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Q63624

- SFR19_RAT

UniProt

Q63624 - SFR19_RAT

Protein

Splicing factor, arginine/serine-rich 19

Gene

Scaf1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    May function in pre-mRNA splicing.1 Publication

    GO - Molecular functioni

    1. protein domain specific binding Source: RGD
    2. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA processing Source: RGD
    2. RNA splicing Source: UniProtKB-KW
    3. transcription from RNA polymerase II promoter Source: RGD

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Splicing factor, arginine/serine-rich 19
    Alternative name(s):
    CTD-binding SR-like protein rA1
    SR-related and CTD-associated factor 1
    Gene namesi
    Name:Scaf1
    Synonyms:Sfrs19
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi708405. Scaf1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12581258Splicing factor, arginine/serine-rich 19PRO_0000299408Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei241 – 2411PhosphoserineBy similarity
    Modified residuei444 – 4441PhosphoserineBy similarity
    Modified residuei449 – 4491PhosphoserineBy similarity
    Modified residuei493 – 4931PhosphoserineBy similarity
    Modified residuei495 – 4951PhosphoserineBy similarity
    Modified residuei512 – 5121PhosphoserineBy similarity
    Modified residuei579 – 5791PhosphoserineBy similarity
    Modified residuei581 – 5811PhosphoserineBy similarity
    Modified residuei693 – 6931PhosphoserineBy similarity
    Modified residuei697 – 6971PhosphoserineBy similarity
    Modified residuei823 – 8231PhosphoserineBy similarity
    Modified residuei878 – 8781PhosphoserineBy similarity
    Modified residuei885 – 8851PhosphoserineBy similarity
    Modified residuei914 – 9141PhosphoserineBy similarity
    Modified residuei925 – 9251PhosphothreonineBy similarity
    Modified residuei938 – 9381PhosphothreonineBy similarity
    Modified residuei950 – 9501PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ63624.
    PRIDEiQ63624.

    PTM databases

    PhosphoSiteiQ63624.

    Expressioni

    Gene expression databases

    GenevestigatoriQ63624.

    Interactioni

    Subunit structurei

    Interacts with POLR2A.1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000027801.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1133 – 1258126Necessary for interaction with the CTD domain of POLR2ABy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi186 – 26984Pro-richAdd
    BLAST
    Compositional biasi193 – 20917Ser-richAdd
    BLAST
    Compositional biasi270 – 28213Glu-richAdd
    BLAST
    Compositional biasi478 – 642165Arg-richAdd
    BLAST
    Compositional biasi712 – 823112Ser-richAdd
    BLAST
    Compositional biasi845 – 87531Lys-richAdd
    BLAST
    Compositional biasi958 – 98528Glu-richAdd
    BLAST
    Compositional biasi1230 – 125728Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the splicing factor SR family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG291550.
    GeneTreeiENSGT00530000063661.
    HOGENOMiHOG000154300.
    HOVERGENiHBG097942.
    InParanoidiQ63624.
    OMAiADTRWGG.
    OrthoDBiEOG7F24SX.
    PhylomeDBiQ63624.
    TreeFamiTF332183.

    Sequencei

    Sequence statusi: Complete.

    Q63624-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEEDESRGK TEESGEDRGD GPPDRDPALS PSAFILRAIQ QAVGSSLQGD     50
    LPNDKDGSRC CGLQWRRCCR SPRSEPRSQE SGGADMATVL DTAADSFLVE 100
    LVSILDPPDT WVPSHLDLQP GESEDVLELV AEVRIGDRDP MPLPVPSLLP 150
    RLRAWRTGKT VSPQSHASRP ACSRHLLTLG TGDGGPAPPP APSSASSSPS 200
    PSPSSSSPSP PPPPPPPPPP ALPAPRFDIY DPFHPTDEAY SPPPAPEQKY 250
    DPFEPTGSNP SSSAGTPSPE EEEEEEEEEE EEGLSQSISR ISETLAGIYD 300
    DNSLSQDFPG DDSPHREPPP PQTLGAPGTP PQADSTRAEG APRRRVFVVG 350
    PEAEACLEGK VSVEVVTTAG GPALPLPPLP PTDPEIEEGE IVQPEEEPRV 400
    AVSLFRAARP RQPPASVATL ASVAAPAAPP ASAPRAPEGD DFLSLHADSD 450
    GEGALQVDLG EPPAPPAADA RWGGLDLRRK ILTQRRERYR QRSASPGPPP 500
    ARKKARRERQ RSGDPAPPDS PTWEAKKHRS RERKLGSHST ARRRSRSRSR 550
    RRSRSRSADR RRGSHRSRSR EKRRRRRRSA SPPPAASSSS SSRRERHRGK 600
    RREGGKKKKK RSRSRAEKRS GDLEKLPAPV PPSGSDRDSR RRGAVPPSIQ 650
    DLTDHDLFAI KRTITVGRPD KTEPRAPSPA PAVSPKREVL YDSEGLSADE 700
    RGAKGDKDRR RSGAASSSSS SREKASRRKA LDGDRGRDRD RSSKKTRPPK 750
    DSAPGSGALP KAPPSSGSSS SSSSCSSRKV KLQSKVAVLI REGVSSTTPA 800
    KDSSSSGLGS IGVKFSRDRE SRSPFLKPDE RAPAEGVKVA PGSTKPKKTK 850
    AKAKAGAKKA KGTKGKTKPS KTRKKVRSGG SSTASGGPGS LKKSKADSCS 900
    QAASAKGTEE TSWSGEERTT KAPSTPPPKV APPPPALTPD SQTVDSSCKT 950
    PEVSFLPEEA SEDTGVRVGA EEEEEEEEEE EEEEEQQPAT TTATSTAAAA 1000
    PSTAPSAGST AGDSGAEDGP AARASQLPTL PPPMPWNLPA GVDCTTSGVL 1050
    ALTALLFKME EANLASRAKA QELIQATNQI LSHRKPPSTL GVTPAPVPTS 1100
    LGLPPGPSSY LLPGSLPIGG CGSTPPTPTG LVPASDKREG SSSSEGRGDT 1150
    DKYLKKLHTQ ERAVEEVKLA IKPYYQKKDI TKEEYKDILR KAVHKICHSK 1200
    SGEINPVKVS NLVRAYVQRY RYFRKHGRKP GDPPGPPRPP KEPGPPDKGG 1250
    PGLPLPPL 1258
    Length:1,258
    Mass (Da):133,856
    Last modified:September 11, 2007 - v2
    Checksum:iBBEC7D4027E2F179
    GO

    Sequence cautioni

    The sequence AAC52657.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011L → V in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti195 – 1951A → G in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti255 – 2551P → A in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti264 – 2641A → G in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti289 – 2891S → R in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti687 – 6871R → G in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti746 – 7483TRP → PRT in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti765 – 7651S → R in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti832 – 8321A → S in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti952 – 9521E → D in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti957 – 9571P → A in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti1076 – 10761A → D in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti1082 – 10821S → R in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti1101 – 11011L → F in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti1106 – 11061G → A in AAC52657. (PubMed:8692929)Curated
    Sequence conflicti1170 – 11701A → S in AAC52657. (PubMed:8692929)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03002356 Genomic DNA. No translation available.
    U49056 mRNA. Translation: AAC52657.1. Different initiation.
    PIRiT31421.
    RefSeqiNP_062257.1. NM_019384.1.
    XP_006229190.1. XM_006229128.1.
    UniGeneiRn.93.

    Genome annotation databases

    EnsembliENSRNOT00000027801; ENSRNOP00000027801; ENSRNOG00000020499.
    GeneIDi56081.
    KEGGirno:56081.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03002356 Genomic DNA. No translation available.
    U49056 mRNA. Translation: AAC52657.1 . Different initiation.
    PIRi T31421.
    RefSeqi NP_062257.1. NM_019384.1.
    XP_006229190.1. XM_006229128.1.
    UniGenei Rn.93.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000027801.

    PTM databases

    PhosphoSitei Q63624.

    Proteomic databases

    PaxDbi Q63624.
    PRIDEi Q63624.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000027801 ; ENSRNOP00000027801 ; ENSRNOG00000020499 .
    GeneIDi 56081.
    KEGGi rno:56081.

    Organism-specific databases

    CTDi 58506.
    RGDi 708405. Scaf1.

    Phylogenomic databases

    eggNOGi NOG291550.
    GeneTreei ENSGT00530000063661.
    HOGENOMi HOG000154300.
    HOVERGENi HBG097942.
    InParanoidi Q63624.
    OMAi ADTRWGG.
    OrthoDBi EOG7F24SX.
    PhylomeDBi Q63624.
    TreeFami TF332183.

    Miscellaneous databases

    NextBioi 611095.
    PROi Q63624.

    Gene expression databases

    Genevestigatori Q63624.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "The C-terminal domain of the largest subunit of RNA polymerase II interacts with a novel set of serine/arginine-rich proteins."
      Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C., Gebara M., Corden J.L.
      Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-1258, FUNCTION, INTERACTION WITH POLR2A.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiSFR19_RAT
    AccessioniPrimary (citable) accession number: Q63624
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 75 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3