U2AF2

U2 small nuclear RNA auxiliary factor 2, also known as U2AF2, is a human gene.

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: U2AF2 U2 small nuclear RNA auxiliary factor 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11338| accessdate = ]

References

PBB_Further_reading
citations =
*cite journal | author=Zhang M, Zamore PD, Carmo-Fonseca M, "et al." |title=Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary factor small subunit. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 18 |pages= 8769–73 |year= 1992 |pmid= 1388271 |doi=
*cite journal | author=Zamore PD, Patton JG, Green MR |title=Cloning and domain structure of the mammalian splicing factor U2AF. |journal=Nature |volume=355 |issue= 6361 |pages= 609–14 |year= 1992 |pmid= 1538748 |doi= 10.1038/355609a0
*cite journal | author=Zamore PD, Green MR |title=Biochemical characterization of U2 snRNP auxiliary factor: an essential pre-mRNA splicing factor with a novel intranuclear distribution. |journal=EMBO J. |volume=10 |issue= 1 |pages= 207–14 |year= 1991 |pmid= 1824937 |doi=
*cite journal | author=Zuo P, Maniatis T |title=The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing. |journal=Genes Dev. |volume=10 |issue= 11 |pages= 1356–68 |year= 1996 |pmid= 8647433 |doi=
*cite journal | author=Zhang WJ, Wu JY |title=Functional properties of p54, a novel SR protein active in constitutive and alternative splicing. |journal=Mol. Cell. Biol. |volume=16 |issue= 10 |pages= 5400–8 |year= 1996 |pmid= 8816452 |doi=
*cite journal | author=Hong W, Bennett M, Xiao Y, "et al." |title=Association of U2 snRNP with the spliceosomal complex E. |journal=Nucleic Acids Res. |volume=25 |issue= 2 |pages= 354–61 |year= 1997 |pmid= 9016565 |doi=
*cite journal | author=Abovich N, Rosbash M |title=Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. |journal=Cell |volume=89 |issue= 3 |pages= 403–12 |year= 1997 |pmid= 9150140 |doi=
*cite journal | author=Tronchère H, Wang J, Fu XD |title=A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA. |journal=Nature |volume=388 |issue= 6640 |pages= 397–400 |year= 1997 |pmid= 9237760 |doi= 10.1038/41137
*cite journal | author=Fleckner J, Zhang M, Valcárcel J, Green MR |title=U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction. |journal=Genes Dev. |volume=11 |issue= 14 |pages= 1864–72 |year= 1997 |pmid= 9242493 |doi=
*cite journal | author=Zhang WJ, Wu JY |title=Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing. |journal=Mol. Cell. Biol. |volume=18 |issue= 2 |pages= 676–84 |year= 1998 |pmid= 9447963 |doi=
*cite journal | author=Wang HY, Lin W, Dyck JA, "et al." |title=SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells. |journal=J. Cell Biol. |volume=140 |issue= 4 |pages= 737–50 |year= 1998 |pmid= 9472028 |doi=
*cite journal | author=Berglund JA, Abovich N, Rosbash M |title=A cooperative interaction between U2AF65 and mBBP/SF1 facilitates branchpoint region recognition. |journal=Genes Dev. |volume=12 |issue= 6 |pages= 858–67 |year= 1998 |pmid= 9512519 |doi=
*cite journal | author=Rudner DZ, Kanaar R, Breger KS, Rio DC |title=Interaction between subunits of heterodimeric splicing factor U2AF is essential in vivo. |journal=Mol. Cell. Biol. |volume=18 |issue= 4 |pages= 1765–73 |year= 1998 |pmid= 9528748 |doi=
*cite journal | author=Lallena MJ, Martínez C, Valcárcel J, Correas I |title=Functional association of nuclear protein 4.1 with pre-mRNA splicing factors. |journal=J. Cell. Sci. |volume=111 ( Pt 14) |issue= |pages= 1963–71 |year= 1998 |pmid= 9645944 |doi=
*cite journal | author=Gozani O, Potashkin J, Reed R |title=A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site. |journal=Mol. Cell. Biol. |volume=18 |issue= 8 |pages= 4752–60 |year= 1998 |pmid= 9671485 |doi=
*cite journal | author=Neubauer G, King A, Rappsilber J, "et al." |title=Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 46–50 |year= 1998 |pmid= 9731529 |doi= 10.1038/1700
*cite journal | author=Davies RC, Calvio C, Bratt E, "et al." |title=WT1 interacts with the splicing factor U2AF65 in an isoform-dependent manner and can be incorporated into spliceosomes. |journal=Genes Dev. |volume=12 |issue= 20 |pages= 3217–25 |year= 1998 |pmid= 9784496 |doi=
*cite journal | author=Ito T, Muto Y, Green MR, Yokoyama S |title=Solution structures of the first and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary factor (U2AF(65)). |journal=EMBO J. |volume=18 |issue= 16 |pages= 4523–34 |year= 1999 |pmid= 10449418 |doi= 10.1093/emboj/18.16.4523
*cite journal | author=Wang X, Bruderer S, Rafi Z, "et al." |title=Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly. |journal=EMBO J. |volume=18 |issue= 16 |pages= 4549–59 |year= 1999 |pmid= 10449420 |doi= 10.1093/emboj/18.16.4549
*cite journal | author=Ladomery MR, Slight J, Mc Ghee S, Hastie ND |title=Presence of WT1, the Wilm's tumor suppressor gene product, in nuclear poly(A)(+) ribonucleoprotein. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36520–6 |year= 2000 |pmid= 10593950 |doi=

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