Reviewed,
UniProtKB/Swiss-Prot Q12449 (AHA1_YEAST)
Last modified
June 16, 2009.
Version 66.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Hsp90 co-chaperone AHA1 Alternative name(s): Activator of Hsp90 ATPase protein 1 | ||||||
| Gene names |
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| Organism | Saccharomyces cerevisiae (Baker's yeast) [Complete proteome] | ||||||
| Taxonomic identifier | 4932 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces |
Protein attributes
| Sequence length | 350 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (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. Ref.4 Ref.5 |
| Subunit structure | |
| Subcellular location | |
| Induction | By heat shock. Ref.4 |
| Miscellaneous | Present with 13939 molecules/cell in log phase SD medium. Ref.7 |
| Sequence similarities | Belongs to the AHA1 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Stress response |
| Cellular component | Cytoplasm |
| Molecular function | Chaperone |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein folding Ref.4 Inferred from mutant phenotype. Source: SGD |
| Cellular component | cytoplasm Ref.4 Inferred from physical interaction. Source: SGD |
| Molecular function | ATPase activator activity Ref.4 Ref.5 Inferred from direct assay. Source: UniProtKB chaperone binding Ref.4Inferred from direct assay. Source: SGD |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| HSP82 | P02829 | 2 | EBI-37072,EBI-8659 | |
| SPE2 | P21182 | 1 | EBI-37072,EBI-5655 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 350 | 350 | Hsp90 co-chaperone AHA1 | PRO_0000215822 | |||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||
| Modified residue | 35 | 1 | Phosphoserine Ref.9 | ||||||||||||||||||||||||
| Modified residue | 49 | 1 | Phosphoserine Ref.9 | ||||||||||||||||||||||||
| Modified residue | 159 | 1 | Phosphoserine Ref.9 | ||||||||||||||||||||||||
| Modified residue | 172 | 1 | Phosphoserine Ref.8 | ||||||||||||||||||||||||
| Modified residue | 173 | 1 | Phosphoserine Ref.9 | ||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||
| Mutagenesis | 53 | 1 | D → A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. Ref.10 | ||||||||||||||||||||||||
| Mutagenesis | 53 | 1 | D → K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. Ref.10 | ||||||||||||||||||||||||
| Mutagenesis | 59 | 1 | R → A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.10 | ||||||||||||||||||||||||
| Mutagenesis | 60 | 1 | K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.10 | ||||||||||||||||||||||||
| Mutagenesis | 62 | 1 | K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.10 | ||||||||||||||||||||||||
| Sequence conflict | 28 | 1 | L → I Ref.10 | ||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Helix | 17 – 28 | 12 | |||||||||||||||||||||||||
| Beta strand | 41 – 44 | 4 | |||||||||||||||||||||||||
| Beta strand | 49 – 53 | 5 | |||||||||||||||||||||||||
| Beta strand | 68 – 78 | 11 | |||||||||||||||||||||||||
| Beta strand | 88 – 99 | 12 | |||||||||||||||||||||||||
| Helix | 104 – 106 | 3 | |||||||||||||||||||||||||
| Beta strand | 110 – 113 | 4 | |||||||||||||||||||||||||
| Helix | 123 – 130 | 8 | |||||||||||||||||||||||||
| Helix | 132 – 150 | 19 | |||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. Zaccaria P.Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [2] | "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. LaBaer J.Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c. |
| [3] | "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: 3515197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-350. |
| [4] | "Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1." 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. Mol. Cell 10:1307-1318(2002) [PubMed: 12504007] [Abstract] Cited for: FUNCTION, INDUCTION, INTERACTION WITH HSP82. |
| [5] | "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: 12604615] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP82. |
| [6] | "Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. |
| [7] | "Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. |
| [8] | "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, MASS SPECTROMETRY. |
| [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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-159 AND SER-173, MASS SPECTROMETRY. |
| [10] | "Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery." Meyer P. EMBO J. 23:511-519(2004) [PubMed: 14739935] [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. |
| [11] | Erratum 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) [PubMed: 15039704] [Abstract] |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Z68194 Genomic DNA. Translation: CAA92357.1. Z68195 Genomic DNA. Translation: CAA92365.1. AY557694 Genomic DNA. Translation: AAS56020.1. U28414 Genomic DNA. Translation: AAA73862.1. | |||||||||||||||||||
| PIR | S61581. | ||||||||||||||||||
| RefSeq | NP_010500.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP:1831N. | ||||||||||||||||||
| IntAct | Q12449. 90 interactions. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PeptideAtlas | Q12449. | ||||||||||||||||||
| PRIDE | Q12449. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | YDR214W. Saccharomyces cerevisiae. [Contig view] | ||||||||||||||||||
| GeneID | 851800. | ||||||||||||||||||
| GenomeReviews | Gene locus YDR214W in contig Z71256_GR. | ||||||||||||||||||
| KEGG | sce:YDR214W. | ||||||||||||||||||
| NMPDR | fig|4932.3.peg.1257. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CYGD | YDR214w. | ||||||||||||||||||
| SGD | S000002622. AHA1. | ||||||||||||||||||
| Yeast-GFP | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | Q12449. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| GermOnline | YDR214W. Saccharomyces cerevisiae. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR013538. Activator_of_Hsp90_ATPase. IPR015310. AHSA1_N. [Graphical view] | ||||||||||||||||||
| Pfam | PF09229. Aha1_N. 1 hit. PF08327. AHSA1. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 969638. | ||||||||||||||||||
Entry information
| Entry name | AHA1_YEAST | ||||||||
| Accession | Primary (citable) accession number: Q12449 Secondary accession number(s): Q02565, Q7LIE3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |
| Yeast Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD |

Clusters with


