HSP90AA1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006986Biological processresponse to unfolded protein
GO_0032728Biological processpositive regulation of interferon-beta production
GO_0003009Biological processskeletal muscle contraction
GO_0009651Biological processresponse to salt stress
GO_0001764Biological processneuron migration
GO_1905323Biological processtelomerase holoenzyme complex assembly
GO_0050821Biological processprotein stabilization
GO_0045040Biological processprotein insertion into mitochondrial outer membrane
GO_0009410Biological processresponse to xenobiotic stimulus
GO_0002230Biological processpositive regulation of defense response to virus by host
GO_0009408Biological processresponse to heat
GO_1902949Biological processpositive regulation of tau-protein kinase activity
GO_0032880Biological processregulation of protein localization
GO_0042307Biological processpositive regulation of protein import into nucleus
GO_0006839Biological processmitochondrial transport
GO_0099072Biological processregulation of postsynaptic membrane neurotransmitter receptor levels
GO_0031396Biological processregulation of protein ubiquitination
GO_0051131Biological processchaperone-mediated protein complex assembly
GO_0045732Biological processpositive regulation of protein catabolic process
GO_0042220Biological processresponse to cocaine
GO_0042981Biological processregulation of apoptotic process
GO_0061684Biological processchaperone-mediated autophagy
GO_0045429Biological processpositive regulation of nitric oxide biosynthetic process
GO_0001934Biological processpositive regulation of protein phosphorylation
GO_0046677Biological processresponse to antibiotic
GO_0043254Biological processregulation of protein-containing complex assembly
GO_0007004Biological processtelomere maintenance via telomerase
GO_0034605Biological processcellular response to heat
GO_0043627Biological processresponse to estrogen
GO_0010592Biological processpositive regulation of lamellipodium assembly
GO_0043335Biological processprotein unfolding
GO_0006457Biological processprotein folding
GO_0098586Biological processcellular response to virus
GO_0009409Biological processresponse to cold
GO_0010659Biological processcardiac muscle cell apoptotic process
GO_0042026Biological processprotein refolding
GO_0002218Biological processactivation of innate immune response
GO_0032273Biological processpositive regulation of protein polymerization
GO_0045793Biological processpositive regulation of cell size
GO_0060452Biological processpositive regulation of cardiac muscle contraction
GO_0097226Cellular componentsperm mitochondrial sheath
GO_0043025Cellular componentneuronal cell body
GO_0009986Cellular componentcell surface
GO_1904813Cellular componentficolin-1-rich granule lumen
GO_0043202Cellular componentlysosomal lumen
GO_0016323Cellular componentbasolateral plasma membrane
GO_0005634Cellular componentnucleus
GO_0097524Cellular componentsperm plasma membrane
GO_0005576Cellular componentextracellular region
GO_0070062Cellular componentextracellular exosome
GO_0005654Cellular componentnucleoplasm
GO_0005886Cellular componentplasma membrane
GO_0016020Cellular componentmembrane
GO_0005739Cellular componentmitochondrion
GO_0032991Cellular componentprotein-containing complex
GO_0034774Cellular componentsecretory granule lumen
GO_0044294Cellular componentdendritic growth cone
GO_0044295Cellular componentaxonal growth cone
GO_0005737Cellular componentcytoplasm
GO_0031526Cellular componentbrush border membrane
GO_0016324Cellular componentapical plasma membrane
GO_0043209Cellular componentmyelin sheath
GO_0048471Cellular componentperinuclear region of cytoplasm
GO_0071682Cellular componentendocytic vesicle lumen
GO_0062023Cellular componentcollagen-containing extracellular matrix
GO_0005829Cellular componentcytosol
GO_0042470Cellular componentmelanosome
GO_0051020Molecular functionGTPase binding
GO_0031625Molecular functionubiquitin protein ligase binding
GO_0042802Molecular functionidentical protein binding
GO_0051022Molecular functionRho GDP-dissociation inhibitor binding
GO_0097110Molecular functionscaffold protein binding
GO_0032564Molecular functiondATP binding
GO_0005524Molecular functionATP binding
GO_0048156Molecular functiontau protein binding
GO_0030911Molecular functionTPR domain binding
GO_0051082Molecular functionunfolded protein binding
GO_0023026Molecular functionMHC class II protein complex binding
GO_0042826Molecular functionhistone deacetylase binding
GO_0070182Molecular functionDNA polymerase binding
GO_0017098Molecular functionsulfonylurea receptor binding
GO_0003729Molecular functionmRNA binding
GO_1990782Molecular functionprotein tyrosine kinase binding
GO_0005525Molecular functionGTP binding
GO_0002134Molecular functionUTP binding
GO_0002135Molecular functionCTP binding
GO_0044325Molecular functiontransmembrane transporter binding
GO_0003723Molecular functionRNA binding
GO_0005515Molecular functionprotein binding
GO_0042803Molecular functionprotein homodimerization activity
GO_0019903Molecular functionprotein phosphatase binding
GO_0030235Molecular functionnitric-oxide synthase regulator activity
GO_0140662Molecular functionATP-dependent protein folding chaperone
GO_0097718Molecular functiondisordered domain specific binding
GO_0016887Molecular functionATP hydrolysis activity

IV. Literature review

[source]
Gene nameHSP90AA1
Protein nameHeat shock protein HSP 90-alpha (EC 3.6.4.10) (Heat shock 86 kDa) (HSP 86) (HSP86) (Lipopolysaccharide-associated protein 2) (LAP-2) (LPS-associated protein 2) (Renal carcinoma antigen NY-REN-38)
Heat shock protein 90 alpha family class A member 1
HSP90AA1 protein
SynonymsHSP90A
HSPCA
HSPC1
DescriptionFUNCTION: 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 mitochondrial outer membrane which promotes host antiviral response . .; FUNCTION: (Microbial infection) Seems to interfere with N.meningitidis NadA-mediated invasion of human cells. Decreasing HSP90 levels increases adhesion and entry of E.coli expressing NadA into human Chang cells; increasing its levels leads to decreased adhesion and invasion. .

AccessionsQ8TBA7
ENST00000553585.5
ENST00000334701.11 [P07900-2]
ENST00000216281.13 [P07900-1]
P07900
A0A0U1RR69
ENST00000557234.1
Q2VPJ6
H0YJF5
ENST00000554401.1
Q96HX7
ENST00000558600.1
G3V2J8
G3V592