp Lys Tyr
180 185 190
Leu Lys Ser Ser Lys Tyr Ile Ala Trp Pro Leu Gln Gly Trp Gln Ala
195 200 205
Thr Phe Gly Gly Gly Asp His Pro Pro Lys Ser Asp Leu Ile Glu Gly
210 215 220
Arg Gly Ile Pro Glu Phe Pro Gly Ile Pro Met Ala Arg Ala Thr Ser
225 230 235 240
Thr Asp Gly Glu Leu Gln Asp Arg Lys Lys Val Arg Val Glu Val Glu
245 250 255
Gln Gly Glu Thr Ser Val Pro Pro Gly Ser Ala Leu Val Gly Pro Ser
260 265 270
Cys Val Met Asp Asp Phe Arg Asp Pro Gln Arg Trp Lys Glu Cys Ala
275 280 285
Lys Gln Gly Lys Met Pro Cys Tyr Phe Asp Leu Ile Glu Glu Asn Val
290 295 300
Tyr Leu Thr Glu Arg Lys Lys Asn Lys Ser His Arg Asp Ile Lys Arg
305 310 315 320
Met Gln Cys Glu Cys Thr Pro Leu Ser Lys Asp Glu Arg Ala Gln Gly
325 330 335
Glu Ile Ala Cys Gly Glu Asp Cys Leu Asn Arg Leu Leu Met Ile Glu
340 345 350
Cys Ser Ser Arg Cys Pro Asn Gly Asp Tyr Cys Ser Asn Arg Arg Phe
355 360 365
Gln Arg Lys Gln His Ala Asp Val Glu Val Ile Leu Thr Glu Lys Lys
370 375 380
Gly Trp Gly Leu Arg Ala Ala Lys Asp Leu Pro Ser Asn Thr Phe Val
385 390 395 400
Leu Glu Tyr Cys Gly Glu Val Leu Asp His Lys Glu Phe Lys Ala Arg
405 410 415
Val Lys Glu Tyr Ala Arg Asn Lys Asn Ile His Tyr Tyr Phe Met Ala
420 425 430
Leu Lys Asn Asp Glu Ile Ile Asp Ala Thr Gln Lys Gly Asn Cys Ser
435 440 445
Arg Phe Met Asn His Ser Cys Glu Pro Asn Cys Glu Thr Gln Lys Trp
450 455 460
Thr Val Asn Gly Gln Leu Arg Val Gly Phe Phe Thr Thr Lys Leu Val
465 470 475 480
Pro Ser Gly Ser Glu Leu Thr Phe Asp Tyr Gln Phe Gln Arg Tyr Gly
485 490 495
Lys Glu Ala Gln Lys Cys Phe Cys Gly Ser Ala Asn Cys Arg Gly Tyr
500 505 510
Leu Gly Gly Glu Asn Arg Val Ser Ile Arg Ala Ala Gly Gly Lys Met
515 520 525
Lys Lys Glu Arg Ser Arg Lys Lys Asp Ser
530 535
<210>5
<211>6652
<212>DNA
<213>智人(Homo sapiens)
<400>5
acagggacct aaggacatca tcctattcta aatctgatcg ggactgtaaa actgagacct 60
cttacttaga gatggaaaga agaggcaagt attcttcaaa actagaaaga gaatctaaaa 120
ggacttcaga aaatgaagca attaaaagat gttgttctcc ccctaatgaa ctgggattcc 180
gacgagggtc atcatattct aagcatgaca gtagtgcttc ccgttataaa tctacccttt 240
caaaacctat acccaagtct gataaattta aaaattcttt ctgttgtaca gaattaaatg 300
aagaaatcaa acaatctcat tcttttagtt tacagacacc ttgttcaaaa ggtagtgaat 360
taagaatgat taataaaaat cctgaaagag aaaaggctgg gtctccagct ccatcaaatc 420
gattaaatga ttcacctact ttaaaaaagc tagatgaatt gcctattttt aagtccgaat 480
ttataacaca tgatagccat gatagtatta aggaattaga ctctttatct aaagtgaaga 540
atgatcaatt aagaagtttt tgtcccatag aattaaatat aaatggatct cctggggcag 600
aatctgattt ggcaacattt tgcacttcta aaactgatgc tgttttaatg acttctgatg 660
atagtgtgac tggatcggaa ttatcccctt tggtcaaagc atgcatgctt tcatcaaatg 720
gatttcagaa tattagtagg tgcaaagaaa aagacttgga tgatacctgc atgctgcata 780
agaagtcaga aagcccattt agagaaacag aacctctggt gtcaccacac caagataaac 840
tcatgtctat gccagttatg actgtggatt attccaaaac agtagttaaa gaaccagttg 900
atacgagggt ttcttgctgc aaaaccaaag attcagacat atactgtact ttgaacgata 960
gcaacccttc tttgtgtaac tctgaagctg aaaatattga gccttcagtt atgaagattt 1020
cttcaaatag ctttatgaat gtgcatttgg aatcaaaacc agttatatgt gatagtagaa 1080
atttgacaga tcactcaaaa tttgcatgtg aagaatataa gcagagcatc ggtagcacta 1140
gttcagcttc tgttaatcat tttgatgatt tatatcaacc tattgggagt tcaggtattg 1200
cttcatctct tcagagtctt ccaccaggaa taaaggtgga cagtctaact ctcttgaaat 1260
gcggagagaa cacatctcca gttctggatg cagtgctaaa gagtaaaaaa agttcagagt 1320
ttttaaagca tgcagggaaa gaaacaatag tagaagtagg tagtgacctt cctgattcag 1380
gaaagggatt tgcttccagg gagaacaggc gtaataatgg gttatctggg aaatgtttgc 1440
aagaggctca aaaagaaggg aattccatat tgcctgaaag aagaggaaga ccagaaatct 1500
ctttagatga aagaggagaa ggaggacatg tgcatacttc tgatgactca gaagttgtat 1560
tttcttcttg tgatttgaat ttaaccatgg aagacagtga tggtgtaact tatgcattaa 1620
agtgtgacag tagtggtcat gccccagaaa ttgtgtctac agttcatgaa gattattctg 1680
gctcttctga aagttcaaat gatgaaagtg attcagaaga tacggattcg gatgatagca 1740
gtattccaag aaaccgtctc cagtctgttg tggttgtgcc aaagaattct actttgccca 1800
tggaagaaac aagtccttgt tcttctcgga gcagtcaaag ttatagacac tattctgacc 1860
attgggaaga tgagagattg gagtcaagga gacatttgta tgaggaaaaa tttgaaagta 1920
tagcaagtaa agcctgtcct caaactgata agtttttcct tcataaagga acagagaaga 1980
atccggaaat ttcttttaca cagtccagta gaaaacaaat agataaccgc ctgcctgaac 2040
tttctcatcc tcagagtgat ggggttgata gtacaagtca tacagatgtg aaatctgacc 2100
ctctgggtca cccaaattca gaggaaaccg tgaaagccaa aataccttct aggcagcaag 2160
aagagctgcc aatttattct tctgattttg aagatgtccc aaataagtct tggcaacaga 2220
ccactttcca aaacaggcca gatagtagac tgggaaaaac agaattgagt ttttcttcct 2280
cttgtgagat accacatgtg gatggcttgc actcatcaga agagctcaga aacttaggtt 2340
gggacttctc tcaagaaaag ccttctgcca cgtatcagca acctgacagt agctatggag 2400
cttgtggtgg acacaagtat cagcaaaatg cagaacagta tggtgggaca cgtgattact 2460
ggcaaggcaa tggttactgg gatccaagat caggtagacc tcctggaact ggggttgtgt 2520
atgatcgaac tcaaggacaa gtaccagatt ccctaacaga tgatcgtgaa gaagaggaga 2580
attgggatca acaggatgga tcccattttt cagaccagtc cgataaattt cttctatccc 2640
ttcagaaaga caaggggtca gtgcaagcac ctgaaataag cagcaattcc attaaggaca 2700
ctttagctgt gaatgaaaag aaagattttt caaaaaactt agaaaaaaat gatatcaaag 2760
atagagggcc tcttaaaaaa aggaggcagg aaatagagag tgattctgaa agtgatggtg 2820
agcttcagga cagaaagaaa gttagagtgg aggtagagca gggagagaca tcagtgcccc 2880
caggttcagc actggttggg ccctcctgtg tcatggatga cttcagggac ccacagcgat 2940
ggaaggaatg tgccaagcaa gggaaaatgc catgttactt tgatcttatt gaagaaaatg 3000
tttatttaac agaaagaaag aagaataaat ctcatcgaga tattaagcga atgcagtgtg 3060
agtgtacacc tctttctaaa gatgaaagag ctcaaggtga aatagcatgt ggggaagatt 3120
gtcttaatcg tcttctcatg attgaatgtt cttctcggtg tccaaatggg gattattgtt 3180
ccaatagacg gtttcagaga aaacagcatg cagatgtgga agtcatactc acagaaaaga 3240
aaggctgggg cttgagagct gccaaagacc ttccttcgaa cacctttgtc ctagaatatt 3300
gtggagaggt actcgatcat aaagagttta aagctcgagt gaaggagtat gcacgaaaca 3360
aaaacatcca ttactatttc atggccctga agaatgatga gataatagat gccactcaaa 3420
aaggaaattg ctctcgtttc atgaatcaca gctgtgaacc aaattgtgaa acccaaaaat 3480
ggactgtgaa cggacaactg agggttgggt tttttaccac caaactggtt ccttcaggct 3540
cagagttaac gtttgactat cagttccaga gatatggaaa agaagcccag aaatgtttct 3600
gcggatcagc caattgccgg ggttacctgg gaggagaaaa cagagtcagc attagagcag 3660
caggagggaa aatgaagaag gaacgatctc gtaagaagga ttcagtggat ggagagctag 3720
aagctctgat ggaaaatggt gagggtctct ctgataaaaa ccaggtgccc agcttatccc 3780
ggctaatggt tagaattgaa actttggagc agaaacttac ctgtctggaa ctcatacaga 3840
acacacactc acagtcctgc ctgaagtcct ttctggaacg tcatgggctg tctttgttgt 3900
ggatctggat ggcagagcta ggtgacggcc gggaaagtaa ccagaagctt caggaagaga 3960
ttataaagac tttggaacac ttgcccattc ctactaaaaa tatgttggag gaaagcaaag 4020
tacttccaat tattcaacgc tggtctcaga ctaagactgc tgtccctccg ttgagtgaag 4080
gagatgggta ttctagtgag aatacatcgc gtgctcatac accactcaac acacctgatc 4140
cttccaccaa gctgagcaca gaagctgaca cagacactcc caagaaacta atgtttcgca 4200
gactgaaaat tataagtgaa aatagcatgg acagtgcaat ctctgatgca accagtgagc 4260
tagaaggcaa ggatggcaaa gaggatcttg atcaattaga aaatgtccct gtagaggaag 4320
aggaagaatt gcagtcacaa cagctactcc cacaacagct gcctgaatgc aaagttgata 4380
gtgaaaccaa catagaagct agtaagctac ctacatctga accagaagct gacgctgaaa 4440
tagagcccaa agagagcaac ggcacaaaac tagaagaacc tattaatgaa gaaacaccat 4500
cccaagatga agaggagggt gtgtctgatg tggagagtga aaggagccaa gaacagccag 4560
ataaaacagt ggatataagt gatttggcca ccaaactcct ggacagttgg aaagacctaa 4620
aggaggtata tcgaattcca aagaaaagtc aaactgaaaa ggaaaacaca acaactgaac 4680
gaggaaggga tgctgttggc ttcagagatc aaacacctgc cccgaagact cctaataggt 4740
caagagagag agacccagac aagcaaactc aaaataaaga gaaaaggaaa cgaagaagct 4800
ccctctcacc accctcttct gcctatgagc ggggaacaaa aaggccagat gacagatatg 4860
atacaccaac ttctaaaaag aaagtacgaa ttaaagaccg caataaactt tctacagagg 4920
aacgccggaa gttgtttgag caagaggtgg ctcaacggga ggctcagaaa caacagcaac 4980
agatgcagaa cctgggaatg acatcaccac tgccctatga ctctcttggt tataatgccc 5040
cgcatcatcc ctttgctggt tacccaccag gttatcccat gcaggcctat gtggatccca 5100
gcaaccctaa tgctggaaag gtgctcctgc ccacacccag catggaccca gtgtgttctc 5160
ctgctcctta tgatcatgct cagcccttgg tgggacattc tacagaaccc ctttctgccc 5220
ctccaccagt accagtggtg ccacatgtgg cagctcctgt ggaagtttcc agttcccagt 5280
atgtggccca gagtgatggt gtagtacacc aagactccag cgttgctgtc ttgccagtgc 5340
cggcccccgg cccagttcag ggacagaatt atagtgtttg ggattcaaac caacagtctg 5400
tcagtgtaca gcagcagtac tctcctgcac agtctcaagc aaccatatat tatcaaggac 5460
agacatgtcc aacagtctat ggtgtgacat caccttattc acagacaact ccaccaattg 5520
tacagagtta tgcccagcca agtcttcagt atatccaggg gcaacagatt ttcacagctc 5580
atccacaagg agtggtggta cagccagccg cagcagtgac tacaatagtt gcaccagggc 5640
agcctcagcc cttgcagcca tctgaaatgg ttgtgacaaa taatctcttg gatctgccgc 5700
ccccctctcc tcccaaacca aaaaccattg tcttacctcc caactggaag acagctcgag 5760
atccagaagg gaagatttat tactaccatg tgatcacaag gcagactcag tgggatcctc 5820
ctacttggga aagcccagga gatgatgcca gccttgagca tgaagctgag atggacctgg 5880
gaactccaac atatgatgaa aaccccatga aggcctcgaa aaagcccaag acagcagaag 5940
cagacacctc cagtgaacta gcaaagaaaa gcaaagaagt attcagaaaa gagatgtccc 6000
agttcatcgt ccagtgcctg aacccttacc ggaaacctga ctgcaaagtg ggaagaatta 6060
ccacaactga agactttaaa catctggctc gcaagctgac tcacggtgtt atgaataagg 6120
agctgaagta ctgtaagaat cctgaggacc tggagtgcaa tgagaatgtg aaacacaaaa 6180
ccaaggagta cattaagaag tacatgcaga agtttggggc tgtttacaaa cccaaagagg 6240
acactgaatt agagtgactg ttgggccagg gtgggaggat gggtggtcag gtaagacaga 6300
ctctagggag aggaaatcct gtgggccttt ctgtcccacc cctgtcagca ctgtgctact 6360
gatgatacat caccctgggg aattcaaccc tgcagatgtc aactgaaggc cacaaaaatg 6420
aactccatct acaagtgatt acctagttgt gagctgttgg catgtggtta gaagccatca 6480
gaggtgcaag ggcttagaaa agaccctggc cagacctgac tccactctta aacctgggtc 6540
ttctccttgg cggtgctgtc agcgcacaga cccatgcgca tccccaccca caacccttta 6600
ccctgatgat ctgtattata ttttaatgta tatgtgaata tattgaaaat aa 6652
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Arg Thr Ser Glu Asn Glu Ala Ile Lys Arg Cys Cys Ser Pro Pro Asn
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Lys Phe Lys Asn Ser Phe Cys Cys Thr Glu Leu Asn Glu Glu Ile Lys
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Gln Ser His Ser Phe Ser Leu Gln Thr Pro Cys Ser Lys Gly Ser Glu
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Leu Arg Met Ile Asn Lys Asn Pro Glu Arg Glu Lys Ala Gly Ser Pro
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Ala Pro Ser Asn Arg Leu Asn Asp Ser Pro Thr Leu Lys Lys Leu Asp
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Glu Leu Pro Ile Phe Lys Ser Glu Phe Ile Thr His Asp Ser His Asp
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Ser Ile Lys Glu Leu Asp Ser Leu Ser Lys Val Lys Asn Asp Gln Leu
145 150 155 160
Arg Ser Phe Cys Pro Ile Glu Leu Asn Ile Asn Gly Ser Pro Gly Ala
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Glu Ser Asp Leu Ala Thr Phe Cys Thr Ser Lys Thr Asp Ala Val Leu
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Met Thr Ser Asp Asp Ser Val Thr Gly Ser Glu Leu Ser Pro Leu Val
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Lys Ala Cys Met Leu Ser Ser Asn Gly Phe Gln Asn Ile Ser Arg Cys
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Lys Glu Lys Asp Leu Asp Asp Thr Cys Met Leu His Lys Lys Ser Glu
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Ser Pro Phe Arg Glu Thr Glu Pro Leu Val Ser Pro His Gln Asp Lys
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Leu Met Ser Met Pro Val Met Thr Val Asp Tyr Ser Lys Thr Val Val
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Asp Ile Tyr Cys Thr Leu Asn Asp Ser Asn Pro Ser Leu Cys Asn Ser
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Glu Ala Glu Asn Ile Glu Pro Ser Val Met Lys Ile Ser Ser Asn Ser
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Phe Met Asn Val His Leu Glu Ser Lys Pro Val Ile Cys Asp Ser Arg
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Asn Leu Thr Asp His Ser Lys Phe Ala Cys Glu Glu Tyr Lys Gln Ser
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Gln Pro Ile Gly Ser Ser Gly Ile Ala Ser Ser Leu Gln Ser Leu Pro
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Ser Thr Val His Glu Asp Tyr Ser Gly Ser Ser Glu Ser Ser Asn Asp
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Ala Lys Ile Pro Ser Arg Gln Gln Glu Glu Leu Pro Ile Tyr Ser Ser
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Ser Cys Glu Ile Pro His Val Asp Gly Leu His Ser Ser Glu Glu Leu
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Gln Gln Pro Asp Ser Ser Tyr Gly Ala Cys Gly Gly His Lys Tyr Gln
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Gln Asn Ala Glu Gln Tyr Gly Gly Thr Arg Asp Tyr Trp Gln Gly Asn
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Ala Lys Gln Gly Lys Met Pro Cys Tyr Phe Asp Leu Ile Glu Glu Asn
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Ala Thr Gln Lys Gly Asn Cys Ser Arg Phe Met Asn His Ser Cys
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Glu Asn Arg Val Ser Ile Arg Ala Ala Gly Gly Lys Met Lys Lys
1190 1195 1200
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1220 1225 1230
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1340 1345 1350
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1355 1360 1365
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Thr Thr Glu Arg Gly Arg Asp Ala Val Gly Phe Arg Asp Gln Thr
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Thr Ala Glu Ala Asp Thr Ser Ser Glu Leu Ala Lys Lys Ser Lys
1955 1960 1965
Glu Val Phe Arg Lys Glu Met Ser Gln Phe Ile Val Gln Cys Leu
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Tyr Met Gln Lys Phe Gly Ala Val Tyr Lys Pro Lys Glu Asp Thr
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Glu Leu Glu
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<210>7
<211>32
<212>DNA
<213>人工序列
<220>
<221>misc_feature
<223>引物
<400>7
ctcagatcta acagggacct aaggacatca tc 32
<210>8
<211>38
<212>DNA
<213>人工序列
<220>
<221>misc_feature
<223>引物
<400>8
cgcggtacct tattttcaat atattcacat atacatta 38
<210>9
<211>31
<212>DNA
<213>人工序列
<220>
<221>misc_feature
<223>引物
<400>9
gcgtcgacgt gatggtgagc ttcaggacag a 31
<210>10
<211>32
<212>DNA
<213>人工序列
<220>
<221>misc_feature
<223>引物
<400>10
aactgcagat gtgaggcaga caagtcattc ca 32
Claims (10)
1.一种分离的人HSPC069SET多肽,其特征在于,该多肽选自下组:
(a)具有SEQ ID NO:2氨基酸序列的多肽;
(b)将SEQ ID NO:2氨基酸序列经过一个或多个氨基酸残基的取代、缺失或添加而形成的,且具有组蛋白甲基转移功能的由(a)衍生的多肽,
附加条件是所述的多肽不具有SEQ ID NO:6所示的氨基酸序列。
2.如权利要求1所述的多肽,其特征在于,该多肽是具有SEQ ID NO:2或4氨基酸序列的多肽。
3.一种分离的多核苷酸,其特征在于,该多核苷酸序列选自下组:
(a)编码如权利要求1所述多肽的多核苷酸;
(b)与多核苷酸(a)互补的多核苷酸。
4.如权利要求3所述的多核苷酸,其特征在于,该多核苷酸编码具有SEQ ID NO:2所示氨基酸序列的多肽。
5.如权利要求3所述的多核苷酸,其特征在于,该多核苷酸的序列选自下组的一种:
(a)具有SEQ ID NO:1中72-3704位的序列;
(b)具有SEQ ID NO:1中1-6731位的序列;
(c)具有SEQ ID NO:3中1-1614位的序列。
6.一种载体,其特征在于,它含有权利要求3所述的多核苷酸。
7.一种遗传工程化的宿主细胞,其特征在于,它含有权利要求6所述的载体。
8.一种多肽的制备方法,其特征在于,该方法包含:
(a)在适合表达的条件下,培养权利要求7所述的宿主细胞;
(b)从培养物中分离出人HSPC069SET蛋白多肽。
9.一种能与权利要求1所述的人HSPC069SET蛋白特异性结合的抗体。
10.一种检测样品中是否存在HSPC069SET蛋白的方法,其特征在于,包括以下步骤:
将样品与权利要求9所述的抗体接触,
观察是否形成抗体复合物,形成了抗体复合物就表示样品中存在HSPC069SET蛋白。
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CN100577800C (zh) * | 2007-01-29 | 2010-01-06 | 中国科学院遗传与发育生物学研究所 | 一种组蛋白甲基化转移酶及其编码基因与应用 |
WO2011160206A1 (en) | 2010-06-23 | 2011-12-29 | Morin Ryan D | Biomarkers for non-hodgkin lymphomas and uses thereof |
US9175331B2 (en) | 2010-09-10 | 2015-11-03 | Epizyme, Inc. | Inhibitors of human EZH2, and methods of use thereof |
CA3176977A1 (en) | 2010-09-10 | 2012-03-15 | Epizyme, Inc. | Inhibitors of human ezh2, and methods of use thereof |
JO3438B1 (ar) | 2011-04-13 | 2019-10-20 | Epizyme Inc | مركبات بنزين مستبدلة بأريل أو أريل غير متجانس |
US10301290B2 (en) * | 2012-04-13 | 2019-05-28 | Epizyme, Inc. | Combination therapy for treating cancer |
CN110041250A (zh) | 2012-10-15 | 2019-07-23 | Epizyme股份有限公司 | 经取代的苯化合物 |
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