Browse HSP90AA1

Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Basic function annotation.
> Subcellular Location, Domain and Function
> Gene Ontology
> KEGG and Reactome Pathway
> Subcellular Location, Domain and Function
 
Subcellular Location Nucleus Cytoplasm Melanosome Cell membrane Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Domain PF02518 Histidine kinase-
PF00183 Hsp90 protein
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 (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). 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 (PubMed:29127155). 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 (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). 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 (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).

> Gene Ontology
 
Biological Process GO:0000060 protein import into nucleus, translocation
GO:0000086 G2/M transition of mitotic cell cycle
GO:0001764 neuron migration
GO:0002429 immune response-activating cell surface receptor signaling pathway
GO:0002431 Fc receptor mediated stimulatory signaling pathway
GO:0002433 immune response-regulating cell surface receptor signaling pathway involved in phagocytosis
GO:0002757 immune response-activating signal transduction
GO:0002764 immune response-regulating signaling pathway
GO:0002768 immune response-regulating cell surface receptor signaling pathway
GO:0003009 skeletal muscle contraction
GO:0003012 muscle system process
GO:0003013 circulatory system process
GO:0003015 heart process
GO:0006457 protein folding
GO:0006606 protein import into nucleus
GO:0006626 protein targeting to mitochondrion
GO:0006809 nitric oxide biosynthetic process
GO:0006839 mitochondrial transport
GO:0006898 receptor-mediated endocytosis
GO:0006909 phagocytosis
GO:0006913 nucleocytoplasmic transport
GO:0006914 autophagy
GO:0006936 muscle contraction
GO:0006937 regulation of muscle contraction
GO:0006941 striated muscle contraction
GO:0006942 regulation of striated muscle contraction
GO:0006970 response to osmotic stress
GO:0006986 response to unfolded protein
GO:0007006 mitochondrial membrane organization
GO:0007008 outer mitochondrial membrane organization
GO:0008015 blood circulation
GO:0008016 regulation of heart contraction
GO:0008361 regulation of cell size
GO:0009266 response to temperature stimulus
GO:0009408 response to heat
GO:0009409 response to cold
GO:0009651 response to salt stress
GO:0010591 regulation of lamellipodium assembly
GO:0010592 positive regulation of lamellipodium assembly
GO:0010657 muscle cell apoptotic process
GO:0010658 striated muscle cell apoptotic process
GO:0010659 cardiac muscle cell apoptotic process
GO:0017038 protein import
GO:0018108 peptidyl-tyrosine phosphorylation
GO:0018212 peptidyl-tyrosine modification
GO:0030031 cell projection assembly
GO:0030032 lamellipodium assembly
GO:0031346 positive regulation of cell projection organization
GO:0031396 regulation of protein ubiquitination
GO:0031647 regulation of protein stability
GO:0032386 regulation of intracellular transport
GO:0032388 positive regulation of intracellular transport
GO:0032535 regulation of cellular component size
GO:0032768 regulation of monooxygenase activity
GO:0033157 regulation of intracellular protein transport
GO:0033158 regulation of protein import into nucleus, translocation
GO:0033160 positive regulation of protein import into nucleus, translocation
GO:0034504 protein localization to nucleus
GO:0034605 cellular response to heat
GO:0035966 response to topologically incorrect protein
GO:0038093 Fc receptor signaling pathway
GO:0038094 Fc-gamma receptor signaling pathway
GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis
GO:0038127 ERBB signaling pathway
GO:0038128 ERBB2 signaling pathway
GO:0042026 protein refolding
GO:0042220 response to cocaine
GO:0042306 regulation of protein import into nucleus
GO:0042307 positive regulation of protein import into nucleus
GO:0042493 response to drug
GO:0043254 regulation of protein complex assembly
GO:0043279 response to alkaloid
GO:0043335 protein unfolding
GO:0043627 response to estrogen
GO:0044057 regulation of system process
GO:0044089 positive regulation of cellular component biogenesis
GO:0044743 intracellular protein transmembrane import
GO:0044744 protein targeting to nucleus
GO:0044770 cell cycle phase transition
GO:0044772 mitotic cell cycle phase transition
GO:0044839 cell cycle G2/M phase transition
GO:0045040 protein import into mitochondrial outer membrane
GO:0045428 regulation of nitric oxide biosynthetic process
GO:0045429 positive regulation of nitric oxide biosynthetic process
GO:0045793 positive regulation of cell size
GO:0045823 positive regulation of heart contraction
GO:0045933 positive regulation of muscle contraction
GO:0045989 positive regulation of striated muscle contraction
GO:0046209 nitric oxide metabolic process
GO:0046677 response to antibiotic
GO:0046822 regulation of nucleocytoplasmic transport
GO:0046824 positive regulation of nucleocytoplasmic transport
GO:0048010 vascular endothelial growth factor receptor signaling pathway
GO:0050821 protein stabilization
GO:0050879 multicellular organismal movement
GO:0050881 musculoskeletal movement
GO:0050999 regulation of nitric-oxide synthase activity
GO:0051131 chaperone-mediated protein complex assembly
GO:0051169 nuclear transport
GO:0051170 nuclear import
GO:0051222 positive regulation of protein transport
GO:0051341 regulation of oxidoreductase activity
GO:0055117 regulation of cardiac muscle contraction
GO:0060047 heart contraction
GO:0060048 cardiac muscle contraction
GO:0060452 positive regulation of cardiac muscle contraction
GO:0060491 regulation of cell projection assembly
GO:0061684 chaperone-mediated autophagy
GO:0065002 intracellular protein transmembrane transport
GO:0070585 protein localization to mitochondrion
GO:0071806 protein transmembrane transport
GO:0072593 reactive oxygen species metabolic process
GO:0072655 establishment of protein localization to mitochondrion
GO:0072657 protein localization to membrane
GO:0090066 regulation of anatomical structure size
GO:0090150 establishment of protein localization to membrane
GO:0090151 establishment of protein localization to mitochondrial membrane
GO:0090257 regulation of muscle system process
GO:0090316 positive regulation of intracellular protein transport
GO:0097581 lamellipodium organization
GO:1900034 regulation of cellular response to heat
GO:1900180 regulation of protein localization to nucleus
GO:1900182 positive regulation of protein localization to nucleus
GO:1902593 single-organism nuclear import
GO:1902743 regulation of lamellipodium organization
GO:1902745 positive regulation of lamellipodium organization
GO:1903320 regulation of protein modification by small protein conjugation or removal
GO:1903409 reactive oxygen species biosynthetic process
GO:1903426 regulation of reactive oxygen species biosynthetic process
GO:1903428 positive regulation of reactive oxygen species biosynthetic process
GO:1903522 regulation of blood circulation
GO:1903524 positive regulation of blood circulation
GO:1903533 regulation of protein targeting
GO:1903829 positive regulation of cellular protein localization
GO:1904407 positive regulation of nitric oxide metabolic process
GO:1904589 regulation of protein import
GO:1904591 positive regulation of protein import
GO:1904951 positive regulation of establishment of protein localization
GO:1990542 mitochondrial transmembrane transport
GO:2000377 regulation of reactive oxygen species metabolic process
GO:2000379 positive regulation of reactive oxygen species metabolic process
GO:2001057 reactive nitrogen species metabolic process
Molecular Function GO:0001884 pyrimidine nucleoside binding
GO:0001948 glycoprotein binding
GO:0002134 UTP binding
GO:0002135 CTP binding
GO:0003729 mRNA binding
GO:0003823 antigen binding
GO:0004713 protein tyrosine kinase activity
GO:0005525 GTP binding
GO:0016887 ATPase activity
GO:0017098 sulfonylurea receptor binding
GO:0019001 guanyl nucleotide binding
GO:0019103 pyrimidine nucleotide binding
GO:0019902 phosphatase binding
GO:0019903 protein phosphatase binding
GO:0023023 MHC protein complex binding
GO:0023026 MHC class II protein complex binding
GO:0030235 nitric-oxide synthase regulator activity
GO:0030911 TPR domain binding
GO:0032551 pyrimidine ribonucleoside binding
GO:0032552 deoxyribonucleotide binding
GO:0032554 purine deoxyribonucleotide binding
GO:0032557 pyrimidine ribonucleotide binding
GO:0032558 adenyl deoxyribonucleotide binding
GO:0032561 guanyl ribonucleotide binding
GO:0032564 dATP binding
GO:0042826 histone deacetylase binding
GO:0044325 ion channel binding
GO:0048156 tau protein binding
GO:0051020 GTPase binding
GO:0051021 GDP-dissociation inhibitor binding
GO:0051022 Rho GDP-dissociation inhibitor binding
GO:0051082 unfolded protein binding
Cellular Component GO:0001726 ruffle
GO:0005775 vacuolar lumen
GO:0005903 brush border
GO:0005929 cilium
GO:0016323 basolateral plasma membrane
GO:0016324 apical plasma membrane
GO:0030139 endocytic vesicle
GO:0031252 cell leading edge
GO:0031253 cell projection membrane
GO:0031256 leading edge membrane
GO:0031514 motile cilium
GO:0031526 brush border membrane
GO:0031983 vesicle lumen
GO:0032587 ruffle membrane
GO:0036126 sperm flagellum
GO:0042470 melanosome
GO:0043025 neuronal cell body
GO:0043202 lysosomal lumen
GO:0043209 myelin sheath
GO:0044297 cell body
GO:0044441 ciliary part
GO:0045177 apical part of cell
GO:0048770 pigment granule
GO:0060205 cytoplasmic membrane-bounded vesicle lumen
GO:0071682 endocytic vesicle lumen
GO:0097223 sperm part
GO:0097226 sperm mitochondrial sheath
GO:0097524 sperm plasma membrane
GO:0098862 cluster of actin-based cell projections
> KEGG and Reactome Pathway
 
KEGG hsa04141 Protein processing in endoplasmic reticulum
hsa04151 PI3K-Akt signaling pathway
hsa04612 Antigen processing and presentation
hsa04621 NOD-like receptor signaling pathway
hsa04914 Progesterone-mediated oocyte maturation
hsa04915 Estrogen signaling pathway
Reactome R-HSA-8854518: AURKA Activation by TPX2
R-HSA-5620912: Anchoring of the basal body to the plasma membrane
R-HSA-3371568: Attenuation phase
R-HSA-422475: Axon guidance
R-HSA-2173782: Binding and Uptake of Ligands by Scavenger Receptors
R-HSA-1640170: Cell Cycle
R-HSA-69278: Cell Cycle, Mitotic
R-HSA-3371556: Cellular response to heat stress
R-HSA-2262752: Cellular responses to stress
R-HSA-380287: Centrosome maturation
R-HSA-5617833: Cilium Assembly
R-HSA-5637810: Constitutive Signaling by EGFRvIII
R-HSA-1236382: Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1280215: Cytokine Signaling in Immune system
R-HSA-1266738: Developmental Biology
R-HSA-1643685: Disease
R-HSA-5663202: Diseases of signal transduction
R-HSA-8863795: Downregulation of ERBB2 signaling
R-HSA-2682334: EPH-Ephrin signaling
R-HSA-3928663: EPHA-mediated growth cone collapse
R-HSA-2029480: Fcgamma receptor (FCGR) dependent phagocytosis
R-HSA-69275: G2/M Transition
R-HSA-74160: Gene Expression
R-HSA-211000: Gene Silencing by RNA
R-HSA-3371511: HSF1 activation
R-HSA-3371571: HSF1-dependent transactivation
R-HSA-168256: Immune System
R-HSA-5663205: Infectious disease
R-HSA-168254: Influenza Infection
R-HSA-168255: Influenza Life Cycle
R-HSA-168273: Influenza Viral RNA Transcription and Replication
R-HSA-168249: Innate Immune System
R-HSA-6785807: Interleukin-4 and 13 signaling
R-HSA-380259: Loss of Nlp from mitotic centrosomes
R-HSA-380284: Loss of proteins required for interphase microtubule organization from the centrosome
R-HSA-1430728: Metabolism
R-HSA-202131: Metabolism of nitric oxide
R-HSA-453274: Mitotic G2-G2/M phases
R-HSA-6798695: Neutrophil degranulation
R-HSA-1852241: Organelle biogenesis and maintenance
R-HSA-5601884: PIWI-interacting RNA (piRNA) biogenesis
R-HSA-380270: Recruitment of mitotic centrosome proteins and complexes
R-HSA-2565942: Regulation of PLK1 Activity at G2/M Transition
R-HSA-2029482: Regulation of actin dynamics for phagocytic cup formation
R-HSA-3000484: Scavenging by Class F Receptors
R-HSA-399954: Sema3A PAK dependent Axon repulsion
R-HSA-373755: Semaphorin interactions
R-HSA-162582: Signal Transduction
R-HSA-1643713: Signaling by EGFR in Cancer
R-HSA-5637812: Signaling by EGFRvIII in Cancer
R-HSA-1227986: Signaling by ERBB2
R-HSA-449147: Signaling by Interleukins
R-HSA-5637815: Signaling by Ligand-Responsive EGFR Variants in Cancer
R-HSA-194138: Signaling by VEGF
R-HSA-1474151: Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-HSA-8852276: The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-5339562: Uptake and actions of bacterial toxins
R-HSA-5336415: Uptake and function of diphtheria toxin
R-HSA-4420097: VEGFA-VEGFR2 Pathway
R-HSA-5218920: VEGFR2 mediated vascular permeability
R-HSA-5653656: Vesicle-mediated transport
R-HSA-203615: eNOS activation
R-HSA-203765: eNOS activation and regulation
R-HSA-192905: vRNP Assembly
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Literatures that report relations between HSP90AA1 and anti-tumor immunity. The specific mechanism were also collected if the literature reports that a gene specifically promotes or inhibits the infiltration or function of T/NK cells.
> Text Mining
 
  Literatures describing the relation between HSP90AA1 and anti-tumor immunity in human cancer.
PMID Cancer type Relation to immunity Evidence sentences
19690146Renal Cell CarcinomaInhibit immunity (T cell function)In the current study, we show that treatment of EphA2(+) tumor cells with the irreversible heat shock protein 90 inhibitor, 17-dimethylaminoethylamino-17-demethoxygeldanamycin (17-DMAG), similarly enhances their recognition by EphA2-specific CD8(+) T-cell lines and clones in vitro via a mechanism that is dependent on proteasome and transporter-associated protein function as well as the retrotranslocation of EphA2 into the tumor cytoplasm.
19671844Hodgkin LymphomaInhibit immunityHeat shock protein 90 inhibitor BIIB021 (CNF2024) depletes NF-kappaB and sensitizes Hodgkin's lymphoma cells for natural killer cell-mediated cytotoxicity.
22396543Hepatocellular CarcinomaPromote immunity (NK cell function)ELISA results showed that the production of HSP60, HSP70, and HSP90 was up-regulated in both cell lines in a stress-specific manner. Acting as a decoy, the HSP-bearing exosomes efficiently stimulated NK cell cytotoxicity and granzyme B production, up-regulated the expression of inhibitory receptor CD94, and down-regulated the expression of activating receptors CD69, NKG2D, and NKp44.
17363539Malignant MelanomaInhibit immunitymAb 4C5 inhibits B16 F10 cell invasion by binding to surface HSP90 because it is not internalized. mAb 4C5 significantly inhibits melanoma metastasis in C57BL/6 mice inoculated with B16 F10 cells.
29478948MelanomaInhibit immunity (T cell function)Targeting HSP70/90 in melanoma cells resulted in reduced induction of immune suppressive cells on a phenotypic and functional basis, for which a more potent effect was observed when HSP90 was inhibited under hypoxic conditions.
28878208MelanomaInhibit immunityHSP90 inhibition enhances cancer immunotherapy by upregulating interferon response genes. We show that inhibition of HSP90 with ganetespib enhances T-cell-mediated killing of patient-derived human melanoma cells by their autologous T cells in vitro and potentiates responses to anti-CTLA4 and anti-PD1 therapy in vivo. Mechanistic studies reveal that HSP90 inhibition results in upregulation of interferon response genes, which are essential for the enhanced killing of ganetespib treated melanoma cells by T cells.
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content High-throughput screening data (e.g. CRISPR-Cas9, shRNA and RNAi) for T cell-mediated killing. Genetic screen techniques can identify mechanisms of tumor cell resistance (e.g., PTPN2) and sensitivity (e.g., APLNR) to killing by cytotoxic T cells, the central effectors of anti-tumor immunity. After comprehensively searching, eight groups of screening data sets were collected in the current database. In this tab, users can check whether their selected genes cause resistance or increase sensitivity to T cell-mediated killing in various data sets.
> High-throughput Screening
  Statistical results of HSP90AA1 in screening data sets for detecting immune reponses.
PMID Screening System Cancer Type Cell Line Data Set Statistical Results Relation to immunity
29301958CRISPR-Cas9 melanomaB16F10Pmel-1 T cell NA/NSNA/NS
29301958CRISPR-Cas9 melanomaB16F10OT-1 T cell NA/NSNA/NS
28783722CRISPR-Cas9 melanomaMel6242CT-CRISPR NA/NSNA/NS
28723893CRISPR-Cas9 melanomaB16GVAX+Anti-PD1 NA/NSNA/NS
28723893CRISPR-Cas9 melanomaB16GVAX NA/NSNA/NS
25691366RNAiBreast cancerMCF7Luc-CTL assay NA/NSNA/NS
24476824shRNAmelanomaB16Primary screen NA/NSNA/NS
24476824shRNAmelanomaB16Secondary screen NA/NSNA/NS
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Transcriptomic and genomic profiling of pre-treated tumor biopsies from responders and non-responders to immunotherapy. These data were used to identify signatures and mechanisms of response to checkpoint blockade (e.g., anti-PDL1 and anti-PD1). One example is that mutations in the gene PBRM1 benefit clinical survival of patients with clear cell renal cell carcinoma. After comprehensively searching, we collected 5 and 6 of transcriptomic and genomic data sets, respectively. In this tab, users can check whether their selected genes have significant difference of expression or mutation between responders and non-responders in various data sets.
> Expression difference between responders and non-responders
> Mutation difference between responders and non-responders
> Expression difference between responders and non-responders
 
Points in the above scatter plot represent the expression difference of HSP90AA1 in various data sets.
No PMID Cancer type Group Drug # Res # NRes Log2 (Fold Change) P value Anno
126997480MelanomaallAnti-PD-1 (pembrolizumab and nivolumab)14120.3620.203
226997480MelanomaMAPKiAnti-PD-1 (pembrolizumab and nivolumab)651.0790.783
326997480Melanomanon-MAPKiAnti-PD-1 (pembrolizumab and nivolumab)87-0.1670.955
428552987Urothelial cancerallAnti-PD-L1 (atezolizumab) 9160.5020.231
528552987Urothelial cancersmokingAnti-PD-L1 (atezolizumab) 590.5790.837
628552987Urothelial cancernon-smokingAnti-PD-L1 (atezolizumab) 470.4110.913
729033130MelanomaallAnti-PD-1 (nivolumab) 2623-0.2110.74
829033130MelanomaNIV3-PROGAnti-PD-1 (nivolumab) 1511-0.3460.908
929033130MelanomaNIV3-NAIVEAnti-PD-1 (nivolumab) 1112-0.0710.983
1029301960Clear cell renal cell carcinoma (ccRCC)allAnti-PD-1 (nivolumab) 480.1070.966
1129301960Clear cell renal cell carcinoma (ccRCC)VEGFRiAnti-PD-1 (nivolumab) 2001
1229301960Clear cell renal cell carcinoma (ccRCC)non-VEGFRiAnti-PD-1 (nivolumab) 280.7060.853
1329443960Urothelial cancerallAnti-PD-L1 (atezolizumab) 682300.1940.0346
> Mutation difference between responders and non-responders
 
Points in the above scatter plot represent the mutation difference of HSP90AA1 in various data sets.
No PMID Cancer type Group Drug # Res # NRes % Mut/Res % Mut/NRes % Diff (R vs NR) Pval Anno
125765070Non-small cell lung cancer (NSCLC)allAnti-PD-1 (pembrolizumab) 14170001
225765070Non-small cell lung cancer (NSCLC)smokingAnti-PD-1 (pembrolizumab) 1030001
325765070Non-small cell lung cancer (NSCLC)non-smokingAnti-PD-1 (pembrolizumab) 4140001
426359337MelanomaallAnti-CTLA-4 (ipilimumab) 277301.4-1.41
526359337MelanomaBRAFiAnti-CTLA-4 (ipilimumab) 0140001
626359337Melanomanon-BRAFiAnti-CTLA-4 (ipilimumab) 275901.7-1.71
726997480MelanomaallAnti-PD-1 (pembrolizumab and nivolumab)21170001
826997480MelanomaMAPKiAnti-PD-1 (pembrolizumab and nivolumab)860001
926997480Melanomanon-MAPKiAnti-PD-1 (pembrolizumab and nivolumab)13110001
1028552987Urothelial cancerallAnti-PD-L1 (atezolizumab) 9160001
1128552987Urothelial cancersmokingAnti-PD-L1 (atezolizumab) 590001
1228552987Urothelial cancernon-smokingAnti-PD-L1 (atezolizumab) 470001
1329033130MelanomaallAnti-PD-1 (nivolumab) 38277.907.90.26
1429033130MelanomaNIV3-PROGAnti-PD-1 (nivolumab) 22139.109.10.519
1529033130MelanomaNIV3-NAIVEAnti-PD-1 (nivolumab) 16146.206.21
1629301960Clear cell renal cell carcinoma (ccRCC)allAnti-PD-1 (nivolumab) 11130001
1729301960Clear cell renal cell carcinoma (ccRCC)VEGFRiAnti-PD-1 (nivolumab) 610001
1829301960Clear cell renal cell carcinoma (ccRCC)non-VEGFRiAnti-PD-1 (nivolumab) 5120001
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Relations between abundance of tumor-infiltrating lymphocytes (TILs) and expression, copy number, methylation, or mutation of HSP90AA1. The immune-related signatures of 28 TIL types from Charoentong's study, which can be viewed in the download page. For each cancer type, the relative abundance of TILs were inferred by using gene set variation analysis (GSVA) based on gene expression profile. In this tab, users can examine which kinds of TILs might be regulated by the current gene.
> Lymphocyte
 
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Relations between three kinds of immunomodulators and expression, copy number, methylation, or mutation of HSP90AA1. These immunomo-dulators were collected from Charoentong's study. In this tab, users can examine which immunomodulators might be regulated by HSP90AA1.
> Immunoinhibitor
> Immunostimulator
> MHC molecule
> Immunoinhibitor
 
> Immunostimulator
 
> MHC molecule
 
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Relations between chemokines (or receptors) and expression, copy number, methylation, or mutation of HSP90AA1. In this tab, users can examine which chemokines (or receptors) might be regulated by the current gene.
> Chemokine
> Receptor
> Chemokine
 
> Receptor
 
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Distribution of HSP90AA1 expression across immune and molecular subtypes.
> Immune subtype
> Molecular subtype
> Immune subtype
 
> Molecular subtype
 
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Associations between HSP90AA1 and clinical features.
> Overall survival analysis
> Cancer stage
> Tumor grade
> Overall survival
 
> Stage
 
> Grade
 
Summary
SymbolHSP90AA1
Nameheat shock protein 90kDa alpha (cytosolic), class A member 1
Aliases Hsp89; Hsp90; FLJ31884; HSP90N; HSPC1; heat shock 90kD protein 1, alpha; heat shock 90kDa protein 1, alpha; ......
Chromosomal Location14q32.33
External Links HGNC, NCBI, Ensembl, Uniprot, GeneCards
Content Drugs targeting HSP90AA1 collected from DrugBank database.
> Drugs from DrugBank database
 

  Details on drugs targeting HSP90AA1.
ID Name Drug Type Targets #Targets
DB00615RifabutinSmall MoleculeHSP90AA1, HSP90B12
DB00716NedocromilSmall MoleculeCYSLTR1, CYSLTR2, FPR1, HSP90AA1, PTGDR5
DB023599-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB02424GeldanamycinSmall MoleculeHSP90AA1, HSP90AB1, HSP90B13
DB025508-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB027549-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-AmineSmall MoleculeHSP90AA1, HSP90AB12
DB028404-(1,3-Benzodioxol-5-Yl)-5-(5-Ethyl-2,4-Dihydroxyphenyl)-2h-Pyrazole-3-Carboxylic AcidSmall MoleculeHSP90AA11
DB030938-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB031378-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9-Pent-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB035049-Butyl-8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB037494-(1h-Imidazol-4-Yl)-3-(5-Ethyl-2,4-Dihydroxy-Phenyl)-1h-PyrazoleSmall MoleculeHSP90AA11
DB038099-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-AmineSmall MoleculeHSP90AA11
DB038999-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-AmineSmall MoleculeHSP90AA11
DB040549-Butyl-8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB04216QuercetinSmall MoleculeACTB, AHR, ATP5A1, ATP5B, ATP5C1, CBR1, CEBPB, CSNK2A1, CSNK2B, CY ......27
DB042548-Benzo[1,3]Dioxol-,5-Ylmethyl-9-Butyl-2-Fluoro-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB045058-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9-Pent-4-Ylnyl-9h-Purin-6-YlamineSmall MoleculeHSP90AA11
DB04588N-[4-(AMINOSULFONYL)BENZYL]-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDESmall MoleculeHSP90AA11
DB05134TanespimycinSmall MoleculeHSP90AA1, HSP90AB12
DB06070SNX-5422Small MoleculeHSP90AA1, HSP90AB12
DB06956N-(4-ACETYLPHENYL)-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDESmall MoleculeHSP90AA11
DB069574-CHLORO-6-(4-{4-[4-(METHYLSULFONYL)BENZYL]PIPERAZIN-1-YL}-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOLSmall MoleculeHSP90AA11
DB069585-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-PIPERAZIN-1-YL-1H-PYRAZOLE-3-CARBOXAMIDESmall MoleculeHSP90AA11
DB069615-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-[4-(morpholin-4-ylmethyl)phenyl]isoxazole-3-carboxamideSmall MoleculeHSP90AA11
DB069645-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)ISOXAZOLE-3-CARBOXAMIDESmall MoleculeHSP90AA11
DB069692-amino-4-[2,4-dichloro-5-(2-pyrrolidin-1-ylethoxy)phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamideSmall MoleculeHSP90AA11
DB071004-CHLORO-6-(4-PIPERAZIN-1-YL-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOLSmall MoleculeHSP90AA11
DB07317(3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-oneSmall MoleculeHSP90AA11
DB073196-(3-BROMO-2-NAPHTHYL)-1,3,5-TRIAZINE-2,4-DIAMINESmall MoleculeHSP90AA11
DB073243-({2-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)ETHYNYL]BENZYL}AMINO)-1,3-OXAZOL-2(3H)-ONESmall MoleculeHSP90AA11
DB07325N-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)METHYL]-3-{[(E)-(2-OXODIHYDROFURAN-3(2H)-YLIDENE)METHYL]AMINO}BENZENESULFONAMIDESmall MoleculeHSP90AA11
DB074955-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-(4-METHOXYPHENYL)-1H-PYRAZOLE-3-CARBOXAMIDESmall MoleculeHSP90AA11
DB075024-bromo-6-(6-hydroxy-1,2-benzisoxazol-3-yl)benzene-1,3-diolSmall MoleculeHSP90AA11
DB075944-[4-(2,3-DIHYDRO-1,4-BENZODIOXIN-6-YL)-3-METHYL-1H-PYRAZOL-5-YL]-6-ETHYLBENZENE-1,3-DIOLSmall MoleculeHSP90AA1, HSP90AB12
DB076014-chloro-6-{5-[(2-morpholin-4-ylethyl)amino]-1,2-benzisoxazol-3-yl}benzene-1,3-diolSmall MoleculeHSP90AA11
DB078778-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINESmall MoleculeHSP90AA1, HSP90AB12
DB081944-methyl-7,8-dihydro-5H-thiopyrano[4,3-d]pyrimidin-2-amineSmall MoleculeHSP90AA11
DB08197(5E,7S)-2-amino-7-(4-fluoro-2-pyridin-3-ylphenyl)-4-methyl-7,8-dihydroquinazolin-5(6H)-one oximeSmall MoleculeHSP90AA11
DB084368-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL-9H-Small MoleculeHSP90AA11
DB084424-{[(2R)-2-(2-methylphenyl)pyrrolidin-1-yl]carbonyl}benzene-1,3-diolSmall MoleculeHSP90AA11
DB084432-(1H-pyrrol-1-ylcarbonyl)benzene-1,3,5-triolSmall MoleculeHSP90AA11
DB085572-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamideSmall MoleculeHSP90AA11
DB087864-(2-methoxyethoxy)-6-methylpyrimidin-2-amineSmall MoleculeHSP90AA11
DB087874-(2,4-dichlorophenyl)-5-phenyldiazenyl-pyrimidin-2-amineSmall MoleculeHSP90AA11
DB087883,6-DIAMINO-5-CYANO-4-(4-ETHOXYPHENYL)THIENO[2,3-B]PYRIDINE-2-CARBOXAMIDESmall MoleculeHSP90AA11
DB087892-AMINO-4-(2,4-DICHLOROPHENYL)-N-ETHYLTHIENO[2,3-D]PYRIMIDINE-6-CARBOXAMIDESmall MoleculeHSP90AA11
DB09130CopperSmall MoleculeA1BG, ACTG1, ACTN1, ACY1, AFM, AGT, AHCY, AHSG, AKR1A1, ANXA4, ANX ......141
DB09221PolaprezincSmall MoleculeFLT1, HSP90AA1, HSP90AB1, IL3, IL6, NGF, PDGFRB, TNF8
DB12442AlvespimycinSmall MoleculeHSP90AA11