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Protein

KH domain-containing, RNA-binding, signal transduction-associated protein 3

Gene

Khdrbs3

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

Functioni

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.1 Publication

GO - Molecular functioni

  • RNA binding Source: UniProtKB
  • single-stranded RNA binding Source: RGD

GO - Biological processi

  • mRNA processing Source: RGD
  • positive regulation of RNA splicing Source: RGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
KH domain-containing, RNA-binding, signal transduction-associated protein 3
Alternative name(s):
Sam68-like mammalian protein 2
Short name:
SLM-2
Short name:
rSLM-2
Gene namesi
Name:Khdrbs3
Synonyms:Slm2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620921. Khdrbs3.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346KH domain-containing, RNA-binding, signal transduction-associated protein 3PRO_0000232524Add
BLAST

Post-translational modificationi

Phosphorylated on tyrosine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JLP1.
PRIDEiQ9JLP1.

PTM databases

iPTMnetiQ9JLP1.
PhosphoSiteiQ9JLP1.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in brain, heart, testis and in Sertoli cells at all stages of spermatogenesis. Expressed in neurons. Detected in cortical layers of the forebrain and in the CA1 to CA4 regions of the hippocampus.2 Publications

Interactioni

Subunit structurei

Self-associates to form homooligomers. Interacts with KHDRBS1, RBMX, RBMY1A1 and with p85 subunit of PI3-kinase (By similarity). Interacts with the splicing regulatory proteins SFRS9, SAFB and YTHDC1. Interacts also with HNRPL and SLM1.By similarity2 Publications

Protein-protein interaction databases

BioGridi248934. 10 interactions.
STRINGi10116.ENSRNOP00000012753.

Structurei

3D structure databases

ProteinModelPortaliQ9JLP1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 12767KHAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi250 – 26112Pro-richAdd
BLAST
Compositional biasi266 – 31651Tyr-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the KHDRBS family.Curated
Contains 1 KH domain.Curated

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiKOG1588. Eukaryota.
COG5176. LUCA.
HOGENOMiHOG000230771.
HOVERGENiHBG079164.
InParanoidiQ9JLP1.
KOiK14942.
PhylomeDBiQ9JLP1.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR032571. Qua1_dom.
IPR032335. Sam68-YY.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
PF16274. Qua1. 1 hit.
PF16568. Sam68-YY. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9JLP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKYLPELM AEKDSLDPSF THALRLVNRE IEKFQKGEAK DEEKYIDVVI
60 70 80 90 100
NKNMKLGQKV LIPVKQFPKF NFVGKLLGPR GNSLKRLQEE TLTKMSILGK
110 120 130 140 150
GSMRDKAKEE ELRKSGEAKY FHLNDDLHVL IEVFAPPAEA YARMGHALED
160 170 180 190 200
IKKFLIPDYN DEIRQAQLQE LTYLNGGSEN ADVPVVRGKS TLRTRGVTTP
210 220 230 240 250
AITRGRGGVT ARPVAVGVPR GTPTPRGVLS TRGPVSRGRG LLTPRARGVP
260 270 280 290 300
PTGYRPPPPP PTQETYGEYD YDDGYSTAYD DQSYDSYDNS YSTPAQSGAD
310 320 330 340
YYDYGHGLGE EAYDSYGQED WTNSRHKAPS ARTAKGVYRE QPYGRY
Length:346
Mass (Da):38,779
Last modified:October 1, 2000 - v1
Checksum:iE218071BE6615544
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152547 mRNA. Translation: AAF73222.1.
RefSeqiNP_071585.1. NM_022249.1.
UniGeneiRn.229046.

Genome annotation databases

GeneIDi64015.
KEGGirno:64015.
UCSCiRGD:620921. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF152547 mRNA. Translation: AAF73222.1.
RefSeqiNP_071585.1. NM_022249.1.
UniGeneiRn.229046.

3D structure databases

ProteinModelPortaliQ9JLP1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248934. 10 interactions.
STRINGi10116.ENSRNOP00000012753.

PTM databases

iPTMnetiQ9JLP1.
PhosphoSiteiQ9JLP1.

Proteomic databases

PaxDbiQ9JLP1.
PRIDEiQ9JLP1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64015.
KEGGirno:64015.
UCSCiRGD:620921. rat.

Organism-specific databases

CTDi10656.
RGDi620921. Khdrbs3.

Phylogenomic databases

eggNOGiKOG1588. Eukaryota.
COG5176. LUCA.
HOGENOMiHOG000230771.
HOVERGENiHBG079164.
InParanoidiQ9JLP1.
KOiK14942.
PhylomeDBiQ9JLP1.

Miscellaneous databases

NextBioi612594.
PROiQ9JLP1.

Family and domain databases

Gene3Di3.30.1370.10. 1 hit.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR032571. Qua1_dom.
IPR032335. Sam68-YY.
[Graphical view]
PfamiPF00013. KH_1. 1 hit.
PF16274. Qua1. 1 hit.
PF16568. Sam68-YY. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 1 hit.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH HNRPL; SFRS9; SAFB AND YTHDC1.
    Tissue: Brain.
  2. "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] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Testis.
  3. "p59(fyn)-mediated phosphorylation regulates the activity of the tissue-specific splicing factor rSLM-1."
    Stoss O., Novoyatleva T., Gencheva M., Olbrich M., Benderska N., Stamm S.
    Mol. Cell. Neurosci. 27:8-21(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLM1, TISSUE SPECIFICITY.

Entry informationi

Entry nameiKHDR3_RAT
AccessioniPrimary (citable) accession number: Q9JLP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 91 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.