Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
HSC70 (human)

Overview
HSC70 Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Isoform 2 may function as an endogenous inhibitory regulator of HSC70 by competing the co- chaperones. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with PACRG and TSC2. Interacts with BAG1. Interacts with SV40 VP1. Interacts with DNAJC7. Interacts with HERC5. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Constitutively synthesized. Ubiquitous. Belongs to the heat shock protein 70 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein; Nucleolus; RNA-binding
Chromosomal Location of Human Ortholog: 11q24.1
Cellular Component: cell-cell adherens junction; cytosol; extracellular matrix; extracellular space; focal adhesion; intracellular; lysosomal lumen; lysosomal membrane; membrane; nucleoplasm; nucleus; plasma membrane; ribonucleoprotein complex; ubiquitin ligase complex
Molecular Function: ATP binding; ATPase activity; enzyme binding; G-protein-coupled receptor binding; heat shock protein binding; protein binding; ubiquitin protein ligase binding; unfolded protein binding
Biological Process: ATP metabolic process; cellular response to starvation; negative regulation of transcription, DNA-dependent; neurotransmitter secretion; nuclear mRNA splicing, via spliceosome; protein refolding; regulation of mRNA stability; regulation of protein complex assembly; regulation of protein stability
Reference #:  P11142 (UniProtKB)
Alt. Names/Synonyms: constitutive heat shock protein 70; Heat shock 70 kDa protein 8; heat shock 70kd protein 10; heat shock 70kD protein 8; heat shock 70kDa protein 8; Heat shock cognate 71 kDa protein; heat shock cognate protein 54; heat shock cognate protein, 71-kDa; HSC54; HSC70; HSC71; HSP71; HSP73; HSP7C; HSPA10; HSPA8; LAP1; lipopolysaccharide-associated protein 1; LPS-associated protein 1; MGC131511; MGC29929; N-myristoyltransferase inhibitor protein 71; NIP71
Gene Symbols: HSPA8
Molecular weight: 70,898 Da
Basal Isoelectric point: 5.37  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

HSC70

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