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KH domain containing, RNA binding, signal transduction associated protein 1 (p21 Ras GTPase-activating protein-associated p62, GAP-associated tyrosine phosphoprotein p62, src-associated in mitosis 68 kD protein, Sam68, p68, KHDRBS1)
Function:
1) recruited & tyrosine phosphorylated by:
a) tyrosine kinase receptors
- T-cell receptor, leptin receptor, insulin receptor
b) non-receptor tyrosine kinases
- LCK, FYN JAK3
2) tyrosine phosphorylated form functions as an adapter protein in signal transduction by binding to SH2 & SH3 domain- containing proteins
3) role in G2-M progression in the cell cycle
4) phosphorylated on Tyr during mitosis
5) binds to src through pTyr-SH2 interaction
6) may be sequestered in the nucleus of interphase cells
- able to interact with src only after breakdown of the nuclear envelope
7) represses CBP-dependent transcriptional activation
8) putative regulator of mRNA stability
9) mediates mRNA nuclear export
10) tyrosine phosphorylation negatively regulates RNA binding
11) isoform 3 is only expressed in growth-arrested cells
- inhibits S phase entry
Structure:
- self-associates to form homo-oligomers when bound to RNA
- KH domain is required for binding to RNA
- acetylatation needed for RNA-binding
Alternative splicing: named isoforms=3
Expression: ubiquitously expressed in all tissue examined
General
phosphoprotein
Properties
SIZE: entity length = 443 aa
MW = 48 kD
COMPARTMENT: cell nucleus
MOTIF: Ser phosphorylation site {S15}
Ser phosphorylation site {S18}
Ser phosphorylation site {S20}
Ser phosphorylation site {S29}
Thr phosphorylation site {T33}
proline-rich region
SITE: 34-41
MOTIF: proline residue (SEVERAL)
glycine-rich region {44-55}
Ser phosphorylation site {S58}
proline-rich region
SITE: 59-89
MOTIF: proline residue (SEVERAL)
Ser phosphorylation site {S113}
KH domain
SITE: 171-197
FOR-BINDING-OF: ribonucleic acid
glycine-rich region {282-292}
proline-rich region
SITE: 295-301
MOTIF: proline residue (SEVERAL)
glycine-rich region {302-332}
proline-rich region
SITE: 334-363
MOTIF: proline residue (SEVERAL)
Database Correlations
OMIM 602489
UniProt Q07666
Pfam PF00013
Entrez Gene 10657
Kegg hsa:10657
References
- UniProt :accession Q07666
- Pawson T.
Protein modules and signalling networks.
Nature. 1995 Feb 16;373(6515):573-80. Review.
PMID: 7531822