USP10

USP10
Identifiers
Aliases	USP10, UBPO, ubiquitin specific peptidase 10
External IDs	OMIM: 609818; MGI: 894652; HomoloGene: 31294; GeneCards: USP10; OMA:USP10 - orthologs
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q24.1 Start 84,699,986 bp[1] End 84,779,922 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 E1 Start 120,637,099 bp[2] End 120,684,299 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence secondary oocyte blood epithelium of colon gastrocnemius muscle monocyte sperm muscle of thigh stromal cell of endometrium Top expressed in tail of embryo epiblast genital tubercle neural layer of retina primitive streak yolk sac abdominal wall lens ventricular zone morula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cysteine-type peptidase activity transmembrane transporter binding p53 binding peptidase activity protein binding cysteine-type endopeptidase activity hydrolase activity RNA binding thiol-dependent deubiquitinase Cellular component cytoplasm endosome nucleoplasm early endosome nucleus cytosol protein-containing complex Biological process ubiquitin-dependent protein catabolic process proteolysis autophagy regulation of autophagy translesion synthesis cellular response to interleukin-1 cellular response to DNA damage stimulus negative regulation of I-kappaB kinase/NF-kappaB signaling DNA repair protein deubiquitination DNA damage response, signal transduction by p53 class mediator Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9100 22224 Ensembl ENSG00000103194 ENSMUSG00000031826 UniProt Q14694 P52479 RefSeq (mRNA) NM_001272075 NM_005153 NM_009462 NM_001310630 RefSeq (protein) NP_001259004 NP_005144 NP_001297559 NP_033488 Location (UCSC) Chr 16: 84.7 – 84.78 Mb Chr 8: 120.64 – 120.68 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ubiquitin specific peptidase 10, also known as USP10, is an enzyme which in humans is encoded by the USP10 gene.^[5]

Function

Ubiquitin is a highly conserved protein that is covalently linked to other proteins to regulate their function and degradation. This gene encodes a member of the ubiquitin-specific protease family of cysteine proteases. The enzyme specifically cleaves ubiquitin from ubiquitin-conjugated protein substrates. The protein is found in the nucleus and cytoplasm. It functions as a co-factor of the DNA-bound androgen receptor complex, and is inhibited by a protein in the Ras-GTPase pathway. The human genome contains several pseudogenes similar to this gene.^[5]

Interactions

USP10 has been shown to interact with G3BP1.^[6] In the endothelium, USP10 regulates Notch signaling by slowing down the degradation of the intracellular domain of NOTCH1. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000103194 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031826 – Ensembl, May 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. "Entrez Gene: USP10 ubiquitin specific peptidase 10".
6. Soncini C, Berdo I, Draetta G (June 2001). "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease". Oncogene. 20 (29): 3869–79. doi:10.1038/sj.onc.1204553. PMID 11439350. S2CID 7515868.
7. Lim R, Sugino T, Nolte H, Andrade J, Zimmermann B, Shi C, Doddaballapur A, Ong YT, Wilhelm K, Fasse JW, Ernst A, Kaulich M, Husnjak K, Boettger T, Guenther S, Braun T, Krüger M, Benedito R, Dikic I, Potente M (April 2019). "Deubiquitinase USP10 regulates Notch signaling in the endothelium". Science. 364 (6436): 188–193. Bibcode:2019Sci...364..188L. doi:10.1126/science.aat0778. hdl:20.500.12105/9685. PMID 30975888. S2CID 109940358.

Further reading

• 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.
• 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. S2CID 2856065.
• Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N (1996). "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 3 (1): 17–24. doi:10.1093/dnares/3.1.17. PMID 8724849.
• Soncini C, Berdo I, Draetta G (2001). "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease". Oncogene. 20 (29): 3869–79. doi:10.1038/sj.onc.1204553. PMID 11439350. S2CID 7515868.
• Fortna A, Kim Y, MacLaren E, Marshall K, Hahn G, Meltesen L, Brenton M, Hink R, Burgers S, Hernandez-Boussard T, Karimpour-Fard A, Glueck D, McGavran L, Berry R, Pollack J, Sikela JM (2006). "Lineage-specific gene duplication and loss in human and great ape evolution". PLOS Biol. 2 (7): E207. doi:10.1371/journal.pbio.0020207. PMC 449870. PMID 15252450.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Faus H, Meyer HA, Huber M, Bahr I, Haendler B (2006). "The ubiquitin-specific protease USP10 modulates androgen receptor function". Mol. Cell. Endocrinol. 245 (1–2): 138–46. doi:10.1016/j.mce.2005.11.011. PMID 16368182. S2CID 24365493.
• Grunda JM, Nabors LB, Palmer CA, Chhieng DC, Steg A, Mikkelsen T, Diasio RB, Zhang K, Allison D, Grizzle WE, Wang W, Gillespie GY, Johnson MR (2007). "Increased expression of thymidylate synthetase (TS), ubiquitin specific protease 10 (USP10) and survivin is associated with poor survival in glioblastoma multiforme (GBM)". J. Neurooncol. 80 (3): 261–74. doi:10.1007/s11060-006-9191-4. PMID 16773218. S2CID 42007677.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (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.
• Deng S, Zhou H, Xiong R, Lu Y, Yan D, Xing T, Dong L, Tang E, Yang H (2007). "Over-expression of genes and proteins of ubiquitin specific peptidases (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by the methods of RFDD-PCR and proteomics". Breast Cancer Res. Treat. 104 (1): 21–30. doi:10.1007/s10549-006-9393-7. PMID 17004105. S2CID 29643544.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.