胱抑素B

血清胱抑素B
已知的結構
PDB	直系同源搜尋: PDBe RCSB
PDBID列表
	1STF、2OCT、4N6V
識別號
別名	CSTB；, CST6, EPM1, EPM1A, PME, STFB, ULD, Cystatin B, CPI-B
外部ID	OMIM：601145 MGI：109514 HomoloGene：79 GeneCards：CSTB
相關疾病
	Unverricht-Lundborg syndrome
基因位置（人類）
染色體	21號染色體
終止	43,776,330 bp
基因位置（小鼠）
染色體	小鼠10號染色體
終止	78,263,456 bp
RNA表現模式
	查閱更多表現資料
基因本體
分子功能	• peptidase inhibitor activity; • 蛋白酶結合; • endopeptidase inhibitor activity; • cysteine-type endopeptidase inhibitor activity; • RNA binding;
細胞組分	• 細胞質; • 核仁; • 外排體; • 胞內; • 細胞核; • 細胞外區域; • 細胞外空間; • 細胞質基質; • secretory granule lumen; • tertiary granule lumen; • ficolin-1-rich granule lumen; • collagen-containing extracellular matrix;
生物學過程	• adult locomotory behavior; • negative regulation of proteolysis; • negative regulation of peptidase activity; • negative regulation of endopeptidase activity; • neutrophil degranulation;
	Sources:Amigo / QuickGO
直系同源
	1476
	13014
	ENSG00000160213
	ENSMUSG00000005054
	P04080
	Q62426
	NM_000100
	NM_007793
	NP_000091
	NP_031819
	維基資料
檢視/編輯人類	檢視/編輯小鼠

胱抑素B（英文：Cystatin-B）是一種在人體中由CSTB基因編碼的蛋白質。^[6]^[7]

胱抑素超家族包括含有多個胱抑素樣序列的蛋白質。一些成員是活性半胱胺酸蛋白酶抑制劑，而其他成員已經失去或可能從未獲得這種抑制活性。超家族中有3個抑制家族，包括1型胱抑素（stefin）、2型胱抑素和激肽原。該基因編碼一種作為細胞內半胱胺酸蛋白酶抑制劑而起作用的stefin。胱抑素B能夠形成由非共價作用力穩定的二聚體，抑制木瓜蛋白酶和組織蛋白酶L1、H和B。胱抑素B被認為在防止蛋白酶從溶體洩漏方面發揮作用。有證據表明，該基因突變是導致進行性肌陣攣性癲癇患者出現主要缺陷的原因。^[7]

交互作用[編輯]

胱抑素B已被證明與組織蛋白酶B產生交互作用。^[8]^[9]

參考文獻[編輯]

^ 與血清胱抑素B相關的疾病；在維基數據上查看/編輯參考.
^ ^2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000160213 - Ensembl, May 2017
^ ^3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000005054 - 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.
^ Pennacchio LA, Lehesjoki AE, Stone NE, Willour VL, Virtaneva K, Miao J, D'Amato E, Ramirez L, Faham M, Koskiniemi M, Warrington JA, Norio R, de la Chapelle A, Cox DR, Myers RM. Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1). Science. Apr 1996, 271 (5256): 1731–4. Bibcode:1996Sci...271.1731P. PMID 8596935. S2CID 84361089. doi:10.1126/science.271.5256.1731.
^ ^7.0 ^7.1 Entrez Gene: CSTB cystatin B (stefin B).
^ Pavlova, Alona; Björk Ingemar. Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases. Biochemistry (United States). Sep 2003, 42 (38): 11326–33. ISSN 0006-2960. PMID 14503883. doi:10.1021/bi030119v.
^ Pol, E; Björk I. Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases. Protein Sci. (United States). Sep 2001, 10 (9): 1729–38. ISSN 0961-8368. PMC 2253190 . PMID 11514663. doi:10.1110/ps.11901.

拓展閱讀[編輯]

Turk V, Bode W. The cystatins: protein inhibitors of cysteine proteinases.. FEBS Lett. 1991, 285 (2): 213–9. PMID 1855589. S2CID 40444629. doi:10.1016/0014-5793(91)80804-C.
Järvinen M, Rinne A, Hopsu-Havu VK. Human cystatins in normal and diseased tissues--a review.. Acta Histochem. 1988, 82 (1): 5–18. PMID 3122506. doi:10.1016/s0065-1281(87)80043-0.
Brown WM, Dziegielewska KM. Friends and relations of the cystatin superfamily--new members and their evolution.. Protein Sci. 1997, 6 (1): 5–12. PMC 2143511 . PMID 9007972. doi:10.1002/pro.5560060102.
Kos J, Lah TT. Cysteine proteinases and their endogenous inhibitors: target proteins for prognosis, diagnosis and therapy in cancer (review).. Oncol. Rep. 1998, 5 (6): 1349–61. PMID 9769367. doi:10.3892/or.5.6.1349.
Stubbs MT, Laber B, Bode W, et al. The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction.. EMBO J. 1990, 9 (6): 1939–47. PMC 551902 . PMID 2347312. doi:10.1002/j.1460-2075.1990.tb08321.x.
Jerala R, Trstenjak M, Lenarcic B, Turk V. Cloning a synthetic gene for human stefin B and its expression in E. coli.. FEBS Lett. 1988, 239 (1): 41–4. PMID 3053245. S2CID 33859701. doi:10.1016/0014-5793(88)80541-6.
Lenarcic B, Kos J, Dolenc I, et al. Cathepsin D inactivates cysteine proteinase inhibitors, cystatins.. Biochem. Biophys. Res. Commun. 1988, 154 (2): 765–72. PMID 3261170. doi:10.1016/0006-291X(88)90206-9.
Ritonja A, Machleidt W, Barrett AJ. Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver.. Biochem. Biophys. Res. Commun. 1985, 131 (3): 1187–92. PMID 3902020. doi:10.1016/0006-291X(85)90216-5.
Spiess E, Brüning A, Gack S, et al. Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level.. J. Histochem. Cytochem. 1994, 42 (7): 917–29. PMID 8014475. doi:10.1177/42.7.8014475 .
Lehesjoki AE, Koskiniemi M, Norio R, et al. Localization of the EPM1 gene for progressive myoclonus epilepsy on chromosome 21: linkage disequilibrium allows high resolution mapping.. Hum. Mol. Genet. 1993, 2 (8): 1229–34. PMID 8104628. doi:10.1093/hmg/2.8.1229.
Pennacchio LA, Myers RM. Isolation and characterization of the mouse cystatin B gene.. Genome Res. 1997, 6 (11): 1103–9. PMID 8938434. doi:10.1101/gr.6.11.1103 .
Lalioti MD, Mirotsou M, Buresi C, et al. Identification of mutations in cystatin B, the gene responsible for the Unverricht-Lundborg type of progressive myoclonus epilepsy (EPM1).. Am. J. Hum. Genet. 1997, 60 (2): 342–51. PMC 1712389 . PMID 9012407.
Lafrenière RG, Rochefort DL, Chrétien N, et al. Unstable insertion in the 5' flanking region of the cystatin B gene is the most common mutation in progressive myoclonus epilepsy type 1, EPM1.. Nat. Genet. 1997, 15 (3): 298–302. PMID 9054946. S2CID 21180258. doi:10.1038/ng0397-298.
Virtaneva K, D'Amato E, Miao J, et al. Unstable minisatellite expansion causing recessively inherited myoclonus epilepsy, EPM1.. Nat. Genet. 1997, 15 (4): 393–6. PMID 9090386. S2CID 24971949. doi:10.1038/ng0497-393.
Bespalova IN, Adkins S, Pranzatelli M, Burmeister M. Novel cystatin B mutation and diagnostic PCR assay in an Unverricht-Lundborg progressive myoclonus epilepsy patient. (PDF). Am. J. Med. Genet. 1997, 74 (5): 467–71. PMID 9342192. doi:10.1002/(SICI)1096-8628(19970919)74:5<467::AID-AJMG1>3.0.CO;2-L. hdl:2027.42/38271 .

外部連結[編輯]

GeneReviews/NCBI/NIH/UW entry on Unverricht-Lundborg Disease or EPM1 （頁面存檔備份，存於網際網路檔案館）
The MEROPS online database for peptidases and their inhibitors: I25.003^{[失效連結]}
PDBe-KB （頁面存檔備份，存於網際網路檔案館） provides an overview of all the structure information available in the PDB for Human Cystatin-B

[1] 與血清胱抑素B相關的疾病；在維基數據上查看/編輯參考.

[refGRCh38Ensembl-2] 2.0 ^2.1 ^2.2 GRCh38: Ensembl release 89: ENSG00000160213 - Ensembl, May 2017

[refGRCm38Ensembl-3] 3.0 ^3.1 ^3.2 GRCm38: Ensembl release 89: ENSMUSG00000005054 - Ensembl, May 2017

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

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

[pmid8596935-6] Pennacchio LA, Lehesjoki AE, Stone NE, Willour VL, Virtaneva K, Miao J, D'Amato E, Ramirez L, Faham M, Koskiniemi M, Warrington JA, Norio R, de la Chapelle A, Cox DR, Myers RM. Mutations in the gene encoding cystatin B in progressive myoclonus epilepsy (EPM1). Science. Apr 1996, 271 (5256): 1731–4. Bibcode:1996Sci...271.1731P. PMID 8596935. S2CID 84361089. doi:10.1126/science.271.5256.1731.

[entrez-7] 7.0 ^7.1 Entrez Gene: CSTB cystatin B (stefin B).

[pmid14503883-8] Pavlova, Alona; Björk Ingemar. Grafting of features of cystatins C or B into the N-terminal region or second binding loop of cystatin A (stefin A) substantially enhances inhibition of cysteine proteinases. Biochemistry (United States). Sep 2003, 42 (38): 11326–33. ISSN 0006-2960. PMID 14503883. doi:10.1021/bi030119v.

[pmid11514663-9] Pol, E; Björk I. Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases. Protein Sci. (United States). Sep 2001, 10 (9): 1729–38. ISSN 0961-8368. PMC 2253190 . PMID 11514663. doi:10.1110/ps.11901.

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