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HSP90AA1 (Heat shock protein HSP 90-alpha) is a gene whose normal job is to hold cell growth in check. The public catalogues list it as a drug target and a tumour suppressor, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Breast cancer.
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.
Open Targets scores its association with cancer at 0.75 (direct and indirect evidence; datatypes clinical 0.63, affected pathway 0.99, literature 1.00, genetic association 0.00, somatic mutation 0.43, animal model 0.52). IntOGen calls it a driver in 1 cohort (0 activating, 1 loss-of-function), covering Invasive Breast Carcinoma.
In plain words · HSP90AA1 (Heat shock protein HSP 90-alpha) is a gene whose normal job is to hold cell growth in check. The public catalogues list it as a drug target and a tumour suppressor, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Breast cancer.
HSP90AA1 (Heat shock protein HSP 90-alpha) is a gene whose normal job is to hold cell growth in check. The public catalogues list it as a drug target and a tumour suppressor, and clinical evidence ties its variants to diagnosis, prognosis or drug response. Tied to Breast cancer.
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.
No product in this corpus aims at HSP90AA1 yet. Because the protein is lost rather than overactive, drugs either restore its function or exploit the weakness its loss leaves (synthetic lethality).
Tumour-specific alteration: the catalogues call it a tumour suppressor (IntOGen finds it knocked out more often than chance); what a medicine would aim at or exploit is the altered form or its loss, absent from normal cells; no corpus medicine is aimed at it yet. HPA HSP90AA1: RNA low tissue specificity; high antibody staining in 3 normal tissues; highest cancer staining testis cancer (5 of 12 high). Distribution: 1 cancer family in the corpus carries a prevalence row, label threshold or catalogue link for it (Breast cancer (all types)); Open Targets associates it with 0 specific cancer types at or above 0.5. (Rule 6 of scripts/fetch-target-specificity.ts.)
Sources: UniProt P07900; IntOGen HSP90AA1; Human Protein Atlas HSP90AA1 tissue; Open Targets ENSG00000080824 associations
First described 1988. Earliest sequence paper UniProt cites for the protein: Hoffmann et al, Gene, 1988, "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens". Source.
Sources: HGNC HGNC:5253 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt P07900 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000080824 (association with cancer (MONDO_0004992) 0.75; (GraphQL API, CC0)); IntOGen HSP90AA1 (driver in 1 cohort (Act 0, LoF 1); Compendium_Cancer_Genes.tsv release 20240920, CC0 1.0)
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. Location: Nucleus; Cytoplasm; Melanosome; Cell membrane (UniProt). Locus 14q32.31 (HGNC).
RNA: low tissue specificity, detected in all normal tissues.
Medium: Bronchus, Duodenum, Epididymis, Gallbladder.
Medium only: breast cancer, cervical cancer, glioma, ovarian cancer.
Human Protein Atlas version 25.1, antibody staining at reliability approved, enhanced or supported; used under CC BY-SA 3.0. Staining counts are patients per level in the atlas cohort, not population prevalence.
Query for this target: (TITLE:"HSP90AA1" OR ABSTRACT:"HSP90AA1" OR TITLE:"heat shock protein 90 alpha family class A member 1" OR ABSTRACT:"heat shock protein 90 alpha family class A member 1" OR TITLE:"Heat shock protein HSP 90-alpha" OR ABSTRACT:"Heat shock protein HSP 90-alpha" OR TITLE:"Hsp89" OR ABSTRACT:"Hsp89" OR TITLE:"Hsp90" OR ABSTRACT:"Hsp90" OR TITLE:"FLJ31884" OR ABSTRACT:"FLJ31884") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about HSP90AA1, not a curated reading list.