This entry represents the RNA recognition motif (RRM) domain of two structurally related heterogenous nuclear ribonucleoproteins, CIRBP (also known as CIRP) and RBM3, both of which belong to a highly conserved cold shock proteins family, characterised by an N-terminal RNA-binding domain and a C-terminal arginine-glycine-rich (RGG) domain []. CIRBP and RBM3 are key factors during early development. They can be induced after exposure to a moderate cold-shock and other cellular stresses such as UV radiation and hypoxia. Despite the similarities between both CIRBP and RBM3 proteins, their biological functions are distinct []. CIRBP is involved in diverse cellular physiological processes, such as cell growth, senescence, and apoptosis. CIRBP has the capacity to bind RNAs, and to modulate them at the post-transcriptional level. For instance, upon UV irradiation, CIRP binds to the 3'-UTR of two stress-responsive transcripts, replication protein A (RPA) and thioredoxin (TRX), thereby stabilizing the bound mRNA and promoting their translation [, ]. RBM3 has certain functions such as anti-apoptotic, cell proliferation enhancement, and a proto-oncogene function []. It can bind to and alter the translation of mRNA []. It associates with the spliceosome and is involved in splicing. It can modulate the translational process and enhances global protein translation. It is also involved in the regulation of miRNA expression [].
