NCBI and Uniprot Product Information
NCBI Description
The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.[provided by RefSeq, Sep 2010]
Uniprot Description
GRP78: 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.
Protein type: Heat shock protein; Chaperone
Chromosomal Location of Human Ortholog: 9q33.3
Cellular Component: cell surface; endoplasmic reticulum; endoplasmic reticulum lumen; endoplasmic reticulum membrane; ER-Golgi intermediate compartment; focal adhesion; integral to endoplasmic reticulum membrane; melanosome; membrane; midbody; mitochondrion; myelin sheath; nucleus; plasma membrane; signalosome; smooth endoplasmic reticulum
Molecular Function: ATP binding; ATPase activity; calcium ion binding; chaperone binding; enzyme binding; glycoprotein binding; misfolded protein binding; protein binding; protein domain specific binding; ribosome binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: cellular response to glucose starvation; cerebellar Purkinje cell layer development; cerebellum structural organization; ER overload response; ER-associated protein catabolic process; negative regulation of apoptosis; negative regulation of transforming growth factor beta receptor signaling pathway; positive regulation of cell migration; positive regulation of protein ubiquitination; substantia nigra development; unfolded protein response; unfolded protein response, activation of signaling protein activity