SF01_MOUSE
ID SF01_MOUSE Reviewed; 653 AA.
AC Q64213; E9QK02; O08817; P70167; Q61454; Q921Z4;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 6.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Splicing factor 1;
DE AltName: Full=CW17;
DE AltName: Full=Mammalian branch point-binding protein;
DE Short=BBP;
DE Short=mBBP;
DE AltName: Full=Transcription factor ZFM1;
DE Short=mZFM;
DE AltName: Full=Zinc finger gene in MEN1 locus;
DE AltName: Full=Zinc finger protein 162;
GN Name=Sf1; Synonyms=Zfm1, Zfp162;
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 [GENOMIC DNA / MRNA] (ISOFORMS CW17 AND CW17E).
RC STRAIN=C57BL/10; TISSUE=Spleen;
RX PubMed=9212169; DOI=10.1089/dna.1997.16.761;
RA Wrehlke C., Schmitt-Wrede H.-P., Qiao Z.D., Wunderlich F.;
RT "Enhanced expression in spleen macrophages of the mouse homolog to the
RT human putative tumor suppressor gene ZFM1.";
RL DNA Cell Biol. 16:761-767(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57B1/10;
RX PubMed=10360842; DOI=10.1089/104454999315303;
RA Wrehlke C., Wiedemeyer W.-R., Schmitt-Wrede H.-P., Mincheva A., Lichter P.,
RA Wunderlich F.;
RT "Genomic organization of mouse gene zfp162 (mzfm).";
RL DNA Cell Biol. 18:419-428(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS CW17E AND 3).
RC STRAIN=C3H/He; TISSUE=Mammary tumor, and Osteoblast;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82 AND TYR-87, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82 AND TYR-87, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Necessary for the ATP-dependent first step of spliceosome
CC assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3'
CC of the pre-mRNA. May act as transcription repressor (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds U2AF2. Interacts with U1 snRNA. Interacts with RBM17.
CC Binds EWSR1, FUS and TAF15 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=CW17;
CC IsoId=Q64213-1; Sequence=Displayed;
CC Name=CW17E;
CC IsoId=Q64213-2; Sequence=VSP_050424;
CC Name=3;
CC IsoId=Q64213-3; Sequence=VSP_008840;
CC -!- TISSUE SPECIFICITY: Detected at intermediate levels in spleen. Lower
CC levels in heart, kidney, brain, liver, testis, bone marrow, adrenal
CC gland, lymph nodes, pancreas and thymus.
CC -!- PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and
CC spliceosome assembly. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000305}.
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DR EMBL; X80159; CAA56440.1; -; mRNA.
DR EMBL; X85802; CAA59797.1; -; mRNA.
DR EMBL; Y08907; CAA70113.1; -; Genomic_DNA.
DR EMBL; Y12838; CAA73359.1; -; Genomic_DNA.
DR EMBL; AC127556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009091; AAH09091.1; -; mRNA.
DR EMBL; BC055370; AAH55370.1; -; mRNA.
DR CCDS; CCDS50368.1; -. [Q64213-3]
DR CCDS; CCDS50369.1; -. [Q64213-2]
DR AlphaFoldDB; Q64213; -.
DR BMRB; Q64213; -.
DR SMR; Q64213; -.
DR ComplexPortal; CPX-5861; SF1-U2AF65 splicing factor complex.
DR DIP; DIP-60453N; -.
DR ELM; Q64213; -.
DR IntAct; Q64213; 2.
DR STRING; 10090.ENSMUSP00000121309; -.
DR iPTMnet; Q64213; -.
DR PhosphoSitePlus; Q64213; -.
DR SwissPalm; Q64213; -.
DR EPD; Q64213; -.
DR jPOST; Q64213; -.
DR MaxQB; Q64213; -.
DR PaxDb; Q64213; -.
DR PeptideAtlas; Q64213; -.
DR PRIDE; Q64213; -.
DR ProteomicsDB; 261501; -. [Q64213-1]
DR ProteomicsDB; 261502; -. [Q64213-2]
DR ProteomicsDB; 261503; -. [Q64213-3]
DR Antibodypedia; 15586; 428 antibodies from 32 providers.
DR Ensembl; ENSMUST00000131252; ENSMUSP00000121309; ENSMUSG00000024949. [Q64213-3]
DR MGI; MGI:1095403; Sf1.
DR VEuPathDB; HostDB:ENSMUSG00000024949; -.
DR eggNOG; KOG0119; Eukaryota.
DR GeneTree; ENSGT00940000157258; -.
DR InParanoid; Q64213; -.
DR OMA; GAAPWHQ; -.
DR TreeFam; TF319159; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR ChiTaRS; Sf1; mouse.
DR PRO; PR:Q64213; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q64213; protein.
DR Bgee; ENSMUSG00000024949; Expressed in retinal neural layer and 85 other tissues.
DR ExpressionAtlas; Q64213; baseline and differential.
DR Genevisible; Q64213; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR GO; GO:0089701; C:U2AF complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IPI:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0033327; P:Leydig cell differentiation; IGI:MGI.
DR GO; GO:0030238; P:male sex determination; IGI:MGI.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:ComplexPortal.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030575; P:nuclear body organization; IMP:MGI.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IGI:MGI.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR031150; BBP/SF1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032570; SF1-HH.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR PANTHER; PTHR11208:SF45; PTHR11208:SF45; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16275; SF1-HH; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Metal-binding; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Spliceosome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15637"
FT CHAIN 2..653
FT /note="Splicing factor 1"
FT /id="PRO_0000050130"
FT DOMAIN 141..222
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 277..296
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 15..19
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 346..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..518
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15637"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15637"
FT MOD_RES 20
FT /note="Phosphoserine; by PKG"
FT /evidence="ECO:0000250|UniProtKB:Q15637"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 87
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15637"
FT VAR_SEQ 529..653
FT /note="TTTTTTSAGTGSIPPWQQQQAAAAASPGTPQMQGNPTMVPLPPGVQPPLPPG
FT APPPPPCSIECLLCLLSSPNSLCLSPNRAARIPPRGSDGPSHESEDFPRPLVTLPGRQP
FT QQRPWWTGWFGKAA -> SLPAAAMARAMRVRTFRAHW (in isoform CW17E)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9212169"
FT /id="VSP_050424"
FT VAR_SEQ 586..653
FT /note="PCSIECLLCLLSSPNSLCLSPNRAARIPPRGSDGPSHESEDFPRPLVTLPGR
FT QPQQRPWWTGWFGKAA -> PPPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMP
FT PFGMPPAPPPPPPQN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008840"
FT CONFLICT 184
FT /note="K -> E (in Ref. 1; CAA59797 and 2; CAA73359)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="P -> S (in Ref. 4; AAH55370)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="P -> L (in Ref. 4; AAH09091)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="P -> T (in Ref. 2; CAA73359/CAA70113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 653 AA; 70403 MW; 5C159302822509D1 CRC64;
MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED
LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH TLITEMVALN
PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK
GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR
KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP
QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA SNPPPPSLMS
TTQSRPPWMN SGPSENRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP
PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP
PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS
IPPWQQQQAA AAASPGTPQM QGNPTMVPLP PGVQPPLPPG APPPPPCSIE CLLCLLSSPN
SLCLSPNRAA RIPPRGSDGP SHESEDFPRP LVTLPGRQPQ QRPWWTGWFG KAA
