Katepsin H

gen koji kodira protein u vrsti Homo sapiens

Katepsin Hkatepsin 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
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

1BZN

Identifikatori
AliasiCTSH, ACC-4, ACC-5, CPSB, minilanac, ACC4, ACC5, katepsin H
Vanjski ID-jeviOMIM: 116820 MGI: 107285 HomoloGene: 36159 GeneCards: CTSH
Lokacija gena (čovjek)
Hromosom 15 (čovjek)
Hrom.Hromosom 15 (čovjek)[1]
Hromosom 15 (čovjek)
Genomska lokacija za CTSH
Genomska lokacija za CTSH
Bend15q25.1Početak78,921,058 bp[1]
Kraj78,949,574 bp[1]
Lokacija gena (miš)
Hromosom 9 (miš)
Hrom.Hromosom 9 (miš)[2]
Hromosom 9 (miš)
Genomska lokacija za CTSH
Genomska lokacija za CTSH
Bend9 E3.1|9 47.4 cMPočetak89,936,205 bp[2]
Kraj89,958,142 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
VrsteČovjekMiš
Entrez
Ensembl
UniProt
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 MbChr 9: 89.94 – 89.96 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/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

uredi

Reference

uredi
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000103811 - Ensembl, maj 2017
  2. ^ a b c 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

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