USP15

Protein-coding gene in the species Homo sapiens

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
| 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[edit]

* USP1 (MIM 603478).

## References[edit]

1. ^ a b c 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. ^ a b "Entrez Gene: USP15 ubiquitin specific peptidase 15".

## Further reading[edit]

* 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. 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.

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* 1w6v: SOLUTION STRUCTURE OF THE DUSP DOMAIN OF HUSP15

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