| USP25 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | USP25, USP21, ubiquitin specific peptidase 25 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 604736 MGI: 1353655 HomoloGene: 8374 GeneCards: USP25 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Ubiquitin specific peptidase 25 is a protein that in humans is encoded by the USP25 gene. [5]
Function
Ubiquitin is a highly conserved 76-amino acid protein involved in regulation of intracellular protein breakdown, cell cycle regulation, and stress response. Ubiquitin is released from degraded proteins by disassembly of the polyubiquitin chains, which is mediated by ubiquitin-specific proteases (USPs), such as USP25 (Valero et al., 1999 [PubMed 10644437]).[supplied by OMIM, Mar 2008].
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000155313 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022867 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Entrez Gene: Ubiquitin specific peptidase 25". Retrieved 2017-10-31.
Further reading
- Valero R, Bayés M, Francisca Sánchez-Font M, González-Angulo O, Gonzàlez-Duarte R, Marfany G (2001). "Characterization of alternatively spliced products and tissue-specific isoforms of USP28 and USP25". Genome Biol. 2 (10): RESEARCH0043. doi:10.1186/gb-2001-2-10-research0043. PMC 57798. PMID 11597335.
- Yamada H, Yanagisawa K, Tokumaru S, Taguchi A, Nimura Y, Osada H, Nagino M, Takahashi T (2008). "Detailed characterization of a homozygously deleted region corresponding to a candidate tumor suppressor locus at 21q11-21 in human lung cancer". Genes Chromosomes Cancer. 47 (9): 810–8. doi:10.1002/gcc.20582. PMID 18523997. S2CID 39369334.
- Meulmeester E, Kunze M, Hsiao HH, Urlaub H, Melchior F (2008). "Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25". Mol. Cell. 30 (5): 610–9. doi:10.1016/j.molcel.2008.03.021. hdl:11858/00-001M-0000-0012-DBA8-3. PMID 18538659.
- Denuc A, Bosch-Comas A, Gonzàlez-Duarte R, Marfany G (2009). "The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition". PLOS ONE. 4 (5): e5571. Bibcode:2009PLoSO...4.5571D. doi:10.1371/journal.pone.0005571. PMC 2679190. PMID 19440361.
- Törkvist L, Halfvarson J, Ong RT, Lördal M, Sjöqvist U, Bresso F, Björk J, Befrits R, Löfberg R, Blom J, Carlson M, Padyukov L, D'Amato M, Seielstad M, Pettersson S (2010). "Analysis of 39 Crohn's disease risk loci in Swedish inflammatory bowel disease patients". Inflamm. Bowel Dis. 16 (6): 907–9. doi:10.1002/ibd.21105. PMID 19760754.
- Cholay M, Reverdy C, Benarous R, Colland F, Daviet L (2010). "Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase". Exp. Cell Res. 316 (4): 667–75. doi:10.1016/j.yexcr.2009.10.023. PMID 19909739.
- Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR (2010). "Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score". Mol. Med. 16 (7–8): 247–53. doi:10.2119/molmed.2009.00159. PMC 2896464. PMID 20379614.
- Kessler BM, Edelmann MJ (2011). "PTMs in conversation: activity and function of deubiquitinating enzymes regulated via post-translational modifications". Cell Biochem. Biophys. 60 (1–2): 21–38. doi:10.1007/s12013-011-9176-6. PMC 3094536. PMID 21480003.
- Blount JR, Burr AA, Denuc A, Marfany G, Todi SV (2012). "Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation". PLOS ONE. 7 (5): e36542. Bibcode:2012PLoSO...736542B. doi:10.1371/journal.pone.0036542. PMC 3348923. PMID 22590560.
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