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U2 small nuclear RNA auxiliary factor 2

U2AF65, U2AF(65), U2 small nuclear ribonucleoprotein auxiliary factor
U2 auxiliary factor (U2AF), comprised of a large and a small subunit, is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA branch site. This gene encodes the U2AF large subunit which contains a sequence-specific RNA-binding region with 3 RNA recognition motifs and an Arg/Ser-rich domain necessary for splicing. The large subunit binds to the polypyrimidine tract of introns early during spliceosome assembly. Multiple transcript variants have been detected for this gene, but the full-length natures of only two have been determined to date. [provided by RefSeq, Jul 2008] (from NCBI)
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Papers using U2AF65 antibodies
Nuclear localization of EGF receptor and its potential new role as a transcription factor
Gottardi Cara, In PLoS ONE, 2000
... , matrin-3 (ab51081), and U2AF65 (ab37483) were obtained from Abcam (Cambridge MA) ...
Papers on U2AF65
hnRNP A1 proofreads 3' splice site recognition by U2AF.
Valcárcel et al., Barcelona, Spain. In Mol Cell, 2012
hnRNP A1 forms a ternary complex with the U2AF heterodimer on AG-containing/uridine-rich RNAs, while it displaces U2AF from non-AG-containing/uridine-rich RNAs, an activity that requires the glycine-rich domain of hnRNP A1
14-3-3 Binding to ataxin-1(ATXN1) regulates its dephosphorylation at Ser-776 and transport to the nucleus.
Orr et al., Minneapolis, United States. In J Biol Chem, 2011
dephosphorylation of pS776-ATXN1 by PP2A regulates the interaction of ATXN1 with the splicing factors RBM17 and U2AF65
Perturbation of U2AF65/NXF1-mediated RNA nuclear export enhances RNA toxicity in polyQ diseases.
Chan et al., Hong Kong, Hong Kong. In Hum Mol Genet, 2011
Perturbation of U2AF65/NXF1-mediated RNA nuclear export enhances RNA toxicity in polyQ diseases.
Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF.
Sattler et al., München, Germany. In Nature, 2011
the molecular mechanisms of the recognition of the 3'-splice-site-associated polypyrimidine tract RNA by the large subunit of the human U2 snRNP auxiliary factor (U2AF65) as a key early step in pre-mRNA splicing
The RNA polymerase II C-terminal domain promotes splicing activation through recruitment of a U2AF65-Prp19 complex.
Manley et al., New York City, United States. In Genes Dev, 2011
U2AF65 binds directly to the phosphorylated C-terminal domain, and that this interaction results in increased recruitment of U2AF65 and PRP19C to the pre-mRNA
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