RBM10, also known as S1-1, is a nuclear RNA-binding protein with domains characteristic of RNA processing proteins. Similar to RBM5, it promotes exon skipping of Fas pre-mRNA as well as selection of an internal 5'-splice site in Bcl-x pre-mRNA []. It preferentially binds to G- and U-rich RNA sequences [].
The OCtamer REpeat (OCRE) has been annotated as a 42-residue sequence motif with 12 tyrosine residues in the spliceosome trans-regulatory elements RBM5 and RBM10 (RBM [RNA-binding motif]), which are known to regulate alternative splicing of Fas and Bcl-x pre-mRNA transcripts []. The structure of the domain consists of an anti-parallel arrangement of six beta strands.
RBM10 contains two N-terminal RNA recognition motifs (RRMs) and an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, and a G-patch/D111 domain. This entry represents the OCRE domain.RBM10, also known as S1-1, is a nuclear RNA-binding protein with domains characteristic of RNA processing proteins.Similar to RBM5, it promotes exon skipping of Fas pre-mRNA as well as selection of an internal 5'-splice site in Bcl-x pre-mRNA []. It preferentially binds to G- and U-rich RNA sequences [].The OCRE (OCtamer REpeat) domain contains five repeats of an 8-residue motif, which were shown to form β-strands. Based on the architectures of proteins containing OCRE domains, a role in RNA metabolism and/or signalling has been proposed [].
