USP15

USP15
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1W6V, 3LMN, 3PPA, 3PV1, 3T9L, 4A3O, 4A3P, 5JJW
Identifiers
Aliases	USP15 , UNPH-2, UNPH4, ubiquitin specific peptidase 15
External IDs	OMIM: 604731; MGI: 101857; HomoloGene: 101542; GeneCards: USP15; OMA:USP15 - orthologs
Gene location (Mouse) Chr. Chromosome 10 (mouse) [1] Band 10|10 D2 Start 122,940,911 bp [1] End 123,032,900 bp [1]
Gene ontology Molecular function ubiquitin modification-dependent histone binding cysteine-type peptidase activity peptidase activity protein binding catalytic activity thiol-dependent deubiquitinase identical protein binding transforming growth factor beta receptor binding cysteine-type endopeptidase activity SMAD binding hydrolase activity Cellular component cytoplasm nucleus cytosol mitochondrion Biological process pathway-restricted SMAD protein phosphorylation ubiquitin-dependent protein catabolic process monoubiquitinated protein deubiquitination BMP signaling pathway proteolysis histone H2B conserved C-terminal lysine deubiquitination transforming growth factor beta receptor signaling pathway protein deubiquitination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9958 14479 Ensembl ENSG00000135655 ENSMUSG00000020124 UniProt Q9Y4E8 Q8R5H1 RefSeq (mRNA) NM_001252078 NM_001252079 NM_006313 NM_001301628 NM_027604 RefSeq (protein) NP_001239007 NP_001239008 NP_006304 NP_001338088 NP_001338089 NP_001338090 NP_001338091 NP_001338092 NP_001338093 NP_001338094 NP_001338095 NP_001288557 NP_081880 Location (UCSC) n/a Chr 10: 122.94 – 123.03 Mb PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

Ubiquitin carboxyl-terminal hydrolase 15 is an enzyme that in humans is encoded by the USP15 gene. ^{[4] [5]}

Ubiquitin is a highly conserved protein involved in the regulation of intracellular protein breakdown, cell cycle regulation, and stress response, which is released from degraded proteins by disassembly of the polyubiquitin chains. The disassembly process is mediated by ubiquitin-specific proteases (USPs). ^[5]

See also

• USP1 (MIM 603478).

References

1. GRCm38: Ensembl release 89: ENSMUSG00000020124 – 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.
4. Puente XS, Sanchez LM, Overall CM, Lopez-Otin C (Jul 2003). "Human and mouse proteases: a comparative genomic approach". Nat Rev Genet. 4 (7): 544–58. doi:10.1038/nrg1111. PMID   12838346. S2CID   2856065.
5. "Entrez Gene: USP15 ubiquitin specific peptidase 15".

Further reading

• Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi: 10.1093/dnares/9.3.99 . PMID   12168954.
• D'Andrea A, Pellman D (1999). "Deubiquitinating enzymes: a new class of biological regulators". Crit. Rev. Biochem. Mol. Biol. 33 (5): 337–52. doi:10.1080/10409239891204251. PMID   9827704.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
• Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID   16964243. S2CID   14294292.
• de Jong RN, Ab E, Diercks T, et al. (2006). "Solution structure of the human ubiquitin-specific protease 15 DUSP domain". J. Biol. Chem. 281 (8): 5026–31. doi: 10.1074/jbc.M510993200 . PMID   16298993.
• Hetfeld BK, Helfrich A, Kapelari B, et al. (2005). "The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1". Curr. Biol. 15 (13): 1217–21. Bibcode:2005CBio...15.1217H. doi: 10.1016/j.cub.2005.05.059 . PMID   16005295. S2CID   15396259.
• Soboleva TA, Jans DA, Johnson-Saliba M, Baker RT (2005). "Nuclear-cytoplasmic shuttling of the oncogenic mouse UNP/USP4 deubiquitylating enzyme". J. Biol. Chem. 280 (1): 745–52. doi: 10.1074/jbc.M401394200 . PMID   15494318.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID   14702039.
• Angelats C, Wang XW, Jermiin LS, et al. (2003). "Isolation and characterization of the mouse ubiquitin-specific protease Usp15". Mamm. Genome. 14 (1): 31–46. doi:10.1007/s00335-002-3035-0. PMID   12532266. S2CID   23215004.
• 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.
• Baker RT, Wang XW, Woollatt E, et al. (1999). "Identification, functional characterization, and chromosomal localization of USP15, a novel human ubiquitin-specific protease related to the UNP oncoprotein, and a systematic nomenclature for human ubiquitin-specific proteases". Genomics. 59 (3): 264–74. doi:10.1006/geno.1999.5879. PMID   10444327.
• Nagase T, Ishikawa K, Miyajima N, et al. (1998). "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (1): 31–9. doi: 10.1093/dnares/5.1.31 . PMID   9628581.