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HSP82 Hsp90 family chaperone HSP82 [ Saccharomyces cerevisiae S288C ]

Gene ID: 855836, updated on 15-Feb-2026
Official Symbol
HSP82
Official Full Name
Hsp90 family chaperone HSP82
Primary source
SGD:S000006161
Locus tag
YPL240C
See related
AllianceGenome:SGD:S000006161; FungiDB:YPL240C; VEuPathDB:YPL240C
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
HSP90
Summary
Enables ATP hydrolysis activity and unfolded protein binding activity. Involved in several processes, including positive regulation of telomere maintenance via telomerase; protein folding; and protein-containing complex assembly. Located in cytoplasm and nucleus. Human ortholog(s) of this gene implicated in multiple sclerosis. Orthologous to several human genes including HSP90AB1 (heat shock protein 90 alpha family class B member 1). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs
all
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See HSP82 in Genome Data Viewer
Location:
chromosome: XVI
Exon count:
1
Sequence:
Chromosome: XVI; NC_001148.4 (96496..98625, complement)

Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene Iqg1p Neighboring gene GTPase-activating protein CIN2 Neighboring gene Yar1p Neighboring gene translation initiation factor eIF2 subunit beta

Genomic Sequence:
NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Related articles in PubMed

  1. Latent effects of Hsp90 mutants revealed at reduced expression levels. Jiang L, et al. PLoS Genet, 2013 Jun. PMID 23825969, Free PMC Article
  2. Intrinsic inhibition of the Hsp90 ATPase activity. Richter K, et al. J Biol Chem, 2006 Apr 21. PMID 16461354
  3. The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis. Mickler M, et al. Nat Struct Mol Biol, 2009 Mar. PMID 19234469
  4. Structural basis of the radicicol resistance displayed by a fungal hsp90. Prodromou C, et al. ACS Chem Biol, 2009 Apr 17. PMID 19236053
  5. Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. Immormino RM, et al. J Mol Biol, 2009 May 22. PMID 19361515, Free PMC Article

See all (410) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions.
    Title: Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions.
  2. Nucleotide exchange is sufficient for Hsp90 functions in vivo.
    Title: Nucleotide exchange is sufficient for Hsp90 functions in vivo.
  3. Hsp90 and metal-binding J-protein family chaperones are not critically involved in cellular iron-sulfur protein assembly and iron regulation in yeast.
    Title: Hsp90 and metal-binding J-protein family chaperones are not critically involved in cellular iron-sulfur protein assembly and iron regulation in yeast.
  4. The Phosphorylation Status of Hsp82 Regulates Mitochondrial Homeostasis During Glucose Sensing in Saccharomyces cerevisiae.
    Title: The Phosphorylation Status of Hsp82 Regulates Mitochondrial Homeostasis During Glucose Sensing in Saccharomyces cerevisiae.
  5. The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.
    Title: The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.
  6. Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance.
    Title: Monitoring the Conformation of the Sba1/Hsp90 Complex in the Presence of Nucleotides with Mn(II)-Based Double Electron-Electron Resonance.
  7. Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.
    Title: Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.
  8. A Single Site Phosphorylation on Hsp82 Ensures Cell Survival during Starvation in Saccharomyces cerevisiae.
    Title: A Single Site Phosphorylation on Hsp82 Ensures Cell Survival during Starvation in Saccharomyces cerevisiae.
  9. Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
    Title: Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.
  10. Controlling protein function by fine-tuning conformational flexibility.
    Title: Controlling protein function by fine-tuning conformational flexibility.
Submit: New GeneRIF Correction See all GeneRIFs (63)
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables ATP binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP hydrolysis activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATP hydrolysis activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables ATP hydrolysis activity IMP
Inferred from Mutant Phenotype
more info
 PubMed 
enables ATP-dependent protein folding chaperone IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
  
enables unfolded protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables unfolded protein binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in 'de novo' protein folding IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in 'de novo' protein folding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in box C/D snoRNP assembly IEA
Inferred from Electronic Annotation
more info
  
involved_in box C/D snoRNP assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in cellular response to heat IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in positive regulation of telomere maintenance via telomerase IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in positive regulation of telomere maintenance via telomerase IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in proteasome assembly IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in proteasome assembly IEA
Inferred from Electronic Annotation
more info
  
involved_in proteasome assembly IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein folding IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein folding IEA
Inferred from Electronic Annotation
more info
  
involved_in protein maturation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein refolding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein stabilization IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in regulation of telomere maintenance IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in response to osmotic stress IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in response to oxygen levels NAS
Non-traceable Author Statement
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm HDA PubMed 
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 
is_active_in perinuclear region of cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
is_active_in plasma membrane IBA
Inferred from Biological aspect of Ancestor
more info
  
part_of protein-containing complex IBA
Inferred from Biological aspect of Ancestor
more info
  
Preferred Names
Hsp90 family chaperone HSP82
NP_015084.1
  • Hsp90 chaperone; functionally redundant with Hsc82p; required for pheromone signaling; negative regulator of the Hsf1p-dependent heat shock response with Cpr7p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; promotes solubility of chaperone-substrate complexes; DNA damage induced nuclear import is Aha1p dependent; protein abundance increases in response to DNA replication stress; human homolog, HSP90AB1, complements null mutant

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001148.4 Reference assembly

    Range
    96496..98625 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001184054.1 → NP_015084.1  Hsp90 family chaperone HSP82

    See identical proteins and their annotated locations for NP_015084.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W3D1, P02829
    UniProtKB/TrEMBL
    A6ZW16, B3LKJ2, G2WNU6, N1NXP6
    Conserved Domains (1) summary
    PTZ00272
    Location:3 → 709
    PTZ00272; heat shock protein 83 kDa (Hsp83); Provisional
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P02829.1

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