U2AF2_MOUSE
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 03-AUG-2022, entry version 187.
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, Pancreas,
RC 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.ENSMUSP00000005041; -.
DR iPTMnet; P26369; -.
DR PhosphoSitePlus; P26369; -.
DR SwissPalm; P26369; -.
DR EPD; P26369; -.
DR jPOST; P26369; -.
DR MaxQB; P26369; -.
DR PaxDb; P26369; -.
DR PeptideAtlas; P26369; -.
DR PRIDE; P26369; -.
DR ProteomicsDB; 298249; -.
DR Antibodypedia; 4399; 277 antibodies from 27 providers.
DR DNASU; 22185; -.
DR Ensembl; ENSMUST00000209099; ENSMUSP00000147013; ENSMUSG00000030435.
DR GeneID; 22185; -.
DR KEGG; mmu:22185; -.
DR UCSC; uc009ezu.3; mouse.
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; 896650at2759; -.
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 BioGRID-ORCS; 22185; 25 hits in 74 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 262 other tissues.
DR ExpressionAtlas; P26369; baseline and differential.
DR Genevisible; P26369; MM.
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; ISO:MGI.
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: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 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 Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01642; U2AF_lg; 1.
DR PROSITE; PS50102; RRM; 3.
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
