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SFR19_MOUSE
ID   SFR19_MOUSE             Reviewed;        1256 AA.
AC   Q5U4C3; Q3UR01;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Splicing factor, arginine/serine-rich 19;
DE   AltName: Full=SR-related and CTD-associated factor 1;
GN   Name=Scaf1; Synonyms=Sfrs19;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Embryonic brain, and Liver;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691; SER-695; SER-912 AND
RP   THR-936, AND 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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-510; SER-518;
RP   SER-577; SER-579; SER-676; SER-682; SER-691; SER-695; SER-910; SER-912;
RP   THR-936 AND SER-939, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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: May function in pre-mRNA splicing. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with POLR2A. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5U4C3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5U4C3-2; Sequence=VSP_027636, VSP_027637;
CC   -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR   EMBL; AK141920; BAE24887.1; -; mRNA.
DR   EMBL; BC042576; AAH42576.1; -; mRNA.
DR   EMBL; BC043138; AAH43138.1; -; mRNA.
DR   EMBL; BC085153; AAH85153.1; -; mRNA.
DR   CCDS; CCDS21225.1; -. [Q5U4C3-1]
DR   RefSeq; NP_001008422.1; NM_001008422.1. [Q5U4C3-1]
DR   RefSeq; XP_006540884.1; XM_006540821.3. [Q5U4C3-1]
DR   RefSeq; XP_011249157.1; XM_011250855.2. [Q5U4C3-1]
DR   AlphaFoldDB; Q5U4C3; -.
DR   SMR; Q5U4C3; -.
DR   BioGRID; 231387; 2.
DR   IntAct; Q5U4C3; 2.
DR   MINT; Q5U4C3; -.
DR   STRING; 10090.ENSMUSP00000082501; -.
DR   iPTMnet; Q5U4C3; -.
DR   PhosphoSitePlus; Q5U4C3; -.
DR   EPD; Q5U4C3; -.
DR   jPOST; Q5U4C3; -.
DR   MaxQB; Q5U4C3; -.
DR   PaxDb; Q5U4C3; -.
DR   PeptideAtlas; Q5U4C3; -.
DR   PRIDE; Q5U4C3; -.
DR   ProteomicsDB; 255394; -. [Q5U4C3-1]
DR   ProteomicsDB; 255395; -. [Q5U4C3-2]
DR   Antibodypedia; 32077; 82 antibodies from 18 providers.
DR   DNASU; 233208; -.
DR   Ensembl; ENSMUST00000085383; ENSMUSP00000082501; ENSMUSG00000038406. [Q5U4C3-1]
DR   Ensembl; ENSMUST00000211735; ENSMUSP00000148251; ENSMUSG00000038406. [Q5U4C3-1]
DR   GeneID; 233208; -.
DR   KEGG; mmu:233208; -.
DR   UCSC; uc009gso.1; mouse. [Q5U4C3-1]
DR   UCSC; uc009gsq.1; mouse. [Q5U4C3-2]
DR   CTD; 58506; -.
DR   MGI; MGI:2141980; Scaf1.
DR   VEuPathDB; HostDB:ENSMUSG00000038406; -.
DR   eggNOG; KOG0825; Eukaryota.
DR   GeneTree; ENSGT00950000183205; -.
DR   HOGENOM; CLU_006936_0_0_1; -.
DR   InParanoid; Q5U4C3; -.
DR   OMA; PDERAPT; -.
DR   OrthoDB; 332377at2759; -.
DR   PhylomeDB; Q5U4C3; -.
DR   TreeFam; TF332183; -.
DR   BioGRID-ORCS; 233208; 5 hits in 73 CRISPR screens.
DR   ChiTaRS; Scaf1; mouse.
DR   PRO; PR:Q5U4C3; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q5U4C3; protein.
DR   Bgee; ENSMUSG00000038406; Expressed in embryonic brain and 208 other tissues.
DR   ExpressionAtlas; Q5U4C3; baseline and differential.
DR   Genevisible; Q5U4C3; MM.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISO:MGI.
DR   GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
DR   InterPro; IPR042841; SCAF1.
DR   PANTHER; PTHR47013; PTHR47013; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Isopeptide bond; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN           1..1256
FT                   /note="Splicing factor, arginine/serine-rich 19"
FT                   /id="PRO_0000299407"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..1030
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1112..1152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1131..1256
FT                   /note="Necessary for interaction with the CTD domain of
FT                   POLR2A"
FT                   /evidence="ECO:0000250"
FT   REGION          1221..1256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..282
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..578
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..613
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..746
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..832
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..873
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..908
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..937
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..985
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1008
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1138..1152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1231..1256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         328
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         442
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         518
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         520
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         579
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         663
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         676
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         682
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         689
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         691
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         695
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         819
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         876
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         883
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         910
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         912
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         923
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   MOD_RES         936
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         939
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         948
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   CROSSLNK        812
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7N4"
FT   VAR_SEQ         161..166
FT                   /note="VSPQSH -> GSCPVA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027636"
FT   VAR_SEQ         167..1256
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027637"
SQ   SEQUENCE   1256 AA;  133842 MW;  E3D3BFCF441FE554 CRC64;
     MEEEDESRGK TEESGEDRGD GPPDRDPALS PSAFILRAIQ QAVGSSLQGD LPNDKDGARC
     RGLRWRRCCR SPRSEPRSQE SGAADTATVL DTAADSFLVE LVSILDPPDT WVPSRLDLQP
     GESEDMLELV AEVRIGDRDP MPLPVPSLFP RLRAWRTGKT VSPQSHASRP ACSRHLTLGT
     GDGGPAPPPA PSSASSSPSP SPSSSSPSPP PPPPPPPPPA LPAPRFDIYD PFHPTDEAYS
     PPPAPEQKYD PFEPTGSNPS SSAGTPSPEE EEEEEEEEEE EGLSQSISRI SETLAGIYDD
     NSLSQDFPGD DSPRREPPPP QTLGAPGTPP QADSTRAEGA PRRRVFVLGP EAEACHEGKV
     SVEVVTAGAP ALSLPPLPPT DPEIEEGEIV QPEEEPRVAV SLFRAARPRQ PPASVATLAS
     VAAPAAPPAS APRAPEGDDF LSLHADSDGE GALQVDLGEP PAPPAADARW GGLDLRRKIL
     TQRRERYRQR SASPGPPPAR KKARRERQRS GDPAPPDSPS WEAKKHRSRE RKLGSHSTAR
     RRSRSRSRRR SRSRSADRRR GGHRSRSREK RRRRRRSASP PPAASSSSSS RRERHRGKRR
     EGGKKKKKRS RSRAEKRSGD LEKLPASVPP SGSDRDSRRR GAVPPSIQDL TDHDLFAIKR
     TITVGRPDKA EPRAPSPAPA VSPKREVLYD SEGLSADERG GKSDKDRRRS GAASSSSSSR
     EKGSRRKALD GDRGRDRDRS SKKTRPPKDS TPGSGPLPKA PPSSGSSSSS SSCSSRKVKL
     QSKVAVLIRE GVSSTTPAKD SSSSGLGSIG VKFSRDRESR SPFLKPDERA PAEVAKVAPG
     SNKPKKTKAK AKAGAKKAKG TKGKTKPSKT RKKVRSGGSS TASGGPGSLK KSKADSCSQA
     ASAKGTEETS WSGEERTTKA PSTPPPKVAP PPPALTPDSQ TVDSSCKTPE VSFLPEEASE
     DTGVRVGAEE EEEEEEEEEE EEEQQPATTT ATSTAAAAPS TAPSAGSTAG DSGAEDGPAA
     RISQLPTLPP PMPWNLPAGV DCTTSGVLAL TALLFKMEEA NLASRAKAQE LIQATNQILS
     HRKPSSTLGV TPAPVPTSLG LPPGPSSYLL PGSLPIGGCG STPPTPTGLA PASDKREGSS
     SSEGRGDTDK YLKKLHTQER AVEEVKLAIK PYYQKKDITK EEYKDILRKA VHKICHSKSG
     EINPVKVSNL VRAYVQRYRY FRKHGRKPGD PPGPPRPPKE PGPPDKGGPG LPLPPL
 
 
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