HSP82 Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288C] - Gene

Summary

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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, Dec 2024]
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Genomic context

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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_001148.4 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001148.4

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions.
Title: Quantitative proteomic analysis reveals unique Hsp90 cycle-dependent client interactions.
Nucleotide exchange is sufficient for Hsp90 functions in vivo.
Title: Nucleotide exchange is sufficient for Hsp90 functions in vivo.
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.
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.
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.
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.
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.
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.
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.
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)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

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 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	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	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 protein targeting to mitochondrion	IPI Inferred from Physical Interaction more info	PubMed
involved_in response to osmotic stress	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	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

General protein information

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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

NCBI Reference Sequences (RefSeq)

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Genome Annotation

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

Reference assembly

Genomic

NC_001148.4 Reference assembly

Range

96496..98625 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001184054.1 → NP_015084.1 TPA: Hsp90 family chaperone HSP82 [Saccharomyces cerevisiae S288C]

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