U2AF2

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]

Full Name

U2 small nuclear RNA auxiliary factor 2

Function

Plays a role in pre-mRNA splicing and 3'-end processing (PubMed:17024186).
By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing (PubMed:21536736).
Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. Positively regulates pre-mRNA 3'-end processing by recruiting the CFIm complex to cleavage and polyadenylation signals (PubMed:17024186).

Biological Process

Biological Process mRNA processing Source:ProtInc1 Publication
Biological Process mRNA splicing, via spliceosome Source:GO_Central1 Publication
Biological Process negative regulation of mRNA splicing, via spliceosome Source:UniProtKB1 Publication
Biological Process negative regulation of protein ubiquitination Source:BHF-UCL1 Publication
Biological Process positive regulation of RNA splicing Source:UniProtKB1 Publication

Cellular Location

Nucleus

PTM

Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA splicing activity of the protein, leading to regulate some, but not all, alternative splicing events.