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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.
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| Protein type: Chaperone; Mitochondrial |
| Chromosomal Location of mouse Ortholog: 1|1 C1.2 |
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Cellular Component:
cell surface; clathrin-coated pit; coated vesicle; cytoplasm; cytosol; early endosome; extracellular exosome; extracellular space; Golgi apparatus; intracellular membrane-bounded organelle; lipopolysaccharide receptor complex; membrane; membrane raft; mitochondrial crista; mitochondrial inner membrane; mitochondrial matrix; mitochondrion; peroxisomal matrix; plasma membrane; protein-containing complex; rough endoplasmic reticulum; secretory granule; zymogen granule
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Molecular Function:
apolipoprotein A-I binding; apolipoprotein binding; ATP binding; chaperone binding; double-stranded RNA binding; enzyme binding; high-density lipoprotein particle binding; hydrolase activity; insulin binding; lipopolysaccharide binding; modification-dependent protein binding; nucleotide binding; p53 binding; protease binding; protein heterodimerization activity; protein-containing complex binding; ubiquitin protein ligase binding; unfolded protein binding
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Biological Process:
'de novo' protein folding; activation of cysteine-type endopeptidase activity involved in apoptotic process; apoptotic mitochondrial changes; B cell activation; B cell cytokine production; B cell proliferation; cellular response to interleukin-7; interaction with symbiont; isotype switching to IgG isotypes; mitochondrion organization; MyD88-dependent toll-like receptor signaling pathway; negative regulation of apoptotic process; negative regulation of apoptotic process in bone marrow; negative regulation of neuron apoptotic process; negative regulation of reactive oxygen species biosynthetic process; positive regulation of apoptotic process; positive regulation of inflammatory response; positive regulation of interferon-alpha production; positive regulation of interferon-gamma production; positive regulation of interleukin-10 production; positive regulation of interleukin-12 production; positive regulation of interleukin-6 production; positive regulation of interleukin-6 secretion; 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 secretion; protein folding; protein import into mitochondrial intermembrane space; protein refolding; protein stabilization; response to unfolded protein; T cell activation
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Reference #:
P63038
(UniProtKB)
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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
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Gene Symbols: Hspd1
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Molecular weight:
60,955 Da
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Basal Isoelectric point:
5.91
Predict pI for various phosphorylation states
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CST Pathways:
Mitochondrial Control of Apoptosis
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Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology®
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