组织蛋白酶W

组织蛋白酶W
识别号
别名	CTSW；, LYPN, cathepsin W
外部ID	OMIM：602364 MGI：1338045 HomoloGene：37471 GeneCards：CTSW
基因位置（人类）
染色体	11号染色体
终止	65,883,741 bp
基因位置（小鼠）
染色体	小鼠19号染色体
终止	5,518,535 bp
RNA表达模式
	查阅更多表达数据
基因本体
分子功能	• 肽酶活性; • cysteine-type endopeptidase activity; • 半胱氨酸型肽酶活性; • 水解酶活性;
细胞组分	• 溶酶体; • 膜; • platelet dense granule lumen; • 细胞外区域; • 细胞外空间; • 内质网;
生物学过程	• proteolysis involved in cellular protein catabolic process; • 免疫反应; • 蛋白酶解; • platelet degranulation;
	Sources:Amigo / QuickGO
直系同源
	1521
	13041
	ENSG00000172543
	ENSMUSG00000024910
	P56202
	P56203
	NM_001335
	NM_009985
	NP_001326
	NP_034115
	维基数据
查看/编辑人类	查看/编辑小鼠

组织蛋白酶W（英语：Cathepsin W）是一种在人体中由CTSW基因编码的蛋白质。^[5]^[6]^[7]

该基因编码的蛋白质是半胱氨酸组织蛋白酶肽酶C1家族的成员，是一种半胱氨酸蛋白酶组织蛋白酶，可能在T细胞溶细胞活性的机制或调节中具有特定功能。编码的蛋白质被发现与自然杀伤细胞和细胞毒性T细胞的内质网内的细胞膜有关。该基因的表达被白细胞介素2上调。^[7]

参见

组织蛋白酶

参考文献

^ ^1.0 ^1.1 ^1.2 GRCh38: Ensembl release 89: ENSG00000172543 - Ensembl, May 2017
^ ^2.0 ^2.1 ^2.2 GRCm38: Ensembl release 89: ENSMUSG00000024910 - Ensembl, May 2017
^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Linnevers C, Smeekens SP, Brömme D. Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes. FEBS Lett. May 1997, 405 (3): 253–9. PMID 9108299. S2CID 45420314. doi:10.1016/S0014-5793(97)00118-X  .
^ Wex T, Levy B, Smeekens SP, Ansorge S, Desnick RJ, Bromme D. Genomic structure, chromosomal localization, and expression of human cathepsin W. Biochem Biophys Res Commun. Aug 1998, 248 (2): 255–61. PMID 9675123. doi:10.1006/bbrc.1998.8954.
^ ^7.0 ^7.1 Entrez Gene: CTSW cathepsin W.

阅读

Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).. Genome Res. 2004, 14 (10B): 2121–7. PMC 528928  . PMID 15489334. doi:10.1101/gr.2596504.
Meinhardt C, Peitz U, Treiber G, et al. Identification of a novel isoform predominantly expressed in gastric tissue and a triple-base pair polymorphism of the cathepsin W gene.. Biochem. Biophys. Res. Commun. 2004, 321 (4): 975–80. PMID 15358123. doi:10.1016/j.bbrc.2004.07.056.
Zhang Z, Henzel WJ. Signal peptide prediction based on analysis of experimentally verified cleavage sites.. Protein Sci. 2005, 13 (10): 2819–24. PMC 2286551  . PMID 15340161. doi:10.1110/ps.04682504.
Strausberg RL, Feingold EA, Grouse LH, et al. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.. Proc. Natl. Acad. Sci. U.S.A. 2003, 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. PMC 139241  . PMID 12477932. doi:10.1073/pnas.242603899  .
Buhling F, Kellner U, Guenther D, et al. Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal tract.. Biol. Chem. 2003, 383 (7–8): 1285–9. PMID 12437118. S2CID 23389714. doi:10.1515/BC.2002.144.
Wex T, Bühling F, Wex H, et al. Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum.. J. Immunol. 2001, 167 (4): 2172–8. PMID 11490002. doi:10.4049/jimmunol.167.4.2172  .
Wex T, Levy B, Wex H, Brömme D. Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like cysteine proteases.. Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology. 2000, 477: 271–80. ISBN 0-306-46383-0. PMID 10849754. doi:10.1007/0-306-46826-3_29.
Brinkworth RI, Tort JF, Brindley PJ, Dalton JP. Phylogenetic relationships and theoretical model of human cathepsin W (lymphopain), a cysteine proteinase from cytotoxic T lymphocytes.. Int. J. Biochem. Cell Biol. 2000, 32 (3): 373–84. PMID 10716634. doi:10.1016/S1357-2725(99)00129-6.
Wex T, Levy B, Wex H, Brömme D. Human cathepsins F and W: A new subgroup of cathepsins.. Biochem. Biophys. Res. Commun. 1999, 259 (2): 401–7. PMID 10362521. doi:10.1006/bbrc.1999.0700.
Brown J, Matutes E, Singleton A, et al. Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase.. Leukemia. 1998, 12 (11): 1771–81. PMID 9823953. doi:10.1038/sj.leu.2401164  .

外部链接

The MEROPS online database for peptidases and their inhibitors: C01.037^{[失效链接]}

[refGRCh38Ensembl-1] 1.0 ^1.1 ^1.2 GRCh38: Ensembl release 89: ENSG00000172543 - Ensembl, May 2017

[refGRCm38Ensembl-2] 2.0 ^2.1 ^2.2 GRCm38: Ensembl release 89: ENSMUSG00000024910 - Ensembl, May 2017

[3] Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9108299-5] Linnevers C, Smeekens SP, Brömme D. Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes. FEBS Lett. May 1997, 405 (3): 253–9. PMID 9108299. S2CID 45420314. doi:10.1016/S0014-5793(97)00118-X  .

[pmid9675123-6] Wex T, Levy B, Smeekens SP, Ansorge S, Desnick RJ, Bromme D. Genomic structure, chromosomal localization, and expression of human cathepsin W. Biochem Biophys Res Commun. Aug 1998, 248 (2): 255–61. PMID 9675123. doi:10.1006/bbrc.1998.8954.

[entrez-7] 7.0 ^7.1 Entrez Gene: CTSW cathepsin W.

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