60 kDa heat shock protein, mitochondrial

Details

Name
60 kDa heat shock protein, mitochondrial
Synonyms
  • 3.6.4.9
  • 60 kDa chaperonin
  • Chaperonin 60
  • CPN60
  • Heat shock protein 60
  • HSP-60
  • HSP60
  • HuCHA60
  • Mitochondrial matrix protein P1
  • P60 lymphocyte protein
Gene Name
HSPD1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049628|60 kDa heat shock protein, mitochondrial
MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGR
TVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLA
RSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDK
EIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQ
DAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAV
KAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKG
KGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDR
VTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIA
KNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLT
TAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
Number of residues
573
Molecular Weight
61054.17
Theoretical pI
Not Available
GO Classification
Functions
apolipoprotein A-I binding / apolipoprotein binding / ATP binding / ATPase activity / chaperone binding / DNA replication origin binding / double-stranded RNA binding / enzyme binding / high-density lipoprotein particle binding / insulin binding / lipopolysaccharide binding / misfolded protein binding / p53 binding / protease binding / protein binding involved in protein folding / protein complex binding / protein heterodimerization activity / RNA binding / single-stranded DNA binding / ubiquitin protein ligase binding / unfolded protein binding
Processes
'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 / chaperone mediated protein folding requiring cofactor / chaperone-mediated protein complex assembly / chaperone-mediated protein folding / detection of misfolded protein / interaction with symbiont / isotype switching to IgG isotypes / 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 import into mitochondrial intermembrane space / protein maturation / protein refolding / protein stabilization / regulation of transcription from RNA polymerase II promoter / response to activity / response to ATP / response to cocaine / response to cold / response to drug / response to estrogen / response to glucocorticoid / response to heat / response to hydrogen peroxide / response to hypoxia / response to ischemia / response to lipopolysaccharide / response to unfolded protein / T cell activation / viral process
Components
cell surface / clathrin-coated pit / coated vesicle / cytoplasm / cytosol / early endosome / extracellular exosome / extracellular matrix / extracellular space / Golgi apparatus / lipopolysaccharide receptor complex / membrane / membrane raft / mitochondrial crista / mitochondrial inner membrane / mitochondrial matrix / mitochondrion / myelin sheath / peroxisomal matrix / plasma membrane / protein complex / rough endoplasmic reticulum / secretory granule / zymogen granule
General Function
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 (PubMed:1346131, PubMed:11422376). 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 (Probable).
Specific Function
Apolipoprotein a-i binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion matrix
Gene sequence
>lcl|BSEQ0049629|60 kDa heat shock protein, mitochondrial (HSPD1)
ATGCTTCGGTTACCCACAGTCTTTCGCCAGATGAGACCGGTGTCCAGGGTACTGGCTCCT
CATCTCACTCGGGCTTATGCCAAAGATGTAAAATTTGGTGCAGATGCCCGAGCCTTAATG
CTTCAAGGTGTAGACCTTTTAGCCGATGCTGTGGCCGTTACAATGGGGCCAAAGGGAAGA
ACAGTGATTATTGAGCAGAGTTGGGGAAGTCCCAAAGTAACAAAAGATGGTGTGACTGTT
GCAAAGTCAATTGACTTAAAAGATAAATACAAAAACATTGGAGCTAAACTTGTTCAAGAT
GTTGCCAATAACACAAATGAAGAAGCTGGGGATGGCACTACCACTGCTACTGTACTGGCA
CGCTCTATAGCCAAGGAAGGCTTCGAGAAGATTAGCAAAGGTGCTAATCCAGTGGAAATC
AGGAGAGGTGTGATGTTAGCTGTTGATGCTGTAATTGCTGAACTTAAAAAGCAGTCTAAA
CCTGTGACCACCCCTGAAGAAATTGCACAGGTTGCTACGATTTCTGCAAACGGAGACAAA
GAAATTGGCAATATCATCTCTGATGCAATGAAAAAAGTTGGAAGAAAGGGTGTCATCACA
GTAAAGGATGGAAAAACACTGAATGATGAATTAGAAATTATTGAAGGCATGAAGTTTGAT
CGAGGCTATATTTCTCCATACTTTATTAATACATCAAAAGGTCAGAAATGTGAATTCCAG
GATGCCTATGTTCTGTTGAGTGAAAAGAAAATTTCTAGTATCCAGTCCATTGTACCTGCT
CTTGAAATTGCCAATGCTCACCGTAAGCCTTTGGTCATAATCGCTGAAGATGTTGATGGA
GAAGCTCTAAGTACACTCGTCTTGAATAGGCTAAAGGTTGGTCTTCAGGTTGTGGCAGTC
AAGGCTCCAGGGTTTGGTGACAATAGAAAGAACCAGCTTAAAGATATGGCTATTGCTACT
GGTGGTGCAGTGTTTGGAGAAGAGGGATTGACCCTGAATCTTGAAGACGTTCAGCCTCAT
GACTTAGGAAAAGTTGGAGAGGTCATTGTGACCAAAGACGATGCCATGCTCTTAAAAGGA
AAAGGTGACAAGGCTCAAATTGAAAAACGTATTCAAGAAATCATTGAGCAGTTAGATGTC
ACAACTAGTGAATATGAAAAGGAAAAACTGAATGAACGGCTTGCAAAACTTTCAGATGGA
GTGGCTGTGCTGAAGGTTGGTGGGACAAGTGATGTTGAAGTGAATGAAAAGAAAGACAGA
GTTACAGATGCCCTTAATGCTACAAGAGCTGCTGTTGAAGAAGGCATTGTTTTGGGAGGG
GGTTGTGCCCTCCTTCGATGCATTCCAGCCTTGGACTCATTGACTCCAGCTAATGAAGAT
CAAAAAATTGGTATAGAAATTATTAAAAGAACACTCAAAATTCCAGCAATGACCATTGCT
AAGAATGCAGGTGTTGAAGGATCTTTGATAGTTGAGAAAATTATGCAAAGTTCCTCAGAA
GTTGGTTATGATGCTATGGCTGGAGATTTTGTGAATATGGTGGAAAAAGGAATCATTGAC
CCAACAAAGGTTGTGAGAACTGCTTTATTGGATGCTGCTGGTGTGGCCTCTCTGTTAACT
ACAGCAGAAGTTGTAGTCACAGAAATTCCTAAAGAAGAGAAGGACCCTGGAATGGGTGCA
ATGGGTGGAATGGGAGGTGGTATGGGAGGTGGCATGTTCTAA
Chromosome Location
2
Locus
2q33.1
External Identifiers
ResourceLink
UniProtKB IDP10809
UniProtKB Entry NameCH60_HUMAN
HGNC IDHGNC:5261
General References
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB09130Copperapproved, investigationalunknownDetails