HSC82

id: P15108
gene_symbol: HSC82
product_type: PROTEIN
status: IN_PROGRESS
taxon:
  id: NCBITaxon:559292
  label: Saccharomyces cerevisiae
description: >-
  HSC82 is the constitutive (cognate) isoform of Hsp90 in S. cerevisiae. It is an ATP-dependent molecular
  chaperone that promotes the maturation, structural maintenance, and proper regulation of specific client
  proteins, particularly those involved in cell cycle control and signal transduction. HSC82 functions as a
  homodimer (and can heterodimerize with HSP82), undergoing an ATP-dependent conformational cycle that acts
  as a molecular clamp on client proteins. It interacts with the same network of co-chaperones as HSP82
  (STI1, AHA1, CDC37, SBA1, CPR6, CPR7, CNS1, SSE1, HCH1). HSC82 is expressed constitutively and accounts
  for the majority of Hsp90 protein under non-stress conditions.
existing_annotations:
# ============================================================================
# IBA ANNOTATIONS
# ============================================================================
- term:
    id: GO:0006457
    label: protein folding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      HSC82/Hsp90 is a well-established protein folding chaperone. IBA annotation is consistent with the
      known function of this conserved chaperone family across eukaryotes.
    action: ACCEPT
    reason: >-
      Protein folding is a core biological process for Hsp90. UniProt describes HSC82 as an "ATP-dependent
      molecular chaperone" that promotes maturation and regulation of client proteins. IMP evidence from
      PMID:7791797 confirms involvement in protein folding.
- term:
    id: GO:0016887
    label: ATP hydrolysis activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      HSC82 has well-characterized ATPase activity essential for its chaperone cycle. IBA annotation is correct.
    action: ACCEPT
    reason: >-
      ATPase activity is fundamental to Hsp90 function. Directly demonstrated by IDA (PMID:18492664).
      UniProt documents the ATP binding and hydrolysis mechanism.
- term:
    id: GO:0032991
    label: protein-containing complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      HSC82 functions as a homodimer and forms complexes with many co-chaperones and client proteins.
    action: ACCEPT
    reason: >-
      HSC82 is a homodimer and forms well-characterized complexes with co-chaperones (STI1, AHA1, SBA1,
      CDC37, CPR6, CPR7, CNS1, SSE1). Also heterodimerizes with HSP82 (PMID:31454312).
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for plasma membrane localization. HSC82 is primarily cytoplasmic but plasma membrane
      association has some HDA support (PMID:16622836).
    action: KEEP_AS_NON_CORE
    reason: >-
      HSC82 is primarily cytoplasmic. Plasma membrane localization is supported by HDA from PMID:16622836
      (plasma membrane proteome study) but is not a core localization. A minor membrane-associated pool
      is plausible.
- term:
    id: GO:0005524
    label: ATP binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      HSC82 binds ATP as part of its chaperone cycle. Well-established by crystallography of Hsp90 orthologs.
    action: ACCEPT
    reason: >-
      ATP binding is essential for Hsp90 function. The N-terminal domain contains the Bergerat ATP-binding
      fold. UniProt documents the ATP binding site residues.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      HSC82 is a cytosolic protein. IBA annotation is correct.
    action: ACCEPT
    reason: >-
      Consistent with HDA evidence for cytoplasm localization (PMID:14562095). Cytosol is the expected
      primary localization for Hsp90.
- term:
    id: GO:0050821
    label: protein stabilization
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      HSC82 stabilizes client proteins as part of its chaperone function. IBA annotation is appropriate.
    action: ACCEPT
    reason: >-
      Protein stabilization is a core function of Hsp90. UniProt describes the role of HSC82 in stabilizing
      calcineurin (CNA2) under salt stress (PMID:11094077).
- term:
    id: GO:0034605
    label: cellular response to heat
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      Although HSC82 is the constitutive isoform, it is still involved in heat stress response.
    action: ACCEPT
    reason: >-
      IMP evidence from PMID:2674684 confirms that both HSP82 and HSC82 are required for growth at
      elevated temperatures. While HSC82 is constitutively expressed, it still contributes to
      thermal tolerance.
- term:
    id: GO:0051082
    label: unfolded protein binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      GO:0051082 is proposed for obsoletion. HSC82 does interact with unfolded/misfolded client proteins
      but its mechanism is better captured by GO:0140662 (ATP-dependent protein folding chaperone).
    action: MODIFY
    reason: >-
      GO:0051082 is proposed for obsoletion. HSC82 is an ATP-dependent foldase; while it does bind
      unfolded/non-native proteins as part of its chaperone cycle, the binding is coupled to ATP-driven
      conformational changes. The more appropriate term is GO:0140662 "ATP-dependent protein folding
      chaperone" which captures both the binding and the active folding mechanism. IDA evidence
      from PMID:9465043 demonstrated binding to denatured substrates, but this is part of the broader
      chaperone activity.
    proposed_replacement_terms:
    - id: GO:0140662
      label: ATP-dependent protein folding chaperone
- term:
    id: GO:0048471
    label: perinuclear region of cytoplasm
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation for perinuclear localization. HSC82 is primarily cytoplasmic; perinuclear
      enrichment is inferred from ortholog data.
    action: KEEP_AS_NON_CORE
    reason: >-
      HSC82 is found in the cytoplasm. Perinuclear localization is inferred from orthologs and may
      represent a minor pool. Not a primary localization.
# ============================================================================
# IEA ANNOTATIONS
# ============================================================================
- term:
    id: GO:0000166
    label: nucleotide binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: >-
      IEA annotation from UniProt keyword mapping. Broader than ATP binding but not incorrect.
    action: ACCEPT
    reason: >-
      Nucleotide binding is a parent term of ATP binding. While more specific IBA and IEA annotations
      for ATP binding exist, this broader IEA annotation is not incorrect.
- term:
    id: GO:0000492
    label: box C/D snoRNP assembly
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: >-
      ARBA machine learning prediction for snoRNP assembly involvement. Supported by IMP evidence.
    action: KEEP_AS_NON_CORE
    reason: >-
      Supported by IMP evidence (PMID:18268103) which showed Hsp90 stabilizes Pih1/Nop17 to maintain
      R2TP complex activity that regulates snoRNA accumulation. This is a legitimate but secondary
      function of Hsp90.
- term:
    id: GO:0005524
    label: ATP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: >-
      IEA annotation for ATP binding. Consistent with IBA and experimental evidence.
    action: ACCEPT
    reason: >-
      Redundant with IBA annotation but correct. ATP binding is a core molecular function of HSC82.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: >-
      IEA annotation for cytoplasm from UniProt subcellular location mapping. Correct.
    action: ACCEPT
    reason: >-
      Consistent with HDA evidence for cytoplasmic localization (PMID:14562095).
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: >-
      IEA annotation for mitochondrial localization from UniProt. Supported by HDA evidence.
    action: KEEP_AS_NON_CORE
    reason: >-
      HSC82 has been detected in mitochondrial proteome studies (PMID:14576278, PMID:16823961). This is
      likely a minor pool; the primary localization is cytoplasmic. Not a core localization.
- term:
    id: GO:0006457
    label: protein folding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: >-
      IEA annotation for protein folding. Redundant with IBA but correct.
    action: ACCEPT
    reason: >-
      Consistent with IBA and experimental annotations for protein folding involvement.
- term:
    id: GO:0016887
    label: ATP hydrolysis activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: >-
      IEA annotation for ATP hydrolysis activity. Redundant with IBA and IDA but correct.
    action: ACCEPT
    reason: >-
      Consistent with IBA and IDA (PMID:18492664) annotations for ATPase activity.
- term:
    id: GO:0043248
    label: proteasome assembly
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: >-
      ARBA prediction for proteasome assembly involvement. Supported by IMP evidence.
    action: KEEP_AS_NON_CORE
    reason: >-
      Supported by IMP evidence (PMID:12853471). Hsp90 assists in proteasome assembly as one of
      its client-dependent functions. Not a core function of HSC82 per se.
- term:
    id: GO:0051082
    label: unfolded protein binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: >-
      IEA annotation for unfolded protein binding. Same issue as IBA annotation - term proposed for obsoletion.
    action: MODIFY
    reason: >-
      GO:0051082 is proposed for obsoletion. Should be replaced with GO:0140662 "ATP-dependent
      protein folding chaperone" which better captures the active chaperone mechanism.
    proposed_replacement_terms:
    - id: GO:0140662
      label: ATP-dependent protein folding chaperone
- term:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro for ATP-dependent protein folding chaperone. This is the correct
      and most informative molecular function term for HSC82.
    action: ACCEPT
    reason: >-
      GO:0140662 is the ideal molecular function term for HSC82/Hsp90. It captures both the ATP
      dependence and the protein folding chaperone activity. This should be considered the primary
      MF annotation for HSC82.
# ============================================================================
# IPI PROTEIN BINDING ANNOTATIONS
# ============================================================================
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:11805826
  review:
    summary: >-
      IPI from large-scale protein complex study. Uninformative "protein binding" annotation.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      "Protein binding" is uninformative for a molecular chaperone that by definition binds many
      proteins. The more informative annotation is GO:0140662 (ATP-dependent protein folding chaperone).
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:11805837
  review:
    summary: >-
      IPI from mass spectrometry study. Uninformative "protein binding" annotation.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15699485
  review:
    summary: >-
      IPI from polyubiquitin conjugate study.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15766533
  review:
    summary: >-
      IPI from large-scale chaperone network study (Zhao et al 2005).
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16429126
  review:
    summary: >-
      IPI from proteome survey.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16554755
  review:
    summary: >-
      IPI from large-scale protein complex study (Krogan et al 2006).
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:18719252
  review:
    summary: >-
      IPI from high-quality binary interaction map.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:19536198
  review:
    summary: >-
      IPI from atlas of chaperone-protein interactions.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21734642
  review:
    summary: >-
      IPI from SAGA/ADA complex study.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23217712
  review:
    summary: >-
      IPI from CDK-dependent Hsp70 phosphorylation study.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25073740
  review:
    summary: >-
      IPI from protein interaction study.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:31454312
  review:
    summary: >-
      IPI from structural pleiotropy study of Hsp90 paralogs. Documents HSP82-HSC82 heterodimerization.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      While the HSP82-HSC82 heterodimerization is biologically interesting, "protein binding"
      is uninformative. The heterodimerization could be captured by GO:0042802 (identical protein binding)
      or a more specific term.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:37070168
  review:
    summary: >-
      IPI from RNA-dependent interactome study.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:37968396
  review:
    summary: >-
      IPI from yeast protein interactome architecture study.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:9819421
  review:
    summary: >-
      IPI from Cns1/Hsp90 interaction study.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Uninformative "protein binding" for a chaperone.
# ============================================================================
# OTHER EXPERIMENTAL ANNOTATIONS
# ============================================================================
- term:
    id: GO:0070482
    label: response to oxygen levels
  evidence_type: NAS
  original_reference_id: PMID:9632766
  review:
    summary: >-
      NAS annotation based on HSC82 involvement in HAP1-mediated heme signaling.
    action: KEEP_AS_NON_CORE
    reason: >-
      HSC82 (like HSP82) forms a complex with HAP1, a transcriptional activator regulated by heme
      (proxy for oxygen). This is a client-dependent function. The NAS evidence is weak but the
      underlying biology is plausible.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: HDA
  original_reference_id: PMID:14562095
  review:
    summary: >-
      High-throughput GFP localization data confirming cytoplasm.
    action: ACCEPT
    reason: >-
      Global protein localization study. Core localization of HSC82.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HDA
  original_reference_id: PMID:14576278
  review:
    summary: >-
      HDA for mitochondrial localization from mitochondrial proteome study.
    action: KEEP_AS_NON_CORE
    reason: >-
      HSC82 was detected in the yeast mitochondrial proteome, suggesting a minor mitochondrial pool.
      Not a primary localization.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HDA
  original_reference_id: PMID:16823961
  review:
    summary: >-
      Additional HDA for mitochondrial localization from mitochondrial proteomics.
    action: KEEP_AS_NON_CORE
    reason: >-
      Consistent with PMID:14576278 for a minor mitochondrial pool. Not a core localization.
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: HDA
  original_reference_id: PMID:16622836
  review:
    summary: >-
      HDA for plasma membrane localization from plasma membrane proteomics study.
    action: KEEP_AS_NON_CORE
    reason: >-
      HSC82 was detected in the plasma membrane proteome, suggesting a minor membrane-associated pool.
      Not a primary localization.
- term:
    id: GO:0034605
    label: cellular response to heat
  evidence_type: IMP
  original_reference_id: PMID:2674684
  review:
    summary: >-
      IMP evidence showing that Hsp90 is essential for growth at elevated temperatures.
    action: ACCEPT
    reason: >-
      Study demonstrated that both HSP82 and HSC82 are required for growth at high temperatures.
      HSC82 is constitutively expressed but still contributes to heat stress tolerance.
- term:
    id: GO:0000492
    label: box C/D snoRNP assembly
  evidence_type: IMP
  original_reference_id: PMID:18268103
  review:
    summary: >-
      IMP evidence showing Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex for snoRNP assembly.
    action: KEEP_AS_NON_CORE
    reason: >-
      Hsp90 acts on the R2TP pathway components (Pih1, Tah1) that are required for snoRNP assembly.
      Client-dependent function, not core.
- term:
    id: GO:0000723
    label: telomere maintenance
  evidence_type: IMP
  original_reference_id: PMID:17954556
  review:
    summary: >-
      IMP evidence showing Hsp90 modulates telomerase activities.
    action: KEEP_AS_NON_CORE
    reason: >-
      Hsp90 chaperones telomerase components. This is a client-dependent function, not a core
      function of HSC82 itself.
- term:
    id: GO:0006457
    label: protein folding
  evidence_type: IMP
  original_reference_id: PMID:7791797
  review:
    summary: >-
      IMP evidence for protein folding from early characterization study.
    action: ACCEPT
    reason: >-
      Core biological process for HSC82/Hsp90. Directly demonstrates the role in protein folding.
- term:
    id: GO:0016887
    label: ATP hydrolysis activity
  evidence_type: IDA
  original_reference_id: PMID:18492664
  review:
    summary: >-
      Direct assay evidence for ATPase activity of HSC82. Intra- and intermonomer interactions
      are required for ATP hydrolysis.
    action: ACCEPT
    reason: >-
      Core molecular function. Direct biochemical measurement of ATPase activity showing that both
      intra- and intermonomer interactions synergistically facilitate ATP hydrolysis.
- term:
    id: GO:0043248
    label: proteasome assembly
  evidence_type: IMP
  original_reference_id: PMID:12853471
  review:
    summary: >-
      IMP evidence for proteasome assembly involvement.
    action: KEEP_AS_NON_CORE
    reason: >-
      HSC82 assists in proteasome assembly as a client-dependent function. Secondary to core
      chaperone activity.
- term:
    id: GO:0051082
    label: unfolded protein binding
  evidence_type: IDA
  original_reference_id: PMID:9465043
  review:
    summary: >-
      IDA evidence for unfolded protein binding. Term proposed for obsoletion.
    action: MODIFY
    reason: >-
      While the experimental evidence is solid (HSC82 does bind unfolded proteins), GO:0051082
      is proposed for obsoletion. The binding of unfolded proteins is part of the ATP-dependent
      chaperone mechanism, better captured by GO:0140662 "ATP-dependent protein folding chaperone."
    proposed_replacement_terms:
    - id: GO:0140662
      label: ATP-dependent protein folding chaperone
core_functions:
- description: >-
    Primary molecular function: ATP-dependent protein folding chaperone. HSC82 binds to
    client proteins and assists their folding through an ATP-dependent conformational cycle.
    Supported by IEA from InterPro, IDA evidence for ATP hydrolysis (PMID:18492664), and
    IDA evidence for unfolded protein binding (PMID:9465043).
  molecular_function:
    id: GO:0140662
    label: ATP-dependent protein folding chaperone
  directly_involved_in:
  - id: GO:0006457
    label: protein folding
  - id: GO:0034605
    label: cellular response to heat
  locations:
  - id: GO:0005737
    label: cytoplasm
- description: >-
    ATPase activity is fundamental to the Hsp90 chaperone cycle. Directly demonstrated by
    IDA (PMID:18492664). Intra- and intermonomer interactions synergistically facilitate
    ATP hydrolysis.
  molecular_function:
    id: GO:0016887
    label: ATP hydrolysis activity
  directly_involved_in:
  - id: GO:0006457
    label: protein folding
  locations:
  - id: GO:0005737
    label: cytoplasm
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000043
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:11805826
  title: Functional organization of the yeast proteome by systematic analysis of protein
    complexes.
  findings: []
- id: PMID:11805837
  title: Systematic identification of protein complexes in Saccharomyces cerevisiae
    by mass spectrometry.
  findings: []
- id: PMID:12853471
  title: The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome.
  findings: []
- id: PMID:14562095
  title: Global analysis of protein localization in budding yeast.
  findings: []
- id: PMID:14576278
  title: The proteome of Saccharomyces cerevisiae mitochondria.
  findings: []
- id: PMID:15699485
  title: Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor
    contributes to the turnover of multiple proteasome targets.
  findings: []
- id: PMID:15766533
  title: 'Navigating the chaperone network: an integrative map of physical and genetic
    interactions mediated by the hsp90 chaperone.'
  findings: []
- id: PMID:16429126
  title: Proteome survey reveals modularity of the yeast cell machinery.
  findings: []
- id: PMID:16554755
  title: Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
  findings: []
- id: PMID:16622836
  title: The plasma membrane proteome of Saccharomyces cerevisiae and its response
    to the antifungal calcofluor.
  findings: []
- id: PMID:16823961
  title: 'Toward the complete yeast mitochondrial proteome: multidimensional separation
    techniques for mitochondrial proteomics.'
  findings: []
- id: PMID:17954556
  title: The hsp90 molecular chaperone modulates multiple telomerase activities.
  findings: []
- id: PMID:18268103
  title: Molecular chaperone Hsp90 stabilizes Pih1/Nop17 to maintain R2TP complex
    activity that regulates snoRNA accumulation.
  findings: []
- id: PMID:18492664
  title: Intra- and intermonomer interactions are required to synergistically facilitate
    ATP hydrolysis in Hsp90.
  findings:
  - statement: Direct biochemical measurement of ATPase activity showing intra- and intermonomer cooperation
- id: PMID:18719252
  title: High-quality binary protein interaction map of the yeast interactome network.
  findings: []
- id: PMID:19536198
  title: 'An atlas of chaperone-protein interactions in Saccharomyces cerevisiae:
    implications to protein folding pathways in the cell.'
  findings: []
- id: PMID:21734642
  title: Combinatorial depletion analysis to assemble the network architecture of
    the SAGA and ADA chromatin remodeling complexes.
  findings: []
- id: PMID:23217712
  title: CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle
    progression.
  findings: []
- id: PMID:25073740
  title: Molecular architecture and function of the SEA complex, a modulator of the TORC1 pathway.
  findings: []
- id: PMID:2674684
  title: hsp82 is an essential protein that is required in higher concentrations for
    growth of cells at higher temperatures.
  findings:
  - statement: Both HSP82 and HSC82 are required for growth at elevated temperatures
- id: PMID:31454312
  title: The role of structural pleiotropy and regulatory evolution in the retention
    of heteromers of paralogs.
  findings: []
- id: PMID:37070168
  title: RNA-dependent interactome allows network-based assignment of RNA-binding
    protein function.
  findings: []
- id: PMID:37968396
  title: The social and structural architecture of the yeast protein interactome.
  findings: []
- id: PMID:7791797
  title: 'Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.'
  findings:
  - statement: Hsp90 is required for protein folding in vivo
- id: PMID:9465043
  title: Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence.
  findings:
  - statement: HSC82 binds unfolded proteins
- id: PMID:9632766
  title: 'Molecular mechanism governing heme signaling in yeast: a higher-order complex
    mediates heme regulation of the transcriptional activator HAP1.'
  findings: []
- id: PMID:9819421
  title: CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that
    suppresses cyclophilin 40 mutations and interacts with Hsp90.
  findings: []
- id: PMID:11094077
  title: Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.
  findings:
  - statement: HSC82 stabilizes and regulates calcineurin (CNA2) under salt stress conditions