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Q9D0B0 (SRSF9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 9
Alternative name(s):
Splicing factor, arginine/serine-rich 9
Gene names
Name:Srsf9
Synonyms:Sfrs9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.3

Subcellular location

Nucleus By similarity.

Post-translational modification

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

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
   DomainRepeat
   LigandRNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: Compara

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Serine/arginine-rich splicing factor 9
PRO_0000081936

Regions

Domain15 – 9076RRM 1
Domain112 – 18877RRM 2
Region189 – 20113Interacts with SAFB1 By similarity
Compositional bias92 – 10110Gly-rich (hinge region)
Compositional bias189 – 20113Arg/Ser-rich (RS domain)

Amino acid modifications

Modified residue1901Phosphoserine By similarity
Modified residue1931Phosphotyrosine By similarity
Modified residue1941Phosphoserine By similarity
Modified residue1961Phosphoserine By similarity
Modified residue2051Phosphoserine Ref.6
Modified residue2091Phosphoserine By similarity
Modified residue2121Phosphoserine Ref.4 Ref.5 Ref.6
Modified residue2171Phosphoserine Ref.5 Ref.6

Experimental info

Sequence conflict2091S → N in BAB31986. Ref.1

Secondary structure

............. 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9D0B0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: DF335337335AED19

FASTA22225,661
        10         20         30         40         50         60 
MSSGWADERG GEGDGRIYVG NLPSDVREKD LEDLFYKYGR IREIELKNRH GLVPFAFVRF 

        70         80         90        100        110        120 
EDPRDAEDAI YGRNGYDYGQ CRLRVEFPRT YGGRGGWPRG ARNGPPTRRS DFRVLVSGLP 

       130        140        150        160        170        180 
PSGSWQDLKD HMREAGDVCY ADVQKDGMGM VEYLRKEDME YALRKLDDTK FRSHEGETSY 

       190        200        210        220 
IRVYPERSTS YGYSRSRSGS RGRDSPYQSR GSPHYFSPFR PY 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, MASS SPECTROMETRY.
Tissue: Teratocarcinoma.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-217, MASS SPECTROMETRY.
Tissue: Liver.
[6]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205; SER-212 AND SER-217, MASS SPECTROMETRY.
Tissue: Melanoma.
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK011621 mRNA. Translation: BAB27740.1.
AK020084 mRNA. Translation: BAB31986.1.
BC012217 mRNA. Translation: AAH12217.1.
IPIIPI00132340.
RefSeqNP_079849.1. NM_025573.3.
UniGeneMm.287826.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WG4NMR-A104-188[»]
ProteinModelPortalQ9D0B0.
SMRQ9D0B0. Positions 10-98, 105-189.
ModBaseSearch...

PTM databases

PhosphoSiteQ9D0B0.

Proteomic databases

PaxDbQ9D0B0.
PRIDEQ9D0B0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031513; ENSMUSP00000031513; ENSMUSG00000029538.
GeneID108014.
KEGGmmu:108014.
UCSCuc008zdq.1. mouse.

Organism-specific databases

CTD8683.
MGIMGI:104896. Srsf9.

Phylogenomic databases

eggNOGCOG0724.
GeneTreeENSGT00700000104103.
HOVERGENHBG002295.
InParanoidQ9D0B0.
KOK12890.
OMADIREHEI.

Gene expression databases

ArrayExpressQ9D0B0.
BgeeQ9D0B0.
CleanExMM_SFRS9.
GenevestigatorQ9D0B0.
GermOnlineENSMUSG00000029538. Mus musculus.

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

EvolutionaryTraceQ9D0B0.
NextBio359885.
SOURCESearch...

Entry information

Entry nameSRSF9_MOUSE
AccessionPrimary (citable) accession number: Q9D0B0
Secondary accession number(s): Q9CRN3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families