Cathepsin H

CTSH
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1BZN
Identifiers
Aliases	CTSH, ACC-4, ACC-5, CPSB, minichain, ACC4, ACC5, cathepsin H
External IDs	OMIM: 116820 MGI: 107285 HomoloGene: 36159 GeneCards: CTSH
Gene location (Human) Chr. Chromosome 15 (human) Band 15q25.1 Start 78,921,058 bp End 78,949,574 bp
Gene location (Mouse) Chr. Chromosome 9 (mouse) Band 9 E3.1|9 47.4 cM Start 89,936,205 bp End 89,958,142 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in optic nerve kidney tubule lower lobe of lung bronchial epithelial cell kidney visceral pleura renal medulla monocyte lymph node upper lobe of lung Top expressed in left lung lobe right lung lobe yolk sac parotid gland proximal tubule cervix left lobe of liver kidney spleen corneal stroma More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptidase activator activity involved in apoptotic process cysteine-type peptidase activity HLA-A specific activating MHC class I receptor activity endopeptidase activity protein binding 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 Cellular component cytosol alveolar lamellar body lysosome 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 Biological process 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 proteolysis 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 apoptotic process activation of cysteine-type endopeptidase activity involved in apoptotic process neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1512 13036 Ensembl ENSG00000103811 ENSMUSG00000032359 UniProt P09668 P49935 RefSeq (mRNA) NM_004390 NM_148979 NM_001319137 NM_007801 NM_001312649 RefSeq (protein) NP_001306066 NP_004381 NP_001299578 NP_031827 Location (UCSC) Chr 15: 78.92 – 78.95 Mb Chr 9: 89.94 – 89.96 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Cathepsin H is a protein that in humans is encoded by the CTSH gene.

The protein encoded by this gene is a cysteine cathepsin, a lysosomal cysteine protease important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene.

Further reading

• 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. S2CID 31004810.
• 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. Bibcode:2002PNAS...9916899M. 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. S2CID 23726105.

External links

• The MEROPS online database for peptidases and their inhibitors: C01.040