ID:HS90B_HUMAN DESCRIPTION: RecName: Full=Heat shock protein HSP 90-beta; Short=HSP 90; AltName: Full=Heat shock 84 kDa; Short=HSP 84; Short=HSP84; 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. 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. SUBUNIT: Homodimer. Interacts with p53/TP53 (By similarity). Forms a complex with CDK6 and Hsp90/HSP90AB1. Interacts with UNC45A. Binding to UNC45A involves 2 UNC45A monomers per HSP90AB1 dimer. Interacts with CHORDC1 and DNAJC7 (By similarity). Interacts with FKBP4. INTERACTION: P04049:RAF1; NbExp=2; IntAct=EBI-352572, EBI-365996; SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. DOMAIN: The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins (By similarity). PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). PTM: ISGylated. PTM: S-nitrosylated; negatively regulates the ATPase activity (Probable). SIMILARITY: Belongs to the heat shock protein 90 family. SEQUENCE CAUTION: Sequence=AAD14062.3; Type=Erroneous initiation; Note=Translation N-terminally extended; Sequence=CAB66478.1; Type=Frameshift; Positions=709;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P08238
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0001890 placenta development GO:0006457 protein folding GO:0006805 xenobiotic metabolic process GO:0006950 response to stress GO:0006986 response to unfolded protein GO:0007004 telomere maintenance via telomerase GO:0009651 response to salt stress GO:0010033 response to organic substance GO:0019062 virion attachment to host cell GO:0021955 central nervous system neuron axonogenesis GO:0030010 establishment of cell polarity GO:0030511 positive regulation of transforming growth factor beta receptor signaling pathway GO:0031396 regulation of protein ubiquitination GO:0032092 positive regulation of protein binding GO:0032435 negative regulation of proteasomal ubiquitin-dependent protein catabolic process GO:0032516 positive regulation of phosphoprotein phosphatase activity GO:0033138 positive regulation of peptidyl-serine phosphorylation GO:0033160 positive regulation of protein import into nucleus, translocation GO:0035690 cellular response to drug GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis GO:0042220 response to cocaine GO:0042493 response to drug GO:0043066 negative regulation of apoptotic process GO:0043312 neutrophil degranulation GO:0043524 negative regulation of neuron apoptotic process GO:0045429 positive regulation of nitric oxide biosynthetic process GO:0045597 positive regulation of cell differentiation GO:0045793 positive regulation of cell size GO:0048675 axon extension GO:0050821 protein stabilization GO:0051131 chaperone-mediated protein complex assembly GO:0051248 negative regulation of protein metabolic process GO:0051897 positive regulation of protein kinase B signaling GO:0051973 positive regulation of telomerase activity GO:0060334 regulation of interferon-gamma-mediated signaling pathway GO:0060338 regulation of type I interferon-mediated signaling pathway GO:0071157 negative regulation of cell cycle arrest GO:0071353 cellular response to interleukin-4 GO:0071407 cellular response to organic cyclic compound GO:0071902 positive regulation of protein serine/threonine kinase activity GO:0097435 supramolecular fiber organization GO:1900034 regulation of cellular response to heat GO:1901389 negative regulation of transforming growth factor beta activation GO:1901799 negative regulation of proteasomal protein catabolic process GO:1902949 positive regulation of tau-protein kinase activity GO:1903660 negative regulation of complement-dependent cytotoxicity GO:1903827 regulation of cellular protein localization GO:1904031 positive regulation of cyclin-dependent protein kinase activity GO:1905323 telomerase holoenzyme complex assembly GO:2000010 positive regulation of protein localization to cell surface