KH domain-containing, RNA-binding, signal transduction-associated protein 3 (Sam68-like mammalian protein 2, SLM-2, Sam68-like phosphotyrosine protein, RNA-binding protein T-Star, KHDRBS3, SALP, SLM2)

Function: 1) RNA-binding protein 2) role in regulation of alternative splicing 3) influences mRNA splice site selection & exon inclusion - splice site selection of VEGF - induces an increased concentration-dependent incorporation of exon in CD44 pre-mRNA by direct binding to purine-rich exonic enhancer 4) role as a negative regulator of cell growth (putative) 5) inhibits cell proliferation 6) RNA-binding abilities are down-regulated by tyrosine kinase PTK6 7) interacts with splicing regulatory proteins SFRS9, SAFB & YTHDC1 8) interacts with HNRPL & SLM1/KHDRBS2 9) interacts with KHDRBS1, RBMX, RBMY1A1 10) interacts with SH3 domain of PI-3-kinase p85 subunit via proline-rich domain 11) interaction with SIAH1 promotes targeting for degradation 12) phosphorylated on tyrosine residues Structure: - self-associates to form homo-oligomers - isoform 1 C-terminal region is Tyr-rich - isoform 2 lacks this C-terminal region, but is also Tyr-phosphorylated - contains 1 KH domain Compartment: - nucleus - localized in a compartment adjacent to nucleolus Alternative splicing: named isoforms=2 Expression: - ubiquitous - higher expression in testis, skeletal muscle, brain - expressed in kidney only in podocytes, glomerular epithelial cells of the kidney - strongly expressed after meiosis Pathology: - role in post-transcriptional regulation of HIV-1 gene expression - induced in proteinuric diseases - down-regulated in immortalized fibroblasts isolated after a proliferative crisis accompanied with massive cell death

General

nuclear protein phosphoprotein RNA-binding protein

Properties

SIZE: MW = 39 kD entity length = 346 aa COMPARTMENT: cell nucleus MOTIF: KH domain SITE: 61-127 FOR-BINDING-OF: ribonucleic acid interaction with SIAH1 {212-251} proline-rich region SITE: 250-261 MOTIF: proline residue (SEVERAL)

Database Correlations

UniProt O75525 Pfam PF00013

References

UniProt :accession O75525