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Q05519 (SRS11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/arginine-rich splicing factor 11
Alternative name(s):
Arginine-rich 54 kDa nuclear protein
Short name=p54
Splicing factor, arginine/serine-rich 11
Gene names
Name:SRSF11
Synonyms:SFRS11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May function in pre-mRNA splicing.

Subunit structure

Interacts with PUF60. Ref.5

Subcellular location

Nucleus. Note: Colocalizes with spliceosome components.

Sequence similarities

Belongs to the splicing factor SR family.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ETS1P149212EBI-1051785,EBI-913209

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q05519-1)

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 2 (identifier: Q05519-2)

The sequence of this isoform differs from the canonical sequence as follows:
     420-420: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Serine/arginine-rich splicing factor 11
PRO_0000081939

Regions

Domain33 – 11381RRM
Repeat247 – 25591
Repeat258 – 26582
Repeat267 – 27483
Repeat275 – 28284
Repeat285 – 29285
Repeat293 – 30086
Repeat302 – 30987
Repeat321 – 32888
Repeat334 – 34189
Repeat346 – 353810
Region247 – 35310710 X 8 AA approximate repeats of R-R-S-R-S-R-S-R
Compositional bias17 – 3115Poly-Gly
Compositional bias252 – 2598Poly-Arg
Compositional bias291 – 2944Poly-Arg
Compositional bias341 – 3499Poly-Arg
Compositional bias397 – 4048Poly-Lys

Amino acid modifications

Modified residue2071Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12
Modified residue4141Phosphoserine Ref.10
Modified residue4341Phosphoserine Ref.8 Ref.10 Ref.12
Modified residue4471Phosphothreonine Ref.10 Ref.12
Modified residue4491Phosphoserine Ref.10 Ref.12
Modified residue4641Phosphoserine Ref.10
Modified residue4831Phosphoserine Ref.6 Ref.9 Ref.10 Ref.12

Natural variations

Alternative sequence4201Missing in isoform 2.
VSP_043376

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: 1211E96DDC0A3182

FASTA48453,542
        10         20         30         40         50         60 
MSNTTVVPST AGPGPSGGPG GGGGGGGGGG GTEVIQVTNV SPSASSEQMR TLFGFLGKID 

        70         80         90        100        110        120 
ELRLFPPDDS PLPVSSRVCF VKFHDPDSAV VAQHLTNTVF VDRALIVVPY AEGVIPDEAK 

       130        140        150        160        170        180 
ALSLLAPANA VAGLLPGGGL LPTPNPLTQI GAVPLAALGA PTLDPALAAL GLPGANLNSQ 

       190        200        210        220        230        240 
SLAADQLLKL MSTVDPKLNH VAAGLVSPSL KSDTSSKEIE EAMKRVREAQ SLISAAIEPD 

       250        260        270        280        290        300 
KKEEKRRHSR SRSRSRRRRT PSSSRHRRSR SRSRRRSHSK SRSRRRSKSP RRRRSHSRER 

       310        320        330        340        350        360 
GRRSRSTSKT RDKKKEDKEK KRSKTPPKSY STARRSRSAS RERRRRRSRS GTRSPKKPRS 

       370        380        390        400        410        420 
PKRKLSRSPS PRRHKKEKKK DKDKERSRDE RERSTSKKKK SKDKEKDRER KSESDKDVKQ 

       430        440        450        460        470        480 
VTRDYDEEEQ GYDSEKEKKE EKKPIETGSP KTKECSVEKG TGDSLRESKV NGDDHHEEDM 


DMSD 

« Hide

Isoform 2 [UniParc].

Checksum: 5A40AFD8B7599976
Show »

FASTA48353,414

References

« Hide 'large scale' references
[1]"Primary structure of a human arginine-rich nuclear protein that colocalizes with spliceosome components."
Chaudhary N., McMahon C., Blobel G.
Proc. Natl. Acad. Sci. U.S.A. 88:8189-8193(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Hepatoma.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterus.
[5]"PUF60: a novel U2AF65-related splicing activity."
Page-McCaw P.S., Amonlirdviman K., Sharp P.A.
RNA 5:1548-1560(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PUF60.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-434, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-483, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-414; SER-434; THR-447; SER-449; SER-464 AND SER-483, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-434; THR-447; SER-449 AND SER-483, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74002 mRNA. Translation: AAA35554.1.
AL353771 Genomic DNA. Translation: CAI22334.1.
AL353771 Genomic DNA. Translation: CAI22335.1.
CH471059 Genomic DNA. Translation: EAX06459.1.
BC040436 mRNA. Translation: AAH40436.1.
IPIIPI00464952.
IPI00641287.
PIRA40988.
RefSeqNP_001177916.1. NM_001190987.1.
NP_004759.1. NM_004768.3.
UniGeneHs.479693.

3D structure databases

ProteinModelPortalQ05519.
ModBaseSearch...

Protein-protein interaction databases

IntActQ05519. 8 interactions.
STRING9606.ENSP00000359988.

PTM databases

PhosphoSiteQ05519.

Polymorphism databases

DMDM8134672.

Proteomic databases

PaxDbQ05519.
PRIDEQ05519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370950; ENSP00000359988; ENSG00000116754.
ENST00000370951; ENSP00000359989; ENSG00000116754.
ENST00000405432; ENSP00000384357; ENSG00000116754.
GeneID9295.
KEGGhsa:9295.
UCSCuc001des.3. human.

Organism-specific databases

CTD9295.
GeneCardsGC01P070672.
HGNCHGNC:10782. SRSF11.
HPAHPA008762.
MIM602010. gene.
neXtProtNX_Q05519.
PharmGKBPA35698.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277302.
HOGENOMHOG000121772.
HOVERGENHBG058422.
InParanoidQ05519.
KOK12899.
OrthoDBEOG4J9N10.
PhylomeDBQ05519.

Enzyme and pathway databases

ReactomeREACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ05519.
BgeeQ05519.
CleanExHS_SFRS11.
GenevestigatorQ05519.
GermOnlineENSG00000116754. Homo sapiens.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRSF11. human.
GenomeRNAi9295.
NextBio34827.
SOURCESearch...

Entry information

Entry nameSRS11_HUMAN
AccessionPrimary (citable) accession number: Q05519
Secondary accession number(s): Q5T758, Q8IWE6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families