U2AF2 Antibody

1. Data show that trans-acting RNA-binding proteins (RBPs) extensively regulate U2 (RNU2) small nuclear RNA auxiliary factor 2 protein (U2AF2) binding in vivo, including enhanced recruitment to 3' splice sites and clearance of introns PMID: 29643205
2. Data suggest that one way heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) regulates exon definition is to modulate the interaction of U2 small nuclear RNA auxiliary factor 2 (U2AF2) with decoy or bona fide 3' splice site (3'ss). PMID: 29650551
3. In summary, we provide insight into the underlying molecular mechanism of U2AF binding to 3' splice sites. PMID: 27799531
4. the most discriminant differences between lincRNAs and mRNAs involve splicing. LincRNAs are less efficiently spliced, which cannot be explained by differences in U1 binding or the density of exonic splicing enhancers but may be partially attributed to lower U2AF65 binding and weaker splicing-related motifs. PMID: 27927715
5. RBM39 is extensively involved in alternative splicing of RNA and helps regulate transcript levels. RBM39 may modulate alternative splicing similarly to U2AF65 by either directly binding to RNA or recruiting other splicing factors, such as U2AF65. PMID: 27354116
6. These findings uncovered a hitherto unappreciated function of CD82 in severing the linkage between U2AF2-mediated CD44 alternative splicing and cancer aggressiveness, with potential prognostic and therapeutic implications in melanoma PMID: 27041584
7. JMJD6 regulated a large set of alternative splicing events, and importantly, its regulated splicing events were significantly overlapped those controlled by U2AF65. PMID: 27899633
8. This study therefore establishes a structural basis for specific UHM-ULM interactions by splicing factors such as U2AF35, U2AF65, RBM39 and SF3b155, and a platform for continued studies of intermolecular interactions governing disease-related alternative splicing in eukaryotic cells. PMID: 27050129
9. The U2AF(65) linker residues between the dual RNA recognition motifs (RRMs) recognize the central nucleotide, whereas the N- and C-terminal RRM extensions recognize the 3' terminus and third nucleotide. PMID: 26952537
10. Nuclear retention of full-length HTT RNA is mediated by splicing factors MBNL1 and U2AF65 PMID: 26218986
11. Serum RNU2-1f may serve as a biomarker for lung cancer detection, prognosis prediction and treatment monitoring. PMID: 26687686
12. U2AF(65) possesses a splicing Inhibitory function that leads to alternative exon skipping. PMID: 26216990
13. The spatial distribution of U2AF65 conformations is found to be highly anisotropic, comprising significantly populated interdomain contacts that appear to be electrostatic in origin. PMID: 24734879
14. reduced U2AF(65) binding is a molecular consequence of disease-relevant mutations, and a structure-guided U2AF(65) variant is capable of manipulating gene expression in eukaryotic cells PMID: 25422459
15. We demonstrated that PRPF40B interacts directly with SF1 and associates with U2AF(65 PMID: 25605964
16. U2AF has the capacity to directly define ~88% of functional 3' splice sites in the human genome; numerous U2AF binding events also occur in intronic locations. PMID: 25326705
17. U2AF65 represents a new route for modulating TRF1 function at telomeres. PMID: 24389012
18. The conserved SPSP motif phosphorylation and the SF1/U2AF interface are essential in vivo. PMID: 23273425
19. The results highlight both local and global conformational selection as a means for universal 3' splice site recognition by U2AF65. PMID: 23376934
20. The REST N exon is a very versatile sequence with a complex array of splicing signals, and its activation in H69 cells depends on the relative amounts of hnRNP H and U2AF65. PMID: 22792276
21. By preventing U2AF65 binding to Alu elements, hnRNP C plays a critical role as a genome-wide sentinel protecting the transcriptome. PMID: 23374342
22. These complementary structural methods demonstrate that diverse splice sites have the opportunity to select compact or extended inter-RRM proximities from the U2AF65 conformational pool PMID: 22702716
23. 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 PMID: 22325350
24. dephosphorylation of pS776-ATXN1 by PP2A regulates the interaction of ATXN1 with the splicing factors RBM17 and U2AF65 PMID: 21835928
25. 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 PMID: 21753750
26. 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 PMID: 21536736
27. the conformational changes that are induced by assembly of the SF1/U2AF(65)/RNA complex serve to position the pre-mRNA splice site optimally for subsequent stages of splicing. PMID: 21146534
28. U2AF 65 promotes 3'-end processing, which contributes to 3'-terminal exon definition in RNA splicing PMID: 12189174
29. U2AF35 RRM is unstructured in solution but its tertiary structure is induced upon binding to U2AF65. PMID: 12297299
30. U2AF65 modulates the function of the PLE (poly(A)-limiting element) PMID: 14576315
31. 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 PMID: 15694343
32. identified and spatially localized sites of direct interaction between U2AF35 and U2AF65 in vivo in live cell nuclei. PMID: 16043505
33. Multiple U2AF65 binding sites within SF3b155 regulate conformational rearrangements during spliceosome assembly. PMID: 16376933
34. Cocrystals of a U2AF65 variant with a deoxyuridine dodecamer diffract X-rays to 2.9 angstroms resolution and contain one complex per asymmetric unit. PMID: 16682775
35. 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 PMID: 16809543
36. 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. PMID: 16940179
37. U2AF65 associates with specific subsets of spliced mRNAs, strongly suggesting that it is involved in novel cellular functions in addition to splicing. PMID: 17137510
38. 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. PMID: 17188295
39. SF1 and U2AF form extraspliceosomal complexes before and after taking part in the assembly of catalytic spliceosomes. PMID: 18285458
40. there is a functional link among apoptosis induction, U2AF65 cleavage, and the regulation of Fas alternative splicing PMID: 18508922
41. Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65. PMID: 18842594
42. Puf60-UHM binds to ULM sequences in the splicing factors SF1, U2AF65, and SF3b155. PMID: 18974054
43. Collectively, the results suggest that both U2AF binding and other steps of U2 snRNP recruitment can be control points in SMN splicing regulation. PMID: 19244360
44. study reveals the splicing factor U2AF65 undergoes posttranslational lysyl-5-hydroxylation catalyzed by Jmjd6 PMID: 19574390

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HGNC: 23156

OMIM: 191318

KEGG: hsa:11338

STRING: 9606.ENSP00000307863

UniGene: Hs.528007