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Protein

Serine/arginine-rich splicing factor 1

Gene

SRSF1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-BTA-109688. Cleavage of Growing Transcript in the Termination Region.
R-BTA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-BTA-72163. mRNA Splicing - Major Pathway.
R-BTA-72165. mRNA Splicing - Minor Pathway.
R-BTA-72187. mRNA 3'-end processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 1
Alternative name(s):
Splicing factor, arginine/serine-rich 1
Gene namesi
Name:SRSF1
Synonyms:SFRS1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus speckle By similarity

  • Note: In nuclear speckles. Shuttles between the nucleus and the cytoplasm.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 248247Serine/arginine-rich splicing factor 1PRO_0000287724Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineSequence analysisBy similarity
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei38 – 381N6-acetyllysine; alternateBy similarity
Cross-linki38 – 38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei93 – 931Asymmetric dimethylarginineBy similarity
Modified residuei97 – 971Asymmetric dimethylarginineBy similarity
Modified residuei109 – 1091Asymmetric dimethylarginineBy similarity
Modified residuei179 – 1791N6-acetyllysineBy similarity
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei201 – 2011PhosphoserineBy similarity
Modified residuei202 – 2021PhosphotyrosineBy similarity
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei238 – 2381PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed (By similarity).By similarity
Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ0VCY7.
PRIDEiQ0VCY7.

Interactioni

Subunit structurei

Consists of two polypeptides of p32 and p33. In vitro, self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Identified in the spliceosome C complex. Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus) (By similarity). Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1. Interacts with NXF1 (By similarity). Interacts with CCNL1, CCNL2 and CDK11B (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000046374.

Structurei

3D structure databases

ProteinModelPortaliQ0VCY7.
SMRiQ0VCY7. Positions 6-102, 116-197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9176RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini121 – 19575RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 24750Interacts with SAFB1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 11320Gly-rich (hinge region)Add
BLAST
Compositional biasi198 – 24750Arg/Ser-rich (RS domain)Add
BLAST

Domaini

The RRM 2 domain plays an important role in governing both the binding mode and the phosphorylation mechanism of the RS domain by SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly directional (C-terminus to N-terminus) phosphorylation reaction in which the RS domain slides through an extended electronegative channel separating the docking groove of SRPK1 and the active site. RRM 2 binds toward the periphery of the active site and guides the directional phosphorylation mechanism. Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling (By similarity).By similarity

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

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ0VCY7.
KOiK12890.
OMAiYIQVKLD.
OrthoDBiEOG76X620.
TreeFamiTF106261.

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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q0VCY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR
60 70 80 90 100
RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG
110 120 130 140 150
GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA
160 170 180 190 200
DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP
210 220 230 240
SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRT
Length:248
Mass (Da):27,745
Last modified:September 5, 2006 - v1
Checksum:iC28A0B2F112EA713
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC119930 mRNA. Translation: AAI19931.1.
RefSeqiNP_001069862.1. NM_001076394.1.
UniGeneiBt.864.

Genome annotation databases

EnsembliENSBTAT00000049486; ENSBTAP00000046374; ENSBTAG00000014766.
GeneIDi615796.
KEGGibta:615796.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC119930 mRNA. Translation: AAI19931.1.
RefSeqiNP_001069862.1. NM_001076394.1.
UniGeneiBt.864.

3D structure databases

ProteinModelPortaliQ0VCY7.
SMRiQ0VCY7. Positions 6-102, 116-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000046374.

Proteomic databases

PaxDbiQ0VCY7.
PRIDEiQ0VCY7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000049486; ENSBTAP00000046374; ENSBTAG00000014766.
GeneIDi615796.
KEGGibta:615796.

Organism-specific databases

CTDi6426.

Phylogenomic databases

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ0VCY7.
KOiK12890.
OMAiYIQVKLD.
OrthoDBiEOG76X620.
TreeFamiTF106261.

Enzyme and pathway databases

ReactomeiR-BTA-109688. Cleavage of Growing Transcript in the Termination Region.
R-BTA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-BTA-72163. mRNA Splicing - Major Pathway.
R-BTA-72165. mRNA Splicing - Minor Pathway.
R-BTA-72187. mRNA 3'-end processing.

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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal skin.

Entry informationi

Entry nameiSRSF1_BOVIN
AccessioniPrimary (citable) accession number: Q0VCY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: September 5, 2006
Last modified: June 8, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.