RNA-binding motif protein 10 (RBM10)

RNA-binding motif protein 10 (RBM10) is a nuclear RNA-binding protein characterized by the presence of two RNA recognition motifs (RRMs), two zinc finger domains, and a G patch motif[1][4]. It is expressed throughout a wide range of human tissues and is involved primarily in the regulation of alternative splicing—the process by which exons are selectively included or excluded from pre-mRNA, thereby generating diverse mRNA isoforms[1][3][4]. RBM10 is known to promote exon skipping through direct binding at splice sites, affecting the expression and function of genes involved in cell proliferation, apoptosis, and development[1][3][4]. RBM10 has also been implicated in mRNA stabilization, regulation of non-coding RNAs, and the cellular response to stress[2][3]. Loss-of-function mutations in RBM10 cause the congenital disorder TARP syndrome, while aberrant expression or mutation is associated with multiple forms of cancer, where RBM10 generally acts as a tumor suppressor but may have context-dependent, pro-tumorigenic effects[2][4]. RBM10 is an established component of the spliceosome complex and interacts with multiple spliceosomal proteins, reflecting its central role in RNA metabolism[4]. No direct, approved drugs are known to target RBM10; however, its regulatory roles in disease suggest it may be a relevant biomarker or future therapeutic target in oncology and rare congenital syndromes[2][4].

Other names

Ribosome biogenesis inhibitor MINAS-60MINAS-60RNA-binding protein 10DXS8237EGPATC9GPATCH9KIAA0122S1-1ZRANB5G patch domain-containing protein 9zinc finger RANBP2-type containing 5TARPSepididymis secretory sperm binding protein