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Showing Protein Heat shock protein HSP 90-beta (HMDBP14537)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP14537
Secondary Accession Numbers None
Name Heat shock protein HSP 90-beta
Synonyms
  1. HSP 90
  2. Heat shock 84 kDa
  3. HSP 84
  4. HSP84
Gene Name HSP90AB1
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 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. They first 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 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). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059).
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
neutrophil degranulation
response to cocaine
Fc-gamma receptor signaling pathway involved in phagocytosis
negative regulation of neuron apoptotic process
protein folding
purinergic nucleotide receptor signaling pathway
positive regulation of protein import into nucleus
central nervous system neuron axonogenesis
virion attachment to host cell
negative regulation of complement-dependent cytotoxicity
response to salt stress
negative regulation of protein metabolic process
negative regulation of transforming growth factor beta activation
positive regulation of cyclin-dependent protein kinase activity
protein stabilization
positive regulation of phosphoprotein phosphatase activity
chaperone-mediated protein complex assembly
establishment of cell polarity
response to drug
positive regulation of tau-protein kinase activity
positive regulation of telomerase activity
positive regulation of cell size
regulation of cellular protein localization
regulation of protein ubiquitination
telomerase holoenzyme complex assembly
positive regulation of protein binding
regulation of interferon-gamma-mediated signaling pathway
regulation of type I interferon-mediated signaling pathway
positive regulation of nitric oxide biosynthetic process
cellular response to organic cyclic compound
xenobiotic metabolic process
negative regulation of proteasomal ubiquitin-dependent protein catabolic process
positive regulation of protein serine/threonine kinase activity
positive regulation of protein kinase B signaling cascade
response to unfolded protein
supramolecular fiber organization
positive regulation of transforming growth factor beta receptor signaling pathway
positive regulation of cell differentiation
negative regulation of proteasomal protein catabolic process
cellular response to interleukin-4
placenta development
telomere maintenance via telomerase
negative regulation of cell cycle arrest
axon extension
positive regulation of peptidyl-serine phosphorylation
cellular response to heat
regulation of cellular response to heat
positive regulation of protein localization to cell surface
Cellular Component
cytosol
cell surface
protein-containing complex
cytoplasm
mitochondrion
extracellular vesicular exosome
plasma membrane
perinuclear region of cytoplasm
aryl hydrocarbon receptor complex
dynein axonemal particle
nucleus
HSP90-CDC37 chaperone complex
ooplasm
sperm head plasma membrane
axonal growth cone
dendritic growth cone
nucleoplasm
basolateral plasma membrane
melanosome
extracellular region
neuronal cell body
inclusion body
brush border membrane
apical plasma membrane
membrane
ficolin-1-rich granule lumen
lysosomal membrane
secretory granule lumen
Molecular Function
protein folding chaperone
protein kinase binding
unfolded protein binding
DNA polymerase binding
histone methyltransferase binding
protein kinase regulator activity
double-stranded RNA binding
CTP binding
histone deacetylase binding
ATP binding
sulfonylurea receptor binding
tau protein binding
TPR domain binding
ubiquitin protein ligase binding
ion channel binding
kinase binding
peptide binding
disordered domain specific binding
dATP binding
heat shock protein binding
RNA binding
protein homodimerization activity
UTP binding
nitric-oxide synthase regulator activity
cadherin binding
ATPase activity
GTP binding
ATP-dependent protein binding
identical protein binding
MHC class II protein complex binding
protein dimerization activity
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 724
Molecular Weight 83263.475
Theoretical pI 5.039
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P08238
UniProtKB/Swiss-Prot Entry Name HS90B_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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