Aliases for HSP90AA1 Gene
- Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 1 2 3
- HSP90A 3 4 6
- HSPCA 3 4 6
- HSPC1 3 4 6
- Lipopolysaccharide-Associated Protein 2 3 4
- Heat Shock 90kDa Protein 1, Alpha 2 3
- Renal Carcinoma Antigen NY-REN-38 3 4
- Heat Shock 90kD Protein 1, Alpha 2 3
- LPS-Associated Protein 2 3 4
- Heat Shock 86 KDa 3 4
- HSPCAL4 3 6
- HSP 86 3 4
- HSP89A 3 6
- HSP86 3 4
External Ids for HSP90AA1 Gene
Previous HGNC Symbols for HSP90AA1 Gene
Previous GeneCards Identifiers for HSP90AA1 Gene
The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids 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. [provided by RefSeq, Jan 2012]
GeneCards Summary for HSP90AA1 Gene
HSP90AA1 (Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 1) is a Protein Coding gene. Diseases associated with HSP90AA1 include lobular neoplasia and neuronal intranuclear inclusion disease. Among its related pathways are PI3K-Akt signaling pathway and Signaling by FGFR. GO annotations related to this gene include protein homodimerization activity and GTP binding. An important paralog of this gene is HSP90AB1.
UniProtKB/Swiss-Prot for HSP90AA1 Gene
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. 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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes.
Hsp90 (90 kDa heat shock protein) is a molecular chaperone that aids protein folding and quality control for a large number of client proteins. Functional Hsp90 operates as dimer and has intrinsic ATPase activity. The Hsp90 dimer acts in concert with other chaperones (e.g. Hsp70) and is regulated by a number of co-chaperones/accessory proteins (e.g. Hop, cdc37). Hsp90 has been shown to interact with >100 proteins and some notable clients include kinases (e.g. Raf-1), nuclear hormone receptors (e.g. estrogen receptors), transcription factors (e.g. p53), GPCRs (e.g. CB2 receptors) and ion channels (e.g. CFTR). In humans, the Hsp90beta isoform is constitutively expressed whereas the Hsp90alpha isoforms is expressed under stress conditions. Hsp90 plays an important role in some tumor cell types by stabilising mutated oncogenic proteins.