RNA-binding protein 5 (RBM5), also known as LUCA15, is a component of complexes involved in 3' splice site recognition and regulates alternative splicing of apoptosis-related genes, including the Fas receptor, c-FLIP []and caspase 2 []. In the case of FAS, it promotes exclusion of exon 6 thereby producing a soluble form of FAS that inhibits apoptosis [, ]. In the case of CASP2/caspase-2, it promotes exclusion of exon 9 thereby producing a catalytically active form of CASP2/Caspase-2 that induces apoptosis [].
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.
RNA-binding protein 6 (RBM6) contains two RNA-binding motifs and shares protein sequence similarity with RBM5 []. RBM6 is targeted to the splicing speckles and nascent transcripts []. It may act mainly as a splicing activator []. The elevated expression of RBM6 has been linked to certain tumours []. A RBM6-CSF1R fusion has been found in acute megakaryoblastic leukemia [].
RNA-binding protein 6 (RBM6) contains two RNA-binding motifs and shares protein sequence similarity with RBM5 []. RBM6 is targeted to the splicing speckles and nascent transcripts []. It may act mainly as a splicing activator []. The elevated expression of RBM6 has been linked to certain tumours []. A RBM6-CSF1R fusion has been found in acute megakaryoblastic leukemia [].RBM6 contains two RNA recognition motifs (RRMs), an OCtamer REpeat (OCRE) domain, two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain. In contrast to RBM5, RBM6 has an additional unique domain, the POZ (poxvirus andzinc finger) domain, which may be involved in protein-protein interactions and inhibit binding of target sequences by zinc fingers. This entry represents the OCRE domain.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 [].
This entry represents the RNA recognition motif 1 (RRM1) of RBM6 (also known as lung cancer antigen NY-LU-12, or protein G16, or RNA-binding protein DEF-3), which has been predicted to be a nuclear factor based on its nuclear localization signal [, , ]. RBM6 shows high sequence similarity to RNA-binding protein 5 (RBM5). Both RBM6 and RBM5 specifically bind poly(G) RNA. They contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain. In contrast to RBM5, RBM6 has two additional unique domains: the decamer repeat occurring more than 20 times, and the POZ (poxvirus and zinc finger) domain. The POZ domain may be involved in protein-protein interactions and inhibit binding of target sequences by zinc fingers [, , ].
This entry represents the RNA recognition motif 2 (RRM2) of RBM6 (also known as lung cancer antigen NY-LU-12, or protein G16, or RNA-binding protein DEF-3), which has been predicted to be a nuclear factor based on its nuclear localization signal [, , ]. RBM6 shows high sequence similarity to RNA-binding protein 5 (RBM5). Both RBM6 and RBM5 specifically bind poly(G) RNA. They contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), two C2H2-type zinc fingers, a nuclear localization signal, and a G-patch/D111 domain. In contrast to RBM5, RBM6 has two additional unique domains: the decamer repeat occurring more than 20 times, and the POZ (poxvirus and zinc finger) domain. The POZ domain may be involved in protein-protein interactions and inhibit binding of target sequences by zinc fingers [, , ].
