SENP2

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SUMO1/sentrin/SMT3 specific peptidase 2
File:PBB Protein SENP2 image.jpg
PDB rendering based on 1tgz.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SENP2 ; AXAM2; DKFZp762A2316; KIAA1331; SMT3IP2
External IDs Template:OMIM5 Template:MGI HomoloGene11005
RNA expression pattern
File:PBB GE SENP2 218122 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

SUMO1/sentrin/SMT3 specific peptidase 2, also known as SENP2, is a human gene.[1]

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][1]

References

  1. 1.0 1.1 "Entrez Gene: SENP2 SUMO1/sentrin/SMT3 specific peptidase 2".

Further reading

  • 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. PMID 12168954.
  • Nagase T, Kikuno R, Ishikawa KI; et al. (2000). "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". DNA Res. 7 (1): 65–73. PMID 10718198.
  • Nishida T, Kaneko F, Kitagawa M, Yasuda H (2001). "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". J. Biol. Chem. 276 (42): 39060–6. doi:10.1074/jbc.M103955200. PMID 11489887.
  • Hang J, Dasso M (2002). "Association of the human SUMO-1 protease SENP2 with the nuclear pore". J. Biol. Chem. 277 (22): 19961–6. doi:10.1074/jbc.M201799200. PMID 11896061.
  • Kadoya T, Yamamoto H, Suzuki T; et al. (2002). "Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin". Mol. Cell. Biol. 22 (11): 3803–19. PMID 11997515.
  • Zhang H, Saitoh H, Matunis MJ (2002). "Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex". Mol. Cell. Biol. 22 (18): 6498–508. PMID 12192048.
  • Best JL, Ganiatsas S, Agarwal S; et al. (2002). "SUMO-1 protease-1 regulates gene transcription through PML". Mol. Cell. 10 (4): 843–55. PMID 12419228.
  • 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. doi:10.1073/pnas.242603899. 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.
  • Reverter D, Lima CD (2005). "A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex". Structure. 12 (8): 1519–31. doi:10.1016/j.str.2004.05.023. PMID 15296745.
  • 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. PMID 15489334.
  • Itahana Y, Yeh ET, Zhang Y (2006). "Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2". Mol. Cell. Biol. 26 (12): 4675–89. doi:10.1128/MCB.01830-05. PMID 16738331.
  • Reverter D, Lima CD (2007). "Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates". Nat. Struct. Mol. Biol. 13 (12): 1060–8. doi:10.1038/nsmb1168. PMID 17099700.

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