gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

SET nuclear oncogene

SET
The protein encoded by this gene inhibits acetylation of nucleosomes, especially histone H4, by histone acetylases (HAT). This inhibition is most likely accomplished by masking histone lysines from being acetylated, and the consequence is to silence HAT-dependent transcription. The encoded protein is part of a complex localized to the endoplasmic reticulum but is found in the nucleus and inhibits apoptosis following attack by cytotoxic T lymphocytes. This protein can also enhance DNA replication of the adenovirus genome. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Oct 2011] (from NCBI)
Papers on SET
Influence of the accessory protein SET on M3 muscarinic receptor phosphorylation and G protein coupling.
GeneRIF
Lanier et al., Paris, France. In Mol Pharmacol, 2012
SET knockdown increased high-affinity binding of agonist in intact cells and membrane preparations.
Overexpression of SET is a recurrent event associated with poor outcome and contributes to protein phosphatase 2A inhibition in acute myeloid leukemia.
GeneRIF
Odero et al., Pamplona, Spain. In Haematologica, 2012
SET overexpression is a key mechanism in the inhibition of PP2A in acute myeloid leukemia.
Accumulation of the SET protein in HEK293T cells and mild oxidative stress: cell survival or death signaling.
GeneRIF
Curti et al., Ribeirão Preto, Brazil. In Mol Cell Biochem, 2012
Suggest that accumulated SET could act via Akt/PTEN either as cell survival signal or as oxidative stress sensor for cell death.
SET oncogene is upregulated in pediatric acute lymphoblastic leukemia.
GeneRIF
Ozbek et al., İstanbul, Turkey. In Tumori, 2012
Results showed that SET is significantly overexpressed in pediatric acute lymphoblastic leukemia samples, and an increased level of SET might contribute to leukemic process.
Role of Template Activating Factor-I as a chaperone in linker histone dynamics.
GeneRIF
Nagata et al., Tsukuba, Japan. In J Cell Sci, 2011
TAF-I is a key molecule that regulates linker histone-mediated chromatin assembly and disassembly
share on facebooktweetadd +1mail to friends