کاتپسین اچ

CTSH
ساختارهای موجود
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1BZN
معین‌کننده‌ها
نام‌های دیگر	CTSH, ACC-4, ACC-5, CPSB, minichain, ACC4, ACC5, cathepsin H
شناسه‌های بیرونی	OMIM: 116820 MGI: 107285 HomoloGene: 36159 GeneCards: CTSH
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)[1]
End	90,076,089 bp[1]
الگوی گسترش RNA
	More reference expression data
هستی‌شناسی ژن
عملکرد ملکولی	• peptidase activator activity involved in apoptotic process; • cysteine-type peptidase activity; • HLA-A specific activating MHC class I receptor activity; • endopeptidase activity; • GO:0001948 پیوند پروتئینی; • cysteine-type endopeptidase activator activity involved in apoptotic process; • cysteine-type endopeptidase activity; • aminopeptidase activity; • serine-type endopeptidase activity; • hydrolase activity; • thyroid hormone binding; • peptidase activity;
ترکیبات سلولی	• سیتوزول; • alveolar lamellar body; • کافنده‌تن; • extracellular exosome; • multivesicular body lumen; • extracellular region; • extracellular space; • secretory granule lumen; • intracellular membrane-bounded organelle; • tertiary granule lumen; • ficolin-1-rich granule lumen; • cytoplasmic ribonucleoprotein granule; • collagen-containing extracellular matrix;
فرایند زیستی	• surfactant homeostasis; • cellular protein metabolic process; • 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; • پروتئین‌کافت; • 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; • مرگ برنامه‌ریزی‌شده یاخته; • activation of cysteine-type endopeptidase activity involved in apoptotic process; • neutrophil degranulation;
	Sources:آمیگو / کوئیک‌گو
هم‌ساخت‌شناسی
	1512
	13036
	ENSG00000103811
	ENSMUSG00000032359
	P09668
	P49935
	NM_148979، XM_005254181، NM_001319137، XM_017021951، XM_017021952، XM_024449852، XM_024449853، XM_024449854، XM_024449855 NM_004390، NM_148979، XM_005254181، NM_001319137، XM_017021951، XM_017021952، XM_024449852، XM_024449853، XM_024449854، XM_024449855
	NM_001312649، XM_011242660 NM_007801، NM_001312649، XM_011242660
	NP_004381، XP_005254238، XP_016877440، XP_016877441، XP_024305620، XP_024305621، XP_024305622، XP_024305623 NP_001306066، NP_004381، XP_005254238، XP_016877440، XP_016877441، XP_024305620، XP_024305621، XP_024305622، XP_024305623
	NP_031827، XP_011240962 NP_001299578، NP_031827، XP_011240962
	ویکی‌داده
مشاهده/ویرایش Human	View/Edit Mouse

کاتپسین اچ (انگلیسی: Cathepsin H‎) یک پروتئین است که در انسان توسط ژن «CTSH» کُدگذاری می‌شود.[4][5]

این پروتئین یک سیستئین پروتئاز لیزوزومی است که برای تجزیهٔ برخی پروتئین‌های لیزوزوم ضروری است.

منابع

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 (Feb 1989). "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H". Biol Chem Hoppe-Seyler. 369 (6): 469–75. doi:10.1515/bchm3.1988.369.1.469. PMID 2849458.
"Entrez Gene: CTSH cathepsin H".

مشارکت‌کنندگان ویکی‌پدیا. «Cathepsin H». در دانشنامهٔ ویکی‌پدیای انگلیسی، بازبینی‌شده در ۲۷ اوت ۲۰۱۹.

برای مطالعهٔ بیشتر

Sawicki G, Warwas M (1990). "Cathepsin H from human placenta". Acta Biochim. Pol. 36 (3–4): 343–51. PMID 2486008.
Fuchs R, Gassen HG (1990). "Nucleotide sequence of human preprocathepsin H, a lysosomal cysteine proteinase". Nucleic Acids Res. 17 (22): 9471. doi:10.1093/nar/17.22.9471. PMC 335148. PMID 2587265.
Chernaia VI, Reva AD (1990). "[Cathepsin H activity in the human brain and human brain neoplasms]". Ukr. Biokhim. Zh. 61 (5): 47–50. PMID 2588347.
Ritonja A, Popović T, Kotnik M, et al. (1988). "Amino acid sequences of the human kidney cathepsins H and L.". FEBS Lett. 228 (2): 341–5. doi:10.1016/0014-5793(88)80028-0. PMID 3342889.
Järvinen M, Rinne A (1983). "Human spleen cysteineproteinase inhibitor. Purification, fractionation into isoelectric variants and some properties of the variants". Biochim. Biophys. Acta. 708 (2): 210–7. doi:10.1016/0167-4838(82)90222-9. PMID 6184075.
Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
Baumgrass R, Williamson MK, Price PA (1997). "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. 12 (3): 447–55. doi:10.1359/jbmr.1997.12.3.447. PMID 9076588.
Söderström M, Salminen H, Glumoff V, et al. (1999). "Cathepsin expression during skeletal development". Biochim. Biophys. Acta. 1446 (1–2): 35–46. doi:10.1016/S0167-4781(99)00068-8. PMID 10395917.
Jokimaa V, Oksjoki S, Kujari H, et al. (2001). "Expression patterns of cathepsins B, H, K, L and S in the human endometrium". Mol. Hum. Reprod. 7 (1): 73–8. doi:10.1093/molehr/7.1.73. PMID 11134363.
Uusitalo H, Hiltunen A, Söderström M, et al. (2001). "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. 67 (5): 382–90. doi:10.1007/s002230001152. PMID 11136537.
Pol E, Björk I (2001). "Role of the single cysteine residue, Cys 3, of human and bovine cystatin B (stefin B) in the inhibition of cysteine proteinases". Protein Sci. 10 (9): 1729–38. doi:10.1110/ps.11901. PMC 2253190. PMID 11514663.
Waghray A, Keppler D, Sloane BF, et al. (2002). "Analysis of a truncated form of cathepsin H in human prostate tumor cells". J. Biol. Chem. 277 (13): 11533–8. doi:10.1074/jbc.M109557200. PMID 11796715.
Brasch F, Ten Brinke A, Johnen G, et al. (2002). "Involvement of cathepsin H in the processing of the hydrophobic surfactant-associated protein C in type II pneumocytes". Am. J. Respir. Cell Mol. Biol. 26 (6): 659–70. doi:10.1165/ajrcmb.26.6.4744. PMID 12034564.
Bühling F, Waldburg N, Krüger S, et al. (2003). "Expression of cathepsins B, H, K, L, and S during human fetal lung development". Dev. Dyn. 225 (1): 14–21. doi:10.1002/dvdy.10134. PMID 12203716.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Jenko S, Dolenc I, Guncar G, et al. (2003). "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. 326 (3): 875–85. doi:10.1016/S0022-2836(02)01432-8. PMID 12581647.
Nagai A, Terashima M, Harada T, et al. (2003). "Cathepsin B and H activities and cystatin C concentrations in cerebrospinal fluid from patients with leptomeningeal metastasis". Clin. Chim. Acta. 329 (1–2): 53–60. doi:10.1016/S0009-8981(03)00023-8. PMID 12589965.
Han SR, Momeni A, Strach K, et al. (2004). "Enzymatically modified LDL induces cathepsin H in human monocytes: potential relevance in early atherogenesis". Arterioscler. Thromb. Vasc. Biol. 23 (4): 661–7. doi:10.1161/01.ATV.0000063614.21233.BF. PMID 12615673.
Dodt J, Reichwein J (2004). "Human cathepsin H: deletion of the mini-chain switches substrate specificity from aminopeptidase to endopeptidase". Biol. Chem. 384 (9): 1327–32. doi:10.1515/BC.2003.149. PMID 14515996.

در ویکی‌انبار پرونده‌هایی دربارهٔ کاتپسین اچ موجود است.

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[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000032359 - Ensembl, May 2017

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

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

[pmid2849458-4] Fuchs R, Machleidt W, Gassen HG (Feb 1989). "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H". Biol Chem Hoppe-Seyler. 369 (6): 469–75. doi:10.1515/bchm3.1988.369.1.469. PMID 2849458.

[entrez-5] "Entrez Gene: CTSH cathepsin H".

آنزیم‌ها
فعالیت	جایگاه فعال جایگاه اتصال سه‌گانه کاتالیزگر Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme کوفاکتور کاتالیز آنزیم
قانون	دگرریختاری Cooperativity بازدارنده آنزیم
تقسیم‌بندی	عدد گروه آنزیم Enzyme superfamily خانواده پروتئین فهرست آنزیم‌ها
سینتیک	سینتیک آنزیمی Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot سینتیک میکائلیس–منتن
انواع	EC1 اکسیدوردوکتاز‌ها (فهرست) EC2 ترانسفراز‌ها (فهرست) EC3 هیدرولاز‌ها (فهرست) EC4 لیاز‌ها (فهرست) EC5 ایزومراز‌ها (فهرست) EC6 لیگاز‌ها (فهرست)