Browse our SENP2 Proteins (SENP2)

Mouse (Murine) SUMO1/sentrin/SMT3 Specific Peptidase 2 (SENP2) interaction partners

1. Data suggest that SENP2 in hepatic stellate cells is involved in regulation of apoptosis in these cells and in development/reversion of liver fibrosis (here, carbon tetrachloride-induced liver fibrosis).

2. Expression of the SENP2 gene was suppressed by theobromine. In vivo knockdown studies showed that AR1 (show TCF20 Proteins) knockdown in mice attenuated the anti-adipogenic effects of theobromine in younger mice. Theobromine suppresses adipocyte differentiation and induced C/EBPbeta (show CEBPB Proteins) degradation by increasing its sumoylation.

3. SENP2 regulates Drp1 (show CRMP1 Proteins) sumoylation and stability critical for mitochondrial morphogenesis.SENP2 plays role in mitochondria mediated neural degeneration.

4. 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)

5. These results reveal the important role of SENP2 in the regulation of myostatin (show MSTN Proteins) expression and myogenesis.

6. SENP2 represses glycolysis and shifts glucose metabolic strategy

7. 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.

8. 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.

9. 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.

10. Senp2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development.

Human SUMO1/sentrin/SMT3 Specific Peptidase 2 (SENP2) interaction partners

1. Data show that Sentrin/SUMO specific protease (SENP2) interacts with N-myc downstream regulated gene 2 (NDRG2 (show NDRG2 Proteins)) and mediates the de-SUMOylation process of NDRG2 (show NDRG2 Proteins).

2. 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.

3. The variability of the SENP1 and SENP2 genes may play a role in breast cancer occurrence.

4. 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).

5. 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.

6. data identify SENP2 as an important regulator of fatty acid metabolism in skeletal muscle

7. SENP2 (show SUMO1 Proteins) regulates the transcriptional function of MEF2A (show MEF2A Proteins) via direct de-SUMOylation.

8. p90RSK-mediated SENP2-T368 phosphorylation is a master switch in disturbed-flow-induced signaling.

9. we show that WWOX required for stabilization of beta-catenin regulated by SENP2 in hepatocellular carcinoma cells

10. ESR1 repression by SENP2 is independent of its SUMO protease activity.