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Protein

Serine/arginine-rich splicing factor 9

Gene

Srsf9

Organism
Mus musculus (Mouse)
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

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:104896. Srsf9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Serine/arginine-rich splicing factor 9PRO_0000081936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei193 – 1931PhosphotyrosineBy similarity
Modified residuei194 – 1941PhosphoserineBy similarity
Modified residuei196 – 1961PhosphoserineBy similarity
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei209 – 2091PhosphoserineBy similarity
Modified residuei212 – 2121PhosphoserineBy similarity
Modified residuei215 – 2151PhosphotyrosineBy similarity
Modified residuei217 – 2171PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9D0B0.
MaxQBiQ9D0B0.
PaxDbiQ9D0B0.
PeptideAtlasiQ9D0B0.
PRIDEiQ9D0B0.

PTM databases

iPTMnetiQ9D0B0.
PhosphoSiteiQ9D0B0.

Expressioni

Gene expression databases

BgeeiQ9D0B0.
CleanExiMM_SFRS9.
ExpressionAtlasiQ9D0B0. baseline and differential.
GenevisibleiQ9D0B0. MM.

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

IntActiQ9D0B0. 2 interactions.
MINTiMINT-4126379.
STRINGi10090.ENSMUSP00000031513.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi113 – 1175Combined sources
Helixi125 – 1328Combined sources
Beta strandi138 – 1447Combined sources
Turni145 – 1473Combined sources
Beta strandi148 – 1558Combined sources
Helixi156 – 16611Combined sources
Beta strandi167 – 1726Combined sources
Beta strandi178 – 1847Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WG4NMR-A104-188[»]
ProteinModelPortaliQ9D0B0.
SMRiQ9D0B0. Positions 10-98, 105-189.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D0B0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 9076RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 18877RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni189 – 20113Interacts with SAFB1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 10110Gly-rich (hinge region)
Compositional biasi189 – 20113Arg/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.
InParanoidiQ9D0B0.
KOiK12890.
OMAiTHERNSQ.
OrthoDBiEOG76X620.
PhylomeDBiQ9D0B0.
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.

Q9D0B0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGWADERG GEGDGRIYVG NLPSDVREKD LEDLFYKYGR IREIELKNRH
60 70 80 90 100
GLVPFAFVRF EDPRDAEDAI YGRNGYDYGQ CRLRVEFPRT YGGRGGWPRG
110 120 130 140 150
ARNGPPTRRS DFRVLVSGLP PSGSWQDLKD HMREAGDVCY ADVQKDGMGM
160 170 180 190 200
VEYLRKEDME YALRKLDDTK FRSHEGETSY IRVYPERSTS YGYSRSRSGS
210 220
RGRDSPYQSR GSPHYFSPFR PY
Length:222
Mass (Da):25,661
Last modified:June 1, 2001 - v1
Checksum:iDF335337335AED19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091S → N in BAB31986 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011621 mRNA. Translation: BAB27740.1.
AK020084 mRNA. Translation: BAB31986.1.
BC012217 mRNA. Translation: AAH12217.1.
CCDSiCCDS19587.1.
RefSeqiNP_079849.1. NM_025573.3.
UniGeneiMm.287826.

Genome annotation databases

EnsembliENSMUST00000031513; ENSMUSP00000031513; ENSMUSG00000029538.
GeneIDi108014.
KEGGimmu:108014.
UCSCiuc008zdq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011621 mRNA. Translation: BAB27740.1.
AK020084 mRNA. Translation: BAB31986.1.
BC012217 mRNA. Translation: AAH12217.1.
CCDSiCCDS19587.1.
RefSeqiNP_079849.1. NM_025573.3.
UniGeneiMm.287826.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WG4NMR-A104-188[»]
ProteinModelPortaliQ9D0B0.
SMRiQ9D0B0. Positions 10-98, 105-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D0B0. 2 interactions.
MINTiMINT-4126379.
STRINGi10090.ENSMUSP00000031513.

PTM databases

iPTMnetiQ9D0B0.
PhosphoSiteiQ9D0B0.

Proteomic databases

EPDiQ9D0B0.
MaxQBiQ9D0B0.
PaxDbiQ9D0B0.
PeptideAtlasiQ9D0B0.
PRIDEiQ9D0B0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031513; ENSMUSP00000031513; ENSMUSG00000029538.
GeneIDi108014.
KEGGimmu:108014.
UCSCiuc008zdq.1. mouse.

Organism-specific databases

CTDi8683.
MGIiMGI:104896. Srsf9.

Phylogenomic databases

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ9D0B0.
KOiK12890.
OMAiTHERNSQ.
OrthoDBiEOG76X620.
PhylomeDBiQ9D0B0.
TreeFamiTF106261.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9D0B0.
PROiQ9D0B0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0B0.
CleanExiMM_SFRS9.
ExpressionAtlasiQ9D0B0. baseline and differential.
GenevisibleiQ9D0B0. MM.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Testis.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "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.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.
  5. "Solution structure of RRM domain in protein BAB31986."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 104-188.

Entry informationi

Entry nameiSRSF9_MOUSE
AccessioniPrimary (citable) accession number: Q9D0B0
Secondary accession number(s): Q9CRN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 120 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.