Pathway candidateNCBI-verifiedprotein-coding

HSP90AB1

heat shock protein 90 alpha family class B member 1

NCBI Gene: 3326 Ensembl GeneCards UniProt: P08238

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

HSP90AB1 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 HSP90AB1 is not, by itself, evidence of anything related to post-drug syndromes.

Gene summary

A protein-coding gene on chromosome 6 (steroid receptor chaperones). Encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation.

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

Protein reference (UniProt)

Protein: Heat shock protein HSP 90-beta
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 linked to its ATPase 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: Cytoplasm; Melanosome; Nucleus; Secreted; Cell membrane; Dynein axonemal particle; Cell surface.

Source: UniProtKB/Swiss-Prot P08238, 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 HSP90AB1 specifically.

Mentioned in 0 corpus records

No corpus record names HSP90AB1 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-beta
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 linked to its ATPase 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: Cytoplasm; Melanosome; Nucleus; Secreted; Cell membrane; Dynein axonemal particle; Cell surface.