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SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. Additionally we are shipping SUMO3 Antibodies (79) and SUMO3 Kits (1) and many more products for this protein.
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Increased post-translational modification of proteins by SUMO-2 (show SUMO2 Proteins)/3 is a cytoprotective response against cell stress induced by ischaemia and reperfusion.
Data suggest that PIASy (show PIAS4 Proteins) exhibits a SIM (show SIM2 Proteins) (SUMO-interacting motif) in addition to the SIM (show SIM2 Proteins) identified in homologous proteins in other species; both SIMs are located near C terminus of PIASy (show PIAS4 Proteins), and both are required for full ligase activity of PIASy (show PIAS4 Proteins); hydrophobic core residues of the new SIM (show SIM2 Proteins) are essential in binding to SUMO-3. (PIASy (show PIAS4 Proteins) = protein inhibitors of activated STAT (show STAT1 Proteins) y; SUMO-3 = small ubiquitin-like modifier 3)
The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation.
FOXP2 (show FOXP2 Proteins) can be modified with all three human SUMO proteins and that PIAS1 (show PIAS1 Proteins) promotes this process.
Small ubiquitin-related modifier 2 (show SUMO2 Proteins)/3 interacts with p65 (show GORASP1 Proteins) and stabilizes it in the cytoplasm in HBV-associated hepatocellular carcinoma.
Data indicate that small ubiquitin-like modifiers SUMO1 (show SUMO1 Proteins), SUMO2 (show SUMO2 Proteins), or SUMO3 were found in nuclear speckles.
Adenovirus E4-ORF3 targets PIAS3 (show PIAS3 Proteins) and together with E1B (show BCKDHB Proteins)-55K remodels SUMO2/SUMO3 Interactions in the nucleus and at virus genome replication domains.
DBC1 modification by Small Ubiquitin-like Modifier 2 (show SUMO2 Proteins)/3 is crucial for p53 (show TP53 Proteins) transactivation under genotoxic stress.
Expression of SUMO1 (show SUMO1 Proteins)/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28 (show LIN28A Proteins)/let-7.
PHD3 SUMOylation occurs at a cluster of four lysines at the C-terminal end of the protein. Furthermore, PHD3 SUMOylation by SUMO2 or SUMO3 contributes to PHD3-mediated repression of HIF1-dependent transcriptional activity.
a regulatory role of ZNF451-1 in fine-tuning physiological PML (show PML Proteins) levels
Results indicate that a functional SUMO1 (show SUMO1 Proteins)-3 expression is essential for emotionality and cognition
Expression levels and not functional differences between SUMO2 (show SUMO2 Proteins) and SUMO3 are critical for normal embryogenesis.
The purpose of this study was to perform a comprehensive analysis of the SUMO3-modified proteome regulated by brain ischemia using a novel SUMO transgenic mouse.
Stress-induced phosphorylation of Thr486 in c-Myb (show MYB Proteins) by p38 (show CRK Proteins) mitogen-activated protein kinases attenuates conjugation of SUMO-2 (show SUMO2 Proteins)/3.
post-ischemic activation of SUMO2 (show SUMO2 Proteins)/3 conjugation may define the fate of neurons exposed to a transient interruption of blood supply
These results suggest that increased Sumo3 in the hippocampus may be correlated with spatial learning ability in old C57BL/6 mice
When alterations in SUMO substrate conjugation occur, global and posttranslational modifications by ubiquitin may play an important role in the mechanisms underlying this Alzheimer disease model.
activation of SUMO2 (show SUMO2 Proteins)/3 conjugation is an endogenous neuroprotective stress response.
These results indicate that the functional role of SUMO-2/3 in the regulation of NFkappaB activity was conserved during evolution.
cyclin E (show CCNE1 Proteins) is dynamically and highly conjugated to SUMO2 (show SUMO2 Proteins)/3 on chromatin, independently of Cdk2 (show CDK2 Proteins) activity and origin activation.
SUM3 promotes plant defense downstream of salicylic acid, while SUM1 (show SUMO1 Proteins) and SUM2 (show SUMO2 Proteins) together prevent salicylic acid accumulation in noninfected plants.
SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002
SMT3 homolog 1
, SMT3 suppressor of mif two 3 homolog 1
, SMT3 suppressor of mif two 3 homolog 3
, small ubiquitin-related modifier 3
, ubiquitin-like protein SMT3A
, ubiquitin-like protein SMT3B
, SMT3 (supressor of mif two, 3) homolog 1
, SMT3 suppressor of mif two 3 homolog 2
, SMT3 suppressor of mif two 3 homolog 3, like
, small ubiquitin-related modifier 3-like
, SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)
, small ubiquitin-related modifier 3 precursor (SMT3 homolog 1)
, Small ubiquitin-related modifier 3