Aliases:This biomarker is also known as:
- heat shock 90kD protein, alpha-like 4,
- Heat shock 86 kDa,
- heat shock 86 kDa,
- heat shock 90kD protein 1, alpha,
- renal carcinoma antigen NY-REN-38,
- Renal carcinoma antigen NY-REN-38,
- HSP 86,
- heat shock protein 90kDa alpha (cytosolic), class A member 1,
- heat shock 90kDa protein 1, alpha,
- heat shock protein HSP 90-alpha,
- heat shock 90kD protein 1, alpha-like 4,
The HSP90AA1 protein, also known as HSP90a, is a molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. HSP90AA1 is a homodimer that assists in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene.
There are no datasets associated with this biomarker.
The following organs have data associated with this biomarker…
HSP90a is important for the stability of and function of a wide range of oncoproteins and has been been identified in serum and lung cancer tissue or cell culture as a candidate lung cancer biomarker.
It has been shown that levels of HSP90a were elevated in lung cancer patients, and that the levels of HSP90a increased along with the clinical state of the NSCLC. HSP90a has been shown to participate in the metastasis of lung cancer. HSP90A is also a member of a 12 protein panel that can discriminate NSCLC from controls with 91% sensitivity and 84% specificity in cross-validated training and 89% sensitivity and 83% specificity in a separate verification set, with similar performance for early and late stage NSCLC.
External Resources for HSP90a
- GeneCards entry for human heat shock protein 90 alpha, HSP90AA1
- HGNC entry for human heat shock protein 90 alpha, HSP90AA1
- Protein Reference Sequence for human heat shock protein 90 alpha, HSP90AA1
- UniProtKB/Swiss-Prot entry for human heat shock protein 90 alpha, HSP90AA1
- Xu A, Tian T, Hao J, Liu J, Zhang Z, et al., J Cancer Mol. 2007;3:107ÃƒÂ¢Ã¢â€šÂ¬Ã¢â‚¬Å"112
|UniProt Accession #:||P07900|
|Mutated Sites Count:||190|
|Associated Pubmed ID Count||13|
|Affected Protein Function Sites Count:||4|