SENP2

General Information

Full gene name:SUMO1/sentrin/SMT3 specific peptidase 2 Entrez Gene ID:59343 Location:3q27.2 Synonyms:AXAM2, SMT3IP2 Type:protein-coding

User SNPs

SNPs given by the user that are near or inside this gene:

SNP	Distance (bp)	Direction
rs1470579	180195	downstream

NCBI Summary

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, Apr 2004]

OMIM

OMIM ID:`OMIM ID 608261 `_

NCBI Phenotypes

No phenotypes found linked to this gene.

Gene Ontology

• PML body
• negative regulation of protein binding
• Wnt receptor signaling pathway
• protein binding
• dorsal/ventral axis specification
• positive regulation of protein phosphorylation
• cytoplasm
• SUMO-specific protease activity
• mRNA transport
• regulation of Wnt receptor signaling pathway
• nuclear membrane
• protein domain specific binding
• proteolysis
• protein desumoylation
• nuclear pore
• protein transport

KEGG Pathways

• Wnt signaling pathway
• RNA transport

GeneRIFs

• Data suggest that SENP2 regulates antiviral innate immunity by deSUMOylating IRF3 and conditioning it for ubiquitination and degradation, and provide an example of cross-talk between the ubiquitin and SUMO pathways in innate immunity. [PMID 22028379]
• a mechanism underlying the SENP2-mediated regulation of Mdm2 that is critical for genome integrity in p53-dependent stress responses. [PMID 21183956]
• Affinity Capture-MS [PMID 19394292]
• association with the pore plays an important negative role in the regulation of SENP2 [PMID 11896061]
• Affinity Capture-Western; Reconstituted Complex; Two-hybrid [PMID 20098747]
• Results demonstrate that SENP1 is the most efficient SUMO protease acting on Elk-1, and that SENP3 has little effect on Elk-1. SENP2 has an intermediate effect, but its ability to activate Elk-1 is independent from its SUMO-deconjugating activity. [PMID 20337593]
• The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex. [PMID 22031293]
• SENP2 null cells display biphasic NEMO SUMOylation and activation of IKK and NF-kappaB [PMID 21777808]
• Reconstituted Complex [PMID 19953087]
• Reconstituted Complex [PMID 12192048]
• Biochemical Activity [PMID 12192048]
• Biochemical Activity [PMID 12192048]
• Restricting SENP2 in the nucleus by mutations in the NES impairs its polyubiquitination, whereas a cytoplasm-localized SENP2 made by introducing mutations in the NLS can be efficiently polyubiquitinated. [PMID 16738331]
• cardiac overexpression of SENP2 in the mice with Nkx2.5 haploinsufficiency promoted embryonic lethality and severity of congenital heart diseases (CHDs). [PMID 22155005]
• Mutational analysis and biochemistry provide a mechanism for SENP2 substrate preferences that explains why SENP2 catalyzes SUMO deconjugation more efficiently than processing [PMID 17099700]
• Two-hybrid [PMID 16169070]

PubMed Articles

Recent articles:

• Kim EY et al. “Enhanced desumoylation in murine hearts by overexpressed SENP2 leads to congenital heart defects and cardiac dysfunction.” J Mol Cell Cardiol. 2012 Mar;52(3):638-49. PMID 22155005
• Goeres J et al. “The SUMO-specific isopeptidase SENP2 associates dynamically with nuclear pore complexes through interactions with karyopherins and the Nup107-160 nucleoporin subcomplex.” Mol Biol Cell. 2011 Dec;22(24):4868-82. PMID 22031293
• Ran Y et al. “SENP2 negatively regulates cellular antiviral response by deSUMOylating IRF3 and conditioning it for ubiquitination and degradation.” J Mol Cell Biol. 2011 Oct;3(5):283-92. PMID 22028379
• Lee MH et al. “NF-κB induction of the SUMO protease SENP2: A negative feedback loop to attenuate cell survival response to genotoxic stress.” Mol Cell. 2011 Jul 22;43(2):180-91. PMID 21777808
• Jiang M et al. “SUMO-specific protease 2 in Mdm2-mediated regulation of p53.” Cell Death Differ. 2011 Jun;18(6):1005-15. PMID 21183956
• Witty J et al. “SENP1 participates in the dynamic regulation of Elk-1 SUMOylation.” Biochem J. 2010 May 13;428(2):247-54. PMID 20337593
• Fenner BJ et al. “Expanding the substantial interactome of NEMO using protein microarrays.” PLoS One. 2010 Jan 20;5(1):e8799. PMID 20098747
• Persaud A et al. “Comparison of substrate specificity of the ubiquitin ligases Nedd4 and Nedd4-2 using proteome arrays.” Mol Syst Biol. 2009;5:333. PMID 19953087
• Ouyang J et al. “Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex.” Mol Cell. 2009 Apr 24;34(2):145-54. PMID 19394292
• Barbe L et al. “Toward a confocal subcellular atlas of the human proteome.” Mol Cell Proteomics. 2008 Mar;7(3):499-508. PMID 18029348

Top Pubmed articles linked to gene SENP2 matching any search term:

• Agbor TA et al. “Small ubiquitin-related modifier (SUMO)-1 promotes glycolysis in hypoxia.” J Biol Chem. 2011 Feb 11;286(6):4718-26. PMID 21123177