Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.
Belongs to the NAC-alpha family. Contains 1 NAC-A/B (NAC-alpha/beta) domain. Contains 1 UBA domain.
Phosphorylation of Ser-43 by ILK during cell adhesion may promote nuclear localization. Phosphorylation of Thr-159 by GSK3B may promote proteasome mediated degradation (By similarity). Phosphorylated upon DNA damage, probably by ATM or ATR.
Cytoplasm. Nucleus. Predominantly cytoplasmic. Also found in nucleus.