USP15

From Wikipedia, the free encyclopedia


Ubiquitin specific peptidase 15
PDB rendering based on 1w6v.
Available structures: 1w6v
Identifiers
Symbol(s) USP15; KIAA0529; MGC131982; MGC149838; MGC74854; UNPH4
External IDs OMIM: 604731 MGI101857 HomoloGene38167
Orthologs
Human Mouse
Entrez 9958 14479
Ensembl ENSG00000135655 ENSMUSG00000020124
Uniprot Q9Y4E8 Q3TPH3
Refseq NM_006313 (mRNA)
NP_006304 (protein)
NM_027604 (mRNA)
NP_081880 (protein)
Location Chr 12: 60.94 - 61.09 Mb Chr 10: 122.52 - 122.6 Mb
Pubmed search [1] [2]

Ubiquitin specific peptidase 15, also known as USP15, is a human gene.[1]

Ubiquitin (MIM 191339), a highly conserved protein involved in the regulation of intracellular protein breakdown, cell cycle regulation, and stress response, is released from degraded proteins by disassembly of the polyubiquitin chains. The disassembly process is mediated by ubiquitin-specific proteases (USPs). Also see USP1 (MIM 603478).[supplied by OMIM][1]

[edit] References

[edit] Further reading

  • Puente XS, Sánchez LM, Overall CM, López-Otín C (2003). "Human and mouse proteases: a comparative genomic approach.". Nat. Rev. Genet. 4 (7): 544–58. doi:10.1038/nrg1111. PMID 12838346. 
  • 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. 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. 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: 89. doi:10.1038/msb4100134. 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. 
  • 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. doi:10.1016/j.cub.2005.05.059. PMID 16005295. 
  • 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. 
  • 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. 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. PMID 9628581.