HSP60 chaperone ATPase HSP60 [Saccharomyces cerevisiae S288C] - Gene

Summary

Official Symbol: HSP60
Official Full Name: chaperone ATPase HSP60
Primary source: SGD:S000004249
Locus tag: YLR259C
See related: AllianceGenome:SGD:S000004249; FungiDB:YLR259C; VEuPathDB:YLR259C
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: CPN60; MIF4; MNA2
Summary: Enables several functions, including ATP hydrolysis activity; DNA binding activity; and unfolded protein binding activity. Involved in several processes, including chaperone-mediated protein complex assembly; protein folding; and protein stabilization. Located in mitochondrion. Is active in mitochondrial nucleoid. Human ortholog(s) of this gene implicated in several diseases, including artery disease (multiple); autistic disorder; glucose intolerance; hereditary spastic paraplegia (multiple); and hypomyelinating leukodystrophy 4. Orthologous to human HSPD1 (heat shock protein family D (Hsp60) member 1). [provided by Alliance of Genome Resources, Dec 2024]
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Chromosome XII - NC_001144.5 Genomic Context describing neighboring genes

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP hydrolysis activity	IDA Inferred from Direct Assay more info	PubMed
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables DNA replication origin binding	IDA Inferred from Direct Assay more info	PubMed
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IPI Inferred from Physical Interaction more info	PubMed
enables single-stranded DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info
enables unfolded protein binding	IMP Inferred from Mutant Phenotype more info	PubMed

Process	Evidence Code	Pubs
involved_in 'de novo' protein folding	IEA Inferred from Electronic Annotation more info
involved_in 'de novo' protein folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in chaperone-mediated protein complex assembly	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrial genome maintenance	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrial unfolded protein response	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitochondrion organization	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein import into mitochondrial intermembrane space	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein import into mitochondrial intermembrane space	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein maturation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein refolding	IDA Inferred from Direct Assay more info	PubMed
involved_in protein refolding	IEA Inferred from Electronic Annotation more info
involved_in protein refolding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein stabilization	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
is_active_in mitochondrial inner membrane	IBA Inferred from Biological aspect of Ancestor more info
is_active_in mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
is_active_in mitochondrial nucleoid	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial nucleoid	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HDA more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info

NP_013360.1

Tetradecameric mitochondrial chaperonin; required for ATP-dependent folding of precursor polypeptides and complex assembly; prevents aggregation and mediates protein refolding after heat shock; role in mtDNA transmission; phosphorylated

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