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维基百科

组织蛋白酶H

组织蛋白酶H(英文:Cathepsin H)是一种在人体中由CTSH基因编码的蛋白质[6][7]

组织蛋白酶H
已知的結構
PDB直系同源搜索: PDBe RCSB
識別號
别名CTSH;, ACC-4, ACC-5, CPSB, minichain, ACC4, ACC5, cathepsin H
外部IDOMIM:116820 MGI:107285 HomoloGene:36159 GeneCards:CTSH
相關疾病
躁鬱症、​1型糖尿病[1]
基因位置(人类
染色体15號染色體[2]
基因座15q25.1起始78,921,058 bp[2]
终止78,949,574 bp[2]
RNA表达模式
查阅更多表达数据
直系同源
物種人類小鼠
Entrez
Ensembl
UniProt
mRNA​序列

NM_004390
​NM_148979
​NM_001319137

NM_007801
​NM_001312649

蛋白序列

NP_001306066
​NP_004381

NP_001299578
​NP_031827

基因位置​(UCSC)Chr 15: 78.92 – 78.95 MbChr 9: 89.94 – 89.96 Mb
PubMed​查找[4][5]
維基數據
檢視/編輯人類檢視/編輯小鼠

该基因编码的蛋白质是木瓜样蛋白酶英语Papain-like protease,一种溶酶体半胱氨酸蛋白酶,在溶酶体蛋白质的整体降解中很重要。它由二硫键连接的重链和轻链的二聚体组成,均由单一蛋白质前体产生。编码的蛋白质属于肽酶C1蛋白质家族,既可以作为氨肽酶英语Aminopeptidase,也可以作为内肽酶。该基因的表达增加与前列腺肿瘤的恶性进展有关。该基因已发现了编码不同蛋白异构体的两种转录变体。[7]

参考文献

  1. ^ 與组织蛋白酶H相關的疾病;在維基數據上查看/編輯參考. 
  2. ^ 2.0 2.1 2.2 GRCh38: Ensembl release 89: ENSG00000103811 - Ensembl, May 2017
  3. ^ 3.0 3.1 3.2 GRCm38: Ensembl release 89: ENSMUSG00000032359 - 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. 
  6. ^ Fuchs R, Machleidt W, Gassen HG. Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H. Biol Chem Hoppe-Seyler. Feb 1989, 369 (6): 469–75. PMID 2849458. doi:10.1515/bchm3.1988.369.1.469. 
  7. ^ 7.0 7.1 Entrez Gene: CTSH cathepsin H. 

拓展阅读

  • Sawicki G, Warwas M. Cathepsin H from human placenta.. Acta Biochim. Pol. 1990, 36 (3–4): 343–51. PMID 2486008. 
  • Fuchs R, Gassen HG. Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase.. Nucleic Acids Res. 1990, 17 (22): 9471. PMC 335148 . PMID 2587265. doi:10.1093/nar/17.22.9471. 
  • Chernaia VI, Reva AD. [Cathepsin H activity in the human brain and human brain neoplasms]. Ukr. Biokhim. Zh. 1990, 61 (5): 47–50. PMID 2588347. 
  • Ritonja A, Popović T, Kotnik M, et al. Amino acid sequences of the human kidney cathepsins H and L.. FEBS Lett. 1988, 228 (2): 341–5. PMID 3342889. doi:10.1016/0014-5793(88)80028-0 . 
  • Järvinen M, Rinne A. Human spleen cysteineproteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants.. Biochim. Biophys. Acta. 1983, 708 (2): 210–7. PMID 6184075. doi:10.1016/0167-4838(82)90222-9. 
  • Kato S, Sekine S, Oh SW, et al. Construction of a human full-length cDNA bank.. Gene. 1995, 150 (2): 243–50. PMID 7821789. doi:10.1016/0378-1119(94)90433-2. 
  • Baumgrass R, Williamson MK, Price PA. Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B, D, L, H, and S.. J. Bone Miner. Res. 1997, 12 (3): 447–55. PMID 9076588. doi:10.1359/jbmr.1997.12.3.447 . 
  • Söderström M, Salminen H, Glumoff V, et al. Cathepsin expression during skeletal development.. Biochim. Biophys. Acta. 1999, 1446 (1–2): 35–46. PMID 10395917. doi:10.1016/S0167-4781(99)00068-8. 
  • Jokimaa V, Oksjoki S, Kujari H, et al. Expression patterns of cathepsins B, H, K, L and S in the human endometrium.. Mol. Hum. Reprod. 2001, 7 (1): 73–8. PMID 11134363. doi:10.1093/molehr/7.1.73 . 
  • Uusitalo H, Hiltunen A, Söderström M, et al. Expression of cathepsins B, H, K, L, and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and endochondral ossification in mouse fracture callus.. Calcif. Tissue Int. 2001, 67 (5): 382–90. PMID 11136537. S2CID 31004810. doi:10.1007/s002230001152. 
  • 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. 2001, 10 (9): 1729–38. PMC 2253190 . PMID 11514663. doi:10.1110/ps.11901. 
  • Waghray A, Keppler D, Sloane BF, et al. Analysis of a truncated form of cathepsin H in human prostate tumor cells.. J. Biol. Chem. 2002, 277 (13): 11533–8. PMID 11796715. doi:10.1074/jbc.M109557200 . 
  • Brasch F, Ten Brinke A, Johnen G, et al. Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes.. Am. J. Respir. Cell Mol. Biol. 2002, 26 (6): 659–70. PMID 12034564. doi:10.1165/ajrcmb.26.6.4744. 
  • Bühling F, Waldburg N, Krüger S, et al. Expression of cathepsins B, H, K, L, and S during human fetal lung development.. Dev. Dyn. 2003, 225 (1): 14–21. PMID 12203716. doi:10.1002/dvdy.10134 . 
  • 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 . 
  • Jenko S, Dolenc I, Guncar G, et al. Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases.. J. Mol. Biol. 2003, 326 (3): 875–85. PMID 12581647. doi:10.1016/S0022-2836(02)01432-8. 
  • Nagai A, Terashima M, Harada T, et al. Cathepsin B and H activities and cystatin C concentrations in cerebrospinal fluid from patients with leptomeningeal metastasis.. Clin. Chim. Acta. 2003, 329 (1–2): 53–60. PMID 12589965. doi:10.1016/S0009-8981(03)00023-8. 
  • Han SR, Momeni A, Strach K, et al. Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis.. Arterioscler. Thromb. Vasc. Biol. 2004, 23 (4): 661–7. PMID 12615673. doi:10.1161/01.ATV.0000063614.21233.BF . 
  • Dodt J, Reichwein J. Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase.. Biol. Chem. 2004, 384 (9): 1327–32. PMID 14515996. S2CID 23726105. doi:10.1515/BC.2003.149. 

外部链接

  • The MEROPS online database for peptidases and their inhibitors: C01.040 (页面存档备份,存于互联网档案馆

组织蛋白酶h, 英文, cathepsin, 是一种在人体中由ctsh基因编码的蛋白质, 已知的結構pdb直系同源搜索, pdbe, rcsbpdbid列表1bzn識別號别名ctsh, cpsb, minichain, acc4, acc5, cathepsin, h外部idomim, 116820, 107285, homologene, 36159, genecards, ctsh相關疾病躁鬱症, 1型糖尿病, 基因位置, 人类, 染色体15號染色體, 基因座15q25, 1起始78, 终止78, 基因位置, . 组织蛋白酶H 英文 Cathepsin H 是一种在人体中由CTSH基因编码的蛋白质 6 7 组织蛋白酶H已知的結構PDB直系同源搜索 PDBe RCSBPDBID列表1BZN識別號别名CTSH ACC 4 ACC 5 CPSB minichain ACC4 ACC5 cathepsin H外部IDOMIM 116820 MGI 107285 HomoloGene 36159 GeneCards CTSH相關疾病躁鬱症 1型糖尿病 1 基因位置 人类 染色体15號染色體 2 基因座15q25 1起始78 921 058 bp 2 终止78 949 574 bp 2 基因位置 小鼠 染色体小鼠9号染色体 3 基因座9 E3 1 9 47 4 cM起始89 936 205 bp 3 终止89 958 142 bp 3 RNA表达模式查阅更多表达数据基因本體分子功能 peptidase activator activity involved in apoptotic process 半胱氨酸型肽酶活性 HLA A specific activating MHC class I receptor activity endopeptidase activity 血浆蛋白结合 cysteine type endopeptidase activator activity involved in apoptotic process cysteine type endopeptidase activity aminopeptidase activity serine type endopeptidase activity 水解酶活性 thyroid hormone binding 肽酶活性細胞組分 细胞质基质 alveolar lamellar body 溶酶体 外排體 multivesicular body lumen 細胞外區域 細胞外空間 secretory granule lumen 細胞內膜結合細胞器 tertiary granule lumen ficolin 1 rich granule lumen cytoplasmic ribonucleoprotein granule collagen containing extracellular matrix生物學過程 surfactant homeostasis antigen processing and presentation adaptive immune response bradykinin catabolic process response to retinoic acid membrane protein proteolysis positive regulation of cell migration ERK1 and ERK2 cascade zymogen activation neuropeptide catabolic process positive regulation of epithelial cell migration positive regulation of apoptotic signaling pathway negative regulation of apoptotic process 蛋白酶解 positive regulation of angiogenesis positive regulation of peptidase activity positive regulation of gene expression protein destabilization cellular response to thyroid hormone stimulus positive regulation of cell population proliferation immune response regulating signaling pathway proteolysis involved in cellular protein catabolic process metanephros development dichotomous subdivision of terminal units involved in lung branching T cell mediated cytotoxicity 细胞凋亡 activation of cysteine type endopeptidase activity involved in apoptotic process neutrophil degranulationSources Amigo QuickGO直系同源物種人類小鼠Entrez151213036EnsemblENSG00000103811ENSMUSG00000032359UniProtP09668P49935mRNA 序列NM 004390 NM 148979 NM 001319137NM 007801 NM 001312649蛋白序列NP 001306066 NP 004381NP 001299578 NP 031827基因位置 UCSC Chr 15 78 92 78 95 MbChr 9 89 94 89 96 MbPubMed 查找 4 5 維基數據檢視 編輯人類檢視 編輯小鼠该基因编码的蛋白质是木瓜样蛋白酶 英语 Papain like protease 一种溶酶体半胱氨酸蛋白酶 在溶酶体蛋白质的整体降解中很重要 它由二硫键连接的重链和轻链的二聚体组成 均由单一蛋白质前体产生 编码的蛋白质属于肽酶C1蛋白质家族 既可以作为氨肽酶 英语 Aminopeptidase 也可以作为内肽酶 该基因的表达增加与前列腺肿瘤的恶性进展有关 该基因已发现了编码不同蛋白异构体的两种转录变体 7 参考文献 编辑 與组织蛋白酶H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 ENSG00000103811 Ensembl May 2017 3 0 3 1 3 2 GRCm38 Ensembl release 89 ENSMUSG00000032359 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 Fuchs R Machleidt W Gassen HG Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H Biol Chem Hoppe Seyler Feb 1989 369 6 469 75 PMID 2849458 doi 10 1515 bchm3 1988 369 1 469 7 0 7 1 Entrez Gene CTSH cathepsin H 拓展阅读 编辑Sawicki G Warwas M Cathepsin H from human placenta Acta Biochim Pol 1990 36 3 4 343 51 PMID 2486008 Fuchs R Gassen HG Nucleotide sequence of human preprocathepsin H a lysosomal cysteine proteinase Nucleic Acids Res 1990 17 22 9471 PMC 335148 PMID 2587265 doi 10 1093 nar 17 22 9471 Chernaia VI Reva AD Cathepsin H activity in the human brain and human brain neoplasms Ukr Biokhim Zh 1990 61 5 47 50 PMID 2588347 Ritonja A Popovic T Kotnik M et al Amino acid sequences of the human kidney cathepsins H and L FEBS Lett 1988 228 2 341 5 PMID 3342889 doi 10 1016 0014 5793 88 80028 0 Jarvinen M Rinne A Human spleen cysteineproteinase inhibitor Purification fractionation into isoelectric variants and some properties of the variants Biochim Biophys Acta 1983 708 2 210 7 PMID 6184075 doi 10 1016 0167 4838 82 90222 9 Kato S Sekine S Oh SW et al Construction of a human full length cDNA bank Gene 1995 150 2 243 50 PMID 7821789 doi 10 1016 0378 1119 94 90433 2 Baumgrass R Williamson MK Price PA Identification of peptide fragments generated by digestion of bovine and human osteocalcin with the lysosomal proteinases cathepsin B D L H and S J Bone Miner Res 1997 12 3 447 55 PMID 9076588 doi 10 1359 jbmr 1997 12 3 447 Soderstrom M Salminen H Glumoff V et al Cathepsin expression during skeletal development Biochim Biophys Acta 1999 1446 1 2 35 46 PMID 10395917 doi 10 1016 S0167 4781 99 00068 8 Jokimaa V Oksjoki S Kujari H et al Expression patterns of cathepsins B H K L and S in the human endometrium Mol Hum Reprod 2001 7 1 73 8 PMID 11134363 doi 10 1093 molehr 7 1 73 Uusitalo H Hiltunen A Soderstrom M et al Expression of cathepsins B H K L and S and matrix metalloproteinases 9 and 13 during chondrocyte hypertrophy and endochondral ossification in mouse fracture callus Calcif Tissue Int 2001 67 5 382 90 PMID 11136537 S2CID 31004810 doi 10 1007 s002230001152 Pol E Bjork 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 2001 10 9 1729 38 PMC 2253190 PMID 11514663 doi 10 1110 ps 11901 Waghray A Keppler D Sloane BF et al Analysis of a truncated form of cathepsin H in human prostate tumor cells J Biol Chem 2002 277 13 11533 8 PMID 11796715 doi 10 1074 jbc M109557200 Brasch F Ten Brinke A Johnen G et al Involvement of cathepsin H in the processing of the hydrophobic surfactant associated protein C in type II pneumocytes Am J Respir Cell Mol Biol 2002 26 6 659 70 PMID 12034564 doi 10 1165 ajrcmb 26 6 4744 Buhling F Waldburg N Kruger S et al Expression of cathepsins B H K L and S during human fetal lung development Dev Dyn 2003 225 1 14 21 PMID 12203716 doi 10 1002 dvdy 10134 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 Jenko S Dolenc I Guncar G et al Crystal structure of Stefin A in complex with cathepsin H N terminal residues of inhibitors can adapt to the active sites of endo and exopeptidases J Mol Biol 2003 326 3 875 85 PMID 12581647 doi 10 1016 S0022 2836 02 01432 8 Nagai A Terashima M Harada T et al Cathepsin B and H activities and cystatin C concentrations in cerebrospinal fluid from patients with leptomeningeal metastasis Clin Chim Acta 2003 329 1 2 53 60 PMID 12589965 doi 10 1016 S0009 8981 03 00023 8 Han SR Momeni A Strach K et al Enzymatically modified LDL induces cathepsin H in human monocytes potential relevance in early atherogenesis Arterioscler Thromb Vasc Biol 2004 23 4 661 7 PMID 12615673 doi 10 1161 01 ATV 0000063614 21233 BF Dodt J Reichwein J Human cathepsin H deletion of the mini chain switches substrate specificity from aminopeptidase to endopeptidase Biol Chem 2004 384 9 1327 32 PMID 14515996 S2CID 23726105 doi 10 1515 BC 2003 149 外部链接 编辑The MEROPS online database for peptidases and their inhibitors C01 040 页面存档备份 存于互联网档案馆 生物学主题 取自 https zh wikipedia org w index php title 组织蛋白酶H amp oldid 75000587, 维基百科,wiki,书籍,书籍,图书馆,

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