Cell Senescence Entries for HSPA5

Cell Types
Ovarian cancer
Cell Lines
A2780
Cancer Cell?
Yes
Method
Knockout, Overexpression
Type of senescence
Stress-induced
Senescence Effect
Inhibits
Primary Reference
Li et al. (2014) Cisplatin-induced senescence in ovarian cancer cells is mediated by GRP78. Oncol Rep 31(6)2525-34 (PubMed)

HSPA5 Gene Information

HGNC symbol
HSPA5 
Aliases
BiP; GRP78 
Common name
heat shock protein family A (Hsp70) member 5 
Entrez Id
3309
Description
The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. This protein localizes to the lumen of the endoplasmic reticulum (ER) where it operates as a typical HSP70 chaperone involved in the folding and assembly of proteins in the ER and is a master regulator of ER homeostasis. During cellular stress, as during viral infection or tumorogenesis, this protein interacts with the transmembrane stress sensor proteins PERK (protein kinase R-like endoplasmic reticulum kinase), IRE1 (inositol-requiring kinase 1), and ATF6 (activating transcription factor 6) where it acts as a repressor of the unfolded protein response (UPR) and also plays a role in cellular apoptosis and senescence. Elevated expression and atypical translocation of this protein to the cell surface has been reported in viral infections and some types of cancer cells. At the cell surface this protein may facilitate viral attachment and entry to host cells. This gene is a therapeutic target for the treatment of coronavirus diseases and chemoresistant cancers. [provided by RefSeq, Jul 2020].

HSPA5 Ontologies

Gene Ontology
Process: GO:43066; negative regulation of apoptotic process
GO:30433; ubiquitin-dependent ERAD pathway
GO:30335; positive regulation of cell migration
GO:21762; substantia nigra development
GO:31333; negative regulation of protein-containing complex assembly
GO:42149; cellular response to glucose starvation
GO:1990440; positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress
GO:51085; chaperone cofactor-dependent protein refolding
GO:30968; endoplasmic reticulum unfolded protein response
GO:1903895; negative regulation of IRE1-mediated unfolded protein response
GO:34620; cellular response to unfolded protein
GO:42026; protein refolding
GO:1554; luteolysis
GO:6983; ER overload response
GO:9314; response to radiation
GO:10976; positive regulation of neuron projection development
GO:21589; cerebellum structural organization
GO:21680; cerebellar Purkinje cell layer development
GO:30182; neuron differentiation
GO:30512; negative regulation of transforming growth factor beta receptor signaling pathway
GO:31204; posttranslational protein targeting to membrane, translocation
GO:31398; positive regulation of protein ubiquitination
GO:34975; protein folding in endoplasmic reticulum
GO:34976; response to endoplasmic reticulum stress
GO:35437; maintenance of protein localization in endoplasmic reticulum
GO:42220; response to cocaine
GO:51402; neuron apoptotic process
GO:51603; proteolysis involved in cellular protein catabolic process
GO:60904; regulation of protein folding in endoplasmic reticulum
GO:71236; cellular response to antibiotic
GO:71277; cellular response to calcium ion
GO:71287; cellular response to manganese ion
GO:71320; cellular response to cAMP
GO:71353; cellular response to interleukin-4
GO:71466; cellular response to xenobiotic stimulus
GO:71480; cellular response to gamma radiation
GO:97501; stress response to metal ion
GO:1901998; toxin transport
GO:1903891; regulation of ATF6-mediated unfolded protein response
GO:1903894; regulation of IRE1-mediated unfolded protein response
GO:1903897; regulation of PERK-mediated unfolded protein response
GO:1904313; response to methamphetamine hydrochloride
GO:1990090; cellular response to nerve growth factor stimulus
Cellular component: GO:5634; nucleus
GO:5737; cytoplasm
GO:16020; membrane
GO:32991; protein-containing complex
GO:5783; endoplasmic reticulum
GO:43231; intracellular membrane-bounded organelle
GO:5739; mitochondrion
GO:5925; focal adhesion
GO:5829; cytosol
GO:5788; endoplasmic reticulum lumen
GO:42470; melanosome
GO:9986; cell surface
GO:8180; COP9 signalosome
GO:5793; endoplasmic reticulum-Golgi intermediate compartment
GO:30496; midbody
GO:5789; endoplasmic reticulum membrane
GO:70062; extracellular exosome
GO:30176; integral component of endoplasmic reticulum membrane
GO:5790; smooth endoplasmic reticulum
GO:5886; plasma membrane
GO:34663; endoplasmic reticulum chaperone complex
Function: GO:166; nucleotide binding
GO:5524; ATP binding
GO:16787; hydrolase activity
GO:31625; ubiquitin protein ligase binding
GO:5509; calcium ion binding
GO:5515; protein binding
GO:16887; ATP hydrolysis activity
GO:51082; unfolded protein binding
GO:19904; protein domain specific binding
GO:45296; cadherin binding
GO:19899; enzyme binding
GO:51087; chaperone binding
GO:44183; protein folding chaperone
GO:31072; heat shock protein binding
GO:51787; misfolded protein binding
GO:43022; ribosome binding
Hide GO terms

Homologs of HSPA5 in Model Organisms

Caenorhabditis elegans
hsp-4
Danio rerio
hspa5
Drosophila melanogaster
Hsc70-3
Mus musculus
Hspa5
Rattus norvegicus
Hspa5
Saccharomyces cerevisiae
KAR2
Schizosaccharomyces pombe
bip1

In other databases

GenAge model organism genes
  • A homolog of this gene for Caenorhabditis elegans is present as hsp-4
  • A homolog of this gene for Drosophila melanogaster is present as Hsc70-3
GenDR gene expression
  • A homolog of this gene for Mus musculus is present as Hspa5

External links

OMIM
138120
Ensembl
ENSG00000044574
Entrez Gene
3309
UniGene
743241
1000 Genomes
1000 Genomes
HPRD
GenAtlas
HSPA5
GeneCards
HSPA5