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Q9R226 (KHDR3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
KH domain-containing, RNA-binding, signal transduction-associated protein 3
Alternative name(s):
RNA-binding protein Etoile
Sam68-like mammalian protein 2
Short name=SLM-2
Gene names
Name:Khdrbs3
Synonyms:Salp, Slm2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. May play a role as a negative regulator of cell growth. Inhibits cell proliferation. Involved in splice site selection of vascular endothelial growth factor. Induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer. RNA-binding abilities are down-regulated by tyrosine kinase PTK6. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. Ref.4

Subunit structure

Self-associates to form homooligomers. Interacts with the splicing regulatory proteins SFRS9, SAFB and YTHDC1. Interacts also with HNRPL and SLM1/KHDRBS2. Interacts with KHDRBS1, RBMX, RBMY1A1 and with p85 subunit of PI3-kinase By similarity.

Subcellular location

Nucleus. Note: Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one. Ref.1 Ref.4

Tissue specificity

Highly expressed in testis. Ref.1 Ref.4

Domain

The proline-rich site binds the SH3 domain of the p85 subunit of PI3-kinase.

Post-translational modification

Phosphorylated on tyrosine residues by PTK6. Ref.4

Sequence similarities

Belongs to the KHDRBS family.

Contains 1 KH domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainSH3-binding
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionSH3 domain binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346KH domain-containing, RNA-binding, signal transduction-associated protein 3
PRO_0000232523

Regions

Domain61 – 12767KH
Compositional bias250 – 26112Pro-rich
Compositional bias266 – 31651Tyr-rich

Amino acid modifications

Modified residue51Phosphotyrosine By similarity

Experimental info

Mutagenesis215 – 2173AVG → GVV: Confers SIAH1-mediated degradation and strong SIAH1 binding. Ref.3
Sequence conflict1601N → Y in AAC31753. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R226 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: F061C85FC698FF40

FASTA34638,807
        10         20         30         40         50         60 
MEEKYLPELM AEKDSLDPSF THALRLVNRE IEKFQKGEGK EEEKYIDVVI NKNMKLGQKV 

        70         80         90        100        110        120 
LIPVKQFPKF NFVGKLLGPR GNSLKRLQEE TLTKMSILGK GSMRDKAKEE ELRKSGEAKY 

       130        140        150        160        170        180 
FHLNDDLHVL IEVFAPPAEA YARMGHALEE IKKFLIPDYN DEIRQAQLQE LTYLNGGSEN 

       190        200        210        220        230        240 
ADVPVVRGKS TLRTRGVTTP AITRGRGGVT ARPVAVGVPR GTPTPRGVLS TRGPVSRGRG 

       250        260        270        280        290        300 
LLTPRARGVP PTGYRPPPPP PTQETYGEYD YDDGYGTAYD EQSYDSYDNS YSTPAQSAAD 

       310        320        330        340 
YYDYGHGLSE DAYDSYGQEE WTNSRHKAPS ARTAKGVYRD QPYGRY 

« Hide

References

[1]"T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis."
Venables J.P., Vernet C., Chew S.L., Elliott D.J., Cowmeadow R.B., Wu J., Cooke H.J., Artzt K., Eperon I.C.
Hum. Mol. Genet. 8:959-969(1999) [PubMed: 10332027] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis."
Di Fruscio M., Chen T., Richard S.
Proc. Natl. Acad. Sci. U.S.A. 96:2710-2715(1999) [PubMed: 10077576] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome."
Venables J.P., Dalgliesh C., Paronetto M.P., Skitt L., Thornton J.K., Saunders P.T., Sette C., Jones K.T., Elliott D.J.
Hum. Mol. Genet. 13:1525-1534(2004) [PubMed: 15163637] [Abstract]
Cited for: MUTAGENESIS OF 215-ALA--GLY-217.
[4]"The nuclear tyrosine kinase BRK/Sik phosphorylates and inhibits the RNA-binding activities of the Sam68-like mammalian proteins SLM-1 and SLM-2."
Haegebarth A., Heap D., Bie W., Derry J.J., Richard S., Tyner A.L.
J. Biol. Chem. 279:54398-54404(2004) [PubMed: 15471878] [Abstract]
Cited for: PHOSPHORYLATION BY PTK6, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF079763 mRNA. Translation: AAC31753.1.
AF099092 mRNA. Translation: AAC72396.1.
BC031507 mRNA. Translation: AAH31507.1.
BC057577 mRNA. Translation: AAH57577.1.
IPIIPI00314520.
RefSeqNP_034288.2. NM_010158.2.
UniGeneMm.17964.

3D structure databases

ProteinModelPortalQ9R226.
SMRQ9R226. Positions 2-37, 55-185.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9R226. 1 interaction.
STRINGQ9R226.

PTM databases

PhosphoSiteQ9R226.

Proteomic databases

PRIDEQ9R226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022954; ENSMUSP00000022954; ENSMUSG00000022332.
GeneID13992.
KEGGmmu:13992.
UCSCuc007wbf.1. mouse.

Organism-specific databases

CTD10656.
MGIMGI:1313312. Khdrbs3.

Phylogenomic databases

eggNOGroNOG08706.
GeneTreeENSGT00550000074434.
HOGENOMHBG713086.
HOVERGENHBG079164.
InParanoidQ9R226.
OMAGEYEYDD.
OrthoDBEOG4DBTFN.
PhylomeDBQ9R226.

Gene expression databases

ArrayExpressQ9R226.
BgeeQ9R226.
GenevestigatorQ9R226.
GermOnlineENSMUSG00000022332. Mus musculus.

Family and domain databases

InterProIPR004087. KH.
[Graphical view]
KOK14942.
SMARTSM00322. KH. 1 hit.
[Graphical view]
PROSITEPS50084. KH_TYPE_1. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio284872.
SOURCESearch...

Entry information

Entry nameKHDR3_MOUSE
AccessionPrimary (citable) accession number: Q9R226
Secondary accession number(s): O88624
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: May 1, 2000
Last modified: November 16, 2011
This is version 77 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

SIMILARITY comments

Index of protein domains and families