- SENP8
SUMO/sentrin specific peptidase family member 8, also known as SENP8, is a human
gene .cite web | title = Entrez Gene: SENP8 SUMO/sentrin specific peptidase family member 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=123228| accessdate = ]PBB_Summary
section_title =
summary_text = NEDD8 (MIM 603171) is a ubiquitin-like protein that becomes conjugated to the cullin (see CUL1; MIM 603134) subunit of several ubiquitin ligases. This conjugation, called neddylation, is required for optimal ubiquitin ligase activity. NEDD8-specific deneddylases, such as NEDP1, or DEN1, are required to process the NEDD8 propeptide at a C-terminal diglycine motif and to remove NEDD8 from cullins (Gan-Erdene et al., 2003). [supplied by OMIM] cite web | title = Entrez Gene: SENP8 SUMO/sentrin specific peptidase family member 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=123228| accessdate = ]References
Further reading
*cite journal | author=Mikolajczyk J, Drag M, Békés M, Cao JT, Ronai Z, Salvesen GS. |title=Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs.|journal=J. Biol. Chem. |volume=282 |issue= 36 |pages= 26217–24 |year= 2007 |pmid= 17591783 |doi=10.1074/jbc.M702444200
*cite journal | author=Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, Salvesen GS. |title=Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family. |journal=Biochem J. |volume=409 |issue= 2 |pages= 461–9 |year= 2008 |pmid= 17916063 |doi=10.1042/BJ20070940 PBB_Further_reading
citations =
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Mendoza HM, Shen LN, Botting C, "et al." |title=NEDP1, a highly conserved cysteine protease that deNEDDylates Cullins. |journal=J. Biol. Chem. |volume=278 |issue= 28 |pages= 25637–43 |year= 2003 |pmid= 12730221 |doi= 10.1074/jbc.M212948200
*cite journal | author=Gan-Erdene T, Nagamalleswari K, Yin L, "et al." |title=Identification and characterization of DEN1, a deneddylase of the ULP family. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28892–900 |year= 2003 |pmid= 12759362 |doi= 10.1074/jbc.M302890200
*cite journal | author=Wu K, Yamoah K, Dolios G, "et al." |title=DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28882–91 |year= 2003 |pmid= 12759363 |doi= 10.1074/jbc.M302888200
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Xirodimas DP, Saville MK, Bourdon JC, "et al." |title=Mdm2-mediated NEDD8 conjugation of p53 inhibits its transcriptional activity. |journal=Cell |volume=118 |issue= 1 |pages= 83–97 |year= 2004 |pmid= 15242646 |doi= 10.1016/j.cell.2004.06.016
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Reverter D, Wu K, Erdene TG, "et al." |title=Structure of a complex between Nedd8 and the Ulp/Senp protease family member Den1. |journal=J. Mol. Biol. |volume=345 |issue= 1 |pages= 141–51 |year= 2005 |pmid= 15567417 |doi= 10.1016/j.jmb.2004.10.022
*cite journal | author=Shen LN, Liu H, Dong C, "et al." |title=Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1. |journal=EMBO J. |volume=24 |issue= 7 |pages= 1341–51 |year= 2005 |pmid= 15775960 |doi= 10.1038/sj.emboj.7600628PBB_Controls
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