SENP2

Available structures

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

External IDs

MGI: 1923076 HomoloGene: 11005 GeneCards: SENP2

Gene ontology
Molecular function	• cysteine-type peptidase activity • protein domain specific binding • endopeptidase activity • SUMO-specific protease activity • peptidase activity • protein binding • hydrolase activity • SUMO-specific endopeptidase activity
Cellular component	• cytoplasm • PML body • nuclear body • nuclear membrane • membrane • nuclear pore • nucleoplasm • cytoplasmic vesicle • nucleus
Biological process	• trophoblast giant cell differentiation • mRNA transport • positive regulation of protein phosphorylation • spongiotrophoblast layer development • negative regulation of chromatin binding • labyrinthine layer development • Wnt signaling pathway • negative regulation of protein binding • protein sumoylation • proteolysis • dorsal/ventral axis specification • negative regulation of protein ubiquitination • regulation of G1/S transition of mitotic cell cycle • heart development • regulation of Wnt signaling pathway • protein desumoylation • negative regulation of DNA damage response, signal transduction by p53 class mediator • protein destabilization • transport • negative regulation of signal transduction by p53 class mediator • protein transport • regulation of DNA endoreduplication • regulation of protein metabolic process • positive regulation of protein ubiquitination • fat cell differentiation • positive regulation of transcription from RNA polymerase II promoter
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


59343


75826

Ensembl


ENSG00000163904


ENSMUSG00000022855

UniProt


Q9HC62


Q91ZX6

RefSeq (mRNA)


NM_021627


NM_029457

RefSeq (protein)


NP_067640.2


NP_083733.1

Location (UCSC)

Chr 3: 185.58 – 185.63 Mb

Chr 16: 22.01 – 22.05 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Sentrin-specific protease 2 is an enzyme that in humans is encoded by the SENP2 gene.^[3]^[4]^[5]

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]^[5]

Interactions

SENP2 has been shown to interact with NUP153.^[3]^[6]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
1 2 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.
↑ 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.
1 2 "Entrez Gene: SENP2 SUMO1/sentrin/SMT3 specific peptidase 2".
↑ 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.

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. 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.

PDB gallery

1tgz: Structure of human Senp2 in complex with SUMO-1

1th0: Structure of human Senp2

2io0: Crystal structure of human Senp2 in complex with preSUMO-2

2io1: Crystal structure of human Senp2 in complex with preSUMO-3

2io2: Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1

2io3: Crystal structure of human Senp2 in complex with RanGAP1-SUMO-2

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SENP2

Function

Interactions

References

Further reading