Binding immunoglobulin protein

HSPA5
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3IUC, 3LDL, 3LDN, 3LDO, 3LDP, 5E84, 5E86, 5E85, 5F1X, 5EX5, 5EVZ, 5F2R, 5F0X, 5EY4, 5EXW
Identifiers
Aliases	HSPA5, BIP, GRP78, HEL-S-89n, MIF2, Binding immunoglobulin protein, heat shock protein family A (Hsp70) member 5, GRP78/Bip
External IDs	OMIM: 138120 MGI: 95835 HomoloGene: 3908 GeneCards: HSPA5
Gene location (Human)
Chr.	Chromosome 9 (human)
End	125,241,382 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	34,667,559 bp
RNA expression pattern
	Top expressed in
	vena cava; ; olfactory bulb; ; pericardium; ; corpus epididymis; ; pylorus; ; lower lobe of lung; ; trachea; ; caput epididymis; ; parotid gland; ; cardia;
	Top expressed in
	maxillary prominence; ; primitive streak; ; seminal vesicula; ; vas deferens; ; superior cervical ganglion; ; lacrimal gland; ; spermatid; ; hand; ; somite; ; dermis;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; calcium ion binding; chaperone binding; protein domain specific binding; ribosome binding; misfolded protein binding; ATPase activity; protein binding; enzyme binding; ATP binding; ubiquitin protein ligase binding; unfolded protein binding; cadherin binding; hydrolase activity; heat shock protein binding; protein folding chaperone activity;
Cellular component	cytoplasm; endoplasmic reticulum lumen; endoplasmic reticulum membrane; membrane; focal adhesion; melanosome; myelin sheath; plasma membrane; smooth endoplasmic reticulum; endoplasmic reticulum chaperone complex; cell surface; integral component of endoplasmic reticulum membrane; midbody; endoplasmic reticulum; mitochondrion; COP9 signalosome; extracellular exosome; nucleus; endoplasmic reticulum-Golgi intermediate compartment; extracellular matrix; cytosol; protein-containing complex; intracellular membrane-bounded organelle;
Biological process	cellular response to interleukin-4; regulation of ATF6-mediated unfolded protein response; cellular response to glucose starvation; regulation of protein folding in endoplasmic reticulum; substantia nigra development; positive regulation of cell migration; positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; maintenance of protein localization in endoplasmic reticulum; negative regulation of apoptotic process; protein folding in endoplasmic reticulum; negative regulation of transforming growth factor beta receptor signaling pathway; toxin transport; response to endoplasmic reticulum stress; PERK-mediated unfolded protein response; cerebellum structural organization; ER overload response; endoplasmic reticulum unfolded protein response; ATF6-mediated unfolded protein response; IRE1-mediated unfolded protein response; cerebellar Purkinje cell layer development; regulation of PERK-mediated unfolded protein response; ubiquitin-dependent ERAD pathway; cellular response to antibiotic; negative regulation of protein homodimerization activity; proteolysis involved in cellular protein catabolic process; cellular response to manganese ion; positive regulation of protein ubiquitination; regulation of IRE1-mediated unfolded protein response; response to radiation; positive regulation of neuron projection development; neuron differentiation; response to cocaine; neuron apoptotic process; cellular response to calcium ion; cellular response to cAMP; stress response to metal ion; response to methamphetamine hydrochloride; cellular response to nerve growth factor stimulus; cellular response to gamma radiation; luteolysis; response to unfolded protein; cellular response to heat; Unfolded Protein Response; protein refolding; chaperone cofactor-dependent protein refolding; negative regulation of IRE1-mediated unfolded protein response; posttranslational protein targeting to membrane, translocation;
	Sources:Amigo / QuickGO
Orthologs
	3309
	14828
	ENSG00000044574
	ENSMUSG00000026864
	P11021
	P20029
	NM_005347
	NM_001163434; NM_022310
	NP_005338
	NP_001156906; NP_071705
	Wikidata
View/Edit Human	View/Edit Mouse

Binding immunoglobulin protein (BiPS) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5) is a protein that in humans is encoded by the HSPA5 gene.

BiP is a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER) that binds newly synthesized proteins as they are translocated into the ER, and maintains them in a state competent for subsequent folding and oligomerization. BiP is also an essential component of the translocation machinery and plays a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. BiP is an abundant protein under all growth conditions, but its synthesis is markedly induced under conditions that lead to the accumulation of unfolded polypeptides in the ER.

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