ID U2AF1_HUMAN Reviewed; 240 AA. AC Q01081; Q701P4; Q71RF1; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 244. DE RecName: Full=Splicing factor U2AF 35 kDa subunit; DE AltName: Full=U2 auxiliary factor 35 kDa subunit; DE AltName: Full=U2 small nuclear RNA auxiliary factor 1; DE AltName: Full=U2 snRNP auxiliary factor small subunit; GN Name=U2AF1; Synonyms=U2AF35, U2AFBP; ORFNames=FP793; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 68-89 AND RP 126-151. RC TISSUE=Fetal brain; RX PubMed=1388271; DOI=10.1073/pnas.89.18.8769; RA Zhang M., Zamore P.D., Carmo-Fonseca M., Lamond A.I., Green M.R.; RT "Cloning and intracellular localization of the U2 small nuclear RT ribonucleoprotein auxiliary factor small subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8769-8773(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORMS 1; 2 RP AND 3), AND SUBCELLULAR LOCATION. RC TISSUE=Spleen; RX PubMed=15096518; DOI=10.1074/jbc.m402136200; RA Pacheco T.R.D., Gomes N.L., Benes V., Ansorge W., Wollerton M., Smith C.W., RA Valcarcel J., Carmo-Fonseca M.; RT "Diversity of vertebrate splicing factor U2AF35: identification of RT alternatively spliced U2AF1 mRNAs."; RL J. Biol. Chem. 279:27039-27049(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (JUL-2005) to UniProtKB. RN [8] RP FUNCTION. RX PubMed=8647433; DOI=10.1101/gad.10.11.1356; RA Zuo P., Maniatis T.; RT "The splicing factor U2AF35 mediates critical protein-protein interactions RT in constitutive and enhancer-dependent splicing."; RL Genes Dev. 10:1356-1368(1996). RN [9] RP INTERACTION WITH ZRANB2. RX PubMed=11448987; DOI=10.1083/jcb.200010059; RA Adams D.J., van der Weyden L., Mayeda A., Stamm S., Morris B.J., RA Rasko J.E.J.; RT "ZNF265 -- a novel spliceosomal protein able to induce alternative RT splicing."; RL J. Cell Biol. 154:25-32(2001). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL RP C COMPLEX. RX PubMed=11991638; DOI=10.1017/s1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP FUNCTION, INVOLVEMENT IN MDS, VARIANTS MDS PHE-34; TYR-34 AND ARG-157, AND RP CHARACTERIZATION OF VARIANT MDS PHE-34. RX PubMed=22158538; DOI=10.1038/ng.1031; RA Graubert T.A., Shen D., Ding L., Okeyo-Owuor T., Lunn C.L., Shao J., RA Krysiak K., Harris C.C., Koboldt D.C., Larson D.E., McLellan M.D., RA Dooling D.J., Abbott R.M., Fulton R.S., Schmidt H., Kalicki-Veizer J., RA O'Laughlin M., Grillot M., Baty J., Heath S., Frater J.L., Nasim T., RA Link D.C., Tomasson M.H., Westervelt P., DiPersio J.F., Mardis E.R., RA Ley T.J., Wilson R.K., Walter M.J.; RT "Recurrent mutations in the U2AF1 splicing factor in myelodysplastic RT syndromes."; RL Nat. Genet. 44:53-57(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-39 AND ARG-165, METHYLATION RP [LARGE SCALE ANALYSIS] AT LYS-39 (ISOFORMS 2 AND 3), AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [19] RP FUNCTION, INVOLVEMENT IN MDS, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF RP VARIANTS MDS PHE-34; TYR-34 AND ARG-157. RX PubMed=25311244; DOI=10.1038/leu.2014.303; RA Okeyo-Owuor T., White B.S., Chatrikhi R., Mohan D.R., Kim S., Griffith M., RA Ding L., Ketkar-Kulkarni S., Hundal J., Laird K.M., Kielkopf C.L., RA Ley T.J., Walter M.J., Graubert T.A.; RT "U2AF1 mutations alter sequence specificity of pre-mRNA binding and RT splicing."; RL Leukemia 29:909-917(2015). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [21] RP INTERACTION WITH SDE2 AND SF3B1. RX PubMed=34365507; DOI=10.1093/nar/gkab647; RA Floro J., Dai A., Metzger A., Mora-Martin A., Ganem N.J., Cifuentes D., RA Wu C.S., Dalal J., Lyons S.M., Labadorf A., Flynn R.L.; RT "SDE2 is an essential gene required for ribosome biogenesis and the RT regulation of alternative splicing."; RL Nucleic Acids Res. 49:9424-9443(2021). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 43-146 IN COMPLEX WITH U2AF2, AND RP MUTAGENESIS OF TRP-134. RX PubMed=11551507; DOI=10.1016/s0092-8674(01)00480-9; RA Kielkopf C.L., Rodionova N.A., Green M.R., Burley S.K.; RT "A novel peptide recognition mode revealed by the X-ray structure of a core RT U2AF35/U2AF65 heterodimer."; RL Cell 106:595-605(2001). CC -!- FUNCTION: Plays a critical role in both constitutive and enhancer- CC dependent splicing by mediating protein-protein interactions and CC protein-RNA interactions required for accurate 3'-splice site CC selection. Recruits U2 snRNP to the branch point. Directly mediates CC interactions between U2AF2 and proteins bound to the enhancers and thus CC may function as a bridge between U2AF2 and the enhancer complex to CC recruit it to the adjacent intron. {ECO:0000269|PubMed:22158538, CC ECO:0000269|PubMed:25311244, ECO:0000269|PubMed:8647433}. CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638). CC Heterodimer with U2AF2 (PubMed:11551507). Interacts (via RS domain) CC with PHF5A (via N-terminus) (By similarity). Interacts with ZRANB2 CC (PubMed:11448987). Interacts with SDE2 (PubMed:34365507). Interacts CC with SF3B1 (PubMed:34365507). {ECO:0000250, CC ECO:0000269|PubMed:11448987, ECO:0000269|PubMed:11551507, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:34365507}. CC -!- INTERACTION: CC Q01081; Q10567-3: AP1B1; NbExp=3; IntAct=EBI-632461, EBI-11978055; CC Q01081; P63010: AP2B1; NbExp=3; IntAct=EBI-632461, EBI-432924; CC Q01081; P63010-2: AP2B1; NbExp=3; IntAct=EBI-632461, EBI-11529439; CC Q01081; P54253: ATXN1; NbExp=4; IntAct=EBI-632461, EBI-930964; CC Q01081; Q8N4J0: CARNMT1; NbExp=6; IntAct=EBI-632461, EBI-11963218; CC Q01081; Q86X95: CIR1; NbExp=4; IntAct=EBI-632461, EBI-627102; CC Q01081; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-632461, EBI-2349927; CC Q01081; P61978: HNRNPK; NbExp=4; IntAct=EBI-632461, EBI-304185; CC Q01081; P42858: HTT; NbExp=3; IntAct=EBI-632461, EBI-466029; CC Q01081; Q6NYC1: JMJD6; NbExp=2; IntAct=EBI-632461, EBI-8464037; CC Q01081; P04264: KRT1; NbExp=3; IntAct=EBI-632461, EBI-298429; CC Q01081; O95678: KRT75; NbExp=3; IntAct=EBI-632461, EBI-2949715; CC Q01081; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-632461, EBI-16439278; CC Q01081; P40692: MLH1; NbExp=3; IntAct=EBI-632461, EBI-744248; CC Q01081; Q8N5F7: NKAP; NbExp=2; IntAct=EBI-632461, EBI-721539; CC Q01081; P82979: SARNP; NbExp=3; IntAct=EBI-632461, EBI-347495; CC Q01081; Q13435: SF3B2; NbExp=2; IntAct=EBI-632461, EBI-749111; CC Q01081; Q16560-2: SNRNP35; NbExp=3; IntAct=EBI-632461, EBI-12938570; CC Q01081; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-632461, EBI-539478; CC Q01081; P78362: SRPK2; NbExp=7; IntAct=EBI-632461, EBI-593303; CC Q01081; A7MD48: SRRM4; NbExp=3; IntAct=EBI-632461, EBI-3867173; CC Q01081; Q07955: SRSF1; NbExp=4; IntAct=EBI-632461, EBI-398920; CC Q01081; Q01130: SRSF2; NbExp=3; IntAct=EBI-632461, EBI-627047; CC Q01081; P84103: SRSF3; NbExp=4; IntAct=EBI-632461, EBI-372557; CC Q01081; O43463: SUV39H1; NbExp=2; IntAct=EBI-632461, EBI-349968; CC Q01081; P62995: TRA2B; NbExp=3; IntAct=EBI-632461, EBI-725485; CC Q01081; P26368: U2AF2; NbExp=11; IntAct=EBI-632461, EBI-742339; CC Q01081; P26368-2: U2AF2; NbExp=8; IntAct=EBI-632461, EBI-11097439; CC Q01081; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-632461, EBI-740727; CC Q01081-2; P49760: CLK2; NbExp=3; IntAct=EBI-10176676, EBI-750020; CC Q01081-2; D3DU92: RNPS1; NbExp=3; IntAct=EBI-10176676, EBI-10176640; CC Q01081-2; P78362: SRPK2; NbExp=3; IntAct=EBI-10176676, EBI-593303; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15096518}. Nucleus CC speckle {ECO:0000269|PubMed:15096518, ECO:0000269|PubMed:25311244}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=U2AF35a; CC IsoId=Q01081-1; Sequence=Displayed; CC Name=2; Synonyms=U2AF35b; CC IsoId=Q01081-2; Sequence=VSP_042665; CC Name=3; Synonyms=U2AF35c; CC IsoId=Q01081-3; Sequence=VSP_042665, VSP_042666, VSP_042667; CC Name=4; CC IsoId=Q01081-4; Sequence=VSP_042664; CC -!- DOMAIN: The C-terminal SR-rich domain is required for interactions with CC SR proteins and the splicing regulators TRA and TRA2, and the N- CC terminal domain is required for formation of the U2AF1/U2AF2 CC heterodimer. CC -!- DISEASE: Myelodysplastic syndrome (MDS) [MIM:614286]: A heterogeneous CC group of closely related clonal hematopoietic disorders. All are CC characterized by a hypercellular or hypocellular bone marrow with CC impaired morphology and maturation, dysplasia of the myeloid, CC megakaryocytic and/or erythroid lineages, and peripheral blood CC cytopenias resulting from ineffective blood cell production. Included CC diseases are: refractory anemia (RA), refractory anemia with ringed CC sideroblasts (RARS), refractory anemia with excess blasts (RAEB), CC refractory cytopenia with multilineage dysplasia and ringed CC sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a CC myelodysplastic/myeloproliferative disease. MDS is considered a CC premalignant condition in a subgroup of patients that often progresses CC to acute myeloid leukemia (AML). {ECO:0000269|PubMed:22158538, CC ECO:0000269|PubMed:25311244}. Note=The gene represented in this entry CC may be involved in disease pathogenesis. Mutation altering U2AF1 CC function in the context of specific RNA sequences can lead to aberrant CC alternative splicing of target genes, some of which may be relevant for CC MDS pathogenesis. {ECO:0000269|PubMed:25311244}. CC -!- MISCELLANEOUS: [Isoform 2]: Interacts with U2AF2 and stimulates U2AF CC splicing activity in vitro. Less efficient than isoform 1. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M96982; AAA36619.1; -; mRNA. DR EMBL; AJ627978; CAF29556.1; -; mRNA. DR EMBL; AF370386; AAQ15222.1; -; mRNA. DR EMBL; AP001631; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001748; BAA95534.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09501.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09502.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09504.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09505.1; -; Genomic_DNA. DR EMBL; BC001177; AAH01177.1; -; mRNA. DR EMBL; BC001923; AAH01923.1; -; mRNA. DR CCDS; CCDS13694.1; -. [Q01081-1] DR CCDS; CCDS33574.1; -. [Q01081-2] DR CCDS; CCDS42948.1; -. [Q01081-4] DR PIR; A46179; A46179. DR RefSeq; NP_001020374.1; NM_001025203.1. [Q01081-2] DR RefSeq; NP_001020375.1; NM_001025204.1. [Q01081-4] DR RefSeq; NP_001307575.1; NM_001320646.1. [Q01081-1] DR RefSeq; NP_001307577.1; NM_001320648.1. [Q01081-2] DR RefSeq; NP_001307580.1; NM_001320651.1. [Q01081-4] DR RefSeq; NP_006749.1; NM_006758.2. [Q01081-1] DR PDB; 1JMT; X-ray; 2.20 A; A=43-146. DR PDBsum; 1JMT; -. DR AlphaFoldDB; Q01081; -. DR SMR; Q01081; -. DR BioGRID; 113157; 221. DR BioGRID; 3195698; 49. DR ComplexPortal; CPX-1921; U2 small nuclear ribonucleoprotein auxiliary factor complex. DR CORUM; Q01081; -. DR DIP; DIP-1108N; -. DR IntAct; Q01081; 80. DR MINT; Q01081; -. DR STRING; 9606.ENSP00000291552; -. DR GlyGen; Q01081; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q01081; -. DR PhosphoSitePlus; Q01081; -. DR SwissPalm; Q01081; -. DR BioMuta; U2AF1; -. DR DMDM; 267187; -. DR EPD; Q01081; -. DR jPOST; Q01081; -. DR MassIVE; Q01081; -. DR MaxQB; Q01081; -. DR PaxDb; 9606-ENSP00000291552; -. DR PeptideAtlas; Q01081; -. DR ProteomicsDB; 57906; -. [Q01081-1] DR ProteomicsDB; 57907; -. [Q01081-2] DR ProteomicsDB; 57908; -. [Q01081-3] DR ProteomicsDB; 57909; -. [Q01081-4] DR Pumba; Q01081; -. DR Antibodypedia; 23951; 260 antibodies from 32 providers. DR DNASU; 7307; -. DR Ensembl; ENST00000291552.9; ENSP00000291552.4; ENSG00000160201.12. [Q01081-1] DR Ensembl; ENST00000380276.6; ENSP00000369629.2; ENSG00000160201.12. [Q01081-2] DR Ensembl; ENST00000459639.5; ENSP00000418705.1; ENSG00000160201.12. [Q01081-4] DR Ensembl; ENST00000464750.5; ENSP00000420672.1; ENSG00000160201.12. [Q01081-3] DR GeneID; 102724594; -. DR GeneID; 7307; -. DR KEGG; hsa:102724594; -. DR KEGG; hsa:7307; -. DR MANE-Select; ENST00000291552.9; ENSP00000291552.4; NM_006758.3; NP_006749.1. DR UCSC; uc002zcy.1; human. [Q01081-1] DR AGR; HGNC:12453; -. DR CTD; 7307; -. DR DisGeNET; 102724594; -. DR DisGeNET; 7307; -. DR GeneCards; U2AF1; -. DR HGNC; HGNC:12453; U2AF1. DR HPA; ENSG00000160201; Low tissue specificity. DR MalaCards; U2AF1; -. DR MIM; 191317; gene. DR MIM; 614286; phenotype. DR neXtProt; NX_Q01081; -. DR OpenTargets; ENSG00000160201; -. DR PharmGKB; PA37103; -. DR VEuPathDB; HostDB:ENSG00000160201; -. DR eggNOG; KOG2202; Eukaryota. DR GeneTree; ENSGT00950000183152; -. DR HOGENOM; CLU_059852_4_0_1; -. DR InParanoid; Q01081; -. DR OMA; CSRTHIM; -. DR OrthoDB; 1967949at2759; -. DR PhylomeDB; Q01081; -. DR TreeFam; TF300143; -. DR PathwayCommons; Q01081; -. DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72187; mRNA 3'-end processing. DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination. DR SignaLink; Q01081; -. DR SIGNOR; Q01081; -. DR BioGRID-ORCS; 102724594; 0 hits in 13 CRISPR screens. DR BioGRID-ORCS; 7307; 830 hits in 1158 CRISPR screens. DR ChiTaRS; U2AF1; human. DR EvolutionaryTrace; Q01081; -. DR GeneWiki; U2_small_nuclear_RNA_auxiliary_factor_1; -. DR Pharos; Q01081; Tbio. DR PRO; PR:Q01081; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; Q01081; Protein. DR Bgee; ENSG00000160201; Expressed in adenohypophysis and 99 other cell types or tissues. DR ExpressionAtlas; Q01081; baseline and differential. DR GO; GO:0015030; C:Cajal body; TAS:ProtInc. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL. DR GO; GO:0089701; C:U2AF complex; IDA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0050733; F:RS domain binding; IEA:Ensembl. DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. DR CDD; cd12538; RRM_U2AF35; 1. DR DisProt; DP01456; -. DR Gene3D; 3.30.70.330; -; 1. DR IDEAL; IID00205; -. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR InterPro; IPR003954; RRM_dom_euk. DR InterPro; IPR009145; U2AF_small. DR InterPro; IPR000571; Znf_CCCH. DR PANTHER; PTHR12620:SF11; SPLICING FACTOR U2AF 35 KDA SUBUNIT; 1. DR PANTHER; PTHR12620; U2 SNRNP AUXILIARY FACTOR, SMALL SUBUNIT; 1. DR Pfam; PF00076; RRM_1; 1. DR Pfam; PF00642; zf-CCCH; 2. DR PRINTS; PR01848; U2AUXFACTOR. DR SMART; SM00360; RRM; 1. DR SMART; SM00361; RRM_1; 1. DR SMART; SM00356; ZnF_C3H1; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50102; RRM; 1. DR PROSITE; PS50103; ZF_C3H1; 2. DR Genevisible; Q01081; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Disease variant; Metal-binding; Methylation; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW RNA-binding; Spliceosome; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7" FT CHAIN 2..240 FT /note="Splicing factor U2AF 35 kDa subunit" FT /id="PRO_0000081994" FT DOMAIN 65..147 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT ZN_FING 12..40 FT /note="C3H1-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT ZN_FING 149..176 FT /note="C3H1-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT REGION 183..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 185..205 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..240 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 39 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 145 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 165 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 1..73 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15498874" FT /id="VSP_042664" FT VAR_SEQ 47..66 FT /note="ALLNIYRNPQNSSQSADGLR -> LIQNIYRNPQNSAQTADGSH (in FT isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15096518" FT /id="VSP_042665" FT VAR_SEQ 67..75 FT /note="CAVSDVEMQ -> YHCPLEHLP (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_042666" FT VAR_SEQ 76..240 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_042667" FT VARIANT 34 FT /note="S -> F (in MDS; somatic mutation; affects FT alternative splicing of target sequences resulting in FT increased splicing efficiency, exon skipping and FT alternative splice site utilization; no effect on FT localization to nuclear speckles; dbSNP:rs371769427)" FT /evidence="ECO:0000269|PubMed:22158538, FT ECO:0000269|PubMed:25311244" FT /id="VAR_079637" FT VARIANT 34 FT /note="S -> Y (in MDS; somatic mutation; affects FT alternative splicing of target sequences; FT dbSNP:rs371769427)" FT /evidence="ECO:0000269|PubMed:22158538, FT ECO:0000269|PubMed:25311244" FT /id="VAR_079638" FT VARIANT 157 FT /note="Q -> R (in MDS; somatic mutation; affects FT alternative splicing of target sequences; FT dbSNP:rs371246226)" FT /evidence="ECO:0000269|PubMed:22158538, FT ECO:0000269|PubMed:25311244" FT /id="VAR_079639" FT MUTAGEN 134 FT /note="W->A: Decreases affinity for UAF2 by 3 orders of FT magnitude." FT /evidence="ECO:0000269|PubMed:11551507" FT STRAND 45..53 FT /evidence="ECO:0007829|PDB:1JMT" FT HELIX 64..92 FT /evidence="ECO:0007829|PDB:1JMT" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:1JMT" FT STRAND 104..118 FT /evidence="ECO:0007829|PDB:1JMT" FT HELIX 120..130 FT /evidence="ECO:0007829|PDB:1JMT" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:1JMT" FT MOD_RES Q01081-2:39 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES Q01081-3:39 FT /note="N6-methyllysine" FT /evidence="ECO:0007744|PubMed:24129315" SQ SEQUENCE 240 AA; 27872 MW; 3DA130DCE0B953F6 CRC64; MAEYLASIFG TEKDKVNCSF YFKIGACRHG DRCSRLHNKP TFSQTIALLN IYRNPQNSSQ SADGLRCAVS DVEMQEHYDE FFEEVFTEME EKYGEVEEMN VCDNLGDHLV GNVYVKFRRE EDAEKAVIDL NNRWFNGQPI HAELSPVTDF REACCRQYEM GECTRGGFCN FMHLKPISRE LRRELYGRRR KKHRSRSRSR ERRSRSRDRG RGGGGGGGGG GGGRERDRRR SRDRERSGRF //