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Showing Protein Heat shock protein HSP 90-alpha (HMDBP13744)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 2 metabolites
Identification
HMDB Protein ID HMDBP13744
Secondary Accession Numbers None
Name Heat shock protein HSP 90-alpha
Synonyms
  1. Heat shock 86 kDa
  2. Tumor-specific transplantation 86 kDa antigen
  3. HSP 86
  4. HSP86
  5. TSTA
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. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. 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. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Mediates the association of TOMM70 with IRF3 or TBK1 in mitochodria outer membrane which promotes host antiviral response.
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
protein refolding
response to heat
protein folding
positive regulation of protein import into nucleus
central nervous system neuron axonogenesis
protein stabilization
activation of innate immune response
neuron migration
cellular response to virus
chaperone-mediated protein complex assembly
establishment of cell polarity
positive regulation of cellular protein catabolic process
positive regulation of cytotoxic T cell differentiation
positive regulation of protein polymerization
positive regulation of tau-protein kinase activity
positive regulation of telomerase activity
positive regulation of cell size
protein insertion into mitochondrial outer membrane
regulation of cellular protein localization
regulation of protein ubiquitination
telomerase holoenzyme complex assembly
positive regulation of protein phosphorylation
positive regulation of interferon-beta production
positive regulation of nitric oxide biosynthetic process
positive regulation of lamellipodium assembly
positive regulation of defense response to virus by host
positive regulation of protein kinase B signaling cascade
regulation of apoptotic process
response to unfolded protein
response to antibiotic
telomere maintenance via telomerase
axon extension
positive regulation of peptidyl-serine phosphorylation
nitric oxide biosynthetic process
response to cold
cellular response to heat
Cellular Component
cytosol
cell surface
protein-containing complex
cytoplasm
mitochondrion
plasma membrane
perinuclear region of cytoplasm
nucleus
axonal growth cone
dendritic growth cone
sperm mitochondrial sheath
basolateral plasma membrane
melanosome
myelin sheath
sperm flagellum
sperm plasma membrane
collagen-containing extracellular matrix
neuronal cell body
brush border membrane
apical plasma membrane
neuron projection
Molecular Function
protein folding chaperone
unfolded protein binding
DNA polymerase binding
CTP binding
histone deacetylase binding
Rho GDP-dissociation inhibitor binding
scaffold protein binding
ATP binding
sulfonylurea receptor binding
tau protein binding
TPR domain binding
ubiquitin protein ligase binding
ion channel binding
disordered domain specific binding
dATP binding
protein homodimerization activity
UTP binding
nitric-oxide synthase regulator activity
ATPase activity
GTP binding
GTPase binding
identical protein binding
mRNA binding
protein phosphatase binding
protein tyrosine kinase 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 84787.19
Theoretical pI 5.003
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P07901
UniProtKB/Swiss-Prot Entry Name HS90A_MOUSE
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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