InterPro domain: IPR034201

This entry represents the RNA recognition motif (RRM) of RNPS1 and its eukaryotic homologues. RNPS1 was originally characterised as a general pre-mRNA splicing activator, which activates both constitutive and alternative splicing of pre-mRNA in vitro [ 1 ]. It has been identified as a protein component of the splicing-dependent mRNP complex, or exon-exon junction complex (EJC), and is directly involved in mRNA surveillance [ 2 , 3 ]. Furthermore, RNPS1 is a splicing regulator whose activator function is controlled in part by CK2 (casein kinase II) protein kinase phosphorylation [ 4 ]. It can also function as a squamous-cell carcinoma antigen recognized by T cells-3 (SART3)-binding protein, and is involved in the regulation of mRNA splicing [ 5 ]. RNPS1 contains an N-terminal serine-rich (S) domain, a central RNA recognition motif (RRM), and the C-terminal arginine/serine/proline-rich (R/S/P) domain.

1. Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing. EMBO J. 18, 4560-70
2. Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science 293, 1836-9
3. The abundance of RNPS1, a protein component of the exon junction complex, can determine the variability in efficiency of the Nonsense Mediated Decay pathway. Nucleic Acids Res. 35, 4542-51
4. Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation. Mol. Cell. Biol. 25, 1446-57
5. Binding of a SART3 tumor-rejection antigen to a pre-mRNA splicing factor RNPS1: a possible regulation of splicing by a complex formation. Int. J. Cancer 93, 623-8