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Q63624 (SFR19_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Splicing factor, arginine/serine-rich 19
Alternative name(s):
CTD-binding SR-like protein rA1
SR-related and CTD-associated factor 1
Gene names
Name:Scaf1
Synonyms:Sfrs19
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1258 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function in pre-mRNA splicing. Ref.2

Subunit structure

Interacts with POLR2A. Ref.2

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the splicing factor SR family.

Sequence caution

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

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from mutant phenotype Ref.2. Source: RGD

transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.2. Source: RGD

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein domain specific binding

Inferred from mutant phenotype Ref.2. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12581258Splicing factor, arginine/serine-rich 19
PRO_0000299408

Regions

Region1133 – 1258126Necessary for interaction with the CTD domain of POLR2A By similarity
Compositional bias186 – 26984Pro-rich
Compositional bias193 – 20917Ser-rich
Compositional bias270 – 28213Glu-rich
Compositional bias478 – 642165Arg-rich
Compositional bias712 – 823112Ser-rich
Compositional bias845 – 87531Lys-rich
Compositional bias958 – 98528Glu-rich
Compositional bias1230 – 125728Pro-rich

Amino acid modifications

Modified residue2411Phosphoserine By similarity
Modified residue4441Phosphoserine By similarity
Modified residue4491Phosphoserine By similarity
Modified residue4931Phosphoserine By similarity
Modified residue4951Phosphoserine By similarity
Modified residue5121Phosphoserine By similarity
Modified residue5791Phosphoserine By similarity
Modified residue5811Phosphoserine By similarity
Modified residue6931Phosphoserine By similarity
Modified residue6971Phosphoserine By similarity
Modified residue8231Phosphoserine By similarity
Modified residue8781Phosphoserine By similarity
Modified residue8851Phosphoserine By similarity
Modified residue9141Phosphoserine By similarity
Modified residue9251Phosphothreonine By similarity
Modified residue9381Phosphothreonine By similarity
Modified residue9501Phosphothreonine By similarity

Experimental info

Sequence conflict1011L → V in AAC52657. Ref.2
Sequence conflict1951A → G in AAC52657. Ref.2
Sequence conflict2551P → A in AAC52657. Ref.2
Sequence conflict2641A → G in AAC52657. Ref.2
Sequence conflict2891S → R in AAC52657. Ref.2
Sequence conflict6871R → G in AAC52657. Ref.2
Sequence conflict746 – 7483TRP → PRT in AAC52657. Ref.2
Sequence conflict7651S → R in AAC52657. Ref.2
Sequence conflict8321A → S in AAC52657. Ref.2
Sequence conflict9521E → D in AAC52657. Ref.2
Sequence conflict9571P → A in AAC52657. Ref.2
Sequence conflict10761A → D in AAC52657. Ref.2
Sequence conflict10821S → R in AAC52657. Ref.2
Sequence conflict11011L → F in AAC52657. Ref.2
Sequence conflict11061G → A in AAC52657. Ref.2
Sequence conflict11701A → S in AAC52657. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q63624 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: BBEC7D4027E2F179

FASTA1,258133,856
        10         20         30         40         50         60 
MEEEDESRGK TEESGEDRGD GPPDRDPALS PSAFILRAIQ QAVGSSLQGD LPNDKDGSRC 

        70         80         90        100        110        120 
CGLQWRRCCR SPRSEPRSQE SGGADMATVL DTAADSFLVE LVSILDPPDT WVPSHLDLQP 

       130        140        150        160        170        180 
GESEDVLELV AEVRIGDRDP MPLPVPSLLP RLRAWRTGKT VSPQSHASRP ACSRHLLTLG 

       190        200        210        220        230        240 
TGDGGPAPPP APSSASSSPS PSPSSSSPSP PPPPPPPPPP ALPAPRFDIY DPFHPTDEAY 

       250        260        270        280        290        300 
SPPPAPEQKY DPFEPTGSNP SSSAGTPSPE EEEEEEEEEE EEGLSQSISR ISETLAGIYD 

       310        320        330        340        350        360 
DNSLSQDFPG DDSPHREPPP PQTLGAPGTP PQADSTRAEG APRRRVFVVG PEAEACLEGK 

       370        380        390        400        410        420 
VSVEVVTTAG GPALPLPPLP PTDPEIEEGE IVQPEEEPRV AVSLFRAARP RQPPASVATL 

       430        440        450        460        470        480 
ASVAAPAAPP ASAPRAPEGD DFLSLHADSD GEGALQVDLG EPPAPPAADA RWGGLDLRRK 

       490        500        510        520        530        540 
ILTQRRERYR QRSASPGPPP ARKKARRERQ RSGDPAPPDS PTWEAKKHRS RERKLGSHST 

       550        560        570        580        590        600 
ARRRSRSRSR RRSRSRSADR RRGSHRSRSR EKRRRRRRSA SPPPAASSSS SSRRERHRGK 

       610        620        630        640        650        660 
RREGGKKKKK RSRSRAEKRS GDLEKLPAPV PPSGSDRDSR RRGAVPPSIQ DLTDHDLFAI 

       670        680        690        700        710        720 
KRTITVGRPD KTEPRAPSPA PAVSPKREVL YDSEGLSADE RGAKGDKDRR RSGAASSSSS 

       730        740        750        760        770        780 
SREKASRRKA LDGDRGRDRD RSSKKTRPPK DSAPGSGALP KAPPSSGSSS SSSSCSSRKV 

       790        800        810        820        830        840 
KLQSKVAVLI REGVSSTTPA KDSSSSGLGS IGVKFSRDRE SRSPFLKPDE RAPAEGVKVA 

       850        860        870        880        890        900 
PGSTKPKKTK AKAKAGAKKA KGTKGKTKPS KTRKKVRSGG SSTASGGPGS LKKSKADSCS 

       910        920        930        940        950        960 
QAASAKGTEE TSWSGEERTT KAPSTPPPKV APPPPALTPD SQTVDSSCKT PEVSFLPEEA 

       970        980        990       1000       1010       1020 
SEDTGVRVGA EEEEEEEEEE EEEEEQQPAT TTATSTAAAA PSTAPSAGST AGDSGAEDGP 

      1030       1040       1050       1060       1070       1080 
AARASQLPTL PPPMPWNLPA GVDCTTSGVL ALTALLFKME EANLASRAKA QELIQATNQI 

      1090       1100       1110       1120       1130       1140 
LSHRKPPSTL GVTPAPVPTS LGLPPGPSSY LLPGSLPIGG CGSTPPTPTG LVPASDKREG 

      1150       1160       1170       1180       1190       1200 
SSSSEGRGDT DKYLKKLHTQ ERAVEEVKLA IKPYYQKKDI TKEEYKDILR KAVHKICHSK 

      1210       1220       1230       1240       1250 
SGEINPVKVS NLVRAYVQRY RYFRKHGRKP GDPPGPPRPP KEPGPPDKGG PGLPLPPL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03002356 Genomic DNA. No translation available.
U49056 mRNA. Translation: AAC52657.1. Different initiation.
PIRT31421.
RefSeqNP_062257.1. NM_019384.1.
XP_006229190.1. XM_006229128.1.
UniGeneRn.93.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000027801.

PTM databases

PhosphoSiteQ63624.

Proteomic databases

PaxDbQ63624.
PRIDEQ63624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027801; ENSRNOP00000027801; ENSRNOG00000020499.
GeneID56081.
KEGGrno:56081.

Organism-specific databases

CTD58506.
RGD708405. Scaf1.

Phylogenomic databases

eggNOGNOG291550.
GeneTreeENSGT00530000063661.
HOGENOMHOG000154300.
HOVERGENHBG097942.
InParanoidQ63624.
OMAADTRWGG.
OrthoDBEOG7F24SX.
PhylomeDBQ63624.
TreeFamTF332183.

Gene expression databases

GenevestigatorQ63624.

Family and domain databases

ProtoNetSearch...

Other

NextBio611095.
PROQ63624.

Entry information

Entry nameSFR19_RAT
AccessionPrimary (citable) accession number: Q63624
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families