3.4.22.B71: SENP2 peptidase
This is an abbreviated version!
For detailed information about SENP2 peptidase, go to the full flat file.
Word Map on EC 3.4.22.B71
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3.4.22.B71
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sumoylation
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medicine
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atherosclerosis
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aorta
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d-flow
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d-flow-induced
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erk5
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de-sumoylation
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p90rsk
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senps
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epilepsy
- 3.4.22.B71
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sumoylation
- medicine
- atherosclerosis
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aorta
-
d-flow
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d-flow-induced
- erk5
-
de-sumoylation
-
p90rsk
-
senps
-
epilepsy
Reaction
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Synonyms
(SUMO-1)-specific protease 2, SENP2, sentrin/SUMO-specific protease 2, small ubiquitin-like modifier-specific protease, small ubiquitin-like modifier-specific protease 2, small ubiquitin-related modifier-specific isopeptidase, SUMO-specific isopeptidase, SUMO-specific protease, SUMO-specific protease 2
ECTree
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General Information
General Information on EC 3.4.22.B71 - SENP2 peptidase
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evolution
malfunction
metabolism
physiological function
additional information
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SUMO-specific protease 2 (SENP2) is a de-SUMOylation protease family member
in SENP2 null embryo, SUMOylated Pc2/CBX4 accumulates and Pc2/CBX4 occupancy on the promoters of PcG target genes is markedly increased, leading to repression of Gata4 and Gata6 transcription
malfunction
knockdown of SENP2 leads to a strong attenuation of adipogenesis with a marked decrease in PPARgamma and C/EBPalpha mRNA levels. Knockdown of SENP2 also causes a marked reduction in the level of C/EBPbeta protein but not in that of C/EBPbeta mRNA
malfunction
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SENP2 ablation disturbs the p53-Mdm2 pathway, affecting the expansion of trophoblast progenitors and their maturation
malfunction
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differential localization of nucleoporins upon codepletion of SENP1 and SENP2 in HeLa cells, immunohistochemic analysis, overview
malfunction
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enzyme SENP2 knockout MEF cells show increased glucose uptake and lactate production along with decreased ATP levels. SENP2 knockout embryonic fibroblasts exhibit increased levels of phosphorylated AKT. Inhibiting AKT phosphorylation by LY294002 rescues the phenotype induced by SENP2 deficiency in embryonic fibroblasts. Knockout of SENP2 leads to increased aerobic glycolysis in MEF cells
malfunction
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overexpression of enzyme SENP2 reduces the glucose uptake and lactate production, increasing the cellular ATP levels in MCF-7 cells. The MCF-7 cells overexpressing enzyme SENP2 exhibit decreased expression levels of key glycolytic enzymes and an increased rate of glucose oxidation compared with control MCF-7 cells, indicating inhibited glycolysis but enhanced oxidative mitochondrial respiration. The cells have a reduced amount of phosphorylated AKT
malfunction
RNA interference SENP2 knockdown produces no detectable phenotypes, while overexpression of SENP2, but not other SUMO-specific isopeptidases, causes a defect in chromosome congression that depends on its precise kinetochore targeting. Isozyme SENP2 overexpression uniquely induces prometaphase arrest
malfunction
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silencing the expression of enzyme SENP2 significantly induces the expression of MMP13 , forced MMP13 expression is sufficient to restore cell invasion in SENP2 overexpressed T24 bladder cancer cells
malfunction
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specifically, either RNAi depletion of SENP1/SENP2 or expression of dominantly interfering mutants of these proteins results in increased sumoylation of endogenous Nup153. Catalytically inactive SENP2 maintains specific attributes, although it has enhanced interaction with sumoylated Nup153, overview. Truncated SENP2CD is robustly modified by SUMO2
metabolism
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SENP2 protein is accumulated in response to activity-dependent stimuli which in turn mediated activity dependent-regulation of MEF2A deSUMOylation
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mitotic kinase Aurora-B is a mitotic SUMO substrate and its kinase activity is fine-tuned by the SUMO system
physiological function
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SENP2 in mice reveals its essential role in development of all three trophoblast layers. SENP2 has a specific role in the G-S transition, which is required for mitotic and endoreduplication cell cycles in trophoblast proliferation and differentiation, respectively
physiological function
SENP2 plays a critical role in the control of adipogenesis by desumoylation and stabilization of C/EBPbeta and in turn by promoting the expression of its downstream effectors, such as PPARgamma and C/EBPalpha
physiological function
SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development. SENP2 specifically controls Pc2/CBX4 contained PRC1 activity through regulation of the SUMOylation status of Pc2/CBX4, which facilitates its binding to H3K27me3 in mammalian cells to mediate transcriptional repression
physiological function
enzyme SENP2 is an important mediator of precise spatial and temporal control of sumoylation in mitosis required for chromosome segregation
physiological function
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enzyme SENP2 represses glycolysis and shifts glucose metabolic strategy, in part through inhibition of AKT phosphorylation, function of SENP2 in regulating glucose metabolism, overview
physiological function
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enzyme SENP2 represses glycolysis and shifts glucose metabolic strategy, in part through inhibition of AKT phosphorylation, function of SENP2 in regulating glucose metabolism, overview
physiological function
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nuclear factor-kappaB-mediated increase in the expression of SENP2 promotes the recruitment of peroxisome proliferator-activated receptors PPARdelta and PPARgamma, through deSUMOylation of PPARs, to the promoters of the genes involved in fatty acid oxidation, such as carnitine-palmitoyl transferase-1 and long-chain acyl-CoA synthetase 1. Enzyme overexpression substantially increases fatty acid oxidation in C2C12 myotubes
physiological function
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SENP2, as well as SENP1, regulates the proper localization of nucleoporins, overview. The enzyme interacts with the nucleoporin Nup153 via a dual interface that includes a bridging interaction with the soluble transport receptor importin beta and a SUMO-mediated mechanism, and also with Nup358 and members of the Nup107-160 complex at distinct regions of SENP2 that can independently direct SENP2 to the nuclear rim. SENP1 and SENP2 are not required for localization of the transmembrane proteins nucleoporin POM121 and inner nuclear envelope protein Sun1 or expansion of the interphase nuclear envelope
physiological function
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SENP2, but not SENP1, regulates MEF2A deSUMOylation in an activity dependent manner, enzyme SENP2 markedly enhances the transcription of MEF2A through directly deSUMOylation
physiological function
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SUMO-specific protease 2 suppresses cell migration and invasion through selectively inhibiting the expression of MMP13 in bladder cancer cells, the enzyme has an indispensable role in the regulation of NF-kappaB transcriptional activation and Wnt signaling. The enzyme inhibits bladder cancer cells migration and invasion in vitro
physiological function
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the broad deSUMOylation activity of the enzyme in vitro is essential for embryonic heart development, essential role of small ubiquitin-like modifier-specific protease 2 in myostatin expression and myogenesis, overview. Enzyme SENP2 regulates the transcription of myostatin mainly through deSUMOylation of MEF2A. MEF2A mediates SENP2 activity on the myostatin promoter involving the MEF2 binding site. Enzyme SENP2 inhibits skeletal myogenesis
physiological function
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the SUMO proteases play roles both in processing SUMO during the biogenesis of this peptide moiety and also in reversing SUMO modification on specific targets to control the activities conferred by this posttranslational modification. Specificity of the role for SENP1 and SENP2 in maintaining desumoylation of Nup153
physiological function
adipocyte Senp2 deficiency results in less adipose lipid storage accompanied by an ectopic fat accumulation and insulin resistance under high-fat diet feeding. SET domain bifurcated 1 (Setdb1) is a SUMOylated protein and SUMOylation promotes Setdb1 occupancy on the promoter locus of Pparg and Cebpa genes to suppress their expressions via histone H3K9me3. Senp2 can suppress Setdb1 function by deSUMOylation. In adipocyte Senp2-deficiency mice, accumulation of the SUMOylated Setdb1 suppresses the expression of Pparg and Cebpa genes as well as lipid metabolism-related target genes
physiological function
development of a mouse strain permitting conditional inactivation of SENP2. Mice homozygous for germline deletion of the conditional allele exhibit trophoblast defects and embryonic abnormalities resembling the global SENP2 knockout. SENP2 is dispensable in embryogenesis. Placental expression of SENP2 is necessary and sufficient for embryonic heart and brain development. SENP2-dependent SUMO modification is required in development of all major trophoblast lineages. SENP2 regulates sumoylation of Mdm2 which controls p53 activities critical for G-S transition of mitotic division and endoreduplication in trophoblast proliferation and differentiation, respectively
physiological function
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ectopic expression of SENP2 results in the suppression of proliferation, migration and invasion in osteosarcoma cells, whereas SENP2 knockdown has the opposite effect
physiological function
leptin treatment of C2C12 myotubes causes signal transducer and activator of transcription STAT3 to bind to the Senp2 promoter, inducing its expression. When Senp2 is knocked down in myotubes, leptin-induced expression of fatty acid oxidation-associated enzymes and prolonged increase of fatty acid oxidation are suppressed, but rapid increase of fatty acid oxidation is unaffected. Leptin-induced expression of fatty acid oxidation-associated enzymes is not observed in muscle tissue of SENP2 knockout mice
physiological function
SENP2 inhibits nuclear translocation of beta-catenin, which targets the promotor of MMP13 to activate MMP13 to enhance bladder cancer cell metastasis
physiological function
SENP2 interacts with Smad4 through SENP2 residue 363-400. The same segment is also important for desumoylation of Smad4, and able to relieve sumoylation-mediated TGF-beta repression. The SENP2363-400 segment is critical for TGF-beta-induced cell migration, which is correlated with SENP2363-400 deletion mutant that fails to increase matrix metalloproteinase (MMP)-9 and epithelial-to-mesenchymal transition marker gene expression. The interaction and desumoylation between SENP2 and Smad4 promote cell migration in triple-negative breast cancer cells
physiological function
SENP2 knockdown results in a decrease of E-cadherin and an increase of N-cadherin and fibronectin at both transcript and protein levels. SENP2 overexpression results in deSUMOylation of TGF-betaR I in bladder cancer cells and suppresses TGF-beta signaling and TGF-beta-induced epithelial-mesenchymal transition. SENP2 regulates TGF-beta signaling partly through deSUMOylation of TGFbeta receptor I
physiological function
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the broad deSUMOylation activity of the enzyme in vitro is essential for embryonic heart development, essential role of small ubiquitin-like modifier-specific protease 2 in myostatin expression and myogenesis, overview. Enzyme SENP2 regulates the transcription of myostatin mainly through deSUMOylation of MEF2A. MEF2A mediates SENP2 activity on the myostatin promoter involving the MEF2 binding site. Enzyme SENP2 inhibits skeletal myogenesis
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Correlation of Senp2 and myostatin expression in cachexia
additional information
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SENP2 is a target of SUMO modification and has targeting preference for SUMO paralogues and substrates
additional information
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Correlation of Senp2 and myostatin expression in cachexia
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