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Protein

Serine/arginine-rich splicing factor 9

Gene

Srsf9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in constitutive splicing and can modulate the selection of alternative splice sites. Represses the splicing of MAPT/Tau exon 10 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • response to alkaloid Source: RGD
  • response to toxic substance Source: RGD
  • RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 9
Alternative name(s):
Splicing factor, arginine/serine-rich 9
Gene namesi
Name:Srsf9
Synonyms:Sfrs9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi1309495. Srsf9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 221221Serine/arginine-rich splicing factor 9PRO_0000081937Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei189 – 1891PhosphoserineBy similarity
Modified residuei193 – 1931PhosphoserineBy similarity
Modified residuei195 – 1951PhosphoserineBy similarity
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei208 – 2081PhosphoserineBy similarity
Modified residuei211 – 2111PhosphoserineCombined sources
Modified residuei214 – 2141PhosphotyrosineBy similarity
Modified residuei216 – 2161PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5PPI1.
PRIDEiQ5PPI1.

PTM databases

iPTMnetiQ5PPI1.
PhosphoSiteiQ5PPI1.

Expressioni

Gene expression databases

GenevisibleiQ5PPI1. RN.

Interactioni

Subunit structurei

Interacts with NOL3/ARC/NOP30, NSEP1/YB-1/YB1, SAFB/SAFB1, SRSF6/SFRS6, TRA2B/SFRS10 and C1QBP. May also interact with DUSP11/PIR1 (By similarity). Interacts with KHDRBS3/SLM-2.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001539.

Structurei

3D structure databases

ProteinModelPortaliQ5PPI1.
SMRiQ5PPI1. Positions 9-99, 104-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 8976RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini111 – 18777RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 20013Interacts with SAFB1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi91 – 10010Gly-rich (hinge region)
Compositional biasi188 – 20013Arg/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

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ5PPI1.
KOiK12890.
OMAiTHERNSQ.
OrthoDBiEOG76X620.
PhylomeDBiQ5PPI1.
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.

Q5PPI1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGWADERGG EGDGRIYVGN LPTDVREKDL EDLFYKYGRI REIELKNRHG
60 70 80 90 100
LVPFAFVRFE DPRDAEDAIY GRNGYDYGQC RLRVEFPRAY GGRGGWPRAS
110 120 130 140 150
RNGPPTRRSD FRVLVSGLPP SGSWQDLKDH MREAGDVCYA DVQKDGMGMV
160 170 180 190 200
EYLRKEDMEY ALRKLDDTKF RSHEGETSYI RVYPERGTSY GCSRSRSGSR
210 220
GRDSPYQSRG SPHYFSPFRP Y
Length:221
Mass (Da):25,498
Last modified:January 4, 2005 - v1
Checksum:i1B4E6F847D7A97A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087684 mRNA. Translation: AAH87684.1.
RefSeqiNP_001009255.1. NM_001009255.1.
UniGeneiRn.136718.

Genome annotation databases

EnsembliENSRNOT00000001539; ENSRNOP00000001539; ENSRNOG00000001163.
GeneIDi288701.
KEGGirno:288701.
UCSCiRGD:1309495. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087684 mRNA. Translation: AAH87684.1.
RefSeqiNP_001009255.1. NM_001009255.1.
UniGeneiRn.136718.

3D structure databases

ProteinModelPortaliQ5PPI1.
SMRiQ5PPI1. Positions 9-99, 104-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001539.

PTM databases

iPTMnetiQ5PPI1.
PhosphoSiteiQ5PPI1.

Proteomic databases

PaxDbiQ5PPI1.
PRIDEiQ5PPI1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001539; ENSRNOP00000001539; ENSRNOG00000001163.
GeneIDi288701.
KEGGirno:288701.
UCSCiRGD:1309495. rat.

Organism-specific databases

CTDi8683.
RGDi1309495. Srsf9.

Phylogenomic databases

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ5PPI1.
KOiK12890.
OMAiTHERNSQ.
OrthoDBiEOG76X620.
PhylomeDBiQ5PPI1.
TreeFamiTF106261.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi628577.
PROiQ5PPI1.

Gene expression databases

GenevisibleiQ5PPI1. RN.

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

« Hide 'large scale' publications
  1. "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: Ovary.
  2. "The STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sites."
    Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A., Stamm S.
    J. Biol. Chem. 276:8665-8673(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KHDRBS3.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204; SER-211 AND SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRSF9_RAT
AccessioniPrimary (citable) accession number: Q5PPI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: January 4, 2005
Last modified: May 11, 2016
This is version 92 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.