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. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein
Chromosomal Location of Human Ortholog: 2 B|2 22.94 cM
Cellular Component:  cell surface; cytoplasm; cytosol; endoplasmic reticulum; endoplasmic reticulum chaperone complex; endoplasmic reticulum lumen; endoplasmic reticulum membrane; endoplasmic reticulum-Golgi intermediate compartment; integral component of endoplasmic reticulum membrane; intracellular membrane-bounded organelle; membrane; midbody; mitochondrion; nucleus; plasma membrane; protein-containing complex; smooth endoplasmic reticulum
Molecular Function:  ATP binding; ATPase activity; ATPase activity, coupled; enzyme binding; heat shock protein binding; hydrolase activity; misfolded protein binding; nucleotide binding; protein binding; protein binding involved in protein folding; protein domain specific binding; ribosome binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process:  cellular response to glucose starvation; cellular response to heat; cellular response to interleukin-4; cellular response to unfolded protein; cerebellar Purkinje cell layer development; cerebellum structural organization; chaperone cofactor-dependent protein refolding; endoplasmic reticulum unfolded protein response; ER overload response; maintenance of protein localization in endoplasmic reticulum; negative regulation of apoptotic process; negative regulation of transforming growth factor beta receptor signaling pathway; positive regulation of cell migration; positive regulation of embryonic development; positive regulation of neuron projection development; positive regulation of protein ubiquitination; posttranslational protein targeting to membrane, translocation; protein refolding; proteolysis involved in cellular protein catabolic process; response to endoplasmic reticulum stress; response to unfolded protein; toxin transport; ubiquitin-dependent ERAD pathway
Reference #:  P20029 (UniProtKB)
Alt. Names/Synonyms: 78 kDa glucose-regulated protein; AL022860; AU019543; BiP; D2Wsu141e; D2Wsu17e; Endoplasmic reticulum chaperone BiP; glucose regulated protein, 78 kDa; GRP-78; Grp78; Heat shock 70 kDa protein 5; heat shock 70kD protein 5 (glucose-regulated protein, 78kD); heat shock protein 5; Hsce70; Hspa5; Immunoglobulin heavy chain-binding protein; mBiP; OTTMUSP00000012896; OTTMUSP00000012897; SEZ-7; Sez7
Gene Symbols: Hspa5
Molecular weight: 72,422 Da
Basal Isoelectric point: 5.07  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene