AHSA1
AHSA1 (activator of HSP90 ATPase activity 1) is a co-chaperone that stimulates the ATPase activity of HSP90AA1 and so increases its chaperone activity. It is also known as Aha1, hAha1, p38 and C14orf3. Browse Assay Genie's current range of AHSA1 research reagents below, or read on for the biology behind the target.
AHSA1 acts as a co-chaperone of HSP90AA1. It activates the ATPase activity of HSP90AA1, which leads to an increase in the chaperone activity of HSP90AA1. NCBI Gene annotation describes the protein as enabling Hsp90 protein binding, protein folding chaperone and unfolded protein binding activities. It is involved in the maintenance of unfolded protein and in the positive regulation of ATP-dependent activity.
The AHSA1 protein also takes part in a reciprocal regulatory mechanism for the chaperoning of client proteins. It competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1. It likewise competes with another inhibitory co-chaperone, TSC1, for binding to HSP90AA1. Binding of AHSA1 to HSP90AA1 therefore sets it against these inhibitory partners, and this balance influences how client proteins are handled.
The AHSA1 gene encodes a protein that belongs to the AHA1 family and is located in the cytosol, with an annotated presence in the endoplasmic reticulum. The name reflects its role as an activator of HSP90 ATPase activity. The gene was previously designated chromosome 14 open reading frame 3 (C14orf3), and earlier nomenclature referred to it as AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast). The mouse ortholog is Ahsa1. Researchers studying HSP90 chaperone cycles, client protein folding and co-chaperone competition use AHSA1 as a defined regulatory component of this system.
AHSA1 activates the ATPase activity of HSP90AA1, making it a key co-chaperone for studying how chaperone activity is increased.
AHSA1 is annotated with protein folding chaperone and unfolded protein binding activities, relevant to work on client protein handling.
AHSA1 competes with the inhibitory co-chaperones FNIP1 and TSC1 for HSP90AA1 binding, offering a model of reciprocal regulation.
Its role in maintaining unfolded protein and regulating ATP-dependent activity places AHSA1 within studies of cellular protein quality control.
AHSA1 is a co-chaperone of HSP90AA1. It activates the ATPase activity of HSP90AA1, increasing its chaperone activity. It also competes with the inhibitory co-chaperones FNIP1 and TSC1 for binding to HSP90AA1, providing a reciprocal regulatory mechanism for chaperoning client proteins.
AHSA1 is also called Aha1, hAha1, p38 and C14orf3. Its HGNC full name is activator of HSP90 ATPase activity 1, and earlier names include chromosome 14 open reading frame 3 and AHA1, activator of heat shock 90kDa protein ATPase homolog 1 (yeast).
A mouse ortholog, Ahsa1, is recorded, and the name of the human protein refers to a yeast homolog. AHSA1 belongs to the AHA1 family. Check the datasheet of any product for its validated reactivity.
HSP90AA1 and the inhibitory co-chaperones FNIP1 and TSC1 are functionally linked to AHSA1 through shared binding to HSP90AA1.
Gene and protein annotations from HGNC, NCBI Gene and UniProt O95433; product specifications from Assay Genie datasheets.