SENP3
Protein-coding gene in humans
From Wikipedia, the free encyclopedia
SUMO1/sentrin/SMT3 specific peptidase 3, also known as SENP3, is a protein which in humans is encoded by the SENP3 gene.[5][6]
AliasesSENP3, SMT3IP1, SSP3, Ulp1, SUMO1/sentrin/SMT3 specific peptidase 3, SUMO specific peptidase 3
External IDsOMIM: 612844; MGI: 2158736; HomoloGene: 9236; GeneCards: SENP3; OMA:SENP3 - orthologs
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| Aliases | SENP3, SMT3IP1, SSP3, Ulp1, SUMO1/sentrin/SMT3 specific peptidase 3, SUMO specific peptidase 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 612844; MGI: 2158736; HomoloGene: 9236; GeneCards: SENP3; OMA:SENP3 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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SENP3 together with SENP5, belongs to the Ulp1 branch in yeast and localize to nucleolus through B23/NPM1. SENP3 is associated and regulated by B23/nucleophosmin/NPM1 and involved in the regulation of ribosome biogenesis. SENP3 may be regulated by Arf-Mdm2-p53 pathway.[7]
Further reading
- Yeh ET, Gong L, Kamitani T (2000). "Ubiquitin-like proteins: new wines in new bottles". Gene. 248 (1–2): 1–14. doi:10.1016/S0378-1119(00)00139-6. PMID 10806345.
- Nishida T, Tanaka H, Yasuda H (2000). "A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase". Eur. J. Biochem. 267 (21): 6423–7. doi:10.1046/j.1432-1327.2000.01729.x. PMID 11029585.
- Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
- Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
- Simpson JC, Wellenreuther R, Poustka A, et al. (2001). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
- 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.
- 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.
- Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Wiemann S, Arlt D, Huber W, et al. (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.
- Bouras T, Fu M, Sauve AA, et al. (2005). "SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1". J. Biol. Chem. 280 (11): 10264–76. doi:10.1074/jbc.M408748200. PMID 15632193.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
- Grégoire S, Yang XJ (2005). "Association with class IIa histone deacetylases upregulates the sumoylation of MEF2 transcription factors". Mol. Cell. Biol. 25 (6): 2273–87. doi:10.1128/MCB.25.6.2273-2287.2005. PMC 1061617. PMID 15743823.
- Mehrle A, Rosenfelder H, Schupp I, et al. (2006). "The LIFEdb database in 2006". Nucleic Acids Res. 34 (Database issue): D415–8. doi:10.1093/nar/gkj139. PMC 1347501. PMID 16381901.
- Nousiainen M, Silljé HH, Sauer G, et al. (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
- Gong L, Yeh ET (2006). "Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3". J. Biol. Chem. 281 (23): 15869–77. doi:10.1074/jbc.M511658200. PMID 16608850.
- Olsen JV, Blagoev B, Gnad F, et al. (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.
- Yun C, Wang Y, Mukhopadhyay D, et al. (2008). "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases". J. Cell Biol. 183 (4): 589–95. doi:10.1083/jcb.200807185. PMC 2582899. PMID 19015314.
- Haindl M, Harasim T, Eick D, Muller S (March 2008). "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing". EMBO Rep. 9 (3): 273–9. doi:10.1038/embor.2008.3. PMC 2267381. PMID 18259216.
- Kuo ML, den Besten W, Thomas MC, et al. (2008). "Arf-induced turnover of the nucleolar nucleophosmin-associated SUMO-2/3 protease Senp3". Cell Cycle. 7 (21): 3378–87. doi:10.4161/cc.7.21.6930. PMID 18948745.
