Details of Protein
| General Information of Protein (ID: PRT00594) | |||||
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| Name | Endoplasmic reticulum chaperone BiP (HSPA5) | ||||
| Synonyms |
Click to Show/Hide Synonyms of This Protein
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-binding protein; Hspa5; Grp78
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| Gene Name | Hspa5 | Gene ID | |||
| UniProt ID | |||||
| Family | Hydrolases (EC 3) | ||||
| EC Number | EC: 3.6.4.10 (Click to Show/Hide the Complete EC Tree) | ||||
| Click to Show/Hide the Molecular/Functional Data (Sequence/Structure/Function) of This Protein | |||||
| Sequence |
MMKFTVVAAALLLLGAVRAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGN
RITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKV VEKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDA QRQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDN GVFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRAL SSQHQARIEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEI VLVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDV CPLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLL GTFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIE RMVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVE EKIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSGGPPPTGEEDTSEKDEL |
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| Function | Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate. Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1. Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation. | ||||
| Regulatory Network | |||||
| Full List of Metabolite(s) Regulating This Protein | ||||||
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| Organic acids and derivatives | ||||||
| Leucine | Click to Show/Hide the Full List of Regulating Pair(s): 1 Pair(s) | |||||
| Detailed Information |
Metabo Info
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| Regulating Pair |
Experim Info
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[1] | ||||
| Introduced Variation | Leucine decrease (2 hours) | |||||
| Induced Change | HSPA5 protein phosphorylation levels: increase | |||||
| Summary | Introduced Variation
Induced Change
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| Disease Status | Healthy individual | |||||
| Details | It is reported that leucine decrease causes the increase of HSPA5 protein phosphorylation compared with control group. | |||||
| References | |||||
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| 1 | Phospho-proteomic approach to identify new targets of leucine deprivation in muscle cells. Anal Biochem. 2008 Oct 1;381(1):148-50. | ||||
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