Aliases for HSP90AA2P Gene
- Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 2, Pseudogene 2 3
- HSP90AA2 3 4 6
- HSPCAL3 3 4 6
- Heat Shock 90kDa Protein 1, Alpha-Like 3 2 3
- Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 1 Pseudogene 3
- Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 2 2
- Heat Shock Protein HSP 90-Alpha A2 Pseudogene 4
External Ids for HSP90AA2P Gene
Previous Symbols for HSP90AA2P Gene
HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90AA2 is a cytosolic HSP90 protein. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; MIM 191175) and mitochondria (TRAP1; MIM 606219) (Chen et al., 2005 [PubMed 16269234]). See HSP90AA1 (MIM 140571) for further information on HSP90 proteins.[supplied by OMIM, Aug 2008]
GeneCards Summary for HSP90AA2P Gene
HSP90AA2P (Heat Shock Protein 90kDa Alpha (Cytosolic), Class A Member 2, Pseudogene) is a Pseudogene. Among its related pathways are MAPK Pathway.
UniProtKB/Swiss-Prot for HSP90AA2P Gene
Putative molecular chaperone that may promote the maturation, structural maintenance and proper regulation of specific target proteins.
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.