HSPA5

Gene Information
 
Gene Symbol
HSPA5
 
Aliases
BIP, GRP78, HEL-S-89n, MIF2
 
Entrez Gene ID
 
Gene Name
Heat shock protein family A (Hsp70) member 5
 
Chromosomal Location
9q33.3
 
HGNC ID
 
Summary
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]
 
RefSeq DNA
 
RefSeq mRNA
  e!Ensembl
Gene
Transcript  
Protein

Gene Ontology (GO)

GO ID Ontology Function Evidence Reference
GO:0006986 Biological process Response to unfolded protein IBA 21873635
GO:0021762 Biological process Substantia nigra development HEP 22926577
GO:0030335 Biological process Positive regulation of cell migration IMP 23990668
GO:0030433 Biological process Ubiquitin-dependent ERAD pathway IBA 21873635
GO:0030433 Biological process Ubiquitin-dependent ERAD pathway TAS 19816510
Protein Information
 
Protein Name
Endoplasmic reticulum chaperone BiP, 78 kDa glucose-regulated protein, HSP70 family protein 5, binding-immunoglobulin protein, endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, epididymis secretory sperm binding protein Li 89n, glucose-regulated protein, 78kDa, heat shock 70kDa protein 5 (glucose-regulated protein, 78kDa), heat shock protein 70 family protein 5, heat shock protein family A member 5, immunoglobulin heavy chain-binding protein
 
Function
Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). 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 (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:1550958, PubMed:19538957). 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 (By similarity). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). 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.
 
Refseq Proteins
 
UniProt
 
PDB
 
Pfam
Pfam Accession Pfam ID
PF00012 HSP70
Pathways
 
KEGG
 
Reactome
 

Protein export
Protein processing in endoplasmic reticulum
Antigen processing and presentation
Thyroid hormone synthesis
Prion diseases

 

Regulation of HSF1-mediated heat shock response
ATF6 (ATF6-alpha) activates chaperones
PERK regulates gene expression
IRE1alpha activates chaperones
ATF6 (ATF6-alpha) activates chaperone genes
Antigen Presentation: Folding, assembly and peptide loading of class I MHC

Interactions
 
STRING MINT IntAct
ENSP00000344192 Q16552
    View interactions
     

Associated Diseases

Disease groupDisease NameReferences
Cardiovascular Diseases
Myocardial Infarction
Endocrine System Diseases
PCOS
Neoplasms
Esophagus Neoplasm
Hematopoietic Neoplasms
Myeloid Leukemia
References
 
 
PubMed ID Associated gene/s Associated condition Genetic Mutation Diagnostic Criteria Association with PCOS Ethnicity Conclusion
GRP78 
PCOS, Chronic hyperandrogenemia, Endoplasmic reticulum (ER) homeostasis, glucose metabolism 
 
National Institute of Child Health and Human Development (NICHD) criteria 
Related 
8 women with PCOS and 8 control 
These results suggest that hyperandrogenemic PCOS environment could compromise the endometrial homeostasis confirmed by the decrease in glucose uptake induced by testosterone and exhibited by stromal cells. 

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