Endoplasmic reticulum chaperone BiP

An endoplasmic reticulum chaperone BiP that is encoded in the genome of human. [PRO:DAN]

Synonyms

EC 3.6.4.10;
78 kDa glucose-regulated protein;
GRP-78;
Binding-immunoglobulin protein;
BiP;
Heat shock protein 70 family protein 5;
HSP70 family protein 5;
Heat shock protein family A member 5;
Immunoglobulin heavy chain-b

Research

Bioassay Publications (2)

Timeframe	Studies on this Protein(%)	All Drugs %
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	2 (100.00)	24.3611
2020's	0 (0.00)	2.80

Compounds (10)

Drugs with Inhibition Measurements

Drug	Taxonomy	Measurement	Average (mM)	Bioassay(s)	Publication(s)
dichlorophen	Homo sapiens (human)	IC50	100.0000	1	1
hexachlorophene	Homo sapiens (human)	IC50	9.1000	3	3
triclosan	Homo sapiens (human)	IC50	100.0000	1	1
2,2'-methylenebis(ethyl-6-tert-butylphenol)	Homo sapiens (human)	IC50	100.0000	1	1
2,2'-methylenebis(4-methyl-6-tert-butylphenol)	Homo sapiens (human)	IC50	100.0000	1	1
oxyclozanide	Homo sapiens (human)	IC50	100.0000	1	1
2,2'-bisphenol f	Homo sapiens (human)	IC50	100.0000	1	1
ver 155008	Homo sapiens (human)	IC50	0.8000	1	1

Drugs with Activation Measurements

Drug	Taxonomy	Measurement	Average (mM)	Bioassay(s)	Publication(s)
adenosine diphosphate	Homo sapiens (human)	Kd	3.0000	2	2
8-aminoadenosine	Homo sapiens (human)	Kd	9.6850	3	4
ver 155008	Homo sapiens (human)	Kd	0.1650	3	4

Enables

This protein enables 15 target(s):

Target	Category	Definition
calcium ion binding	molecular function	Binding to a calcium ion (Ca2+). [GOC:ai]
protein binding	molecular function	Binding to a protein. [GOC:go_curators]
ATP binding	molecular function	Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
ATP hydrolysis activity	molecular function	Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. [RHEA:13065]
enzyme binding	molecular function	Binding to an enzyme, a protein with catalytic activity. [GOC:jl]
protein domain specific binding	molecular function	Binding to a specific domain of a protein. [GOC:go_curators]
ubiquitin protein ligase binding	molecular function	Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. [GOC:vp]
ribosome binding	molecular function	Binding to a ribosome. [GOC:go_curators]
cadherin binding	molecular function	Binding to cadherin, a type I membrane protein involved in cell adhesion. [GOC:bf]
unfolded protein binding	molecular function	Binding to an unfolded protein. [GOC:ai]
protein-folding chaperone binding	molecular function	Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. [PMID:10585443]
misfolded protein binding	molecular function	Binding to a misfolded protein. [GOC:ai]
ATP-dependent protein folding chaperone	molecular function	Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis. [PMID:27365453]
protein folding chaperone	molecular function	Binding to a protein or a protein-containing complex to assist the protein folding process. [GOC:mtg_cambridge_2009]
heat shock protein binding	molecular function	Binding to a heat shock protein, a protein synthesized or activated in response to heat shock. [GOC:mah, GOC:vw]

Located In

This protein is located in 16 target(s):

Target	Category	Definition
nucleus	cellular component	A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
cytoplasm	cellular component	The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
mitochondrion	cellular component	A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]
endoplasmic reticulum	cellular component	The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732]
endoplasmic reticulum lumen	cellular component	The volume enclosed by the membranes of the endoplasmic reticulum. [ISBN:0198547684]
endoplasmic reticulum membrane	cellular component	The lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah]
endoplasmic reticulum-Golgi intermediate compartment	cellular component	A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport. [GOC:pr, PMID:16723730]
cytosol	cellular component	The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
plasma membrane	cellular component	The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]
focal adhesion	cellular component	A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). [GOC:aruk, GOC:bc, ISBN:0124325653, ISBN:0815316208, PMID:10419689, PMID:12191915, PMID:15246682, PMID:1643657, PMID:16805308, PMID:19197329, PMID:23033047, PMID:26923917, PMID:28796323, PMID:8314002]
cell surface	cellular component	The external part of the cell wall and/or plasma membrane. [GOC:jl, GOC:mtg_sensu, GOC:sm]
membrane	cellular component	A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194]
midbody	cellular component	A thin cytoplasmic bridge formed between daughter cells at the end of cytokinesis. The midbody forms where the contractile ring constricts, and may persist for some time before finally breaking to complete cytokinesis. [ISBN:0815316194]
melanosome	cellular component	A tissue-specific, membrane-bounded cytoplasmic organelle within which melanin pigments are synthesized and stored. Melanosomes are synthesized in melanocyte cells. [GOC:jl, PMID:11584301]
intracellular membrane-bounded organelle	cellular component	Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators]
extracellular exosome	cellular component	A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894]

Active In

This protein is active in 4 target(s):

Target	Category	Definition
endoplasmic reticulum lumen	cellular component	The volume enclosed by the membranes of the endoplasmic reticulum. [ISBN:0198547684]
cytoplasm	cellular component	The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
nucleus	cellular component	A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators]
membrane	cellular component	A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194]

Part Of

This protein is part of 3 target(s):

Target	Category	Definition
COP9 signalosome	cellular component	A protein complex that catalyzes the deneddylation of proteins, including the cullin component of SCF ubiquitin E3 ligase; deneddylation increases the activity of cullin family ubiquitin ligases. The signalosome is involved in many regulatory process, including some which control development, in many species; also regulates photomorphogenesis in plants; in many species its subunits are highly similar to those of the proteasome. [PMID:11019806, PMID:12186635, PMID:14570571]
protein-containing complex	cellular component	A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. [GOC:dos, GOC:mah]
endoplasmic reticulum chaperone complex	cellular component	A protein complex that is located in the endoplasmic reticulum and is composed of chaperone proteins, including BiP, GRP94; CaBP1, protein disulfide isomerase (PDI), ERdj3, cyclophilin B, ERp72, GRP170, UDP-glucosyltransferase, and SDF2-L1. [PMID:12475965]

Involved In

This protein is involved in 25 target(s):

Target	Category	Definition
ER overload response	biological process	The series of molecular signals initiated by the accumulation of normal or misfolded proteins in the endoplasmic reticulum and leading to activation of transcription by NF-kappaB. [PMID:10390516]
cerebellum structural organization	biological process	The process that contributes to the act of creating the structural organization of the cerebellum. This process pertains to the physical shaping of a rudimentary structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills. [GO_REF:0000021, GOC:cls, GOC:dgh, GOC:dph, GOC:jid, ISBN:0838580343]
cerebellar Purkinje cell layer development	biological process	The process whose specific outcome is the progression of the cerebellar Purkinje cell layer over time, from its formation to the mature structure. The Purkinje cell layer lies just underneath the molecular layer of the cerebellar cortex. It contains the neuronal cell bodies of the Purkinje cells that are arranged side by side in a single layer. Candelabrum interneurons are vertically oriented between the Purkinje cells. Purkinje neurons are inhibitory and provide the output of the cerebellar cortex through axons that project into the white matter. Extensive dendritic trees from the Purkinje cells extend upward in a single plane into the molecular layer where they synapse with parallel fibers of granule cells. [GO_REF:0000021, GOC:cls, GOC:dgh, GOC:dph, GOC:jid, ISBN:0838580343]
substantia nigra development	biological process	The progression of the substantia nigra over time from its initial formation until its mature state. The substantia nigra is the layer of gray substance that separates the posterior parts of the cerebral peduncles (tegmentum mesencephali) from the anterior parts; it normally includes a posterior compact part with many pigmented cells (pars compacta) and an anterior reticular part whose cells contain little pigment (pars reticularis). [GO_REF:0000021, GOC:cls, GOC:dgh, GOC:dph, GOC:jid, ISBN:0838580343, ISBN:0878937420]
positive regulation of cell migration	biological process	Any process that activates or increases the frequency, rate or extent of cell migration. [GOC:go_curators]
negative regulation of transforming growth factor beta receptor signaling pathway	biological process	Any process that stops, prevents, or reduces the frequency, rate or extent of any TGF-beta receptor signaling pathway. [GOC:mah]
endoplasmic reticulum unfolded protein response	biological process	The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation. [GOC:mah, PMID:12042763]
post-translational protein targeting to membrane, translocation	biological process	The process in which a protein translocates through the ER membrane posttranslationally. [PMID:12518317, PMID:8707814]
negative regulation of protein-containing complex assembly	biological process	Any process that stops, prevents, or reduces the frequency, rate or extent of protein complex assembly. [GOC:mah]
positive regulation of protein ubiquitination	biological process	Any process that activates or increases the frequency, rate or extent of the addition of ubiquitin groups to a protein. [GOC:mah]
protein folding in endoplasmic reticulum	biological process	A protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation). [GOC:mah, GOC:vw]
response to endoplasmic reticulum stress	biological process	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. [GOC:cjm, GOC:mah]
maintenance of protein localization in endoplasmic reticulum	biological process	Any process in which a protein is maintained in the endoplasmic reticulum and prevented from moving elsewhere. These include sequestration within the endoplasmic reticulum, protein stabilization to prevent transport elsewhere and the active retrieval of proteins that escape the endoplasmic reticulum. [GOC:bf, GOC:vw]
ERAD pathway	biological process	The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. [GOC:bf, GOC:PARL, PMID:20940304, PMID:21969857]
cellular response to glucose starvation	biological process	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of glucose. [GOC:jl]
negative regulation of apoptotic process	biological process	Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis]
positive regulation of transcription by RNA polymerase II	biological process	Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH]
regulation of protein folding in endoplasmic reticulum	biological process	Any process that modulates the rate, frequency or extent of the protein folding process that takes place in the endoplasmic reticulum (ER). Secreted, plasma membrane and organelle proteins are folded in the ER, assisted by chaperones and foldases (protein disulphide isomerases), and additional factors required for optimal folding (ATP, Ca2+ and an oxidizing environment to allow disulfide bond formation). [GOC:dph, GOC:tb]
cellular response to interleukin-4	biological process	Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-4 stimulus. [GOC:mah]
regulation of ATF6-mediated unfolded protein response	biological process	Any process that modulates the frequency, rate or extent of the ATF6-mediated unfolded protein response. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22013210]
regulation of IRE1-mediated unfolded protein response	biological process	Any process that modulates the frequency, rate or extent of the IRE1-mediated unfolded protein response. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22013210]
negative regulation of IRE1-mediated unfolded protein response	biological process	Any process that stops, prevents or reduces the frequency, rate or extent of the IRE1-mediated unfolded protein response. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22013210]
regulation of PERK-mediated unfolded protein response	biological process	Any process that modulates the frequency, rate or extent of the PERK-mediated unfolded protein response. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22013210]
chaperone cofactor-dependent protein refolding	biological process	The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release. [GOC:rb]
protein refolding	biological process	The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones. [GOC:mb]