HSPA6 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006986Biological processresponse to unfolded protein
GO_0034605Biological processcellular response to heat
GO_0070370Biological processcellular heat acclimation
GO_0042026Biological processprotein refolding
GO_0051085Biological processchaperone cofactor-dependent protein refolding
GO_0005576Cellular componentextracellular region
GO_0070062Cellular componentextracellular exosome
GO_0034774Cellular componentsecretory granule lumen
GO_0005814Cellular componentcentriole
GO_0072562Cellular componentblood microparticle
GO_1904813Cellular componentficolin-1-rich granule lumen
GO_0005829Cellular componentcytosol
GO_0008180Cellular componentCOP9 signalosome
GO_0005737Cellular componentcytoplasm
GO_0005634Cellular componentnucleus
GO_0019899Molecular functionenzyme binding
GO_0044183Molecular functionprotein folding chaperone
GO_0031072Molecular functionheat shock protein binding
GO_0051082Molecular functionunfolded protein binding
GO_0140662Molecular functionATP-dependent protein folding chaperone
GO_0005524Molecular functionATP binding
GO_0005515Molecular functionprotein binding
GO_0016887Molecular functionATP hydrolysis activity

IV. Literature review

[source]
Gene nameHSPA6
Protein nameHeat shock 70 kDa protein 6 (Heat shock 70 kDa protein B')
SynonymsHSP70B'
DescriptionFUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release . .

AccessionsENST00000309758.6
P17066