- SENP2
SUMO1/sentrin/SMT3 specific peptidase 2, also known as SENP2, is a human
gene .cite web | title = Entrez Gene: SENP2 SUMO1/sentrin/SMT3 specific peptidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=59343| accessdate = ]PBB_Summary
section_title =
summary_text = SUMO1 (UBL1; MIM 601912) is a small ubiquitin-like protein that can be covalently conjugated to other proteins. SENP2 is one of a group of enzymes that process newly synthesized SUMO1 into the conjugatable form and catalyze the deconjugation of SUMO1-containing species. [supplied by OMIM] cite web | title = Entrez Gene: SENP2 SUMO1/sentrin/SMT3 specific peptidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=59343| 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=Nakajima D, Okazaki N, Yamakawa H, "et al." |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99–106 |year= 2003 |pmid= 12168954 |doi=
*cite journal | author=Nagase T, Kikuno R, Ishikawa KI, "et al." |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65–73 |year= 2000 |pmid= 10718198 |doi=
*cite journal | author=Nishida T, Kaneko F, Kitagawa M, Yasuda H |title=Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39060–6 |year= 2001 |pmid= 11489887 |doi= 10.1074/jbc.M103955200
*cite journal | author=Hang J, Dasso M |title=Association of the human SUMO-1 protease SENP2 with the nuclear pore. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19961–6 |year= 2002 |pmid= 11896061 |doi= 10.1074/jbc.M201799200
*cite journal | author=Kadoya T, Yamamoto H, Suzuki T, "et al." |title=Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin. |journal=Mol. Cell. Biol. |volume=22 |issue= 11 |pages= 3803–19 |year= 2002 |pmid= 11997515 |doi=
*cite journal | author=Zhang H, Saitoh H, Matunis MJ |title=Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. |journal=Mol. Cell. Biol. |volume=22 |issue= 18 |pages= 6498–508 |year= 2002 |pmid= 12192048 |doi=
*cite journal | author=Best JL, Ganiatsas S, Agarwal S, "et al." |title=SUMO-1 protease-1 regulates gene transcription through PML. |journal=Mol. Cell |volume=10 |issue= 4 |pages= 843–55 |year= 2002 |pmid= 12419228 |doi=
*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=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=Reverter D, Lima CD |title=A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex. |journal=Structure |volume=12 |issue= 8 |pages= 1519–31 |year= 2005 |pmid= 15296745 |doi= 10.1016/j.str.2004.05.023
*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=Itahana Y, Yeh ET, Zhang Y |title=Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2. |journal=Mol. Cell. Biol. |volume=26 |issue= 12 |pages= 4675–89 |year= 2006 |pmid= 16738331 |doi= 10.1128/MCB.01830-05
*cite journal | author=Reverter D, Lima CD |title=Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 12 |pages= 1060–8 |year= 2007 |pmid= 17099700 |doi= 10.1038/nsmb1168PBB_Controls
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