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Q08170 (SRSF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Serine/arginine-rich splicing factor 4
Alternative name(s):
Pre-mRNA-splicing factor SRP75
SRP001LB
Splicing factor, arginine/serine-rich 4
Gene names
Name:SRSF4
Synonyms:SFRS4, SRP75
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10. Ref.8

Subunit structure

Found in a pre-mRNA splicing complex with SRSF4/SFRS4, SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Interacts with PNN. Ref.7 Ref.9

Subcellular location

Nucleus speckle Ref.9.

Post-translational modification

Extensively phosphorylated on serine residues in the RS domain.

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 diversityPolymorphism
   DomainRepeat
   LigandRNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Traceable author statement. Source: Reactome

RNA splicing, via transesterification reactions

Traceable author statement Ref.1. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement. Source: Reactome

mRNA processing

Traceable author statement Ref.1. Source: ProtInc

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay Ref.8. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Serine/arginine-rich splicing factor 4
PRO_0000081925

Regions

Domain2 – 7271RRM 1
Domain104 – 17774RRM 2
Compositional bias72 – 9726Gly-rich (hinge region)
Compositional bias179 – 494316Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue781Phosphoserine Ref.11
Modified residue4311Phosphoserine Ref.11 Ref.13

Natural variations

Natural variant2531E → D. Ref.1
Corresponds to variant rs2230679 [ dbSNP | Ensembl ].
VAR_052230
Natural variant3381G → A. Ref.1
Corresponds to variant rs2230677 [ dbSNP | Ensembl ].
VAR_052231
Natural variant3561G → S. Ref.1
Corresponds to variant rs2230678 [ dbSNP | Ensembl ].
VAR_052232
Natural variant4381Q → E.
Corresponds to variant rs1049928 [ dbSNP | Ensembl ].
VAR_052233

Experimental info

Sequence conflict351N → D AA sequence Ref.6
Sequence conflict318 – 3225SRGRS → EQGQE in AAA36649. Ref.1
Sequence conflict436 – 4383TNQ → RNE in AAA36649. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q08170 [UniParc].

Last modified May 15, 2002. Version 2.
Checksum: 5BBAB917C218C20A

FASTA49456,678
        10         20         30         40         50         60 
MPRVYIGRLS YQARERDVER FFKGYGKILE VDLKNGYGFV EFDDLRDADD AVYELNGKDL 

        70         80         90        100        110        120 
CGERVIVEHA RGPRRDGSYG SGRSGYGYRR SGRDKYGPPT RTEYRLIVEN LSSRCSWQDL 

       130        140        150        160        170        180 
KDYMRQAGEV TYADAHKGRK NEGVIEFVSY SDMKRALEKL DGTEVNGRKI RLVEDKPGSR 

       190        200        210        220        230        240 
RRRSYSRSRS HSRSRSRSRH SRKSRSRSGS SKSSHSKSRS RSRSGSRSRS KSRSRSQSRS 

       250        260        270        280        290        300 
RSKKEKSRSP SKEKSRSRSH SAGKSRSKSK DQAEEKIQNN DNVGKPKSRS PSRHKSKSKS 

       310        320        330        340        350        360 
RSRSQERRVE EEKRGSVSRG RSQEKSLRQS RSRSRSKGGS RSRSRSRSKS KDKRKGRKRS 

       370        380        390        400        410        420 
REESRSRSRS RSKSERSRKR GSKRDSKAGS SKKKKKEDTD RSQSRSPSRS VSKEREHAKS 

       430        440        450        460        470        480 
ESSQREGRGE SENAGTNQET RSRSRSNSKS KPNLPSESRS RSKSASKTRS RSKSRSRSAS 

       490 
RSPSRSRSRS HSRS 

« Hide

References

« Hide 'large scale' references
[1]"Human SR proteins and isolation of a cDNA encoding SRp75."
Zahler A.M., Neugebauer K.M., Stolk J.A., Roth M.B.
Mol. Cell. Biol. 13:4023-4028(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANTS ASP-253; ALA-338 AND SER-356.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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].
[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].
Tissue: Lymph.
[5]"Sequencing of human chromosome 1."
Connolly K.S., Gunning K.M., Davis C.A., Kadner K., Subramanian S., Miguel T., Lewis K.D., Fridlyand J., Alcivare D., Benke J.A., Bondoc M., Bowen E., Chiang A., Critz P., Jaklevic M.A., Lindo K., Lindquist K., Miller C. expand/collapse author list , Patel S., Piscia C., Riley B.E., Rojeski H., Sarmiento R., Yu C., Montenegro M., Aerts A., Chung A., Abrajano A., Baker M., Gau C., Jett J., Ko C., Beall K., Woolley J.P., Conboy J., Fang J.F., Narla M., Stultz J.L., Kimmerly W., Martin C.H.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-192.
[6]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-45; 84-89; 126-137; 140-154 AND 172-179.
[7]"A coactivator of pre-mRNA splicing."
Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.
Genes Dev. 12:996-1009(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA SPLICING COMPLEX WITH SRSF5; SNRNP70; SNRPA1; SRRM1 AND SRRM2.
[8]"Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors."
Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.
J. Neurochem. 88:1078-1090(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Pinin/DRS/memA interacts with SRp75, SRm300 and SRrp130 in corneal epithelial cells."
Zimowska G., Shi J., Munguba G., Jackson M.R., Alpatov R., Simmons M.N., Shi Y., Sugrue S.P.
Invest. Ophthalmol. Vis. Sci. 44:4715-4723(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PNN, SUBCELLULAR LOCATION.
[10]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-78 AND SER-431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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-431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14076 mRNA. Translation: AAA36649.1.
BT007415 mRNA. Translation: AAP36083.1.
AL590729, AL357500 Genomic DNA. Translation: CAI14326.1.
AL357500, AL590729 Genomic DNA. Translation: CAH71635.1.
BC002781 mRNA. Translation: AAH02781.1.
AC004236 Genomic DNA. Translation: AAC04476.1.
PIRA48133.
RefSeqNP_005617.2. NM_005626.4.
UniGeneHs.469970.

3D structure databases

ProteinModelPortalQ08170.
SMRQ08170. Positions 2-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112327. 39 interactions.
IntActQ08170. 22 interactions.
MINTMINT-1410521.

PTM databases

PhosphoSiteQ08170.

Polymorphism databases

DMDM20981726.

Proteomic databases

PaxDbQ08170.
PeptideAtlasQ08170.
PRIDEQ08170.

Protocols and materials databases

DNASU6429.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373795; ENSP00000362900; ENSG00000116350.
GeneID6429.
KEGGhsa:6429.
UCSCuc001bro.3. human.

Organism-specific databases

CTD6429.
GeneCardsGC01M029474.
H-InvDBHIX0160019.
HGNCHGNC:10786. SRSF4.
HPAHPA050975.
MIM601940. gene.
neXtProtNX_Q08170.
PharmGKBPA35702.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOVERGENHBG002295.
InParanoidQ08170.
KOK12893.
OMAREHAKSE.
OrthoDBEOG7H1JPR.
PhylomeDBQ08170.
TreeFamTF351335.

Enzyme and pathway databases

ReactomeREACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ08170.
BgeeQ08170.
CleanExHS_SFRS4.
GenevestigatorQ08170.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRSF4. human.
GeneWikiSFRS4.
GenomeRNAi6429.
NextBio24969.
PROQ08170.
SOURCESearch...

Entry information

Entry nameSRSF4_HUMAN
AccessionPrimary (citable) accession number: Q08170
Secondary accession number(s): Q5VXP1, Q9BUA4, Q9UEB5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 15, 2002
Last modified: April 16, 2014
This is version 138 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

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