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    AHA1 Aha1p [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851800, updated on 28-Oct-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, Oct 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. A chemical compound inhibiting the Aha1-Hsp90 chaperone complex. Stiegler SC, et al. J Biol Chem, 2017 Oct 13. PMID 28851842, Free PMC Article
    4. Hsp90 Sensitivity to ADP Reveals Hidden Regulation Mechanisms. Halpin JC, et al. J Mol Biol, 2017 Sep 15. PMID 28822683, Free PMC Article
    5. 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

    See all (92) 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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