RNA-binding motif protein 25 (RBM25)

RNA-binding motif protein 25 (RBM25) is an evolutionarily conserved nuclear RNA-binding protein involved in the regulation of alternative pre-mRNA splicing. It acts as a global splicing factor, influencing the inclusion or exclusion of large numbers of cassette exons across the human genome and interacting with core spliceosome components. RBM25 is crucial for proper cell viability and regulates apoptosis by controlling the splicing of BCL2L1 (Bcl-x), shifting the balance toward the pro-apoptotic Bcl-xS isoform. Its actions mediating alternative splicing also impact the MYC oncogene in acute myeloid leukemia. Disruption or misregulation of RBM25-driven splicing events has been implicated in cancer, cardiovascular disease, and may have broader relevance to neurodegenerative disorders. RBM25 contains a PWI domain that creates a unique nucleic acid binding platform and can be regulated by lysine methylation, which modulates interactions with other splicing factors such as SRSF2. RBM25 is not currently a direct drug target but is pivotal as a molecular regulator in health and disease.

Other names

RNA-binding protein 25RNPC7RED120S164fSAP94NET52Snu71Arg/Glu/Asp-rich protein of 120 kDaProtein S164RNA-binding region-containing protein 7Functional spliceosome-associated protein 94U1 small nuclear ribonucleoprotein 1SNRP homolog

Not applicable; no drugs are documented to directly target RBM25. Drugs affecting splicing in general (e.g., spliceosome inhibitors) may theoretically affect RBM25 indirectly.