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AHSA1
Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Belongs to the AHA1 family. Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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| Protein type: Chaperone |
| Chromosomal Location of human Ortholog: 14q24.3 |
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Cellular Component:
cytosol; endoplasmic reticulum
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Molecular Function:
ATPase activator activity; Hsp90 protein binding; protein binding; protein-folding chaperone binding
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Biological Process:
positive regulation of ATP-dependent activity; protein folding
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Reference #:
O95433
(UniProtKB)
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Alt. Names/Synonyms: Activator of 90 kDa heat shock protein ATPase homolog 1; activator of HSP90 ATPase activity 1; AHA1; AHA1, activator of heat shock 90kDa protein ATPase homolog 1; AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast); AHSA1; C14orf3; hAha1; p38
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Gene Symbols: AHSA1
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Molecular weight:
38,274 Da
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Basal Isoelectric point:
5.41
Predict pI for various phosphorylation states
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Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology®
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