Katepsin H

Katepsin H – katepsin B3, benzoilarginin-naftilamidna hidrolaza (BANA), katepsin Ba, aleurain, N-benzoilarginin-beta-naftilamidna hidrolaza – je proteinski enzim EC 3.4.22.16 koji je kod ljudi kodiran sa gen CTSH.^{[5][6][7][8][9]}

CTSH
Dostupne strukture PDB Pretraga ortologa: PDBe RCSB Spisak PDB ID kodova 1BZN
Identifikatori
Aliasi	CTSH, ACC-4, ACC-5, CPSB, minilanac, ACC4, ACC5, katepsin H
Vanjski ID-jevi	OMIM: 116820 MGI: 107285 HomoloGene: 36159 GeneCards: CTSH
Lokacija gena (čovjek) Hrom. Hromosom 15 (čovjek)[1] Bend 15q25.1 Početak 78,921,058 bp[1] Kraj 78,949,574 bp[1]
Lokacija gena (miš) Hrom. Hromosom 9 (miš)[2] Bend 9 E3.1|9 47.4 cM Početak 89,936,205 bp[2] Kraj 89,958,142 bp[2]
Obrazac RNK ekspresije Više referentnih podataka o ekspresiji
Ontologija gena Molekularna funkcija • peptidase activator activity involved in apoptotic process • cysteine-type peptidase activity • HLA-A specific activating MHC class I receptor activity • endopeptidase activity • GO:0001948, GO:0016582 vezivanje za proteine • cysteine-type endopeptidase activator activity involved in apoptotic process • cysteine-type endopeptidase activity • aminopeptidase activity • serine-type endopeptidase activity • hydrolase activity • thyroid hormone binding • GO:0070122 peptidase activity Ćelijska komponenta • citosol • alveolar lamellar body • Lizozom • Egzosom • multivesicular body lumen • extracellular region • Vanćelijsko • secretory granule lumen • intracellular membrane-bounded organelle • tertiary granule lumen • ficolin-1-rich granule lumen • cytoplasmic ribonucleoprotein granule • collagen-containing extracellular matrix Biološki proces • 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 • Proteoliza • positive regulation of angiogenesis • positive regulation of peptidase activity • GO:1901313 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 • GO:0097285 apoptoza • activation of cysteine-type endopeptidase activity involved in apoptotic process • neutrophil degranulation Izvori:Amigo / QuickGO
Ortolozi
Vrste	Čovjek	Miš
Entrez	1512	13036
Ensembl	ENSG00000103811	ENSMUSG00000032359
UniProt	P09668	P49935
RefSeq (mRNK)	NM_004390 NM_148979 NM_001319137	NM_007801 NM_001312649
RefSeq (bjelančevina)	NP_001306066 NP_004381	NP_001299578 NP_031827
Lokacija (UCSC)	Chr 15: 78.92 – 78.95 Mb	Chr 9: 89.94 – 89.96 Mb
PubMed pretraga	[3]	[4]
Wikipodaci
Pogledaj/uredi – čovjek Pogledaj/uredi – miš

Protein kojeg kodira ovaj gen je lizosomna cistein proteinaza, važna u ukupnom razlaganju lizosomnih proteina. Sastoji se od dimera od disulfidno-povezanih teških i lahkih lanaca, oba proizvedena iz jednog prekursorskog proteina. Kodirani protein, koji pripada proteinskoj porodici peptidaza C1, može djelovati i kao aminopeptidaza i kao endopeptidaza. Povećana ekspresija ovog gena je u korelaciji sa malignom progresijom tumora prostate. Dvije varijante transkripta kodirane su iz različitih izoformi ovog gena.^[10][11][12]

Također pogledajte

• Enzim
• Katepsin

Reference

1. GRCh38: Ensembl release 89: ENSG00000103811 - Ensembl, maj 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032359 - Ensembl, maj 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.
5. Alberts B. (2002)ː Molecular biology of the cell. Garland Science, New York, ISBN 0-8153-3218-1.
6. Bajrović K, Jevrić-Čaušević A., Hadžiselimović R., Ed. (2005): Uvod u genetičko inženjerstvo i biotehnologiju. Institut za genetičko inženjerstvo i biotehnologiju (INGEB), Sarajevo, ISBN 9958-9344-1-8.
7. Voet D., Voet J. (1995): Biochemistry, 2nd Ed. Wiley, http://www.wiley.com/college/math/chem/cg/sales/voet.html.
8. Kapur Pojskić L., Ed. (2014): Uvod u genetičko inženjerstvo i biotehnologiju, 2. izdanje. Institut za genetičko inženjerstvo i biotehnologiju (INGEB), Sarajevo, ISBN 978-9958-9344-8-3.
9. Međedović S., Maslić E., Hadžiselimović R. (2000): Biologija 2. Svjetlost, Sarajevo, ISBN 9958-10-222-6.
10. Barrett, A.J. and Kirschke, H. (1981). "Cathepsin B, cathepsin H and cathepsin L". Methods Enzymol. 80: 535–561. PMID 7043200.CS1 održavanje: više imena: authors list (link)
11. Brömme, D., Bescherer, K., Kirschke, H. and Fittkau, S. (1987). "Enzyme-substrate interactions in the hydrolysis of peptides by cathepsins B and H from rat liver". Biochem. J. 245: 381–385. PMID 3663163.CS1 održavanje: više imena: authors list (link)
12. Fuchs, R., Machleidt, W. and Gassen, H.G. (1988). "Molecular cloning and sequencing of a cDNA coding for mature human kidney cathepsin H". Biol. Chem. Hoppe-Seyler. 369: 469–475. PMID 2849458.CS1 održavanje: više imena: authors list (link)

Vanjski linkovi