SCUBA

HSPA6 — Heat shock protein family A (Hsp70) member 6

HSPA6 belongs to a gene co-expression module in 12 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

HSPA6's module in each cell type

Cell typeModuleShares the module with
CD19⁺ B cellsHeat Shock Response
Stress
BAG3, CHORDC1, DDIT4, DEDD2, DNAJA4, DNAJB1, DNAJB4, DNAJB6 +13 moreView in SCUBA
CD4⁺ T cellsHeat-shock response
Stress
AHSA1, BAG3, CACYBP, CCDC117, DNAJB6, DYNLL1, FKBP4, GADD45G +5 moreView in SCUBA
CD8⁺ T cellsHeat Shock Response
Stress
DNAJA4, DNAJB1, DNAJB4, HSPA1A, HSPA1B, HSPB1, PLIN2, RGS2 +3 moreView in SCUBA
EndothelialNF-κB Activation
Inflammation
C2CD4B, ICAM5, IER3, MAP3K8, NFKBIA, NFKBID, PMAIP1, PTGS2 +5 moreView in SCUBA
FibroblastsBMP-ID Stress Response
Stress
BHLHE40, CCDC184, CFAP20, FOXC2, GADD45G, GDF15, GDNF, HAS1 +9 moreView in SCUBA
Gamma-delta T cellsHeat Shock Response
Stress
AHSA1, BAG3, CACYBP, CCT4, CHORDC1, DNAJA1, DNAJB1, DNAJB4 +13 more
Lymphatic endothelialHeat Shock Response
Stress
BAG3, DNAJB1, DNAJB4, HSP90AA1, HSPA1A, HSPA1B, HSPB1, HSPE1 +3 moreView in SCUBA
MacrophagesEarly response genes
Inflammatory
ATF3, BAG3, BTG2, CGAS, DNAJA1, DNAJA4, DNAJB1, DNAJB4 +39 moreView in SCUBA
MonocytesCo-chaperone Proteostasis
Stress
AHSA1, ALAS1, BAG3, CACYBP, FBXL14, FKBP4, HSPB1, SERPINH1 +2 moreView in SCUBA
Mucosal-associated invariant T cellHeat Shock Response
Stress
AHSA1, BAG3, CACYBP, CAPG, CHORDC1, CSF1, DNAJA4, DNAJB4 +13 more
Natural Killer cellsInducible HSP70 Stress
Stress
BAG3, DNAJB1, FKBP4, HSPA1A, HSPA1B, HSPA4, HSPB1, RHOB +2 moreView in SCUBA
NeutrophilsHeat Shock Response
Stress
ATP6V0C, CYB5D1, DNAJA1, DUSP2, GNG10, HMOX1, HSP90AA1, HSP90AB1 +4 more

About the gene

SynonymsHSP70B'
Chromosome1: 161524540-161526894
Predicted locationIntracellular
Essential geneNo
Protein classPlasma proteins, Predicted intracellular proteins
Biological processStress response

Function

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

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.