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UniProtKB/Swiss-Prot entry Q12449


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AHA1_YEAST
Primary accession number Q12449
Secondary accession numbers Q02565 Q7LIE3
Integrated into Swiss-Prot on November 23, 2004
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 58)
Name and origin of the protein
Protein name Hsp90 co-chaperone AHA1
Synonym Activator of Hsp90 ATPase protein 1
Gene name
Name: AHA1
OrderedLocusNames: YDR214W
ORFNames: YD8142.16, YD8142B.06
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-350.
DOI=10.1038/320283a0; PubMed=3515197 [NCBI, ExPASy, EBI, Israel, Japan]
Hartshorne T.A., Blumberg H., Young E.T.;
"Sequence homology of the yeast regulatory protein ADR1 with Xenopus transcription factor TFIIIA.";
Nature 320:283-287(1986).
[4]
FUNCTION, INDUCTION, AND INTERACTION WITH HSP82.
DOI=10.1016/S1097-2765(02)00785-2; PubMed=12504007 [NCBI, ExPASy, EBI, Israel, Japan]
Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., Cramer R., Mollapour M., Workman P., Piper P.W., Pearl L.H., Prodromou C.;
"Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.";
Mol. Cell 10:1307-1318(2002).
[5]
FUNCTION, AND INTERACTION WITH HSP82.
DOI=10.1074/jbc.M212761200; PubMed=12604615 [NCBI, ExPASy, EBI, Israel, Japan]
Lotz G.P., Lin H., Harst A., Obermann W.M.J.;
"Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.";
J. Biol. Chem. 278:17228-17235(2003).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-159 AND SER-173, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[10]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-156 IN COMPLEX WITH HSP82, AND MUTAGENESIS OF ASP-53; ARG-59; LYS-60 AND LYS-62.
DOI=10.1038/sj.emboj.7600060; PubMed=14739935 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer P.;
"Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery.";
EMBO J. 23:511-519(2004).
[11]
ERRATUM.
DOI=10.1038/sj.emboj.7600141; PubMed=15039704 [NCBI, ExPASy, EBI, Israel, Japan]
Meyer P., Prodromou C., Liao C., Hu B., Mark Roe S., Vaughan C.K., Vlasic I., Panaretou B., Piper P.W., Pearl L.H.;
EMBO J. 23:1402-1410(2004).
Comments
  • FUNCTION: 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.
  • SUBUNIT: Monomer. Interacts with HSP82.
  • INTERACTION:
    P02829:HSP82; NbExp=2; IntAct=EBI-37072, EBI-8659;
    P21182:SPE2; NbExp=1; IntAct=EBI-37072, EBI-5655;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • INDUCTION: By heat shock.
  • MISCELLANEOUS: Present with 13939 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the AHA1 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Z68194; CAA92357.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z68195; CAA92365.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557694; AAS56020.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28414; AAA73862.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S61581; S61581.
RefSeq NP_010500.1; -.
3D structure databases
PDB
1USU; X-ray; 2.15 A; B=1-156.[ExPASy / RCSB / EBI]
1USV; X-ray; 2.70 A; B/D/F/H=1-156.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1USU; -.
1USV; -.
ModBase Q12449.
Protein-protein interaction databases
DIP DIP:1831N; -.
IntAct Q12449; -.
Organism-specific databases
CYGD YDR214w; -.
SGD S000002622; AHA1.
Yeast-GFP YDR214W.
Gene expression databases
GermOnline YDR214W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from physical interaction from SGD).
GO:0001671; Molecular function: ATPase activator activity (inferred from direct assay from UniProtKB).
GO:0030189; Molecular function: chaperone activator activity (inferred from direct assay from SGD).
GO:0051087; Molecular function: chaperone binding (inferred from direct assay from SGD).
GO:0006457; Biological process: protein folding (inferred from mutant phenotype from SGD).
GO:0006950; Biological process: response to stress (inferred from expression pattern from SGD).
QuickGo view.
Family and domain databases
InterPro IPR013538; AHSA1.
IPR015310; AHSA1_N.
Graphical view of domain structure.
Pfam PF09229; Aha1_N; 1.
PF08327; AHSA1; 1.
Pfam graphical view of domain structure.
BLOCKS Q12449.
Proteomic databases
PeptideAtlas Q12449; -.
Genome annotation databases
Ensembl YDR214W; Saccharomyces cerevisiae. [Contig view]
GeneID 851800; -.
GenomeReviews Z71256_GR; YDR214W.
KEGG sce:YDR214W; -.
NMPDR fig|4932.3.peg.1257; -.
Phylogenomic databases
HOGENOM Q12449; -.
Other
LinkHub Q12449; -.
ProtoNet Q12449.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chaperone; Complete proteome; Cytoplasm; Phosphoprotein; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   350  350     Hsp90 co-chaperone AHA1. PRO_0000215822
MOD_RES   35    35        Phosphoserine. 
MOD_RES   49    49        Phosphoserine. 
MOD_RES   159   159        Phosphoserine. 
MOD_RES   172   172        Phosphoserine. 
MOD_RES   173   173        Phosphoserine. 
MUTAGEN   53    53        D->A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. 
MUTAGEN   53    53        D->K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. 
MUTAGEN   59    59        R->A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 
MUTAGEN   60    60        K->A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 
MUTAGEN   62    62        K->A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 
CONFLICT   28    28        L -> I (in Ref. 10). 
HELIX   17    28  12      
STRAND   41    44  4      
STRAND   49    53  5      
STRAND   68    78  11      
STRAND   88    99  12      
HELIX   104   106  3      
STRAND   110   113  4      
HELIX   123   130  8      
HELIX   132   150  19      
Sequence information
Length: 350 AA [This is the length of the unprocessed precursor] Molecular weight: 39436 Da [This is the MW of the unprocessed precursor] CRC64: 06DF6B40EB5050BE [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI EGDCEVNQRK 

        70         80         90        100        110        120 
GKVISLFDLK ITVLIEGHVD SKDGSALPFE GSINVPEVAF DSEASSYQFD ISIFKETSEL 

       130        140        150        160        170        180 
SEAKPLIRSE LLPKLRQIFQ QFGKDLLATH GNDIQVPESQ VKSNYTRGNQ KSSFTEIKDS 

       190        200        210        220        230        240 
ASKPKKNALP SSTSTSAPVS STNKVPQNGS GNSTSIYLEP TFNVPSSELY ETFLDKQRIL 

       250        260        270        280        290        300 
AWTRSAQFFN SGPKLETKEK FELFGGNVIS ELVSCEKDKK LVFHWKLKDW SAPFNSTIEM 

       310        320        330        340        350 
TFHESQEFHE TKLQVKWTGI PVGEEDRVRA NFEEYYVRSI KLTFGFGAVL 

Q12449 in FASTA format

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