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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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Top mentioned proteins: CAN, U2AF35, STEP, SF-1, ACID
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
Mammalian splicing factor SF1 interacts with SURP domains of U2 snRNP-associated proteins.
Krämer et al., Genève, Switzerland. In Nucleic Acids Res, Jan 2016
The 65-kDa subunit of U2 snRNP auxiliary factor (U2AF65) interacts with SF1 and was shown to recruit the U2 snRNP to the spliceosome.
SAM68 is a physiological regulator of SMN2 splicing in spinal muscular atrophy.
Sette et al., Roma, Italy. In J Cell Biol, Nov 2015
Mechanistically, SAM68 binds to SMN2 pre-mRNA, favoring recruitment of the splicing repressor hnRNP A1 and interfering with that of U2AF65 at the 3' splice site of exon 7.
Splicing inhibition of U2AF65 leads to alternative exon skipping.
Shen et al., Kwangju, South Korea. In Proc Natl Acad Sci U S A, Sep 2015
U2 snRNP auxiliary factor 65 kDa (U2AF(65)) is a general splicing factor that contacts polypyrimidine (Py) tract and promotes prespliceosome assembly.
Nuclear retention of full-length HTT RNA is mediated by splicing factors MBNL1 and U2AF65.
Rudnicki et al., Baltimore, United States. In Sci Rep, 2014
The splicing and nuclear export factor U2AF65 has the opposite effect, decreasing expHTT nuclear retention and increasing expression of expHTT protein.
Gastrointestinal tract tumors and cell lines possess differential splicing factor expression and tumor associated mRNA isoform formation profiles.
Kanopka et al., Vilnius, Lithuania. In Cancer Biomark, 2014
We present experimental evidence that splicing factor SRSF1, SRSF2, U2AF35, U2AF65 and KHSRP expression levels in gastrointestinal tract (colon, gastric and pancreatic) tumors differ compare to healthy tissues and in cell lines, derived from corresponding organs.
CPEB1 coordinates alternative 3'-UTR formation with translational regulation.
Méndez et al., Barcelona, Spain. In Nature, 2013
CPEB1 binding to pre-mRNAs not only directs the use of alternative polyadenylation sites, but also changes alternative splicing by preventing U2AF65 recruitment.
Direct competition between hnRNP C and U2AF65 protects the transcriptome from the exonization of Alu elements.
Ule et al., United Kingdom. In Cell, 2013
Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites.
Cancer-Associated Perturbations in Alternative Pre-messenger RNA Splicing.
Chabot et al., Sherbrooke, Canada. In Cancer Treat Res, 2012
Introns are identified by the binding of U1 snRNP to the 5' splice site and the U2AF65/U2AF35 complex to the 3' splice site.
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.
The structure of human cleavage factor I(m) hints at functions beyond UGUA-specific RNA binding: a role in alternative polyadenylation and a potential link to 5' capping and splicing.
Doublié et al., Burlington, United States. In Rna Biol, 2011
Our study illustrated the molecular basis for UGUA recognition by the CFI(m) complex, suggested a possible mechanism for CFI(m) mediated alternative polyadenylation, and revealed potential links between CFI(m) and other mRNA processing factors, such as the 20 kDa subunit of the cap binding protein (CBP20), and the splicing regulator U2AF65.
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
An active role for splicing in 3'-end formation.
Martinson, Los Angeles, United States. In Wiley Interdiscip Rev Rna, 2011
First, the splicing factor, U2AF65, interacts with the CP factor, CFI(m).
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
The branchpoint binding protein: in and out of the spliceosome cycle.
Rymond, Lexington, United States. In Adv Exp Med Biol, 2009
The QUA1 homodimerization motif found upstream of the KH-QUA2 sequence in other STAR/GSG family members is absent in BBP and replaced by a site for the phylogenetically conserved binding partner, Mud2/U2AF65.
Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing.
Böttger et al., Oxford, United Kingdom. In Science, 2009
study reveals the splicing factor U2AF65 undergoes posttranslational lysyl-5-hydroxylation catalyzed by Jmjd6
Intron removal requires proofreading of U2AF/3' splice site recognition by DEK.
Valcárcel et al., Barcelona, Spain. In Science, 2006
DEK enforces 3' splice site discrimination by U2AF; DEK phosphorylated at serines 19 and 32 associates with U2AF35, facilitates the U2AF35-AG interaction and prevents binding of U2AF65 to pyrimidine tracts not followed by AG
Multiple RNA binding domains (RBDs) just don't add up.
Williams et al., New Haven, United States. In Nucleic Acids Res, 1995
In the cases of heterogenous nuclear ribonucleoprotein A1 (hnRNP A1), yeast poly-A binding protein and splicing factor U2AF65, the individual free energy of binding of the RBDs for RNA are not strictly additive.
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