HSC82 Hsp90 family chaperone HSC82 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Gene symbol: HSC82
Gene description: Hsp90 family chaperone HSC82
Primary source: SGD:S000004798
Locus tag: YMR186W
See related: AllianceGenome:SGD:S000004798
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 cellular protein-containing complex assembly; cellular response to heat; and telomere maintenance. Located in mitochondrion and plasma membrane. Human ortholog(s) of this gene implicated in multiple sclerosis. Orthologous to several human genes including HSP90AA1 (heat shock protein 90 alpha family class A member 1) and HSP90AB1 (heat shock protein 90 alpha family class B member 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (632355..634472)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
Mutation or inhibition of Hsp90 resulted in decreased accumulation of Ura2, indicating it is an Hsp90 client. Cpr6 interacted with Ura2 in the absence of stable Cpr6-Hsp90 interaction, suggesting a direct interaction.
Title: Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis.
Hsc82 is more critical than Hsp82 for growth at 37 degrees C in the absence of mitochondrial DNA.
Title: Hsp90 and mitochondrial proteases Yme1 and Yta10/12 participate in ATP synthase assembly in Saccharomyces cerevisiae.
show that amino-terminal ATP-binding site residue is a conserved, strong regulator of Hsp90 functions, including ATP hydrolysis and chaperone activity.
Title: Hsp90 is regulated by a switch point in the C-terminal domain.
Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90.
Title: Structural-thermodynamic relationships of interactions in the N-terminal ATP-binding domain of Hsp90.
Hsp90 prevented the death of calcineurin- and Cmk2-deficient cells.
Title: Nonapoptotic death of Saccharomyces cerevisiae cells that is stimulated by Hsp90 and inhibited by calcineurin and Cmk2 in response to endoplasmic reticulum stresses.
These data support a conserved three-state chaperone cycle where the conformational equilibrium varies between species, implicating evolutionary tuning to meet the particular client protein and metabolic environment of an organism.
Title: Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.

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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-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 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 cellular response to heat	IMP Inferred from Mutant Phenotype 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 folding	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in protein stabilization	IBA Inferred from Biological aspect of Ancestor more info
involved_in telomere maintenance	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
located_in cytoplasm	HDA 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 mitochondrion	HDA more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
is_active_in perinuclear region of cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in plasma membrane	HDA more info	PubMed
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 HSC82

NP_013911.1

Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication

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_001145.3 Reference assembly

Range

632355..634472

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182692.1 → NP_013911.1 TPA: Hsp90 family chaperone HSC82 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013911.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W010, P15108

UniProtKB/TrEMBL

A0A140HDC6, A0A8H4BYU4, A6ZMP7, B3LM73, G2WKP1

Conserved Domains (1) summary

PTZ00272
Location:4 → 705

PTZ00272; heat shock protein 83 kDa (Hsp83); Provisional

Nucleotide		Protein
Heading	Accession and Version	Protein

Protein Accession	Links
Protein Accession	GenPept Link	UniProtKB Link
6XLB_A.1
6XLB_B.1
6XLC_A.1
6XLC_B.1
6XLD_A.1
6XLD_B.1
6XLE_A.1
6XLE_B.1
6XLF_A.1
6XLF_B.1
6XLG_A.1
6XLG_B.1
6XLH_A.1
6XLH_B.1
P15108.4