Details of Drug Off-Target (DOT)

General Information of Drug Off-Target (DOT) (ID: OTLG1WPK)

DOT Name Heat shock protein HSP 90-alpha (HSP90AA1)
Synonyms 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
Gene Name HSP90AA1
UniProt ID
HS90A_HUMAN
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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PDB ID
1BYQ ; 1OSF ; 1UY6 ; 1UY7 ; 1UY8 ; 1UY9 ; 1UYC ; 1UYD ; 1UYE ; 1UYF ; 1UYG ; 1UYH ; 1UYI ; 1UYK ; 1UYL ; 1YC1 ; 1YC3 ; 1YC4 ; 1YER ; 1YES ; 1YET ; 2BSM ; 2BT0 ; 2BUG ; 2BYH ; 2BYI ; 2BZ5 ; 2C2L ; 2CCS ; 2CCT ; 2CCU ; 2FWY ; 2FWZ ; 2H55 ; 2JJC ; 2K5B ; 2QF6 ; 2QFO ; 2QG0 ; 2QG2 ; 2UWD ; 2VCI ; 2VCJ ; 2WI1 ; 2WI2 ; 2WI3 ; 2WI4 ; 2WI5 ; 2WI6 ; 2WI7 ; 2XAB ; 2XDK ; 2XDL ; 2XDS ; 2XDU ; 2XDX ; 2XHR ; 2XHT ; 2XHX ; 2XJG ; 2XJJ ; 2XJX ; 2XK2 ; 2YE2 ; 2YE3 ; 2YE4 ; 2YE5 ; 2YE6 ; 2YE7 ; 2YE8 ; 2YE9 ; 2YEA ; 2YEB ; 2YEC ; 2YED ; 2YEE ; 2YEF ; 2YEG ; 2YEH ; 2YEI ; 2YEJ ; 2YI0 ; 2YI5 ; 2YI6 ; 2YI7 ; 2YJW ; 2YJX ; 2YK2 ; 2YK9 ; 2YKB ; 2YKC ; 2YKE ; 2YKI ; 2YKJ ; 3B24 ; 3B25 ; 3B26 ; 3B27 ; 3B28 ; 3BM9 ; 3BMY ; 3D0B ; 3EKO ; 3EKR ; 3FT5 ; 3FT8 ; 3HEK ; 3HHU ; 3HYY ; 3HYZ ; 3HZ1 ; 3HZ5 ; 3INW ; 3INX ; 3K97 ; 3K98 ; 3K99 ; 3MNR ; 3O0I ; 3OW6 ; 3OWB ; 3OWD ; 3Q6M ; 3Q6N ; 3QDD ; 3QTF ; 3R4M ; 3R4N ; 3R4O ; 3R4P ; 3R91 ; 3R92 ; 3RKZ ; 3RLP ; 3RLQ ; 3RLR ; 3T0H ; 3T0Z ; 3T10 ; 3T1K ; 3T2S ; 3TUH ; 3VHA ; 3VHC ; 3VHD ; 3WHA ; 3WQ9 ; 4AIF ; 4AWO ; 4AWP ; 4AWQ ; 4B7P ; 4BQG ; 4BQJ ; 4CGQ ; 4CGU ; 4CGV ; 4CGW ; 4CWF ; 4CWN ; 4CWO ; 4CWP ; 4CWQ ; 4CWR ; 4CWS ; 4CWT ; 4EEH ; 4EFT ; 4EFU ; 4EGH ; 4EGI ; 4EGK ; 4FCP ; 4FCQ ; 4FCR ; 4HY6 ; 4JQL ; 4L8Z ; 4L90 ; 4L91 ; 4L93 ; 4L94 ; 4LWE ; 4LWF ; 4LWG ; 4LWH ; 4LWI ; 4NH7 ; 4NH8 ; 4O04 ; 4O05 ; 4O07 ; 4O09 ; 4O0B ; 4R3M ; 4U93 ; 4W7T ; 4XIP ; 4XIQ ; 4XIR ; 4XIT ; 4YKQ ; 4YKR ; 4YKT ; 4YKU ; 4YKW ; 4YKX ; 4YKY ; 4YKZ ; 5CF0 ; 5FNC ; 5FND ; 5FNF ; 5GGZ ; 5J20 ; 5J27 ; 5J2V ; 5J2X ; 5J64 ; 5J6L ; 5J6M ; 5J6N ; 5J80 ; 5J82 ; 5J86 ; 5J8M ; 5J8U ; 5J9X ; 5LNY ; 5LNZ ; 5LO0 ; 5LO1 ; 5LO5 ; 5LO6 ; 5LQ9 ; 5LR1 ; 5LR7 ; 5LRL ; 5LRZ ; 5LS1 ; 5M4E ; 5M4H ; 5NYH ; 5NYI ; 5OCI ; 5OD7 ; 5ODX ; 5T21 ; 5VYY ; 5XQD ; 5XQE ; 5XR5 ; 5XR9 ; 5XRB ; 5XRD ; 5XRE ; 5ZR3 ; 6B99 ; 6B9A ; 6CEO ; 6CYG ; 6CYH ; 6EI5 ; 6EL5 ; 6ELN ; 6ELO ; 6ELP ; 6EY8 ; 6EY9 ; 6EYA ; 6EYB ; 6F1N ; 6FCJ ; 6FDP ; 6GP4 ; 6GP8 ; 6GPF ; 6GPH ; 6GPO ; 6GPP ; 6GPR ; 6GPT ; 6GPW ; 6GPY ; 6GQ6 ; 6GQR ; 6GQS ; 6GQU ; 6GR1 ; 6GR3 ; 6GR4 ; 6GR5 ; 6HHR ; 6KSQ ; 6LR9 ; 6LSZ ; 6LT8 ; 6LTI ; 6LTK ; 6N8X ; 6OLX ; 6TN4 ; 6TN5 ; 6U98 ; 6U99 ; 6U9A ; 6U9B ; 7DMC ; 7KRJ ; 7KW7 ; 7L7I ; 7L7J ; 7LSZ ; 7LT0 ; 7RXZ ; 7RY0 ; 7RY1 ; 7S8Y ; 7S8Z ; 7S90 ; 7S95 ; 7S98 ; 7S99 ; 7S9F ; 7S9G ; 7S9H ; 7S9I ; 7UR3 ; 8AGI ; 8AGJ ; 8AGL ; 8B7I ; 8B7J ; 8FFV ; 8FFW ; 8X2R
EC Number
3.6.4.10
Pfam ID
PF13589 ; PF00183
Sequence
MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR
YESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFME
ALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPM
GRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKED
KEEEKEKEEKESEDKPEIEDVGSDEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRN
PDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNN
IKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKC
LELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDY
CTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKT
LVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIV
TSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVK
DLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLE
GDDDTSRMEEVD
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 mitochondrial outer membrane which promotes host antiviral response ; (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.
KEGG Pathway
Protein processing in endoplasmic reticulum (hsa04141 )
PI3K-Akt sig.ling pathway (hsa04151 )
Necroptosis (hsa04217 )
Antigen processing and presentation (hsa04612 )
NOD-like receptor sig.ling pathway (hsa04621 )
IL-17 sig.ling pathway (hsa04657 )
Th17 cell differentiation (hsa04659 )
Progesterone-mediated oocyte maturation (hsa04914 )
Estrogen sig.ling pathway (hsa04915 )
Salmonella infection (hsa05132 )
Pathways in cancer (hsa05200 )
Chemical carcinogenesis - receptor activation (hsa05207 )
Prostate cancer (hsa05215 )
Lipid and atherosclerosis (hsa05417 )
Fluid shear stress and atherosclerosis (hsa05418 )
Reactome Pathway
Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants (R-HSA-1236382 )
Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation (R-HSA-1474151 )
DDX58/IFIH1-mediated induction of interferon-alpha/beta (R-HSA-168928 )
vRNP Assembly (R-HSA-192905 )
Regulation of actin dynamics for phagocytic cup formation (R-HSA-2029482 )
eNOS activation (R-HSA-203615 )
Regulation of PLK1 Activity at G2/M Transition (R-HSA-2565942 )
Scavenging by Class F Receptors (R-HSA-3000484 )
HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand (R-HSA-3371497 )
HSF1 activation (R-HSA-3371511 )
Attenuation phase (R-HSA-3371568 )
HSF1-dependent transactivation (R-HSA-3371571 )
Loss of Nlp from mitotic centrosomes (R-HSA-380259 )
Recruitment of mitotic centrosome proteins and complexes (R-HSA-380270 )
Loss of proteins required for interphase microtubule organization from the centrosome (R-HSA-380284 )
Recruitment of NuMA to mitotic centrosomes (R-HSA-380320 )
Sema3A PAK dependent Axon repulsion (R-HSA-399954 )
VEGFA-VEGFR2 Pathway (R-HSA-4420097 )
VEGFR2 mediated vascular permeability (R-HSA-5218920 )
Uptake and function of diphtheria toxin (R-HSA-5336415 )
PIWI-interacting RNA (piRNA) biogenesis (R-HSA-5601884 )
Anchoring of the basal body to the plasma membrane (R-HSA-5620912 )
Constitutive Signaling by EGFRvIII (R-HSA-5637810 )
Regulation of necroptotic cell death (R-HSA-5675482 )
Interleukin-4 and Interleukin-13 signaling (R-HSA-6785807 )
Neutrophil degranulation (R-HSA-6798695 )
The role of GTSE1 in G2/M progression after G2 checkpoint (R-HSA-8852276 )
AURKA Activation by TPX2 (R-HSA-8854518 )
Downregulation of ERBB2 signaling (R-HSA-8863795 )
ESR-mediated signaling (R-HSA-8939211 )
Extra-nuclear estrogen signaling (R-HSA-9009391 )
RHOBTB2 GTPase cycle (R-HSA-9013418 )
Estrogen-dependent gene expression (R-HSA-9018519 )
Chaperone Mediated Autophagy (R-HSA-9613829 )
Constitutive Signaling by Overexpressed ERBB2 (R-HSA-9634285 )
Aggrephagy (R-HSA-9646399 )
Drug-mediated inhibition of ERBB2 signaling (R-HSA-9652282 )
Signaling by ERBB2 KD Mutants (R-HSA-9664565 )
Resistance of ERBB2 KD mutants to trastuzumab (R-HSA-9665233 )
Resistance of ERBB2 KD mutants to sapitinib (R-HSA-9665244 )
Resistance of ERBB2 KD mutants to tesevatinib (R-HSA-9665245 )
Resistance of ERBB2 KD mutants to neratinib (R-HSA-9665246 )
Resistance of ERBB2 KD mutants to osimertinib (R-HSA-9665247 )
Resistance of ERBB2 KD mutants to afatinib (R-HSA-9665249 )
Resistance of ERBB2 KD mutants to AEE788 (R-HSA-9665250 )
Resistance of ERBB2 KD mutants to lapatinib (R-HSA-9665251 )
Signaling by ERBB2 ECD mutants (R-HSA-9665348 )
Signaling by ERBB2 TMD/JMD mutants (R-HSA-9665686 )
Drug resistance in ERBB2 TMD/JMD mutants (R-HSA-9665737 )
Potential therapeutics for SARS (R-HSA-9679191 )
SARS-CoV-2 activates/modulates innate and adaptive immune responses (R-HSA-9705671 )
Signaling by ERBB2 (R-HSA-1227986 )

Molecular Interaction Atlas (MIA) of This DOT

Molecular Interaction Atlas (MIA) Jump to Detail Molecular Interaction Atlas of This DOT
This DOT Affected the Drug Response of 2 Drug(s)
Drug Name Drug ID Highest Status Interaction REF
NVP-LAQ824 DM8JWNA Phase 3 Heat shock protein HSP 90-alpha (HSP90AA1) increases the Apoptosis ADR of NVP-LAQ824. [46]
Protoporphyrin IX DMWYE7A Investigative Heat shock protein HSP 90-alpha (HSP90AA1) decreases the response to substance of Protoporphyrin IX. [47]
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5 Drug(s) Affected the Post-Translational Modifications of This DOT
Drug Name Drug ID Highest Status Interaction REF
Valproate DMCFE9I Approved Valproate increases the methylation of Heat shock protein HSP 90-alpha (HSP90AA1). [1]
Arsenic DMTL2Y1 Approved Arsenic affects the methylation of Heat shock protein HSP 90-alpha (HSP90AA1). [9]
TAK-243 DM4GKV2 Phase 1 TAK-243 decreases the sumoylation of Heat shock protein HSP 90-alpha (HSP90AA1). [27]
PMID28870136-Compound-52 DMFDERP Patented PMID28870136-Compound-52 decreases the phosphorylation of Heat shock protein HSP 90-alpha (HSP90AA1). [28]
Coumarin DM0N8ZM Investigative Coumarin increases the phosphorylation of Heat shock protein HSP 90-alpha (HSP90AA1). [28]
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41 Drug(s) Affected the Gene/Protein Processing of This DOT
Drug Name Drug ID Highest Status Interaction REF
Ciclosporin DMAZJFX Approved Ciclosporin increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [2]
Acetaminophen DMUIE76 Approved Acetaminophen increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [3]
Doxorubicin DMVP5YE Approved Doxorubicin increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [4]
Cupric Sulfate DMP0NFQ Approved Cupric Sulfate decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [5]
Cisplatin DMRHGI9 Approved Cisplatin decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [6]
Estradiol DMUNTE3 Approved Estradiol decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [7]
Ivermectin DMDBX5F Approved Ivermectin decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [8]
Quercetin DM3NC4M Approved Quercetin decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [10]
Arsenic trioxide DM61TA4 Approved Arsenic trioxide increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [11]
Vorinostat DMWMPD4 Approved Vorinostat decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [12]
Decitabine DMQL8XJ Approved Decitabine decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [13]
Marinol DM70IK5 Approved Marinol decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [14]
Selenium DM25CGV Approved Selenium decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [15]
Phenobarbital DMXZOCG Approved Phenobarbital decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [16]
Fulvestrant DM0YZC6 Approved Fulvestrant increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [7]
Dexamethasone DMMWZET Approved Dexamethasone increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [17]
Cannabidiol DM0659E Approved Cannabidiol increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [18]
Bortezomib DMNO38U Approved Bortezomib decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [19]
Nicotine DMWX5CO Approved Nicotine increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [20]
Simvastatin DM30SGU Approved Simvastatin increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [21]
Thiopental DMGP8AX Approved Thiopental increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [23]
Curcumin DMQPH29 Phase 3 Curcumin decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [24]
Tocopherol DMBIJZ6 Phase 2 Tocopherol decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [15]
ACYLINE DM9GRTK Phase 2 ACYLINE increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [25]
Benzo(a)pyrene DMN7J43 Phase 1 Benzo(a)pyrene increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [26]
THAPSIGARGIN DMDMQIE Preclinical THAPSIGARGIN decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [29]
Celastrol DMWQIJX Preclinical Celastrol decreases the activity of Heat shock protein HSP 90-alpha (HSP90AA1). [30]
Bisphenol A DM2ZLD7 Investigative Bisphenol A increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [31]
Trichostatin A DM9C8NX Investigative Trichostatin A affects the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [13]
Sulforaphane DMQY3L0 Investigative Sulforaphane increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [32]
chloropicrin DMSGBQA Investigative chloropicrin increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [33]
Deguelin DMXT7WG Investigative Deguelin increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [34]
3R14S-OCHRATOXIN A DM2KEW6 Investigative 3R14S-OCHRATOXIN A increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [35]
methyl p-hydroxybenzoate DMO58UW Investigative methyl p-hydroxybenzoate increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [36]
Glyphosate DM0AFY7 Investigative Glyphosate decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [37]
GALLICACID DM6Y3A0 Investigative GALLICACID decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [38]
QUERCITRIN DM1DH96 Investigative QUERCITRIN affects the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [40]
AHPN DM8G6O4 Investigative AHPN decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [41]
OXYBENZONE DMMZYX6 Investigative OXYBENZONE increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [43]
Linalool DMGZQ5P Investigative Linalool increases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [44]
Paraoxon DMN4ZKC Investigative Paraoxon decreases the expression of Heat shock protein HSP 90-alpha (HSP90AA1). [45]
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⏷ Show the Full List of 41 Drug(s)
2 Drug(s) Affected the Protein Interaction/Cellular Processes of This DOT
Drug Name Drug ID Highest Status Interaction REF
Gefitinib DM15F0X Approved Gefitinib increases the secretion of Heat shock protein HSP 90-alpha (HSP90AA1). [22]
4-hydroxy-2-nonenal DM2LJFZ Investigative 4-hydroxy-2-nonenal affects the binding of Heat shock protein HSP 90-alpha (HSP90AA1). [39]
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1 Drug(s) Affected the Biochemical Pathways of This DOT
Drug Name Drug ID Highest Status Interaction REF
cinnamaldehyde DMZDUXG Investigative cinnamaldehyde increases the metabolism of Heat shock protein HSP 90-alpha (HSP90AA1). [42]
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