HSPA1A

HSPA1A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1HJO, 1S3X, 1XQS, 2E88, 2E8A, 2LMG, 3A8Y, 3ATU, 3ATV, 3AY9, 3D2E, 3D2F, 3JXU, 3LOF, 4IO8, 4J8F, 4PO2, 4WV5, 4WV7, 5AR0, 5AQZ, 3Q49,%%s3D2E
Identifiers
Aliases	HSPA1A, HEL-S-103, HSP70-1, HSP70-1A, HSP70I, HSP72, HSPA1, HSP70.1, heat shock protein family A (Hsp70) member 1A, HSP70.2, HSP70-2, HSP70
External IDs	OMIM: 140550; MGI: 96244; HomoloGene: 74294; GeneCards: HSPA1A; OMA:HSPA1A - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	31,817,946 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	35,191,132 bp
RNA expression pattern
	Top expressed in
	gallbladder; ; ventricular zone; ; C1 segment; ; right auricle of heart; ; ganglionic eminence; ; blood; ; right lobe of liver; ; muscle layer of sigmoid colon; ; left ventricle; ; substantia nigra;
	Top expressed in
	corneal stroma; ; conjunctival fornix; ; vestibular membrane of cochlear duct; ; ciliary body; ; plantaris muscle; ; retinal pigment epithelium; ; skin of external ear; ; Ileal epithelium; ; iris; ; esophagus;
	More reference expression data
	n/a
Gene ontology
Molecular function	nucleotide binding; heat shock protein binding; signaling receptor binding; C3HC4-type RING finger domain binding; ATPase activity; virus receptor activity; histone deacetylase binding; protein folding chaperone activity; G protein-coupled receptor binding; ATP binding; enzyme binding; ubiquitin protein ligase binding; protein binding; transcription corepressor activity; cadherin binding; RNA binding; denatured protein binding; protein N-terminus binding; unfolded protein binding; disordered domain specific binding; misfolded protein binding;
Cellular component	blood microparticle; centriole; nucleoplasm; inclusion body; focal adhesion; perinuclear region of cytoplasm; ubiquitin ligase complex; cytosol; extracellular region; ficolin-1-rich granule lumen; centrosome; microtubule organizing center; cytoskeleton; nucleus; cytoplasm; mitochondrion; endoplasmic reticulum; aggresome; nuclear speck; vesicle; extracellular exosome; COP9 signalosome; protein-containing complex; ribonucleoprotein complex;
Biological process	cellular response to oxidative stress; regulation of mRNA stability; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; positive regulation of NF-kappaB transcription factor activity; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; cellular heat acclimation; negative regulation of inclusion body assembly; positive regulation of tumor necrosis factor-mediated signaling pathway; negative regulation of cell death; positive regulation of gene expression; viral entry into host cell; regulation of cell death; ATP metabolic process; negative regulation of protein ubiquitination; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; positive regulation of endoribonuclease activity; positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; regulation of protein ubiquitination; positive regulation of interleukin-8 production; regulation of cellular response to heat; cellular response to heat; negative regulation of transforming growth factor beta receptor signaling pathway; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; neutrophil degranulation; negative regulation of transcription from RNA polymerase II promoter in response to stress; protein refolding; positive regulation of microtubule nucleation; regulation of mitotic spindle assembly; mRNA catabolic process; response to unfolded protein; negative regulation of cell population proliferation; negative regulation of cell growth; negative regulation of apoptotic process; protein stabilization; chaperone-mediated protein complex assembly; positive regulation of RNA splicing; Unfolded Protein Response; positive regulation of erythrocyte differentiation; chaperone cofactor-dependent protein refolding; lysosomal transport; response to heat; telomere maintenance; DNA repair;
	Sources:Amigo / QuickGO
Orthologs
	3303
	193740
ENSG00000234475; ENSG00000204389; ENSG00000237724; ENSG00000235941; ENSG00000215328;
	n/a
	ENSMUSG00000091971
	P0DMV8; P0DMV9
	Q61696
	NM_005345
	NM_010479
	NP_005337; NP_005336; NP_005336; NP_005336.3; NP_005337.2
	NP_034609
	Wikidata
View/Edit Human	View/Edit Mouse

Heat shock 70 kDa protein 1, also termed Hsp72, is a protein that in humans is encoded by the HSPA1A gene. As a member of the heat shock protein 70 family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize or degrade mutant proteins. In addition, Hsp72 also facilitates DNA repair. Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation. It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence and aging, and inflammatory diseases such as Diabetes mellitus type 2 and rheumatoid arthritis.