SENP2

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) Band 3q27.2 Start 185,582,496 bp End 185,633,551 bp
Gene location (Mouse) Chr. Chromosome 16 (mouse) Band 16|16 B1 Start 21,828,234 bp End 21,868,019 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon sural nerve gastrocnemius muscle corpus callosum islet of Langerhans prefrontal cortex ovary ganglionic eminence internal globus pallidus monocyte Top expressed in spermatocyte seminiferous tubule spermatid olfactory tubercle visual cortex somite superior frontal gyrus abdominal wall soleus muscle cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cysteine-type peptidase activity endopeptidase activity peptidase activity protein binding hydrolase activity SUMO-specific endopeptidase activity protein domain specific binding Cellular component cytoplasm nuclear membrane membrane nuclear pore nucleoplasm 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 by RNA polymerase II 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: 21.83 – 21.87 Mb PubMed search
Wikidata
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Sentrin-specific protease 2 is an enzyme that in humans is encoded by the SENP2 gene.

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 protease enzymes that process newly synthesized SUMO1 into the conjugatable form and catalyze the deconjugation of SUMO1-containing species.[supplied by OMIM]

Interactions

SENP2 has been shown to interact with NUP153.

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. S2CID 12234952.
• 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. S2CID 25139166.