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
>拼箱| BSEQ0049628 | 60 kDa热休克蛋白,mitochondrial MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGR TVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLA RSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDK EIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQ DAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAV KAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKG KGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDR VTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIA KNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLT TAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
Number of residues
573
分子量
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/Tcell activation/病毒的过程
Components
cell surface/clathrin-coated pit/coated vesicle/cytoplasm/cytosol/early endosome/extracellular exosome/extracellular matrix/extracellular space/Golgi apparatus/lipopolysaccharide receptor complex/membrane/膜筏/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
Resource Link
UniProtKB ID P10809
UniProtKB Entry Name CH60_HUMAN
HGNC ID HGNC:5261
General References
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Drug Relations

Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details
DB09130 Copper approved, investigational unknown Details