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0CH60_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameHSPD1
Description60 kda heat shock protein, mitochondrial precursor (hsp60) (60 kda chaperonin) (cpn60) (heat shock protein 60) (hsp-60) (mitochondrial matrix protein p1) (p60 lymphocyte protein) (hucha60).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005759 mitochondrial matrix (NAS)
0005524 ATP binding (NAS)
0030150 mitochondrial matrix protein import (NAS)
0006457 protein folding (NAS)
0006986 response to unfolded protein (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases.owever.tructural information from other protein molecules is required for correct folding and subsequent assembly into oligomers . These helper molecules are referred to as molecular chaperones. subfamily of which are the chaperonins .hich include 10 kDa and 60 kDa proteins. These are found in abundance in prokaryotes.hloroplasts and mitochondria. They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees centigrade ).nd are stress-induced.cting to stabilise or protect disassembled polypeptides under heat-shock conditions .The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between 6 to 8 identical subunits.hereas the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings.ach ring containing 7 identical subunits . These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The cpn10 and cpn60 oligomers also require Mg2+-ATP in order to interact to form a functional complex.lthough the mechanism of this interaction is as yet unknown . This chaperonin complex is essential for the correct folding and assembly of polypeptides into oligomeric structures.f which the chaperonins themselves are not a part . The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.The 60 kDa form of chaperonin is the immunodominant antigen of patients with Legionnaires disease .nd is thought to play a role in the protection of the Legionella bacteria from oxygen radicals within macrophages. This hypothesis is based on the finding that the cpn60 gene is upregulated in response to hydrogen peroxide. source of oxygen radicals. Cpn60 has also been found to display strong antigenicity in many bacterial species .nd has the potential for inducing immune protection against unrelated bacterial infections. The RuBisCO subunit binding protein (which has been implicated in the assembly of RuBisCO) and cpn60 have been found to be evolutionary homologues.he RuBisCO subunit binding protein having the C-terminal Gly-Gly-Met repeat found in all bacterial cpn60 sequences. Although the precise function of this repeat is unknown.t is thought to be important as it is also found in 70 kDa heat-shock proteins . The crystal structure of Escherichia coli GroEL has been resolved to 2.8A . The TCP-1 family of proteins act as molecular chaperones for tubulin.ctin and probably some other proteins. They are weakly.ut significantly.elated to the cpn60/groEL chaperonin family.
  IPR002423:Chaperonin Cpn60/TCP-1
The assembly of proteins has been thought to be the sole result of properties inherent in the primary sequence of polypeptides themselves. In some cases.owever.tructural information from other protein molecules is required for correct folding and subsequent assembly into oligomers . These helper molecules are referred to as molecular chaperones. subfamily of which are the chaperonins . They are required for normal cell growth (as demonstrated by the fact that no temperature sensitive mutants for the chaperonin genes can be found in the temperature range 20 to 43 degrees centigrade ).nd are stress-induced.cting to stabilise or protect disassembled polypeptides under heat-shock conditions . Type I chaperonins present in eubacteria.itochondria and chloroplasts require the concerted action of 2 proteins.haperonin 60 (cpn60) and chaperonin 10 (cpn10). Type II chaperonins.ound in eukaryotic cytosol and in Archaebacteria.omprise only a cpn60 member.The 10 kDa chaperonin (cpn10 - or groES in bacteria) exists as a ring-shaped oligomer of between 6 to 8 identical subunits.hereas the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings.ach ring containing 7 identical subunits . These ring structures assemble by self-stimulation in the presence of Mg2+-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides as isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg2+-ATP dependent manner . The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.The 60 kDa form of chaperonin is the immunodominant antigen of patients with Legionnaires disease .nd is thought to play a role in the protection of the Legionella spp. bacteria from oxygen radicals within macrophages. This hypothesis is based on the finding that the cpn60 gene is upregulated in response to hydrogen peroxide. source of oxygen radicals. Cpn60 has also been found to display strong antigenicity in many bacterial species .nd has the potential for inducing immune protection against unrelated bacterial infections. The RuBisCO subunit binding protein (which has been implicated in the assembly of RuBisCO) and cpn60 have been found to be evolutionary homologues.he RuBisCO subunit binding protein having the C-terminal Gly-Gly-Met repeat found in all bacterial cpn60 sequences. Although the precise function of this repeat is unknown.t is thought to be important as it is also found in 70 kDa heat-shock proteins . The crystal structure of Escherichia coli GroEL has been resolved to 2.8A .
  IPR001844:Chaperonin Cpn60
Partially folded polypeptide chains.ither newly made by ribosomes or emerging from mature proteins unfolded by stress.un the risk of aggregating with one another to the detriment of the organism. Folding of newly synthesised polypeptides in the crowded cellular environment requires the assistance of molecular chaperone proteins.uch as the large bacterial chaperonins GroEL and GroES. GroEL and GroES prevent aggregation by encapsulating individual chains within the so-called Anfinsen cage provided by the GroELGroES complex.here they can fold in isolation from one another . GroEL consists of two heptameric rings of identical ATPase subunits stacked back to back.ontaining a cage in each ring. Each subunit consists of three domains. The equatorial domain contains the nucleotide binding site and is connected by a flexible intermediate domain with the apical domain. The latter presents several hydrophobic amino-acid side chains at the top of the ring.rientated towards the cavity of the cage. These side chains are involved in binding either a partially folded polypeptide chain or a single molecule of GroES.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008950:GroEL-like chaperone, ATPase
Partially folded polypeptide chains.ither newly made by ribosomes or emerging from mature proteins unfolded by stress.un the risk of aggregating with one another to the detriment of the organism. Folding of newly synthesised polypeptides in the crowded cellular environment requires the assistance of molecular chaperone proteins.uch as the large bacterial chaperonins GroEL and GroES. GroEL and GroES prevent aggregation by encapsulating individual chains within the so-called Anfinsen cage provided by the GroELGroES complex.here they can fold in isolation from one another . GroEL consists of two heptameric rings of identical ATPase subunits stacked back to back.ontaining a cage in each ring. Each subunit consists of three domains. The equatorial domain contains the nucleotide binding site and is connected by a flexible intermediate domain with the apical domain. The latter presents several hydrophobic amino-acid side chains at the top of the ring.rientated towards the cavity of the cage. These side chains are involved in binding either a partially folded polypeptide chain or a single molecule of GroES.This family consists of GroEL.ound in bacteria.rganelles derived from bacteria.nd occasionally in archaeal species. The bacterial GroEL/GroES group I chaperonin is replaced by a group II chaperonin.sually called the thermosome in archaeal species.nd CCT (chaperone-containing TCP) in eukaryotes. GroEL.hermosome subunits.nd CCT subunits all fall under the scope of .
  IPR012723:chaperonin GroEL
IPR002423:Cpn60_TCP1 
Evalue:-188.346786499023 
Location:47-550
SequencesProtein: CH60_HUMAN (573 aa)
mRNA: CR619688 NM_002156
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK04077
  Level 3 annotation:
    chaperonin GroEL (Hsp60)
  Level 2 annotation:
    Protein folding and associated processing
    Prion disease
    Type I diabetes mellitus
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 205 residues, 198059554-198060167Exon2: 61 residues, 198060826-198061005Exon3: 60 residues, 198061285-198061460Exon4: 84 residues, 198061970-198062216Exon5: 35 residues, 198063165-198063265Exon6: 58 residues, 198066292-198066461Exon7: 33 residues, 198067125-198067219Exon8: 34 residues, 198067625-198067721Exon9: 29 residues, 198068262-198068345Exon10: 86 residues, 198070108-198070361Exon11: 60 residues, 198071643-198071819Exon12: 47 residues, 198072750-198072885Exon13: 2 residues, -Jump to CH60_HUMANExon1: 120 residues, 198059810-198060167Exon2: 61 residues, 198060826-198061005Exon3: 60 residues, 198061285-198061460Exon4: 84 residues, 198061970-198062216Exon5: 35 residues, 198063165-198063265Exon6: 58 residues, 198066292-198066461Exon7: 33 residues, 198067125-198067219Exon8: 32 residues, 198067631-198067721Exon9: 29 residues, 198068262-198068345Exon10: 86 residues, 198070108-198070361Exon11: 60 residues, 198071643-198071819Exon12: 17 residues, 198072750-198072795Exon13: 2 residues, -Jump to CH60_HUMAN  
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