SENP2

Sentrin-specific protease 2 is an enzyme that in humans is encoded by the SENP2 gene.[5][6][7]

SENP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1TGZ, 1TH0, 2IO0, 2IO1, 2IO2, 2IO3, 3ZO5, 5AEK
Identifiers
Aliases	SENP2, AXAM2, SMT3IP2, SUMO1/sentrin/SMT3 specific peptidase 2, SUMO specific peptidase 2
External IDs	OMIM: 608261 MGI: 1923076 HomoloGene: 11005 GeneCards: SENP2
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q27.2 Start 185,582,496 bp[1] End 185,633,551 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 B1 Start 22,009,484 bp[2] End 22,049,269 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • cysteine-type peptidase activity • endopeptidase activity • peptidase activity • GO:0001948 protein binding • hydrolase activity • SUMO-specific isopeptidase activity • SUMO-specific endopeptidase activity • protein domain specific binding Cellular component • cytoplasm • nuclear membrane • membrane • nuclear pore • nucleoplasm • cell nucleus • cytosol • nuclear body • PML body • cytoplasmic vesicle Biological process • mRNA transport • Wnt signaling pathway • protein sumoylation • proteolysis • negative regulation of protein ubiquitination • regulation of Wnt signaling pathway • protein destabilization • protein transport • positive regulation of protein ubiquitination • positive regulation of protein phosphorylation • heart development • dorsal/ventral axis specification • protein desumoylation • negative regulation of protein binding • regulation of DNA endoreduplication • negative regulation of chromatin binding • negative regulation of DNA damage response, signal transduction by p53 class mediator • fat cell differentiation • positive regulation of transcription from RNA polymerase II promoter • regulation of protein metabolic process • trophoblast giant cell differentiation • labyrinthine layer development • spongiotrophoblast layer development • negative regulation of signal transduction by p53 class mediator • regulation of G1/S transition of mitotic cell cycle Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	59343	75826
Ensembl	ENSG00000163904	ENSMUSG00000022855
UniProt	Q9HC62	Q91ZX6
RefSeq (mRNA)	NM_021627	NM_029457 NM_001357424
RefSeq (protein)	NP_067640	NP_083733 NP_001344353
Location (UCSC)	Chr 3: 185.58 – 185.63 Mb	Chr 16: 22.01 – 22.05 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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][7]

Interactions

SENP2 has been shown to interact with NUP153.[5][8]

References

1. GRCh38: Ensembl release 89: ENSG00000163904 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022855 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Hang J, Dasso M (May 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.
6. Nishida T, Kaneko F, Kitagawa M, Yasuda H (October 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.
7. "Entrez Gene: SENP2 SUMO1/sentrin/SMT3 specific peptidase 2".
8. Zhang H, Saitoh H, Matunis MJ (September 2002). "Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex". Mol. Cell. Biol. 22 (18): 6498–508. doi:10.1128/MCB.22.18.6498-6508.2002. PMC 135644. PMID 12192048.

Further reading

• Mikolajczyk J, Drag M, Békés M, Cao JT, Ronai Z, Salvesen GS (2007). "Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs". J. Biol. Chem. 282 (36): 26217–24. doi:10.1074/jbc.M702444200. PMID 17591783.
• Drag M, Mikolajczyk J, Krishnakumar IM, Huang Z, Salvesen GS (2008). "Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family". Biochem. J. 409 (2): 461–9. doi:10.1042/BJ20070940. PMID 17916063.
• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. CiteSeerX 10.1.1.500.923. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (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. doi:10.1093/dnares/7.1.65. PMID 10718198.
• Kadoya T, Yamamoto H, Suzuki T, Yukita A, Fukui A, Michiue T, Asahara T, Tanaka K, Asashima M, Kikuchi A (2002). "Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin". Mol. Cell. Biol. 22 (11): 3803–19. doi:10.1128/MCB.22.11.3803-3819.2002. PMC 133821. 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. doi:10.1128/MCB.22.18.6498-6508.2002. PMC 135644. PMID 12192048.
• Best JL, Ganiatsas S, Agarwal S, Changou A, Salomoni P, Shirihai O, Meluh PB, Pandolfi PP, Zon LI (2002). "SUMO-1 protease-1 regulates gene transcription through PML". Mol. Cell. 10 (4): 843–55. doi:10.1016/S1097-2765(02)00699-8. PMID 12419228.
• Reverter D, Lima CD (2004). "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.
• 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. PMC 1489137. PMID 16738331.
• Reverter D, Lima CD (2006). "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.