a member of the HSP family of molecular chaperones required for endoplasmic reticulum integrity and stress-induced autophagy. Plays a central role in regulating the unfolded protein response (UPR), and is an obligatory component of autophagy in mammalian cells.. May play an important role in cellular adaptation and oncogenic survival. One of the client proteins of GRP78 is protein double-stranded RNA-activated protein-like endoplasmic reticulum kinase (PERK). Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Note: This description may include information from UniProtKB.
Molecular Function: protein domain specific binding; protein binding; chaperone binding; ubiquitin protein ligase binding; ATPase activity; unfolded protein binding; ribosome binding; calcium ion binding; misfolded protein binding; ATP binding
Biological Process: ATP catabolic process; platelet activation; ER-associated protein catabolic process; cerebellum structural organization; unfolded protein response; cerebellar Purkinje cell layer development; cellular response to glucose starvation; unfolded protein response, activation of signaling protein activity; substantia nigra development; cellular protein metabolic process; platelet degranulation; positive regulation of protein ubiquitination; blood coagulation; negative regulation of transforming growth factor beta receptor signaling pathway; ER overload response; negative regulation of apoptosis; positive regulation of cell migration
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.