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Q12449

- AHA1_YEAST

UniProt

Q12449 - AHA1_YEAST

Protein

Hsp90 co-chaperone AHA1

Gene

AHA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.2 Publications

    GO - Molecular functioni

    1. ATPase activator activity Source: UniProtKB
    2. chaperone binding Source: SGD
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to heat Source: SGD
    2. positive regulation of ATPase activity Source: GOC
    3. protein folding Source: SGD

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29796-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hsp90 co-chaperone AHA1
    Alternative name(s):
    Activator of Hsp90 ATPase protein 1
    Gene namesi
    Name:AHA1
    Ordered Locus Names:YDR214W
    ORF Names:YD8142.16, YD8142B.06
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR214w.
    SGDiS000002622. AHA1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531D → A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. 1 Publication
    Mutagenesisi53 – 531D → K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. 1 Publication
    Mutagenesisi59 – 591R → A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication
    Mutagenesisi60 – 601K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication
    Mutagenesisi62 – 621K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 350350Hsp90 co-chaperone AHA1PRO_0000215822Add
    BLAST

    Proteomic databases

    MaxQBiQ12449.
    PaxDbiQ12449.
    PeptideAtlasiQ12449.

    Expressioni

    Inductioni

    By heat shock.1 Publication

    Gene expression databases

    GenevestigatoriQ12449.

    Interactioni

    Subunit structurei

    Monomer. Interacts with HSP82.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSC82P151083EBI-37072,EBI-8666
    HSP82P028297EBI-37072,EBI-8659

    Protein-protein interaction databases

    BioGridi32268. 85 interactions.
    DIPiDIP-1831N.
    IntActiQ12449. 37 interactions.
    MINTiMINT-401882.

    Structurei

    Secondary structure

    1
    350
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 2812
    Beta strandi32 – 343
    Beta strandi41 – 444
    Beta strandi49 – 535
    Beta strandi55 – 573
    Beta strandi68 – 7811
    Beta strandi82 – 854
    Beta strandi88 – 9912
    Helixi104 – 1063
    Beta strandi110 – 1134
    Helixi123 – 1308
    Helixi132 – 15019

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1USUX-ray2.15B1-156[»]
    1USVX-ray2.70B/D/F/H1-156[»]
    ProteinModelPortaliQ12449.
    SMRiQ12449. Positions 9-153, 213-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12449.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AHA1 family.Curated

    Phylogenomic databases

    eggNOGiCOG5580.
    GeneTreeiENSGT00390000006429.
    HOGENOMiHOG000191277.
    OMAiPEVSHEN.
    OrthoDBiEOG7Q5HQC.

    Family and domain databases

    Gene3Di3.30.530.20. 1 hit.
    InterProiIPR013538. Activator_of_Hsp90_ATPase.
    IPR015310. AHSA1_N.
    IPR023393. START-like_dom.
    [Graphical view]
    PfamiPF09229. Aha1_N. 1 hit.
    PF08327. AHSA1. 1 hit.
    [Graphical view]
    SMARTiSM01000. Aha1_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF103111. SSF103111. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q12449-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI    50
    EGDCEVNQRK GKVISLFDLK ITVLIEGHVD SKDGSALPFE GSINVPEVAF 100
    DSEASSYQFD ISIFKETSEL SEAKPLIRSE LLPKLRQIFQ QFGKDLLATH 150
    GNDIQVPESQ VKSNYTRGNQ KSSFTEIKDS ASKPKKNALP SSTSTSAPVS 200
    STNKVPQNGS GNSTSIYLEP TFNVPSSELY ETFLDKQRIL AWTRSAQFFN 250
    SGPKLETKEK FELFGGNVIS ELVSCEKDKK LVFHWKLKDW SAPFNSTIEM 300
    TFHESQEFHE TKLQVKWTGI PVGEEDRVRA NFEEYYVRSI KLTFGFGAVL 350
    Length:350
    Mass (Da):39,436
    Last modified:November 1, 1996 - v1
    Checksum:i06DF6B40EB5050BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti28 – 281L → I(PubMed:14739935)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z68194 Genomic DNA. Translation: CAA92357.1.
    Z68195 Genomic DNA. Translation: CAA92365.1.
    AY557694 Genomic DNA. Translation: AAS56020.1.
    U28414 Genomic DNA. Translation: AAA73862.1.
    BK006938 Genomic DNA. Translation: DAA12058.1.
    PIRiS61581.
    RefSeqiNP_010500.3. NM_001180522.3.

    Genome annotation databases

    EnsemblFungiiYDR214W; YDR214W; YDR214W.
    GeneIDi851800.
    KEGGisce:YDR214W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z68194 Genomic DNA. Translation: CAA92357.1 .
    Z68195 Genomic DNA. Translation: CAA92365.1 .
    AY557694 Genomic DNA. Translation: AAS56020.1 .
    U28414 Genomic DNA. Translation: AAA73862.1 .
    BK006938 Genomic DNA. Translation: DAA12058.1 .
    PIRi S61581.
    RefSeqi NP_010500.3. NM_001180522.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1USU X-ray 2.15 B 1-156 [» ]
    1USV X-ray 2.70 B/D/F/H 1-156 [» ]
    ProteinModelPortali Q12449.
    SMRi Q12449. Positions 9-153, 213-348.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32268. 85 interactions.
    DIPi DIP-1831N.
    IntActi Q12449. 37 interactions.
    MINTi MINT-401882.

    Proteomic databases

    MaxQBi Q12449.
    PaxDbi Q12449.
    PeptideAtlasi Q12449.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR214W ; YDR214W ; YDR214W .
    GeneIDi 851800.
    KEGGi sce:YDR214W.

    Organism-specific databases

    CYGDi YDR214w.
    SGDi S000002622. AHA1.

    Phylogenomic databases

    eggNOGi COG5580.
    GeneTreei ENSGT00390000006429.
    HOGENOMi HOG000191277.
    OMAi PEVSHEN.
    OrthoDBi EOG7Q5HQC.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29796-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q12449.
    NextBioi 969638.
    PROi Q12449.

    Gene expression databases

    Genevestigatori Q12449.

    Family and domain databases

    Gene3Di 3.30.530.20. 1 hit.
    InterProi IPR013538. Activator_of_Hsp90_ATPase.
    IPR015310. AHSA1_N.
    IPR023393. START-like_dom.
    [Graphical view ]
    Pfami PF09229. Aha1_N. 1 hit.
    PF08327. AHSA1. 1 hit.
    [Graphical view ]
    SMARTi SM01000. Aha1_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103111. SSF103111. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Sequence homology of the yeast regulatory protein ADR1 with Xenopus transcription factor TFIIIA."
      Hartshorne T.A., Blumberg H., Young E.T.
      Nature 320:283-287(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-350.
    5. Cited for: FUNCTION, INDUCTION, INTERACTION WITH HSP82.
    6. "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."
      Lotz G.P., Lin H., Harst A., Obermann W.M.J.
      J. Biol. Chem. 278:17228-17235(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSP82.
    7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery."
      Meyer P.
      EMBO J. 23:511-519(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-156 IN COMPLEX WITH HSP82, MUTAGENESIS OF ASP-53; ARG-59; LYS-60 AND LYS-62.

    Entry informationi

    Entry nameiAHA1_YEAST
    AccessioniPrimary (citable) accession number: Q12449
    Secondary accession number(s): D6VSJ8, Q02565, Q7LIE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 13939 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3