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HCH1 Hch1p [ Saccharomyces cerevisiae S288C ]

Gene ID: 855440, updated on 4-Feb-2024

Summary

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Gene symbol
HCH1
Gene description
Hch1p
Primary source
SGD:S000005225
Locus tag
YNL281W
See related
AllianceGenome:SGD:S000005225
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables ATPase activator activity and chaperone binding activity. Involved in protein folding. Located in cytoplasm and nucleus. Orthologous to human AHSA1 (activator of HSP90 ATPase activity 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:
chromosome: XIV
Exon count:
1
Sequence:
Chromosome: XIV; NC_001146.8 (108467..108928)

Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Wsc2p Neighboring gene Pop3p Neighboring gene delta(14)-sterol reductase Neighboring gene pheromone-regulated protein PRM1

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway. Ran F, et al. J Biol Chem, 2010 Apr 30. PMID 20177068, Free PMC Article
  2. The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation. Mercier R, et al. Nat Commun, 2019 Mar 20. PMID 30894538, Free PMC Article
  3. The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922. Armstrong H, et al. PLoS One, 2012. PMID 23166640, Free PMC Article
  4. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. Meyer P, et al. EMBO J, 2004 Mar 24. PMID 15039704, Free PMC Article
  5. A mutation in the catalytic loop of Hsp90 specifically impairs ATPase stimulation by Aha1p, but not Hch1p. Horvat NK, et al. J Mol Biol, 2014 Jun 12. PMID 24726918

See all (53) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Phosphorylation of human Hsp90alpha at the highly conserved tyrosine (Y) 627 affects it conformation and function. Y627 is not phosphorylated in yeast, but study demonstrated that the non-conserved yeast co-chaperone, Hch1, modifies yeast Hsp90 (Hsp82) through Y606E phosphomimetic mutation raising the possibility that this post-translational modification in higher eukaryotes represents an evolutionary substitution for ...
    Title: An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.
  2. The work here suggests that both Hch1p and Aha1p regulate Hsp90 function through interaction with the catalytic loop but do so in different ways.
    Title: A mutation in the catalytic loop of Hsp90 specifically impairs ATPase stimulation by Aha1p, but not Hch1p.
  3. The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922.
    Title: The co-chaperone Hch1 regulates Hsp90 function differently than its homologue Aha1 and confers sensitivity to yeast to the Hsp90 inhibitor NVP-AUY922.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables ATPase activator activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATPase activator activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATPase activator activity IEA
Inferred from Electronic Annotation
more info
  
enables protein-folding chaperone binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein-folding chaperone binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in positive regulation of ATP-dependent activity IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein folding IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in protein folding IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in protein folding IPI
Inferred from Physical Interaction
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm HDA 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 HDA PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
  

General protein information

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Preferred Names
Hch1p
NP_014118.1
  • Heat shock protein regulator; binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; role in regulating Hsp90 inhibitor drug sensitivity; GFP-fusion protein localizes to the cytoplasm and nucleus; protein abundance increases in response to DNA replication stress

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

  1. NC_001146.8 Reference assembly

    Range
    108467..108928
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001183119.1 → NP_014118.1  TPA: Hch1p [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_014118.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6W0R3, P53834
    UniProtKB/TrEMBL
    A0A6A5Q567, A6ZRG4, B3LPC0, C7GP83, C8ZGP0, G2WLI5, N1NZV9
    Conserved Domains (1) summary
    COG5580
    Location:1 → 153
    COG5580; Activator of HSP90 ATPase [Posttranslational modification, protein turnover, chaperones]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P53834.1

Gene LinkOut

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