U2AF1_HUMAN
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 03-AUG-2022, entry version 235.
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 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: Interacts (via RS domain) with PHF5A (via N-terminus) (By
CC similarity). Identified in the spliceosome C complex. Heterodimer with
CC U2AF2. Interacts with ZRANB2. {ECO:0000250,
CC ECO:0000269|PubMed:11448987, ECO:0000269|PubMed:11551507,
CC ECO:0000269|PubMed:11991638}.
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}.
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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; 195.
DR BioGRID; 3195698; 44.
DR ComplexPortal; CPX-1921; U2 small nuclear ribonucleoprotein auxiliary factor complex.
DR CORUM; Q01081; -.
DR DIP; DIP-1108N; -.
DR IntAct; Q01081; 77.
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; Q01081; -.
DR PeptideAtlas; Q01081; -.
DR PRIDE; Q01081; -.
DR ProteomicsDB; 57906; -. [Q01081-1]
DR ProteomicsDB; 57907; -. [Q01081-2]
DR ProteomicsDB; 57908; -. [Q01081-3]
DR ProteomicsDB; 57909; -. [Q01081-4]
DR Antibodypedia; 23951; 237 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 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; NDGEDRW; -.
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 11 CRISPR screens.
DR BioGRID-ORCS; 7307; 796 hits in 1080 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 97 other tissues.
DR ExpressionAtlas; Q01081; baseline and differential.
DR Genevisible; Q01081; HS.
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 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; PTHR12620; 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; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
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
