ID SFR19_RAT Reviewed; 1258 AA. AC Q63624; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 27-MAR-2024, entry version 117. DE RecName: Full=Splicing factor, arginine/serine-rich 19; DE AltName: Full=CTD-binding SR-like protein rA1; DE AltName: Full=SR-related and CTD-associated factor 1; GN Name=Scaf1; Synonyms=Sfrs19; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-1258, FUNCTION, AND INTERACTION WITH RP POLR2A. RC TISSUE=Hippocampus; RX PubMed=8692929; DOI=10.1073/pnas.93.14.6975; RA Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M., RA Corden J.L.; RT "The C-terminal domain of the largest subunit of RNA polymerase II RT interacts with a novel set of serine/arginine-rich proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241; SER-512; SER-520; RP SER-678; SER-684; SER-693; SER-697; SER-914 AND THR-950, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: May function in pre-mRNA splicing. CC {ECO:0000269|PubMed:8692929}. CC -!- SUBUNIT: Interacts with POLR2A. {ECO:0000269|PubMed:8692929}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC52657.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AABR03002356; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U49056; AAC52657.1; ALT_INIT; mRNA. DR PIR; T31421; T31421. DR RefSeq; NP_062257.1; NM_019384.1. DR RefSeq; XP_008757631.2; XM_008759409.2. DR RefSeq; XP_008757632.1; XM_008759410.2. DR RefSeq; XP_017445105.1; XM_017589616.1. DR AlphaFoldDB; Q63624; -. DR SMR; Q63624; -. DR STRING; 10116.ENSRNOP00000072566; -. DR iPTMnet; Q63624; -. DR PhosphoSitePlus; Q63624; -. DR PaxDb; 10116-ENSRNOP00000027801; -. DR Ensembl; ENSRNOT00000081430.2; ENSRNOP00000072566.1; ENSRNOG00000056946.2. DR Ensembl; ENSRNOT00055009085; ENSRNOP00055006928; ENSRNOG00055005646. DR Ensembl; ENSRNOT00060013253; ENSRNOP00060010065; ENSRNOG00060008031. DR Ensembl; ENSRNOT00065049375; ENSRNOP00065040506; ENSRNOG00065028633. DR GeneID; 56081; -. DR KEGG; rno:56081; -. DR AGR; RGD:708405; -. DR CTD; 58506; -. DR RGD; 708405; Scaf1. DR eggNOG; KOG0825; Eukaryota. DR GeneTree; ENSGT00950000183205; -. DR HOGENOM; CLU_006936_0_0_1; -. DR InParanoid; Q63624; -. DR OMA; ADTRWGG; -. DR OrthoDB; 5407065at2759; -. DR PhylomeDB; Q63624; -. DR TreeFam; TF332183; -. DR PRO; PR:Q63624; -. DR Proteomes; UP000002494; Chromosome 1. DR Bgee; ENSRNOG00000056946; Expressed in frontal cortex and 19 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; ISO:RGD. DR GO; GO:0006397; P:mRNA processing; IMP:RGD. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:RGD. DR InterPro; IPR042841; SCAF1. DR PANTHER; PTHR47013; SPLICING FACTOR, ARGININE/SERINE-RICH 19; 1. DR PANTHER; PTHR47013:SF1; SPLICING FACTOR, ARGININE_SERINE-RICH 19; 1. DR Genevisible; Q63624; RN. PE 1: Evidence at protein level; KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Ubl conjugation. FT CHAIN 1..1258 FT /note="Splicing factor, arginine/serine-rich 19" FT /id="PRO_0000299408" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 159..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 370..398 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 410..1034 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1114..1154 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1133..1258 FT /note="Necessary for interaction with the CTD domain of FT POLR2A" FT /evidence="ECO:0000250" FT REGION 1223..1258 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 185..226 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 268..283 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 287..309 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 473..492 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 531..580 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 594..615 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 692..713 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 722..748 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 762..781 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 796..811 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 815..834 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 845..875 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 876..910 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 925..939 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 968..987 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 988..1010 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1140..1154 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1233..1258 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 329 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 444 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 449 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 495 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 512 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 520 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 579 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 665 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 678 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 684 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 691 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 693 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 697 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 821 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 823 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 878 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 885 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 912 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5U4C3" FT MOD_RES 914 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 925 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 938 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT MOD_RES 941 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5U4C3" FT MOD_RES 950 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:22673903" FT CROSSLNK 814 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H7N4" FT CONFLICT 101 FT /note="L -> V (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 195 FT /note="A -> G (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="P -> A (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 264 FT /note="A -> G (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 289 FT /note="S -> R (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 687 FT /note="R -> G (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 746..748 FT /note="TRP -> PRT (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 765 FT /note="S -> R (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 832 FT /note="A -> S (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 952 FT /note="E -> D (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 957 FT /note="P -> A (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 1076 FT /note="A -> D (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 1082 FT /note="S -> R (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 1101 FT /note="L -> F (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 1106 FT /note="G -> A (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" FT CONFLICT 1170 FT /note="A -> S (in Ref. 2; AAC52657)" FT /evidence="ECO:0000305" SQ SEQUENCE 1258 AA; 133856 MW; BBEC7D4027E2F179 CRC64; MEEEDESRGK TEESGEDRGD GPPDRDPALS PSAFILRAIQ QAVGSSLQGD LPNDKDGSRC CGLQWRRCCR SPRSEPRSQE SGGADMATVL DTAADSFLVE LVSILDPPDT WVPSHLDLQP GESEDVLELV AEVRIGDRDP MPLPVPSLLP RLRAWRTGKT VSPQSHASRP ACSRHLLTLG TGDGGPAPPP APSSASSSPS PSPSSSSPSP PPPPPPPPPP ALPAPRFDIY DPFHPTDEAY SPPPAPEQKY DPFEPTGSNP SSSAGTPSPE EEEEEEEEEE EEGLSQSISR ISETLAGIYD DNSLSQDFPG DDSPHREPPP PQTLGAPGTP PQADSTRAEG APRRRVFVVG PEAEACLEGK VSVEVVTTAG GPALPLPPLP PTDPEIEEGE IVQPEEEPRV AVSLFRAARP RQPPASVATL ASVAAPAAPP ASAPRAPEGD DFLSLHADSD GEGALQVDLG EPPAPPAADA RWGGLDLRRK ILTQRRERYR QRSASPGPPP ARKKARRERQ RSGDPAPPDS PTWEAKKHRS RERKLGSHST ARRRSRSRSR RRSRSRSADR RRGSHRSRSR EKRRRRRRSA SPPPAASSSS SSRRERHRGK RREGGKKKKK RSRSRAEKRS GDLEKLPAPV PPSGSDRDSR RRGAVPPSIQ DLTDHDLFAI KRTITVGRPD KTEPRAPSPA PAVSPKREVL YDSEGLSADE RGAKGDKDRR RSGAASSSSS SREKASRRKA LDGDRGRDRD RSSKKTRPPK DSAPGSGALP KAPPSSGSSS SSSSCSSRKV KLQSKVAVLI REGVSSTTPA KDSSSSGLGS IGVKFSRDRE SRSPFLKPDE RAPAEGVKVA PGSTKPKKTK AKAKAGAKKA KGTKGKTKPS KTRKKVRSGG SSTASGGPGS LKKSKADSCS QAASAKGTEE TSWSGEERTT KAPSTPPPKV APPPPALTPD SQTVDSSCKT PEVSFLPEEA SEDTGVRVGA EEEEEEEEEE EEEEEQQPAT TTATSTAAAA PSTAPSAGST AGDSGAEDGP AARASQLPTL PPPMPWNLPA GVDCTTSGVL ALTALLFKME EANLASRAKA QELIQATNQI LSHRKPPSTL GVTPAPVPTS LGLPPGPSSY LLPGSLPIGG CGSTPPTPTG LVPASDKREG SSSSEGRGDT DKYLKKLHTQ ERAVEEVKLA IKPYYQKKDI TKEEYKDILR KAVHKICHSK SGEINPVKVS NLVRAYVQRY RYFRKHGRKP GDPPGPPRPP KEPGPPDKGG PGLPLPPL //