ID   U2AF2_MOUSE             Reviewed;         475 AA.
AC   P26369;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 195.
DE   RecName: Full=Splicing factor U2AF 65 kDa subunit;
DE   AltName: Full=U2 auxiliary factor 65 kDa subunit;
DE   AltName: Full=U2 snRNP auxiliary factor large subunit;
GN   Name=U2af2; Synonyms=U2af65;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SL/AM;
RX   PubMed=1594454; DOI=10.1093/nar/20.9.2374;
RA   Sailer A., Macdonald N.J., Weissmann C.;
RT   "Cloning and sequencing of the murine homologue of the human splicing
RT   factor U2AF65.";
RL   Nucleic Acids Res. 20:2374-2374(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH U2AF1L4.
RX   PubMed=16819553; DOI=10.1038/ni1361;
RA   Heyd F., ten Dam G., Moeroey T.;
RT   "Auxiliary splice factor U2AF26 and transcription factor Gfi1 cooperate
RT   directly in regulating CD45 alternative splicing.";
RL   Nat. Immunol. 7:859-867(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Plays a role in pre-mRNA splicing and 3'-end processing. By
CC       recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to
CC       the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA,
CC       may couple transcription to splicing. Required for the export of mRNA
CC       out of the nucleus, even if the mRNA is encoded by an intron-less gene.
CC       Positively regulates pre-mRNA 3'-end processing by recruiting the CFIm
CC       complex to cleavage and polyadenylation signals.
CC       {ECO:0000250|UniProtKB:P26368}.
CC   -!- SUBUNIT: Interacts with U2AF1L4 (PubMed:16819553). Heterodimer with
CC       U2AF1. Binds unphosphorylated SF1. Interacts with SCAF11 and SNW1.
CC       Interacts with ZRSR2/U2AF1-RS2. Interacts with RBM17. Interacts with
CC       PRPF19; the interaction is direct. Interacts with POLR2A (via the C-
CC       terminal domain); Interacts with PRPF19; the interaction is direct.
CC       Interacts with POLR2A (via the C-terminal domain); recruits PRPF19 and
CC       the Prp19 complex to the pre-mRNA. Interacts with KHDC4 (Isoform 2).
CC       Interacts with ZRSR2. Interacts with the SF3B complex composed of
CC       SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A (By similarity).
CC       Interacts (via N-terminus) with CPSF7 (via C-terminus); this
CC       interaction stimulates pre-mRNA 3'-end processing by promoting the
CC       recruitment of the CFIm complex to cleavage and polyadenylation signals
CC       (By similarity). {ECO:0000250|UniProtKB:P26368,
CC       ECO:0000269|PubMed:16819553}.
CC   -!- INTERACTION:
CC       P26369; Q15637: SF1; Xeno; NbExp=3; IntAct=EBI-8321355, EBI-744603;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA
CC       splicing activity of the protein, leading to regulate some, but not
CC       all, alternative splicing events. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA45875.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X64587; CAA45874.1; -; mRNA.
DR   EMBL; X64587; CAA45875.1; ALT_INIT; mRNA.
DR   EMBL; AK078496; BAC37309.1; -; mRNA.
DR   CCDS; CCDS57476.1; -.
DR   PIR; S22646; S22646.
DR   RefSeq; NP_001192160.1; NM_001205231.1.
DR   PDB; 2M52; NMR; -; A=371-475.
DR   PDB; 3V4M; X-ray; 1.80 A; A/B=372-475.
DR   PDB; 4RU2; X-ray; 2.20 A; B/D/F/H/J/L/N/P/R=85-112.
DR   PDB; 4Z2X; X-ray; 2.15 A; A/B=371-475.
DR   PDB; 5CXT; X-ray; 2.20 A; B/D/F/H/J/L/N/P/R=85-112.
DR   PDBsum; 2M52; -.
DR   PDBsum; 3V4M; -.
DR   PDBsum; 4RU2; -.
DR   PDBsum; 4Z2X; -.
DR   PDBsum; 5CXT; -.
DR   AlphaFoldDB; P26369; -.
DR   BMRB; P26369; -.
DR   SMR; P26369; -.
DR   BioGRID; 204400; 77.
DR   ComplexPortal; CPX-5861; SF1-U2AF65 splicing factor complex.
DR   IntAct; P26369; 2.
DR   STRING; 10090.ENSMUSP00000147013; -.
DR   GlyGen; P26369; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P26369; -.
DR   PhosphoSitePlus; P26369; -.
DR   SwissPalm; P26369; -.
DR   EPD; P26369; -.
DR   jPOST; P26369; -.
DR   MaxQB; P26369; -.
DR   PaxDb; 10090-ENSMUSP00000005041; -.
DR   PeptideAtlas; P26369; -.
DR   ProteomicsDB; 298249; -.
DR   Pumba; P26369; -.
DR   Antibodypedia; 4399; 299 antibodies from 27 providers.
DR   DNASU; 22185; -.
DR   Ensembl; ENSMUST00000209099.2; ENSMUSP00000147013.2; ENSMUSG00000030435.17.
DR   GeneID; 22185; -.
DR   KEGG; mmu:22185; -.
DR   UCSC; uc009ezu.3; mouse.
DR   AGR; MGI:98886; -.
DR   CTD; 11338; -.
DR   MGI; MGI:98886; U2af2.
DR   VEuPathDB; HostDB:ENSMUSG00000030435; -.
DR   eggNOG; KOG0120; Eukaryota.
DR   GeneTree; ENSGT00940000155556; -.
DR   InParanoid; P26369; -.
DR   OMA; MTQWDIK; -.
DR   OrthoDB; 101932at2759; -.
DR   PhylomeDB; P26369; -.
DR   TreeFam; TF314111; -.
DR   Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-MMU-72187; mRNA 3'-end processing.
DR   Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-MMU-9629569; Protein hydroxylation.
DR   BioGRID-ORCS; 22185; 28 hits in 79 CRISPR screens.
DR   ChiTaRS; U2af2; mouse.
DR   PRO; PR:P26369; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P26369; Protein.
DR   Bgee; ENSMUSG00000030435; Expressed in ventricular zone and 265 other cell types or tissues.
DR   ExpressionAtlas; P26369; baseline and differential.
DR   GO; GO:0000243; C:commitment complex; IBA:GO_Central.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000974; C:Prp19 complex; IEA:Ensembl.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR   GO; GO:0071004; C:U2-type prespliceosome; ISO:MGI.
DR   GO; GO:0089701; C:U2AF complex; ISO:MGI.
DR   GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0140678; F:molecular function inhibitor activity; ISO:MGI.
DR   GO; GO:0008187; F:poly-pyrimidine tract binding; IBA:GO_Central.
DR   GO; GO:0030628; F:pre-mRNA 3'-splice site binding; ISO:MGI.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISO:MGI.
DR   GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR   GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IDA:UniProtKB.
DR   CDD; cd12230; RRM1_U2AF65; 1.
DR   CDD; cd12231; RRM2_U2AF65; 1.
DR   CDD; cd12232; RRM3_U2AF65; 1.
DR   Gene3D; 3.30.70.330; -; 3.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR006529; U2AF_lg.
DR   NCBIfam; TIGR01642; U2AF_lg; 1.
DR   PANTHER; PTHR23139; RNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR23139:SF9; SPLICING FACTOR U2AF 65 KDA SUBUNIT; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR   PROSITE; PS50102; RRM; 3.
DR   Genevisible; P26369; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Hydroxylation; Isopeptide bond; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; RNA-binding; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   CHAIN           2..475
FT                   /note="Splicing factor U2AF 65 kDa subunit"
FT                   /id="PRO_0000081989"
FT   DOMAIN          149..231
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          259..337
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          385..466
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..93
FT                   /note="Required for interaction with PRPF19"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   REGION          17..47
FT                   /note="Necessary and sufficient to stimulate pre-mRNAs 3'-
FT                   end cleavage in a CFIm complex-dependent manner"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..46
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   MOD_RES         15
FT                   /note="5-hydroxylysine; by JMJD6; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         70
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         276
FT                   /note="5-hydroxylysine; by JMJD6"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   CROSSLNK        15
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   CROSSLNK        70
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P26368"
FT   STRAND          376..383
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   HELIX           386..388
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   STRAND          389..391
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   HELIX           392..407
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   STRAND          412..416
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   TURN            427..430
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   STRAND          431..438
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   HELIX           439..449
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   STRAND          454..457
FT                   /evidence="ECO:0007829|PDB:2M52"
FT   STRAND          460..464
FT                   /evidence="ECO:0007829|PDB:3V4M"
FT   HELIX           466..470
FT                   /evidence="ECO:0007829|PDB:3V4M"
SQ   SEQUENCE   475 AA;  53517 MW;  2D81375CD8FC7251 CRC64;
     MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR
     RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA
     LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ
     APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE
     NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK
     GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSLPST INQTPVTLQV
     PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP
     VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW
//