InterPro domain: IPR034268

This entry represents the RNA recognition motif (RRM) of RBM25, which is a RNA-binding protein that acts as a regulator of alternative pre-mRNA splicing. It localizes to the nuclear speckles and associates with multiple splicing components, including splicing cofactors SRm160/300, U snRNAs, assembled splicing complexes, and spliced mRNAs. It may play an important role in pre-mRNA processing by coupling splicing with mRNA 3'-end formation. It can activate proapoptotic Bcl-xS 5'ss by binding to the exonic splicing enhancer, CGGGCA, and stabilize the pre-mRNA-U1 snRNP through interaction with hLuc7A, a U1 snRNP-associated factor [ 1 ]. It has been shown to function in cardiac sodium channel splicing regulation of human heart failure [ 2 , 3 ].

RBM25 contains a well conserved RNA recognition motif (RRM), at the N terminus, a RE/RD-rich (ER) central region, and a C-terminal proline-tryptophan-isoleucine (PWI) motif.

Proteins containing this domain include Usp107 from S. pombe. Usp107 is a component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA [ 4 ].

1. Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site selection. Mol. Cell. Biol. 28, 5924-36
2. Role of RBM25/LUC7L3 in abnormal cardiac sodium channel splicing regulation in human heart failure. Circulation 124, 1124-31
3. RBM25/LUC7L3 function in cardiac sodium channel splicing regulation of human heart failure. Trends Cardiovasc. Med. 23, 5-8
4. Proteomic analysis of the U1 snRNP of Schizosaccharomyces pombe reveals three essential organism-specific proteins. Nucleic Acids Res. 35, 1391-401