Protein Domain : RBM3/CIRBP, RNA recognition motif IPR034278

Type	Domain
Description	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 [].
Short Name	RBM3/CIRBP_RRM