| Identification |
|---|
| HMDB Protein ID
| HMDBP13820 |
| Secondary Accession Numbers
| None |
| Name
| Heat shock protein HSP 90-alpha |
| Synonyms
|
Not Available
|
| Gene Name
| HSP90AA1 |
| Protein Type
| Unknown |
| Biological Properties |
|---|
| General Function
| Not Available |
| Specific Function
| 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. 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. 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. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. |
| Pathways
|
- Antigen processing and presentation
- Chemical carcinogenesis - receptor activation
- Estrogen signaling pathway
- Fluid shear stress and atherosclerosis
- IL-17 signaling pathway
- Lipid and atherosclerosis
- Necroptosis
- NOD-like receptor signaling pathway
- PI3K-Akt signaling pathway
- Progesterone-mediated oocyte maturation
- Prostate cancer
- Protein processing in endoplasmic reticulum
- Salmonella infection
- Th17 cell differentiation
|
| Reactions
| Not Available |
| GO Classification
|
| Biological Process |
| response to heat |
| protein stabilization |
| cellular response to heat |
| response to antibiotic |
| response to cold |
| protein folding |
| Cellular Component |
| cytoplasm |
| protein-containing complex |
| myelin sheath |
| melanosome |
| neuronal cell body |
| perinuclear region of cytoplasm |
| nucleus |
| plasma membrane |
| cytosol |
| Molecular Function |
| ATPase activity |
| ATP binding |
| unfolded protein binding |
| disordered domain specific binding |
|
| Cellular Location
|
Not Available
|
| Gene Properties |
|---|
| Chromosome Location
| Not Available |
| Locus
| Not Available |
| SNPs
| Not Available |
| Gene Sequence
|
Not Available
|
| Protein Properties |
|---|
| Number of Residues
| 733 |
| Molecular Weight
| 84772.09 |
| Theoretical pI
| 5.003 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
Not Available
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| A5A6K9 |
| UniProtKB/Swiss-Prot Entry Name
| HS90A_PANTR |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| Not Available |
| GeneCard ID
| Not Available |
| GenAtlas ID
| Not Available |
| HGNC ID
| Not Available |
| References |
|---|
| General References
| - Sakate R, Suto Y, Imanishi T, Tanoue T, Hida M, Hayasaka I, Kusuda J, Gojobori T, Hashimoto K, Hirai M: Mapping of chimpanzee full-length cDNAs onto the human genome unveils large potential divergence of the transcriptome. Gene. 2007 Sep 1;399(1):1-10. doi: 10.1016/j.gene.2007.04.013. Epub 2007 Apr 20. [PubMed:17574350 ]
|
