HSPA8

HSPA8
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3AGY, 3AGZ, 3ESK, 3FZF, 3FZH, 3FZK, 3FZL, 3FZM, 4HWI, 3LDQ, 3M3Z, 4H5N, 4H5R, 4H5T, 4H5V, 4H5W, 4KBQ
Identifiers
Aliases	HSPA8, HEL-33, HEL-S-72p, HSC54, HSC70, HSC71, HSP71, HSP73, HSPA10, LAP-1, LAP1, NIP71, heat shock protein family A (Hsp70) member 8
External IDs	OMIM: 600816; MGI: 105384; HomoloGene: 68524; GeneCards: HSPA8; OMA:HSPA8 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	123,063,230 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	40,721,383 bp
RNA expression pattern
	Top expressed in
	corpus callosum; ; superior frontal gyrus; ; right hemisphere of cerebellum; ; prefrontal cortex; ; right frontal lobe; ; ventricular zone; ; gonad; ; ganglionic eminence; ; right testis; ; primary visual cortex;
	Top expressed in
	tail of embryo; ; genital tubercle; ; ventricular zone; ; ganglionic eminence; ; ovary; ; Mesencephalon; ; neural tube; ; right kidney; ; hippocampus proper; ; proximal tubule;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; heat shock protein binding; unfolded protein binding; phosphatidylserine binding; C3HC4-type RING finger domain binding; protein binding; MHC class II protein complex binding; enzyme binding; G protein-coupled receptor binding; ATP binding; ubiquitin protein ligase binding; ATPase activity; RNA binding; cadherin binding; protein-macromolecule adaptor activity; protein folding chaperone activity; chaperone binding; misfolded protein binding; clathrin-uncoating ATPase activity;
Cellular component	cytoplasm; cytosol; late endosome; blood microparticle; membrane; focal adhesion; ubiquitin ligase complex; melanosome; myelin sheath; plasma membrane; clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; intracellular anatomical structure; Prp19 complex; nucleoplasm; lysosomal membrane; lysosomal lumen; nucleolus; spliceosomal complex; lumenal side of lysosomal membrane; extracellular exosome; nucleus; presynapse; extracellular matrix; extracellular region; extracellular space; secretory granule lumen; ficolin-1-rich granule lumen; lysosome; autophagosome; axon; dendrite; terminal bouton; presynaptic cytosol; postsynaptic cytosol; chaperone complex; ribonucleoprotein complex;
Biological process	chaperone-mediated autophagy; mRNA splicing, via spliceosome; late endosomal microautophagy; regulation of transcription, DNA-templated; regulation of protein stability; regulation of mRNA stability; positive regulation of mRNA splicing, via spliceosome; cellular response to starvation; mRNA processing; chaperone-mediated autophagy translocation complex disassembly; transcription, DNA-templated; chaperone cofactor-dependent protein refolding; regulation of cell cycle; regulation of protein complex stability; ATP metabolic process; response to unfolded protein; clathrin coat disassembly; protein folding; protein refolding; regulation of cellular response to heat; viral process; negative regulation of transcription, DNA-templated; neurotransmitter secretion; regulation of protein-containing complex assembly; negative regulation of supramolecular fiber organization; regulation of protein import; RNA splicing; protein methylation; neutrophil degranulation; modulation by host of viral process; positive regulation by host of viral genome replication; membrane organization; protein targeting to lysosome involved in chaperone-mediated autophagy; axo-dendritic transport; vesicle-mediated transport; cytokine-mediated signaling pathway; cellular response to heat; Unfolded Protein Response; slow axonal transport;
	Sources:Amigo / QuickGO
Orthologs
	3312
	15481
	ENSG00000109971
	ENSMUSG00000015656
	P11142
	P63017
	NM_006597; NM_153201
	NM_031165; NM_001364480
	NP_006588; NP_694881
	NP_112442; NP_001351409
	Wikidata
View/Edit Human	View/Edit Mouse

Heat shock 70 kDa protein 8 also known as heat shock cognate 71 kDa protein or Hsc70 or Hsp73 is a heat shock protein that in humans is encoded by the HSPA8 gene on chromosome 11. 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. Its functions contribute to biological processes including signal transduction, apoptosis, autophagy, protein homeostasis, and cell growth and differentiation. It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence, and aging.