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The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1\; MIM 601912) is required for numerous biologic processes. Additionally we are shipping ULP1 Antibodies (62) and many more products for this protein.
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The present study examined dynamic changes in SENP3 expression in the cerebral cortex and in its cellular localization.
The p53-independent tumor suppressive functions of p19(Arf) may be mediated by its ability to antagonize Senp3, thereby inducing cell cycle arrest by abnormally elevating the cellular levels of SUMOylated proteins.
High SENP3 expression is associated with stomach neoplasms.
SENP3, which is increased in gastric cancer cells, potentiates the transcriptional activity of FOXC2 (show FOXC2 Proteins) through de-SUMOylation, in favor of the induction of specific mesenchymal gene expression in gastric cancer metastasis.
Evidence show that mTOR (show FRAP1 Proteins)-mediated phosphorylation of SENP3 facilitates the interaction with NPM1 (show NPM1 Proteins), thereby promoting nucleolar targeting.
SENP3 is associated with MLL1/MLL2 complexes and catalyzes deSUMOylation of RbBP5 (show RBBP5 Proteins).
ROS (show ROS1 Proteins) induced SENP3 redistribution from the nucleoli to the nucleoplasm.
In a novel adaptive pathway to extreme cell stress, dynamic changes in SENP3 stability and regulation of Drp1 SUMOylation are crucial determinants of cell fate.
The shift of HIF-1 (show HIF1A Proteins) transactivation by reactive oxidative species is correlated with and dependent on the biphasic redox sensing of SENP3 that leads to the differential SENP3/p300 (show EP300 Proteins) interaction and the consequent fluctuation in the p300 (show EP300 Proteins) SUMOylation status.
These results suggest that SMT3IP1 is a new regulator of the p53 (show TP53 Proteins)-Mdm2 (show MDM2 Proteins) pathway.
Hsp90 (show HSP90 Proteins)/SENP3 association protects SENP3 from CHIP-mediated ubiquitination and subsequent degradation, but this effect of Hsp90 (show HSP90 Proteins) requires the presence of CHIP.
SENP3-mediated de-conjugation of SUMO2 (show SUMO2 Proteins)/3 from promyelocytic leukemia (show PML Proteins) is correlated with accelerated cell proliferation under mild oxidative stress.
The reversible posttranslational modification of proteins by the addition of small ubiquitin-like SUMO proteins (see SUMO1\; MIM 601912) is required for numerous biologic processes. SUMO-specific proteases, such as SENP3, are responsible for the initial processing of SUMO precursors to generate a C-terminal diglycine motif required for the conjugation reaction. They also have isopeptidase activity for the removal of SUMO from high molecular mass SUMO conjugates (Di Bacco et al., 2006
SUMO-1-specific protease 3
, SUMO/sentrin specific protease 3
, sentrin-specific protease 3
, sentrin/SUMO-specific protease SENP3
, smt3-specific isopeptidase 1
, sentrin/SUMO-specific protease 3
, SUMO/sentrin specific peptidase 3