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