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Reviewed, UniProtKB/Swiss-Prot Q13247 (SFRS6_HUMAN)

Last modified July 7, 2009. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Splicing factor, arginine/serine-rich 6
Alternative name(s):
    Pre-mRNA-splicing factor SRP55
Gene names
Name: SFRS6
Synonyms: SRP55
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Plays a role in constitutive splicing and can modulate the selection of alternative splice sites.

Subunit structure

Binds SFRS12.

Subcellular location

Nucleus.

Post-translational modification

Extensively phosphorylated on serine residues in the RS domain By similarity.

Sequence similarities

Belongs to the splicing factor SR family.

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processmRNA splice site selection Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHAQP273481EBI-745230,EBI-359854

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform SRP55-1 (identifier: Q13247-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform SRP55-2 (identifier: Q13247-2)

The sequence of this isoform differs from the canonical sequence as follows:
     86-135: SGGGGYSSRR...LKDFMRQAGE → MTNGAEAVST...EAMTTAAFCH
     136-344: Missing.
Isoform SRP55-3 (identifier: Q13247-3)

The sequence of this isoform differs from the canonical sequence as follows:
     313-344: RSVSPPPKRATSRSRSRSRSKSRSRSRSSSRD → LKLGARFMSQQGTESLYSLASSC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Splicing factor, arginine/serine-rich 6
PRO_0000081930

Regions

Domain1 – 7272RRM 1
Domain110 – 18374RRM 2
Compositional bias87 – 904Gly-rich (hinge region)
Compositional bias184 – 343160Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue451Phosphoserine Ref.7
Modified residue2591Phosphoserine Ref.7
Modified residue2971Phosphoserine Ref.7 Ref.11
Modified residue2991Phosphoserine Ref.7 Ref.11
Modified residue3011Phosphoserine Ref.7 Ref.6
Modified residue3031Phosphoserine Ref.7 Ref.11 Ref.8 Ref.9 Ref.10
Modified residue3141Phosphoserine Ref.7 Ref.11 Ref.6 Ref.9
Modified residue3161Phosphoserine Ref.7 Ref.11 Ref.6 Ref.9

Natural variations

Alternative sequence86 – 13550SGGGG…RQAGE → MTNGAEAVSTEAKMTAFPDW PWLFHTLCDPCPMTLWLTLP EAMTTAAFCH in isoform SRP55-2.
VSP_005869
Alternative sequence136 – 344209Missing in isoform SRP55-2.
VSP_005870
Alternative sequence313 – 34432RSVSP…SSSRD → LKLGARFMSQQGTESLYSLA SSC in isoform SRP55-3.
VSP_005871
Natural variant1451R → Q in a colorectal cancer sample; somatic mutation. Ref.13
VAR_035489

Experimental info

Sequence conflict641R → H in AAA93073. Ref.1
Sequence conflict641R → H in AAA93071. Ref.1
Sequence conflict641R → H in AAA93072. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform SRP55-1 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 72305506CE948B94

FASTA34439,587
        10         20         30         40         50         60 
MPRVYIGRLS YNVREKDIQR FFSGYGRLLE VDLKNGYGFV EFEDSRDADD AVYELNGKEL 

        70         80         90        100        110        120 
CGERVIVEHA RGPRRDRDGY SYGSRSGGGG YSSRRTSGRD KYGPPVRTEY RLIVENLSSR 

       130        140        150        160        170        180 
CSWQDLKDFM RQAGEVTYAD AHKERTNEGV IEFRSYSDMK RALDKLDGTE INGRNIRLIE 

       190        200        210        220        230        240 
DKPRTSHRRS YSGSRSRSRS RRRSRSRSRR SSRSRSRSIS KSRSRSRSRS KGRSRSRSKG 

       250        260        270        280        290        300 
RKSRSKSKSK PKSDRGSHSH SRSRSKDEYE KSRSRSRSRS PKENGKGDIK SKSRSRSQSR 

       310        320        330        340 
SNSPLPVPPS KARSVSPPPK RATSRSRSRS RSKSRSRSRS SSRD 

« Hide

Isoform SRP55-2.

Checksum: 2D03ECF8A6F25E19
Show »

FASTA13515,498
Isoform SRP55-3.

Checksum: 396E9091AD0B7DD1
Show »

FASTA33538,419

References

« Hide 'large scale' references
[1]"Identification and characterization of three members of the human SR family of pre-mRNA splicing factors."
Screaton G.R., Caceres J.F., Mayeda A., Bell M.V., Plebanski M., Jackson D.G., Bell J.I., Krainer A.R.
EMBO J. 14:4336-4349(1995) [PubMed: 7556075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SRP55-1; SRP55-2 AND SRP55-3).
Tissue: Colon.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed: 11780052] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SRP55-1).
Tissue: Placenta.
[4]"SR proteins: a conserved family of pre-mRNA splicing factors."
Zahler A.M., Lane W.S., Stolk J.A., Roth M.B.
Genes Dev. 6:837-847(1992) [PubMed: 1577277] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-27 AND 47-55.
[5]"Identification and characterization of a novel serine-arginine-rich splicing regulatory protein."
Barnard D.C., Patton J.G.
Mol. Cell. Biol. 20:3049-3057(2000) [PubMed: 10757789] [Abstract]
Cited for: INTERACTION WITH SFRS12.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-314 AND SER-316, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-259; SER-297; SER-299; SER-301; SER-303; SER-314 AND SER-316, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-314 AND SER-316, MASS SPECTROMETRY.
[10]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, MASS SPECTROMETRY.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-299; SER-303; SER-314 AND SER-316, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-145.
+Additional computationally mapped references.

Cross-references

Sequence databases

U30883 mRNA. Translation: AAA93073.1.
U30828 mRNA. Translation: AAA93071.1.
U30829 mRNA. Translation: AAA93072.1.
AL031681 Genomic DNA. Translation: CAB43960.1.
BC006832 mRNA. Translation: AAH06832.1.
IPIIPI00012345.
IPI00018203.
IPI00215879.
PIRS59043.
RefSeqNP_006266.2.
UniGeneHs.6891

3D structure databases

HSSPHSSP built from PDB template 1HD1 based on UniProtKB Q14103.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13247. 5 interactions.

PTM databases

PhosphoSiteQ13247.

Proteomic databases

PRIDEQ13247.

Genome annotation databases

EnsemblENSG00000124193. Homo sapiens. [Contig view]
GeneID6431.
KEGGhsa:6431.
UCSCuc002xkj.1. human.

Organism-specific databases

GeneCardsGC20P041519.
H-InvDBHIX0015826.
HGNCHGNC:10788. SFRS6.
MIM601944. gene.
PharmGKBPA35704.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ13247.
HOVERGENQ13247.
OMAQ13247. XGGGGYS.

Enzyme and pathway databases

ReactomeREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1788. Transcription.
REACT_6167. Influenza Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ13247.
BgeeQ13247.
CleanExHS_SFRS6.
GermOnlineENSG00000124193. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 2 hits.
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio24979.
SOURCESearch...

Entry information

Entry nameSFRS6_HUMAN
AccessionPrimary (citable) accession number: Q13247
Secondary accession number(s): Q13244 expand/collapse secondary AC list , Q13245, Q96J06, Q9UJB8, Q9Y3N7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 15, 2002
Last modified: July 7, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents