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Protein

Serine/arginine-rich splicing factor 4

Gene

SRSF4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in alternative splice site selection during pre-mRNA splicing. Represses the splicing of MAPT/Tau exon 10.1 Publication

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. hematopoietic progenitor cell differentiation Source: Ensembl
  3. mRNA 3'-end processing Source: Reactome
  4. mRNA export from nucleus Source: Reactome
  5. mRNA processing Source: ProtInc
  6. mRNA splicing, via spliceosome Source: Reactome
  7. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  8. RNA splicing Source: Reactome
  9. RNA splicing, via transesterification reactions Source: ProtInc
  10. termination of RNA polymerase II transcription Source: Reactome
  11. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 4
Alternative name(s):
Pre-mRNA-splicing factor SRP75
SRP001LB
Splicing factor, arginine/serine-rich 4
Gene namesi
Name:SRSF4
Synonyms:SFRS4, SRP75
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10786. SRSF4.

Subcellular locationi

Nucleus speckle 1 Publication

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB-SubCell
  2. nucleoplasm Source: HPA
  3. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35702.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Serine/arginine-rich splicing factor 4PRO_0000081925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781Phosphoserine1 Publication
Modified residuei431 – 4311Phosphoserine2 Publications

Post-translational modificationi

Extensively phosphorylated on serine residues in the RS domain.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ08170.
PaxDbiQ08170.
PeptideAtlasiQ08170.
PRIDEiQ08170.

PTM databases

PhosphoSiteiQ08170.

Expressioni

Gene expression databases

BgeeiQ08170.
CleanExiHS_SFRS4.
ExpressionAtlasiQ08170. baseline and differential.
GenevestigatoriQ08170.

Organism-specific databases

HPAiHPA050975.

Interactioni

Subunit structurei

Found in a pre-mRNA splicing complex with SRSF4/SFRS4, SRSF5/SFRS5, SNRNP70, SNRPA1, SRRM1 and SRRM2. Interacts with PNN.2 Publications

Protein-protein interaction databases

BioGridi112327. 39 interactions.
IntActiQ08170. 23 interactions.
MINTiMINT-1410521.

Structurei

3D structure databases

ProteinModelPortaliQ08170.
SMRiQ08170. Positions 3-78, 93-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7271RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini104 – 17774RRM 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi72 – 9726Gly-rich (hinge region)Add
BLAST
Compositional biasi179 – 494316Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ08170.
KOiK12893.
OMAiREHAKSE.
OrthoDBiEOG7H1JPR.
PhylomeDBiQ08170.
TreeFamiTF351335.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08170-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRVYIGRLS YQARERDVER FFKGYGKILE VDLKNGYGFV EFDDLRDADD
60 70 80 90 100
AVYELNGKDL CGERVIVEHA RGPRRDGSYG SGRSGYGYRR SGRDKYGPPT
110 120 130 140 150
RTEYRLIVEN LSSRCSWQDL KDYMRQAGEV TYADAHKGRK NEGVIEFVSY
160 170 180 190 200
SDMKRALEKL DGTEVNGRKI RLVEDKPGSR RRRSYSRSRS HSRSRSRSRH
210 220 230 240 250
SRKSRSRSGS SKSSHSKSRS RSRSGSRSRS KSRSRSQSRS RSKKEKSRSP
260 270 280 290 300
SKEKSRSRSH SAGKSRSKSK DQAEEKIQNN DNVGKPKSRS PSRHKSKSKS
310 320 330 340 350
RSRSQERRVE EEKRGSVSRG RSQEKSLRQS RSRSRSKGGS RSRSRSRSKS
360 370 380 390 400
KDKRKGRKRS REESRSRSRS RSKSERSRKR GSKRDSKAGS SKKKKKEDTD
410 420 430 440 450
RSQSRSPSRS VSKEREHAKS ESSQREGRGE SENAGTNQET RSRSRSNSKS
460 470 480 490
KPNLPSESRS RSKSASKTRS RSKSRSRSAS RSPSRSRSRS HSRS
Length:494
Mass (Da):56,678
Last modified:May 15, 2002 - v2
Checksum:i5BBAB917C218C20A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351N → D AA sequence (PubMed:1577277)Curated
Sequence conflicti318 – 3225SRGRS → EQGQE in AAA36649. (PubMed:8321209)Curated
Sequence conflicti436 – 4383TNQ → RNE in AAA36649. (PubMed:8321209)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti253 – 2531E → D.1 Publication
Corresponds to variant rs2230679 [ dbSNP | Ensembl ].
VAR_052230
Natural varianti338 – 3381G → A.1 Publication
Corresponds to variant rs2230677 [ dbSNP | Ensembl ].
VAR_052231
Natural varianti356 – 3561G → S.1 Publication
Corresponds to variant rs2230678 [ dbSNP | Ensembl ].
VAR_052232
Natural varianti438 – 4381Q → E.
Corresponds to variant rs1049928 [ dbSNP | Ensembl ].
VAR_052233

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS333.1.
PIRiA48133.
RefSeqiNP_005617.2. NM_005626.4.
UniGeneiHs.469970.

Genome annotation databases

EnsembliENST00000373795; ENSP00000362900; ENSG00000116350.
GeneIDi6429.
KEGGihsa:6429.
UCSCiuc001bro.3. human.

Polymorphism databases

DMDMi20981726.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS333.1.
PIRiA48133.
RefSeqiNP_005617.2. NM_005626.4.
UniGeneiHs.469970.

3D structure databases

ProteinModelPortaliQ08170.
SMRiQ08170. Positions 3-78, 93-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112327. 39 interactions.
IntActiQ08170. 23 interactions.
MINTiMINT-1410521.

PTM databases

PhosphoSiteiQ08170.

Polymorphism databases

DMDMi20981726.

Proteomic databases

MaxQBiQ08170.
PaxDbiQ08170.
PeptideAtlasiQ08170.
PRIDEiQ08170.

Protocols and materials databases

DNASUi6429.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373795; ENSP00000362900; ENSG00000116350.
GeneIDi6429.
KEGGihsa:6429.
UCSCiuc001bro.3. human.

Organism-specific databases

CTDi6429.
GeneCardsiGC01M029474.
H-InvDBHIX0160019.
HGNCiHGNC:10786. SRSF4.
HPAiHPA050975.
MIMi601940. gene.
neXtProtiNX_Q08170.
PharmGKBiPA35702.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ08170.
KOiK12893.
OMAiREHAKSE.
OrthoDBiEOG7H1JPR.
PhylomeDBiQ08170.
TreeFamiTF351335.

Enzyme and pathway databases

ReactomeiREACT_1597. Transport of Mature mRNA derived from an Intron-Containing Transcript.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSRSF4. human.
GeneWikiiSFRS4.
GenomeRNAii6429.
NextBioi24969.
PROiQ08170.
SOURCEiSearch...

Gene expression databases

BgeeiQ08170.
CleanExiHS_SFRS4.
ExpressionAtlasiQ08170. baseline and differential.
GenevestigatoriQ08170.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiSRSF4_HUMAN
AccessioniPrimary (citable) accession number: Q08170
Secondary accession number(s): Q5VXP1, Q9BUA4, Q9UEB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 15, 2002
Last modified: February 4, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.