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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

SMT3 suppressor of mif two 3 homolog 2

This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus have been cleaved off. Numerous pseudogenes have been reported for this gene. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Smt3, Ubiquitin, DAPI, CAN, Ubc9
Papers using SUMO-2 antibodies
A C/EBP beta isoform recruits the SWI/SNF complex to activate myeloid genes
Wang Ju-Ming et al., In Nucleic Acids Research, 1998
... Antibodies against SUMO2/3 were purchased from Abcam (Cambridge, MA, USA) ...
Papers on SUMO-2
Molecular Basis for Phosphorylation Dependent SUMO Recognition by the DNA Repair Protein RAP80.
Spyracopoulos et al., Canada. In J Biol Chem, Jan 2016
RAP80 also contains a SUMO interacting motif (SIM) just upstream of the tandem UIMs that has been shown to specifically bind the SUMO-2 isoform.
Pc2-mediated SUMOylation of WWOX is essential for its suppression of DU145 prostate tumorigenesis.
Oh et al., Taejŏn, South Korea. In Febs Lett, Jan 2016
Ectopic WWOX was shown to associate with SUMO2/3 or E2 Ubc9.
Identification of RNF168 as a PML nuclear body regulator.
Frappier et al., Toronto, Canada. In J Cell Sci, Jan 2016
The association of RNF168 with PML NBs resulted in increased ubiquitylation and SUMO2 modification of PML proteins.
Mps1 is SUMO-modified during the cell cycle.
Dai et al., Heidelberg, Germany. In Oncotarget, Jan 2016
Mps1 was modified by both SUMO-1 and SUMO-2.
Non-native conformers of CFTR NBD1 are recognized by Hsp27 and conjugated to SUMO-2 for degradation.
Frizzell et al., Pittsburgh, United States. In J Biol Chem, Jan 2016
Similar to FL CFTR, F508del NBD1 expression was reduced 50-60% by Hsp27, it interacted preferentially with the mutant, and was modified primarily by SUMO-2.
Divergent signaling via SUMO modification: Potential for CFTR modulation.
Frizzell et al., Pittsburgh, United States. In Am J Physiol Cell Physiol, Dec 2015
A new pathway that contributes to mutant CFTR degradation is mediated by the small heat shock protein, Hsp27, which cooperates with Ubc9, the E2 enzyme for SUMOylation, to selectively conjugate mutant CFTR with SUMO-2/3.
Evolution of SUMO Function and Chain Formation in Insects.
Martín et al., Barcelona, Spain. In Mol Biol Evol, Dec 2015
However, the analysis of insect genomes shows that basal insects contain two SUMO genes, orthologous to vertebrate SUMO1 and SUMO2/3.
High-Pressure NMR Spectroscopy Reveals Functional Sub-states of Ubiquitin and Ubiquitin-Like Proteins.
Kitahara, Kusatsu, Japan. In Subcell Biochem, 2014
The high-energy states are conserved among ubiquitin-like post-translational modifiers, ubiquitin, NEDD8, and SUMO-2, showing the E1-E2-E3 cascade reaction.
SUMO and ischemic tolerance.
Hallenbeck et al., Bethesda, United States. In Neuromolecular Med, 2013
The discovery of massive SUMOylation (by both SUMO-1 and SUMO-2/3) occurring in the brains of 13-lined ground squirrels (Ictidomys tridecemlineatus) during hibernation torpor had opened the door to the studies on SUMO and ischemic tolerance reviewed here.
Cystic fibrosis transmembrane conductance regulator degradation: cross-talk between the ubiquitylation and SUMOylation pathways.
Frizzell et al., Pittsburgh, United States. In Febs J, 2013
Hsp27 promoted the SUMOylation of mutant CFTR by the SUMO-2 paralogue, which can form poly-chains.
Sumoylation in gene regulation, human disease, and therapeutic action.
Chiang et al., Montréal, Canada. In F1000prime Rep, 2012
Sumoylation has been well studied at the molecular and cellular levels, focusing mostly on site-specific conjugation of human SUMO1, SUMO2, and SUMO3, as well as their homologues in various species.
Correlation of increased hippocampal Sumo3 with spatial learning ability in old C57BL/6 mice.
Chen et al., Hefei, China. In Neurosci Lett, 2012
These results suggest that increased Sumo3 in the hippocampus may be correlated with spatial learning ability in old C57BL/6 mice
SUMO binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function.
Hayward et al., Baltimore, United States. In J Virol, 2012
SUMO2 binding by the Epstein-Barr virus protein kinase BGLF4 is crucial for BGLF4 function.
A 15q24 microdeletion in transient myeloproliferative disease (TMD) and acute megakaryoblastic leukaemia (AMKL) implicates PML and SUMO3 in the leukaemogenesis of TMD/AMKL.
Kulozik et al., Heidelberg, Germany. In Br J Haematol, 2012
The 15q24 microdeletion may thus represent the first genetic hit to initiate leukaemogenesis and implicates PML and SUMO3 as novel components of the leukaemogenic network in TMD/AMKL.
SUMO-2/3 conjugates accumulating under heat shock or MG132 treatment result largely from new protein synthesis.
Knejzlík et al., Praha, Czech Republic. In Biochim Biophys Acta, 2012
SUMO-2/3 conjugates accumulating under the heat shock or MG132 treatment result largely from new protein synthesis.
Analysis of global sumoylation changes occurring during keratinocyte differentiation.
Wilson et al., College Station, United States. In Plos One, 2011
sumoylation of proteins during keratinocyte differentiation is a complex process which likely reflects and contributes to the biochemical changes that drive differentiation.
Coronin 2A mediates actin-dependent de-repression of inflammatory response genes.
Glass et al., San Diego, United States. In Nature, 2011
SUMOylated LXRs block NCoR turnover by binding to a conserved SUMO2/SUMO3-interaction motif in CORO2A and preventing actin recruitment.
The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress.
Solomon et al., London, United Kingdom. In Nature, 2010
Here we report that BRCA1 is modified by small ubiquitin-like modifier (SUMO) in response to genotoxic stress, and co-localizes at sites of DNA damage with SUMO1, SUMO2/3 and the SUMO-conjugating enzyme Ubc9.
Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks.
Jackson et al., Cambridge, United Kingdom. In Nature, 2010
Here, we show that SUMO1, SUMO2 and SUMO3 accumulate at DSB sites in mammalian cells, with SUMO1 and SUMO2/3 accrual requiring the E3 ligase enzymes PIAS4 and PIAS1.
PIASy mediates NEMO sumoylation and NF-kappaB activation in response to genotoxic stress.
Miyamoto et al., Madison, United States. In Nat Cell Biol, 2006
PIASy preferentially stimulates site-selective modification of NEMO by SUMO-1, but not SUMO-2 and SUMO-3, in vitro.
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