Aliases for HSP90AB1 Gene
External Ids for HSP90AB1 Gene
Previous HGNC Symbols for HSP90AB1 Gene
Previous GeneCards Identifiers for HSP90AB1 Gene
This gene 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. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes. [provided by RefSeq, Dec 2012]
GeneCards Summary for HSP90AB1 Gene
HSP90AB1 (Heat Shock Protein 90 Alpha Family Class B Member 1) is a Protein Coding gene. Diseases associated with HSP90AB1 include Bronchitis and Larynx Cancer. Among its related pathways are Allograft rejection and Nucleotide-binding domain, leucine rich repeat containing receptor (NLR) signaling pathways. GO annotations related to this gene include poly(A) RNA binding and protein kinase binding. An important paralog of this gene is HSP90AA1.
UniProtKB/Swiss-Prot for HSP90AB1 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 (PubMed:16478993, PubMed:19696785). 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. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823).
Hsp90 (90 kDa heat shock protein) is a molecular chaperone that aids protein folding and quality control for a large number of 'client' proteins. Hsp90 operates as dimer and has intrinsic ATPase activity. The Hsp90 dimer acts in concert with other chaperones (e.g. Hsp70).