Cirbp
Domain
Both the RRM domain and the arginine, glycine (RGG) rich domain are necessary for binding to the TXN 3'-untranslated region (By similarity). Both the RRM domain and the arginine, glycine (RGG) rich domain (RGG repeats) are necessary for optimal recruitment into SGs upon cellular stress. The C-terminal domain containing RGG repeats is necessary for translational repression.
Function
Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN.
Post-translational modifications
Methylated on arginine residues. Methylation of the RGG motifs is a prerequisite for recruitment into SGs.
Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by GSK3B increases RNA-binding activity to the TXN 3'-UTR transcript upon exposure to UV radiation (By similarity).
Tissue Specificity
Ubiquitous.
Cellular localization
- Nucleus
- Nucleoplasm
- Cytoplasm
- Translocates from the nucleus to the cytoplasm after exposure to UV radiation (By similarity). Translocates from the nucleus to the cytoplasm into stress granules upon various cytoplasmic stresses, such as osmotic and heat shocks. Its recruitment into stress granules occurs in the absence of TIAR proteins.
Alternative names
Cirp, Cirbp, Cold-inducible RNA-binding protein, A18 hnRNP, Glycine-rich RNA-binding protein CIRP