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Validated All-in-One™ qPCR Primer for U2AF2(NM_007279.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
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].
Gene References into function
- U2AF 65 promotes 3'-end processing, which contributes to 3'-terminal exon definition in RNA splicing
- U2AF35 RRM is unstructured in solution but its tertiary structure is induced upon binding to U2AF65.
- U2AF65 modulates the function of the PLE (poly(A)-limiting element)
- two members of the U2AF65 family of proteins, hCC1.3, which we call CAPERalpha, and a related protein, CAPERbeta, regulate both steroid hormone receptor-mediated transcription and alternative splicing
- identified and spatially localized sites of direct interaction between U2AF35 and U2AF65 in vivo in live cell nuclei.
- Multiple U2AF65 binding sites within SF3b155 regulate conformational rearrangements during spliceosome assembly.
- Cocrystals of a U2AF65 variant with a deoxyuridine dodecamer diffract X-rays to 2.9 angstroms resolution and contain one complex per asymmetric unit.
- 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
- Results describe the roles of the two subunits of U2AF, U2AF65 and 35, in the selection between alternative 3' splice sites associated with polypyrimidine tracts of different strengths.
- a direct role of the U2AF 65/CF I(m) 59 interaction in the functional coordination of splicing and 3' end processing.
- U2AF65 associates with specific subsets of spliced mRNAs, strongly suggesting that it is involved in novel cellular functions in addition to splicing.
- This rare, high-resolution view of an important member of the RNA recognition motifs class of RNA-binding domains highlights the role of alternative side-chain conformations in RNA recognition.
- SF1 and U2AF form extraspliceosomal complexes before and after taking part in the assembly of catalytic spliceosomes.
- there is a functional link among apoptosis induction, U2AF65 cleavage, and the regulation of Fas alternative splicing
- Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65.
- Puf60-UHM binds to ULM sequences in the splicing factors SF1, U2AF65, and SF3b155.