Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
Home | Login
About PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Search / Browse Functions
Protein Page:
HSP70

Overview
HSP70 a critical chaperone protein that has a high affinity for unfolded polypeptide chains. It binds extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In cooperation with other chaperones, hsp70 stabilizes preexistent proteins against aggregation and mediates the folding of newly translated polypeptides in the cytosol as well as within organelles. Mitochondrial HSP70 is crucial to the import process: mutant forms of HSP70 fail to import precursor proteins. Is anti-apoptotic in sympathetic neurones and mediates this effect primarily by suppressing c-Jun transcriptional signalling. Interacts with tau protein and mediates proper folding of tau. Can promote the degradation of tau protein. Triptolide, a potential therapeutic agent for progression/metastasis of pancreatic cancer, causes pancreatic cancer cell death by induction of apoptosis, an effect mediated by the inhibition of HSP70. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 6p21.33
Cellular Component: centriole; centrosome; cytoplasm; cytosol; endoplasmic reticulum; extracellular region; focal adhesion; inclusion body; mitochondrion; nuclear speck; nucleoplasm; nucleus; perinuclear region of cytoplasm; protein complex; ribonucleoprotein complex; ubiquitin ligase complex; vesicle
Molecular Function: ATP binding; ATPase activity; ATPase activity, coupled; cadherin binding; denatured protein binding; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; histone deacetylase binding; protein binding; protein N-terminus binding; receptor binding; RNA binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: activation of NF-kappaB transcription factor; ATP metabolic process; chaperone-mediated protein complex assembly; mRNA catabolic process; negative regulation of apoptosis; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of protein ubiquitination; negative regulation of transforming growth factor beta receptor signaling pathway; neutrophil degranulation; positive regulation of interleukin-8 production; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein refolding; protein stabilization; regulation of mRNA stability; regulation of protein ubiquitination; response to unfolded protein
Reference #:  P0DMV8 (UniProtKB)
Alt. Names/Synonyms: dnaK-type molecular chaperone HSP70-1; Heat shock 70 kDa protein 1/2; Heat shock 70 kDa protein 1A/1B; heat shock 70kD protein 1A/1B; heat shock 70kDa protein 1A/1B; heat shock-induced protein; HSP70-1; HSP70-1/HSP70-2; HSP70-1A; HSP70.1/HSP70.2; HSP70I; HSP71; HSP72; HSPA1; HSPA1A; HSPA1B
Gene Symbols: HSPA1A; HSPA1B
Molecular weight: 70,052 Da
Basal Isoelectric point: 5.48  Predict pI for various phosphorylation states
CST Pathways:  Inhibition of Apoptosis
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HSP70

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script

STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein