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SENP2 regulates Drp1 sumoylation and stability critical for mitochondrial morphogenesis.SENP2 plays role in mitochondria mediated neural degeneration.
This study identified an animal model of SUDEP, which is caused by alteration of a posttranslational protein modification pathway (SUMOylation) on a unique voltage-gated potassium channel (Kv7.2/Kv7.3)
These results reveal the important role of SENP2 in the regulation of myostatin (show MSTN Proteins) expression and myogenesis.
SENP2 represses glycolysis and shifts glucose metabolic strategy
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.
a mechanism underlying the SENP2-mediated regulation of Mdm2 (show MDM2 Proteins) that is critical for genome integrity in p53 (show TP53 Proteins)-dependent stress responses.
SENP2 de-SUMOylates PPARgamma (show PPARG Proteins) in myotubes, and de-SUMOylation of PPARgamma (show PPARG Proteins) selectively increases the expression of some PPARgamma (show PPARG Proteins) target genes.
Senp2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development.
These results establish a critical role for SENP2 in the regulation of adipogenesis by desumoylation.
SUMO-1 protease-1 regulates gene transcription through PML (show PML Proteins).
Data demonstrate that downregulation of SENP2 (show SUMO1 Proteins) is correlated with poor prognosis in bladder cancer; SENP2 (show SUMO1 Proteins) inhibits TGF-beta (show TGFB1 Proteins) signaling and TGF-beta (show TGFB1 Proteins)-induced EMT (show ITK Proteins) of bladder cancer cell; and that its overexpression contributes to suppress bladder cancer cell invasion and metastasis through deSUMOylation of TGF-betaRI.
The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence.
SENP2 (show SUMO1 Proteins) inhibits MMP13 (show MMP13 Proteins) expression in BC cells through de-SUMOylation of TBL1 (show TBL1X Proteins)/TBLR1 (show TBL1XR1 Proteins), which inhibits nuclear translocation of beta-catenin (show CTNNB1 Proteins).
miR (show MLXIP Proteins)-181b targets SENP2 (show SUMO1 Proteins) and positively regulated NF-kappaB (show NFKB1 Proteins) activity. NF-kappaB (show NFKB1 Proteins) activation by DNA damage in GBM cells confers resistance to radiation-induced death.
data identify SENP2 as an important regulator of fatty acid metabolism in skeletal muscle
SENP2 (show SUMO1 Proteins) regulates the transcriptional function of MEF2A (show MEF2A Proteins) via direct de-SUMOylation.
p90RSK-mediated SENP2-T368 phosphorylation is a master switch in disturbed-flow-induced signaling.
we show that WWOX required for stabilization of beta-catenin regulated by SENP2 in hepatocellular carcinoma cells
ESR1 repression by SENP2 is independent of its SUMO protease activity.
Many nucleoporins are mislocalized and, in some cases, reduced in level when SENP1 and SENP2 are codepleted.
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.
SUMO-1 protease 1
, SUMO-1 protease-1
, SUMO-1/Smt3-specific isopeptidase 2
, SUMO/sentrin specific protease 2
, sentrin-specific protease 2
, sentrin/SUMO-specific protease SENP2
, SMT3-specific isopeptidase 2
, SUMO1/sentrin/SMT3 specific protease 2
, Axin-associating molecule
, SUMO/sentrin specific peptidase 2