HSP60 Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. Belongs to the chaperonin (HSP60) family. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Mitochondrial
Chromosomal Location of mouse Ortholog: 1|1 C1.2
Cellular Component:  cell surface; clathrin-coated pit; coated vesicle; cytoplasm; cytosol; early endosome; extracellular exosome; extracellular space; Golgi cisterna; intracellular membrane-bounded organelle; lipopolysaccharide receptor complex; membrane; migrasome; mitochondrial crista; mitochondrial inner membrane; mitochondrial matrix; mitochondrion; peroxisomal matrix; plasma membrane; protein-containing complex; secretory granule; sperm midpiece; sperm plasma membrane; zymogen granule
Molecular Function:  apolipoprotein A-I binding; apolipoprotein binding; ATP binding; ATP-dependent protein folding chaperone; double-stranded RNA binding; enzyme binding; high-density lipoprotein particle binding; isomerase activity; lipopolysaccharide binding; modification-dependent protein binding; nucleotide binding; p53 binding; protein-containing complex binding; protein-folding chaperone binding; ubiquitin protein ligase binding
Biological Process:  activation of cysteine-type endopeptidase activity involved in apoptotic process; adhesion of symbiont to host; apoptotic mitochondrial changes; B cell activation; B cell proliferation; biological process involved in interaction with symbiont; cellular response to interleukin-7; interferon-alpha production; isotype switching to IgG isotypes; mitochondrial unfolded protein response; MyD88-dependent toll-like receptor signaling pathway; negative regulation of apoptotic process; negative regulation of apoptotic process in bone marrow cell; negative regulation of neuron apoptotic process; negative regulation of reactive oxygen species biosynthetic process; positive regulation of apoptotic process; positive regulation of interferon-alpha production; positive regulation of interleukin-10 production; positive regulation of interleukin-12 production; positive regulation of interleukin-6 production; positive regulation of macrophage activation; positive regulation of T cell activation; positive regulation of T cell mediated immune response to tumor cell; positive regulation of tumor necrosis factor production; positive regulation of type II interferon production; protein folding; protein import into mitochondrial intermembrane space; protein refolding; protein stabilization; response to unfolded protein; T cell activation; type II interferon production
Reference #:  P63038 (UniProtKB)
Alt. Names/Synonyms: 60 kDa chaperonin; 60 kDa heat shock protein, mitochondrial; 60kDa; CH60; chaperonin 60; CPN60; heat shock 60kDa protein 1 (chaperonin); heat shock protein 1 (chaperonin); heat shock protein 60; heat shock protein, 60 kDa; Hsp; HSP-60; HSP-65; Hsp60; Hspd1; mitochondrial matrix protein P1; OTTMUSP00000024365
Gene Symbols: Hspd1
Molecular weight: 60,955 Da
Basal Isoelectric point: 5.91  Predict pI for various phosphorylation states
CST Pathways:  Mitochondrial Control of Apoptosis
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein