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.
Protein type: Chaperone
Chromosomal Location of Human Ortholog: 12|12 D2
Cellular Component:  cytoplasm; cytosol; endoplasmic reticulum
Molecular Function:  ATPase activator activity; chaperone binding; Hsp90 protein binding; protein binding
Biological Process:  positive regulation of ATPase activity
Reference #:  Q8BK64 (UniProtKB)
Alt. Names/Synonyms: Activator of 90 kDa heat shock protein ATPase homolog 1; AHA1; AHA1, activator of heat shock 90kDa protein ATPase homolog 1; AHA1, activator of heat shock protein ATPase 1; AHA1, activator of heat shock protein ATPase homolog 1; AHA1, activator of heat shock protein ATPase homolog 1 (yeast); Ahsa1; BC023857; MGC36589; MGC36618; p38
Gene Symbols: Ahsa1
Molecular weight: 38,117 Da
Basal Isoelectric point: 5.41  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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AHSA1

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene