AHA1 BASIC INFORMATION
| Standard Name | AHA1 1 |
|---|---|
| Systematic Name | YDR214W |
| Feature Type | ORF, Verified |
| Description | Co-chaperone that binds to Hsp82p and activates its ATPase activity; similar to Hch1p; expression is regulated by stresses such as heat shock (1, 2 and see Summary Paragraph)
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| Name Description | Activator of Heat shock protein 90 ATPase 1 |
| GO Annotations | All AHA1 GO evidence and references |
|---|---|
| View Computational GO annotations for AHA1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
| Mutant Phenotype | All AHA1 Phenotype details and references |
|---|---|
| Large-scale survey | |
| null |
| Interactions | AHA1 All interactions details and references |
|---|---|
| 65 total interaction(s) for 43 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB |
|---|
| Primary SGDID | S000002622 |
|---|
ADDITIONAL INFORMATION for AHA1
SUMMARY PARAGRAPH for AHA1
AHA1 and the closely related gene HCH1 encode cochaperones that regulate the activity of members of the HSP90 family (Hsp82p and Hsc82p in S. cerevisiae; 1, 3). The presence of Aha1p and Hch1p, although not required for ATP hydrolysis, is able to stimulate the Expression of AHA1 is induced by stress, a process mediated by the transcriptional activator Hsf1p which binds to three heat shock elements in the AHA1 promoter (1). AHA1 is not required for growth under optimal conditions but is essential for survival in cells under stress (1, 3). Aha1p is a highly conserved protein with similar proteins identified in S. pombe, worms, plants, flies, mice, and humans (3).
REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for AHA1]
| 1) | Panaretou B, et al. (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 10(6):1307-18 |
| 2) | Siligardi G, et al. (2004) Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle. J Biol Chem 279(50):51989-98 |
| 3) | Lotz GP, et al. (2003) 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(19):17228-35 |
| 4) | Meyer P, et al. (2004) Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J 23(6):1402-10 |




