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AHA1 Aha1p [ Saccharomyces cerevisiae S288C ]

Gene ID: 851800, updated on 3-Nov-2024

Summary

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Official Symbol
AHA1
Official Full Name
Aha1p
Primary source
SGD:S000002622
Locus tag
YDR214W
See related
AllianceGenome:SGD:S000002622; FungiDB:YDR214W; VEuPathDB:YDR214W
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 protein-folding chaperone binding activity. Involved in protein folding. Acts upstream of or within protein import into nucleus. Located in cytoplasm and nucleus. Orthologous to several human genes including AHSA1 (activator of HSP90 ATPase activity 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See AHA1 in Genome Data Viewer
Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (892875..893927)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene chaperonin-containing T-complex alpha subunit TCP1 Neighboring gene Upc2p Neighboring gene uncharacterized protein Neighboring gene DNA-binding transcription factor ADR1

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001136.10

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism. Schulze A, et al. Nat Chem Biol, 2016 Aug. PMID 27322067, Free PMC Article
  2. DNA damage-induced nuclear import of HSP90α is promoted by Aha1. Fangaria N, et al. Mol Biol Cell, 2022 Dec 1. PMID 36260391, Free PMC Article
  3. Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions. Meyer P, et al. Mol Cell, 2003 Mar. PMID 12667448
  4. A chemical compound inhibiting the Aha1-Hsp90 chaperone complex. Stiegler SC, et al. J Biol Chem, 2017 Oct 13. PMID 28851842, Free PMC Article
  5. Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms. Halpin JC, et al. J Mol Biol, 2017 Sep 15. PMID 28822683, Free PMC Article

See all (93) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation.
    Title: The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation.
  2. A chemical compound inhibiting the Aha1-Hsp90 chaperone complex
    Title: A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.
  3. 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.
  4. Aha1 facilitates the progression of the Hsp90 co-chaperone cycle.
    Title: Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle.
  5. an interaction between Aha1 and residues near the C terminus of Mal63
    Title: Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway.
  6. For maximum activation of Hsp90, the two domains of Aha1 bind to sites in the middle and N-terminal domains of Hsp90 in a sequential manner.
    Title: Asymmetric activation of the hsp90 dimer by its cochaperone aha1.
  7. binding of N-Aha1 promotes a conformational switch in the middle-segment catalytic loop (370-390) of Hsp90 that releases the catalytic Arg 380
    Title: Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.
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 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 
acts_upstream_of_or_within protein import into nucleus IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytoplasm IPI
Inferred from Physical Interaction
more info
 PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 

General protein information

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Preferred Names
Aha1p
NP_010500.3
  • Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; involved in the nuclear import of Hsp82p after DNA damage; expression is regulated by stresses such as heat shock; 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_001136.10 Reference assembly

    Range
    892875..893927
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180522.3 → NP_010500.3  TPA: Aha1p [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010500.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VSJ8, Q02565, Q12449, Q7LIE3
    UniProtKB/TrEMBL
    B5VGA4, N1PAF6
    Conserved Domains (1) summary
    COG5580
    Location:1 → 350
    COG5580; Activator of HSP90 ATPase [Posttranslational modification, protein turnover, chaperones]
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
Q12449.1

Gene LinkOut

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