Pathway candidateNCBI-verifiedprotein-coding

HSP90AA1

heat shock protein 90 alpha family class A member 1

NCBI Gene: 3320 Ensembl GeneCards UniProt: P07900

Pathway candidate — not linked to PFS or PSSD by any record here

HSP90AA1 is in the library because it belongs to the receptor chaperones family. No study, report or commentary in the corpus names it, so a variant in HSP90AA1 is not, by itself, evidence of anything related to post-drug syndromes.

Gene summary

A protein-coding gene on chromosome 14 (steroid receptor chaperones). The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones.

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: Heat shock protein HSP 90-alpha
Function (excerpt): Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone.
Subcellular location: Nucleus; Cytoplasm; Melanosome; Cell membrane; Mitochondrion.

Source: UniProtKB/Swiss-Prot P07900, release 2026_03, licensed CC BY 4.0. This is the protein’s normal biology, not evidence about post-drug syndromes; associated conditions are inherited disorders of the gene, not PFS, PSSD or PRSD.

Why its pathway is in the library

Chaperone/co-chaperone control of steroid-receptor folding and sensitivity is a regulatory layer above the receptors themselves, tied to stress-axis signaling.

Written for the whole receptor chaperones family, not for HSP90AA1 specifically.

Mentioned in 0 corpus records

No corpus record names HSP90AA1 directly yet. It is in the library because it sits in a pathway the corpus tracks (Receptor chaperones).

Also in steroid receptor chaperones

All 14 genes

Browse by family on the gene families page.

Gene summary

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: Heat shock protein HSP 90-alpha
Function (excerpt): Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone.
Subcellular location: Nucleus; Cytoplasm; Melanosome; Cell membrane; Mitochondrion.