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Hsp82p and Hsc82p associate with many co-chaperones which both positively and negatively regulate Hsp82p/Hsc82p function. Hsp82p/Hsc82p co-chaperones include Sti1p, Cdc37p, Cns1p, Sba1p, Cpr6p, Cpr7p, Sse1p, Hch1p, and Aha1p (28 and references therein and reviewed in 21). One common method by which these partner proteins regulate Hsp82p/Hsc82p activity is through the inhibition/enhancement of ATP hydrolysis. Mechanistically, this can occur through direct interference of ATP binding or by alteration of Hsp82p/Hsc82p protein conformation such that ATP binding is affected (7, 29).

HSP82 and HSC82 are highly conserved among eukaryotes and the presence of at least one of the HSP90 gene product family members is essential for viability in yeast, Drosophila, and humans (18 and references therein). Overexpression of HSP82 in S. cerevisiae has been shown to increase the virulence of the yeast in mice (30). Human HSP90 (OMIM and OMIM) is being explored as a target for cancer therapeutics due to its role in folding oncogenic protein kinases and because inhibition of chaperone activity by ATP analogs has been shown to promote substrate protein degradation via the ubiquitin-dependent proteasomal pathway (31, 32, 33).", "date_edited": "2006-06-12"}, "literature_overview": {"primary_count": 269, "additional_count": 326, "review_count": 94, "go_count": 13, "phenotype_count": 17, "disease_count": 0, "interaction_count": 216, "regulation_count": 13, "ptm_count": 14, "funComplement_count": 5, "htp_count": 17, "total_count": 807}, "disease_overview": {"manual_disease_terms": [], "htp_disease_terms": [], "computational_annotation_count": 0, "date_last_reviewed": null}, "ecnumbers": [], "URS_ID": null, "main_strain": "S288C", "genetic_position": -137.0, "regulation_overview": {"regulator_count": 37, "target_count": 0, "paragraph": {"text": "Transcription upregulated by Hsf1p in response to heat; protein activity regulated by Ppt1p in response to starvation", "date_edited": "2023-07-21", "references": [{"id": 607863, "display_name": "Zarzov P, et al. (1997)", "citation": "Zarzov P, et al. (1997) A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication. J Cell Sci 110 ( Pt 16):1879-91", "pubmed_id": 9296388, "link": "/reference/S000053234", "year": 1997, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1242/jcs.110.16.1879"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/9296388"}]}, {"id": 2249403, "display_name": "Shang X, et al. (2020)", "citation": "Shang X, et al. (2020) A Single Site Phosphorylation on Hsp82 Ensures Cell Survival during Starvation in Saccharomyces cerevisiae. J Mol Biol 432(21):5809-5824", "pubmed_id": 32920053, "link": "/reference/S000287683", "year": 2020, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1016/j.jmb.2020.09.003"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/32920053"}]}]}}, "reference_mapping": {"598167": 1, "552023": 2, "624001": 3, "623989": 4, "618987": 5, "609799": 6, "607503": 7, "553898": 8, "495064": 9, "633785": 10, "401342": 11, "398398": 12, "2148853": 13, "2471192": 14, "635219": 15, "572597": 16, "548588": 17, "629928": 18, "606804": 19, "522372": 20, "524669": 21, "648693": 22, "524273": 23, "519187": 24, "519294": 25, "519190": 26, "519184": 27, "535323": 28, "555468": 29, "646831": 30, "519181": 31, "519178": 32, "519175": 33, "607331": 34}, "history": [{"category": "Name", "history_type": "LSP", "note": "Name: HSP82", "date_created": "2000-05-19", "references": [{"id": 552023, "display_name": "Mortimer RK, et al. (1989)", "citation": "Mortimer RK, et al. (1989) Genetic map of Saccharomyces cerevisiae, edition 10. Yeast 5(5):321-403", "pubmed_id": 2678811, "link": "/reference/S000073208", "year": 1989, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1002/yea.320050503"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/2678811"}]}, {"id": 598167, "display_name": "Mortimer RK, et al. (1992)", "citation": "Mortimer RK, et al. (1992) Genetic and physical maps of Saccharomyces cerevisiae, Edition 11. Yeast 8(10):817-902", "pubmed_id": 1413997, "link": "/reference/S000056506", "year": 1992, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1002/yea.320081002"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/1413997"}]}]}, {"category": "Name", "history_type": "LSP", "note": "Name: HSP90", "date_created": "2010-02-16", "references": [{"id": 607331, "display_name": "Gross DS, et al. (1990)", "citation": "Gross DS, et al. (1990) Promoter function and in situ protein/DNA interactions upstream of the yeast HSP90 heat shock genes. Antonie Van Leeuwenhoek 58(3):175-86", "pubmed_id": 2256678, "link": "/reference/S000053413", "year": 1990, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1007/BF00548930"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/2256678"}]}]}, {"category": "Mapping", "history_type": "SEQUENCE", "note": "Mapping: Edition 10: HSP90 is located 250 bp from cin2", "date_created": "1989-10-01", "references": [{"id": 552023, "display_name": "Mortimer RK, et al. (1989)", "citation": "Mortimer RK, et al. (1989) Genetic map of Saccharomyces cerevisiae, edition 10. Yeast 5(5):321-403", "pubmed_id": 2678811, "link": "/reference/S000073208", "year": 1989, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1002/yea.320050503"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/2678811"}]}]}, {"category": "Mapping", "history_type": "SEQUENCE", "note": "Mapping: Edition 11: HSP90 has been renamed HSP82", "date_created": "1992-10-01", "references": [{"id": 598167, "display_name": "Mortimer RK, et al. (1992)", "citation": "Mortimer RK, et al. (1992) Genetic and physical maps of Saccharomyces cerevisiae, Edition 11. Yeast 8(10):817-902", "pubmed_id": 1413997, "link": "/reference/S000056506", "year": 1992, "urls": [{"display_name": "DOI full text", "link": "http://dx.doi.org/10.1002/yea.320081002"}, {"display_name": "PubMed", "link": "http://www.ncbi.nlm.nih.gov/pubmed/1413997"}]}]}], "complexes": [{"format_name": "CPX-1276", "display_name": "HMC complex"}]}, tabs: {"id": 1284631, "protein_tab": true, "interaction_tab": true, "summary_tab": true, "go_tab": true, "sequence_section": true, "expression_tab": true, "phenotype_tab": true, "literature_tab": true, "wiki_tab": false, "regulation_tab": true, "sequence_tab": true, "history_tab": true, "homology_tab": true, "disease_tab": false} }; HSP82 | SGD

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HSP82 / YPL240C Overview

Standard Name
HSP82 1 2
Systematic Name
YPL240C
SGD ID
SGD:S000006161
Aliases
HSP90 34
Feature Type
ORF , Verified
Description
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 3 4 5 6 7 8 9 11 12 13 14
Name Description
Heat Shock Protein 10
Paralog
HSC82
Comparative Info
Sequence Details

Sequence

The S. cerevisiae Reference Genome sequence is derived from laboratory strain S288C. Download DNA or protein sequence, view genomic context and coordinates. Click "Sequence Details" to view all sequence information for this locus, including that for other strains.

Summary
HSP82 is on the left arm of chromosome XVI between CIN2 GTPase-activating protein and YAR1 nucleocytoplasmic shuttling assembly chaperone; coding sequence is 2130 nucleotides long with many, many SNPs; HSP82 has paralog HSC82 that arose from the whole genome duplication

Analyze Sequence

S288C only

BLASTN | BLASTP | Design Primers | Restriction Fragment Map | Restriction Fragment Sizes | Six-Frame Translation

S288C vs. other species

BLASTN vs. fungi | BLASTP at NCBI | BLASTP vs. fungi

S288C vs. other strains

Strain Alignment | Variant Viewer

Protein Details

Protein

Basic sequence-derived (length, molecular weight, isoelectric point) and experimentally-determined (median abundance, median absolute deviation) protein information. Click "Protein Details" for further information about the protein such as half-life, abundance, domains, domains shared with other proteins, protein sequence retrieval for various strains, physico-chemical properties, protein modification sites, and external identifiers for the protein.

Summary
Hsp82p is 709 amino acids long, very long-lived, and high in abundance; contains 7 Hsp90 domains; undergoes various post-translational modifications including methylation, acetylation, phosphorylation, succinylation, sumoylation, and ubiquitinylation at 29 residues; protein abundance increases in response to DNA replication stress
Length (a.a.)
709
Mol. Weight (Da)
81368.7
Isoelectric Point
4.54
Median Abundance (molecules/cell)
86723 +/- 51088
Half-life (hr)
65.0

Alleles

Curated mutant alleles for the specified gene, listed alphabetically. Click on the allele name to open the allele page. Click "SGD search" to view all alleles in search results.

View all HSP82 alleles in SGD search

Gene Ontology Details

Gene Ontology

GO Annotations consist of four mandatory components: a gene product, a term from one of the three Gene Ontology (GO) controlled vocabularies (Molecular Function, Biological Process, and Cellular Component), a reference, and an evidence code. SGD has manually curated and high-throughput GO Annotations, both derived from the literature, as well as computational, or predicted, annotations. Click "Gene Ontology Details" to view all GO information and evidence for this locus as well as biological processes it shares with other genes.

Summary
Unfolded protein-binding ATPase (chaperone); involved in folding of nascent proteins, mitochondrial targeting, and assembly of multiprotein complexes, such as proteasome and box C/D snoRNP; localizes in cytoplasm

View computational annotations

Molecular Function

Manually Curated

Biological Process

Manually Curated

Cellular Component

Manually Curated

Complex

Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.

Phenotype Details

Phenotype

Phenotype annotations for a gene are curated single mutant phenotypes that require an observable (e.g., "cell shape"), a qualifier (e.g., "abnormal"), a mutant type (e.g., null), strain background, and a reference. In addition, annotations are classified as classical genetics or high-throughput (e.g., large scale survey, systematic mutation set). Whenever possible, allele information and additional details are provided. Click "Phenotype Details" to view all phenotype annotations and evidence for this locus as well as phenotypes it shares with other genes.

Summary
Non-essential gene in reference strain S288C; null mutant is sensitive to freeze-thaw; some point mutations cause sensitivity to heat, hyperosmotic stress, Calcofluor White, geldanamycin and radicicol, decreased competitive fitness, slow exponential growth and decreased budding

Classical Genetics

conditional
null
overexpression
unspecified
reduction of function
dominant negative

Large-scale Survey

null
reduction of function
Interaction Details

Interaction

Interaction annotations are curated by BioGRID and include physical or genetic interactions observed between at least two genes. An interaction annotation is composed of the interaction type, name of the interactor, assay type (e.g., Two-Hybrid), annotation type (e.g., manual or high-throughput), and a reference, as well as other experimental details. Click "Interaction Details" to view all interaction annotations and evidence for this locus, including an interaction visualization.

Summary
The hsp82 null mutant is viable; the null mutant of paralog hsc82 is viable; the hsp82 hsc82 double mutant is inviable or displays a growth defect; Hsp82p interacts physically with proteins involved in translation, HSP82 interacts genetically with genes involved in transcription

2994 total interactions for 1872 unique genes

Physical Interactions

  • Affinity Capture-MS: 1206
  • Affinity Capture-RNA: 14
  • Affinity Capture-Western: 120
  • Biochemical Activity: 8
  • Co-crystal Structure: 7
  • Co-localization: 1
  • Co-purification: 3
  • FRET: 3
  • PCA: 1
  • Protein-peptide: 2
  • Proximity Label-MS: 4
  • Reconstituted Complex: 76
  • Two-hybrid: 226

Genetic Interactions

  • Dosage Growth Defect: 1
  • Dosage Lethality: 2
  • Dosage Rescue: 15
  • Negative Genetic: 20
  • Phenotypic Enhancement: 5
  • Phenotypic Suppression: 15
  • Positive Genetic: 2
  • Synthetic Growth Defect: 968
  • Synthetic Lethality: 279
  • Synthetic Rescue: 16
Regulation Details

Regulation

The number of putative Regulators (genes that regulate it) and Targets (genes it regulates) for the given locus, based on experimental evidence. This evidence includes data generated through high-throughput techniques. Click "Regulation Details" to view all regulation annotations, shared GO enrichment among regulation Targets, and a regulator/target diagram for the locus.

Summary
Transcription upregulated by Hsf1p in response to heat; protein activity regulated by Ppt1p in response to starvation
Regulators
37
Targets
0
Expression Details

Expression

Expression data are derived from records contained in the Gene Expression Omnibus (GEO), and are first log2 transformed and normalized. Referenced datasets may contain one or more condition(s), and as a result there may be a greater number of conditions than datasets represented in a single clickable histogram bar. The histogram division at 0.0 separates the down-regulated (green) conditions and datasets from those that are up-regulated (red). Click "Expression Details" to view all expression annotations and details for this locus, including a visualization of genes that share a similar expression pattern.

Summary Paragraph

A summary of the locus, written by SGD Biocurators following a thorough review of the literature. Links to gene names and curated GO terms are included within the Summary Paragraphs.

Last Updated: 2006-06-12

Literature Details

Literature

All manually curated literature for the specified gene, organized into topics according to their relevance to the gene (Primary Literature, Additional Literature, or Review). Click "Literature Details" to view all literature information for this locus, including shared literature between genes.

Primary
269
Additional
326
Reviews
94

Resources

AlphaFold Protein Structure | Entrez Gene | Entrez RefSeq Protein | FungiDB | Search all NCBI | UniParc | UniProtKB