AHSA1

gene
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Also known as p38Aha1hAha1

Summary

AHSA1 (activator of HSP90 ATPase activity 1, HGNC:1189) is a protein-coding gene on chromosome 14q24.3, encoding Activator of 90 kDa heat shock protein ATPase homolog 1 (O95433). Acts as a co-chaperone of HSP90AA1.

Enables several functions, including ATPase activator activity; Hsp90 protein binding activity; and unfolded protein binding activity. Involved in maintenance of unfolded protein and positive regulation of ATP-dependent activity. Located in cytosol.

Source: NCBI Gene 10598 — RefSeq curated summary.

At a glance

  • Clinical variants (ClinVar): 55 total — 1 pathogenic
  • Druggable target: yes
  • MANE Select transcript: NM_012111

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:1189
Approved symbolAHSA1
Nameactivator of HSP90 ATPase activity 1
Location14q24.3
Locus typegene with protein product
StatusApproved
Aliasesp38, Aha1, hAha1
Ensembl geneENSG00000100591
Ensembl biotypeprotein_coding
OMIM608466
Entrez10598

Gene structure

Transcript identifiers

Ensembl transcripts: 21 — 14 protein_coding, 4 retained_intron, 2 protein_coding_CDS_not_defined, 1 nonsense_mediated_decay

ENST00000216479, ENST00000535854, ENST00000553374, ENST00000554156, ENST00000555133, ENST00000555457, ENST00000555473, ENST00000555517, ENST00000555729, ENST00000556369, ENST00000556866, ENST00000556963, ENST00000557476, ENST00000855620, ENST00000855621, ENST00000855622, ENST00000855623, ENST00000855624, ENST00000855625, ENST00000920448, ENST00000962103

RefSeq mRNA: 2 — MANE Select: NM_012111 NM_001321441, NM_012111

CCDS: CCDS9863

Canonical transcript exons

ENST00000216479 — 9 exons

ExonStartEnd
ENSE000006593327746459877464686
ENSE000022315157745809377458269
ENSE000025182657746907777469472
ENSE000034591657746216077462242
ENSE000034946997746553977465667
ENSE000035021477746845777468508
ENSE000035579597746808377468184
ENSE000036036427746264277462759
ENSE000036063797745961677459806

Expression profiles

Bgee: expression breadth ubiquitous, 302 present calls, max score 99.12.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 107.8111 / max 1359.0198, expressed in 1827 samples.

FANTOM5 promoters (3 alternative TSS)

Promoter IDTPM avgSamples expressed
14078198.90671827
1407827.90851595
1407800.9959603

Top tissues by expression

303 total, by Bgee expression score (0-100, higher = more expressed):

TissueAnatomy IDExpression scoreQuality
oocyteCL:000002399.12gold quality
right testisUBERON:000453498.98gold quality
secondary oocyteCL:000065598.97gold quality
left testisUBERON:000453398.94gold quality
right uterine tubeUBERON:000130298.92gold quality
cortical plateUBERON:000534398.73gold quality
ventricular zoneUBERON:000305398.63gold quality
ganglionic eminenceUBERON:000402398.62gold quality
hindlimb stylopod muscleUBERON:000425298.39gold quality
C1 segment of cervical spinal cordUBERON:000646998.37gold quality
Brodmann (1909) area 9UBERON:001354098.33gold quality
adrenal tissueUBERON:001830398.32gold quality
prefrontal cortexUBERON:000045198.31gold quality
right frontal lobeUBERON:000281098.30gold quality
body of uterusUBERON:000985398.26gold quality
lower esophagus muscularis layerUBERON:003583398.25gold quality
lower esophagusUBERON:001347398.24gold quality
mucosa of transverse colonUBERON:000499198.23gold quality
esophagogastric junction muscularis propriaUBERON:003584198.17gold quality
right adrenal glandUBERON:000123398.15gold quality
left adrenal glandUBERON:000123498.15gold quality
rectumUBERON:000105298.13gold quality
olfactory segment of nasal mucosaUBERON:000538698.12gold quality
left adrenal gland cortexUBERON:003582598.11gold quality
muscle layer of sigmoid colonUBERON:003580598.06gold quality
cerebellar hemisphereUBERON:000224598.01gold quality
adenohypophysisUBERON:000219697.99gold quality
cerebellar cortexUBERON:000212997.98gold quality
islet of LangerhansUBERON:000000697.96gold quality
testisUBERON:000047397.96gold quality

Single-cell (SCXA)

Detected in 1 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-ANND-3no0.00

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

18 targeting AHSA1, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNAMax scoreAvg scoremiRNA target_count
HSA-MIR-4789-3P99.9970.752484
HSA-MIR-448799.9664.581252
HSA-MIR-1212999.7267.451311
HSA-MIR-453099.6966.471509
HSA-MIR-46699.6770.852863
HSA-MIR-4524A-5P99.5771.731193
HSA-MIR-4524B-5P99.5771.681195
HSA-MIR-431199.3170.473041
HSA-MIR-6814-5P99.0366.681273
HSA-MIR-92299.0267.231838
HSA-MIR-374B-3P98.6368.241360
HSA-MIR-378H98.4366.16545
HSA-MIR-3190-3P97.6166.951406
HSA-MIR-874-5P96.9363.921014
HSA-MIR-449196.5366.20935
HSA-MIR-465796.5366.57895
HSA-MIR-4740-5P96.2567.96726
HSA-MIR-432393.9363.89656

Literature-anchored findings (GeneRIF, showing 17)

  • stimulates the inherent ATPase activity of Hsp90 (PMID:12504007)
  • Hsp90 cochaperones modulate Hsp90-dependent stability of CFTR protein folding in the endoplasmic reticulum (PMID:17110338)
  • Data propose a model for Aha1 in the Hsp90 ATPase cycle where Aha1 regulates dwell time of Hsp90, and suggest Aha1 activity integrates chaperone function with client folding energetics by modulating ATPase sensitive dimer structural transitions. (PMID:20089831)
  • The interaction of Aha1 with Hsp90 and its co-chaperones in rabbit reticulocyte lysate (RRL) and in HeLa cell extracts, was characterized. (PMID:22504172)
  • Hsp90 phosphorylation on tyrosine313 promotes recruitment of AHA1, which stimulates Hsp90 ATPase activity, furthering the chaperoning process. (PMID:22727666)
  • Modulation of Hsp90 activity by AHA1 regulates VEGF signaling to eNOS and angiogenesis. (PMID:22859491)
  • Aha1 may promote disposal of folding defective proteins by the cellular protein quality control. (PMID:25378400)
  • These results suggest that differences in the middle domain of Hsp90alpha and Hsp90beta may be responsible for the isoform-specific interactions with selected proteins. (PMID:25486457)
  • Aha1 colocalized with tau pathology in brain tissue, and this association positively correlated with Alzheimer disease progression. (PMID:28827321)
  • Data support the multi-step nature of the Hsp90/Aha1-interaction, where the N-terminal domain of Aha1 interacts with both Hsp90 M domains upon induction of a partially closed conformation of the Hsp90 dimer. In addition, the data indicate that the C-terminal domain of Aha1 can adopt several conformations leading to a dynamic, polymorphic complex. (PMID:31299134)
  • Aha-type co-chaperones: the alpha or the omega of the Hsp90 ATPase cycle? (PMID:31782942)
  • AHA1 upregulates IDH1 and metabolic activity to promote growth and metastasis and predicts prognosis in osteosarcoma. (PMID:33468990)
  • Identification of AHSA1 as a Potential Therapeutic Target for Breast Cancer: Bioinformatics Analysis and in vitro Studies. (PMID:35034596)
  • The Prognostic and Immunotherapeutic Significance of AHSA1 in Pan-Cancer, and Its Relationship With the Proliferation and Metastasis of Hepatocellular Carcinoma. (PMID:35757728)
  • p23 and Aha1: Distinct Functions Promote Client Maturation. (PMID:36520307)
  • Human Aha1’s N-terminal extension confers it holdase activity in vitro. (PMID:37486705)
  • Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide that inhibits ATPase stimulation. (PMID:38937628)

Cross-species orthologs

6 orthologs

OrganismSymbolGene ID
danio_rerioahsa1aENSDARG00000028664
danio_rerioahsa1bENSDARG00000100317
mus_musculusAhsa1ENSMUSG00000021037
rattus_norvegicusAhsa1ENSRNOG00000048981
drosophila_melanogasterCG1416FBGN0032961
caenorhabditis_elegansWBGENE00007235

Protein

Protein identifiers

Activator of 90 kDa heat shock protein ATPase homolog 1O95433 (reviewed: O95433)

Alternative names: p38

All UniProt accessions (6): O95433, G3V3W9, G3V438, H0YJ63, H0YJG7, H0YJU2

UniProt curated annotations — full annotation on UniProt →

Function. Acts as a co-chaperone of HSP90AA1. Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity. Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins. Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins.

Subunit / interactions. Interacts with HSPCA/HSP90. Interacts (phosphorylated on Tyr-223) with HSP90AA1; the interaction activates HSP90AA1 ATPase activity. Interacts with HSP90AB1. Interacts with GCH1. Interacts with SRPK1. Interacts with FLCN. (Microbial infection) Interacts with vesicular stomatitis virus glycoprotein (VSV G) (via cytoplasmic tail).

Subcellular location. Cytoplasm. Cytosol. Endoplasmic reticulum.

Tissue specificity. Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.

Post-translational modifications. Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.

Induction. By heat shock and treatment with the HSP90 inhibitor 17-demethoxygeldanamycin (17AAG).

Similarity. Belongs to the AHA1 family.

Isoforms (2)

UniProt IDNamesCanonical?
O95433-11yes
O95433-22

RefSeq proteins (2): NP_001308370, NP_036243* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR013538ASHA1/2-like_CDomain
IPR015310AHSA1-like_NDomain
IPR023393START-like_dom_sfHomologous_superfamily
IPR036338Aha1Homologous_superfamily

Pfam: PF08327, PF09229

UniProt features (37 total): strand 14, helix 7, modified residue 5, turn 5, cross-link 2, chain 1, sequence conflict 1, splice variant 1, mutagenesis site 1

Structure

Experimental structures (PDB)

5 structures.

PDBMethodResolution (Å)
8Z3HX-RAY DIFFRACTION1.5
8Z3JX-RAY DIFFRACTION1.52
1X53SOLUTION NMR
7DMDSOLUTION NMR
7DMESOLUTION NMR

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-O95433-F181.100.51

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Post-translational modifications (7): 3, 193, 212, 223, 258, 182, 203

Mutagenesis-validated functional residues (1):

PositionPhenotype
223phosphomimetic mutant. increases the binding to hsp90aa1 resulting in tsc1 dissociation from hsp90aa1.

Function

Pathways and Gene Ontology

Reactome pathways

0 pathways

MSigDB gene sets: 182 (showing top): GSE45365_CD8A_DC_VS_CD11B_DC_IFNAR_KO_DN, BASSO_B_LYMPHOCYTE_NETWORK, STARK_PREFRONTAL_CORTEX_22Q11_DELETION_DN, MORF_HDAC2, GARGALOVIC_RESPONSE_TO_OXIDIZED_PHOSPHOLIPIDS_BLUE_UP, PUJANA_CHEK2_PCC_NETWORK, YORDY_RECIPROCAL_REGULATION_BY_ETS1_AND_SP100_DN, WEI_MYCN_TARGETS_WITH_E_BOX, GOBP_PROTEIN_MATURATION, GOBP_POSITIVE_REGULATION_OF_MOLECULAR_FUNCTION, chr14q24, MORF_BUB3, GOBP_PROTEIN_FOLDING, GOBP_REGULATION_OF_PROTEIN_STABILITY, TIEN_INTESTINE_PROBIOTICS_24HR_UP

GO Biological Process (3): protein folding (GO:0006457), positive regulation of ATP-dependent activity (GO:0032781), obsolete maintenance of unfolded protein (GO:0036506)

GO Molecular Function (7): ATPase activator activity (GO:0001671), protein folding chaperone (GO:0044183), cadherin binding (GO:0045296), obsolete unfolded protein binding (GO:0051082), protein-folding chaperone binding (GO:0051087), Hsp90 protein binding (GO:0051879), protein binding (GO:0005515)

GO Cellular Component (4): endoplasmic reticulum (GO:0005783), cytosol (GO:0005829), extracellular exosome (GO:0070062), cytoplasm (GO:0005737)

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
ATP-dependent activity2
cytoplasm2
cellular anatomical structure2
cellular process1
protein maturation1
regulation of ATP-dependent activity1
positive regulation of molecular function1
molecular function activator activity1
molecular_function1
protein folding1
cell adhesion molecule binding1
protein binding1
heat shock protein binding1
binding1
endomembrane system1
intracellular membrane-bounded organelle1
extracellular vesicle1
intracellular anatomical structure1

Protein interactions and networks

STRING

1975 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
AHSA1HSP90AA1P07900998
AHSA1HSP90AB1P08238995
AHSA1PTGES3Q15185974
AHSA1STIP1P31948968
AHSA1HSPA4P34932953
AHSA1CDC37Q16543935
AHSA1FKBP4Q02790895
AHSA1UNC45AQ9H3U1827
AHSA1CFTRP13569808
AHSA1DNAJB1P25685795
AHSA1DNAJA1P31689722
AHSA1HSPA8P11142717
AHSA1SRPK1Q96SB4717
AHSA1STUB1Q9UNE7710
AHSA1UNC45BQ8IWX7703

IntAct

112 interactions, top by confidence:

ABTypeScore
AHSA1HSP90AB1psi-mi:“MI:0882”(atpase reaction)0.770
HSP90AB1AHSA1psi-mi:“MI:0915”(physical association)0.770
CFTRESYT2psi-mi:“MI:0914”(association)0.710
CFTRESYT2psi-mi:“MI:2364”(proximity)0.710
HSP90AA1CHUKpsi-mi:“MI:0914”(association)0.670
AHSA1HSP90AA1psi-mi:“MI:0915”(physical association)0.660
CFTRHAX1psi-mi:“MI:0914”(association)0.610
AICDADNAJA2psi-mi:“MI:0914”(association)0.570
AHSA1EGFRpsi-mi:“MI:0915”(physical association)0.550
EGFRAHSA1psi-mi:“MI:0915”(physical association)0.550
HSP90AA1USP19psi-mi:“MI:0914”(association)0.530
GCH1AHSA1psi-mi:“MI:0915”(physical association)0.510
AHSA1GCH1psi-mi:“MI:0915”(physical association)0.510
CFTRPLEKHG3psi-mi:“MI:0914”(association)0.480
AHSA1H2BC21psi-mi:“MI:0915”(physical association)0.400
IRF3AHSA1psi-mi:“MI:0915”(physical association)0.400
repAHSA1psi-mi:“MI:0915”(physical association)0.370
OTUB1EPM2Apsi-mi:“MI:0914”(association)0.350
NFKB1NFKB1psi-mi:“MI:0914”(association)0.350
JUNTPM3psi-mi:“MI:0914”(association)0.350

BioGRID (394): AHSA1 (Affinity Capture-MS), AHSA1 (Affinity Capture-Western), ACADM (Co-fractionation), AHSA1 (Co-fractionation), AHSA1 (Co-fractionation), AHSA1 (Co-fractionation), AHSA1 (Co-fractionation), AHSA1 (Co-fractionation), AHSA1 (Co-fractionation), AHSA1 (Co-fractionation), AHSA1 (Co-fractionation), ASNS (Co-fractionation), ATP5C1 (Co-fractionation), C12orf10 (Co-fractionation), CCT6A (Co-fractionation)

ESM2 similar proteins: A6QQC0, A8MVJ9, B8ARK7, B9RBT0, G5ECQ8, G5EES6, I1R9A6, O82631, O94436, O95433, P06625, P08240, P13021, P32192, P34685, P40123, P40124, P52481, P53834, Q01518, Q03606, Q08163, Q11208, Q12449, Q16KN5, Q3MHE8, Q3SYV4, Q55DB6, Q5NBJ3, Q5R5X8, Q5YLB4, Q719I0, Q7EYV7, Q7KRR5, Q7PWB1, Q7XVN7, Q7XWV4, Q8BK64, Q8N9S3, Q9CYT6

Diamond homologs: A6QQC0, O95433, Q55DB6, Q719I0, Q8BK64, Q8N9S3, P53834

SIGNOR signaling

4 interactions.

AEffectBMechanism
AHSA1“up-regulates activity”HSP90AA1binding
AHSA1“up-regulates activity”HSP90AB1binding
AHSA1“up-regulates activity”GCH1binding
ABL1“up-regulates activity”AHSA1phosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 128 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

PathwayPartnersFoldFDR
Signaling by ERBB2 ECD mutants535.7×1e-04
Apoptotic execution phase525.3×1e-04
Signaling by ERBB2 TMD/JMD mutants525.3×1e-04
Signaling by ERBB2 KD Mutants522.5×1e-04
Downregulation of ERBB2 signaling520.2×2e-04
HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand612.3×3e-04
ESR-mediated signaling810.9×1e-04
Infectious disease123.2×1e-02

GO biological processes:

GO termPartnersFoldFDR
intrinsic apoptotic signaling pathway515.6×6e-03
JNK cascade511.8×9e-03
protein folding119.9×2e-05
positive regulation of ERK1 and ERK2 cascade85.9×9e-03
protein phosphorylation95.3×9e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

55 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic1
Likely pathogenic0
Uncertain significance32
Likely benign3
Benign7

Top pathogenic / likely-pathogenic (1)

Variant IDHGVSClassification
2426709NC_000014.8:g.(?77893959)(78082922_?)delPathogenic

SpliceAI

675 predictions. Top by Δscore:

VariantEffectΔscore
14:77458266:ACTGG:Adonor_loss1.0000
14:77458267:CTGGT:Cdonor_loss1.0000
14:77458268:TGGTG:Tdonor_loss1.0000
14:77458269:GGTGA:Gdonor_loss1.0000
14:77458270:G:GGdonor_gain1.0000
14:77458270:G:Tdonor_loss1.0000
14:77458271:T:Gdonor_loss1.0000
14:77459611:TGCAG:Tacceptor_loss1.0000
14:77459612:GCA:Gacceptor_loss1.0000
14:77459614:A:ACacceptor_loss1.0000
14:77459614:A:AGacceptor_gain1.0000
14:77459614:AG:Aacceptor_gain1.0000
14:77459614:AGGAC:Aacceptor_gain1.0000
14:77459615:G:GTacceptor_gain1.0000
14:77459615:GG:Gacceptor_gain1.0000
14:77459615:GGAC:Gacceptor_gain1.0000
14:77459615:GGACG:Gacceptor_gain1.0000
14:77459802:GACAG:Gdonor_gain1.0000
14:77459804:CAGGT:Cdonor_loss1.0000
14:77459805:AGGTA:Adonor_loss1.0000
14:77459807:G:GGdonor_gain1.0000
14:77459807:GT:Gdonor_loss1.0000
14:77459808:T:Adonor_loss1.0000
14:77462636:A:AGacceptor_gain1.0000
14:77462641:GATTA:Gacceptor_gain1.0000
14:77462757:CAGGT:Cdonor_loss1.0000
14:77462758:AGG:Adonor_loss1.0000
14:77462759:GGTA:Gdonor_loss1.0000
14:77462760:G:GCdonor_loss1.0000
14:77462761:T:Gdonor_loss1.0000

AlphaMissense

2216 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
14:77458220:T:AW11R1.000
14:77458220:T:CW11R1.000
14:77458222:G:CW11C1.000
14:77458222:G:TW11C1.000
14:77458252:C:AN21K1.000
14:77458252:C:GN21K1.000
14:77458262:T:AW25R1.000
14:77458262:T:CW25R1.000
14:77458264:G:CW25C1.000
14:77458264:G:TW25C1.000
14:77458265:C:AH26N1.000
14:77458265:C:GH26D1.000
14:77459616:G:CW27C1.000
14:77459616:G:TW27C1.000
14:77459752:C:AR73S1.000
14:77459752:C:GR73G1.000
14:77459753:G:CR73P1.000
14:77459755:A:GK74E1.000
14:77459756:A:TK74I1.000
14:77459757:A:CK74N1.000
14:77459757:A:TK74N1.000
14:77458217:C:AR10S0.999
14:77458221:G:CW11S0.999
14:77458241:G:CD18H0.999
14:77458250:A:GN21D0.999
14:77458254:T:AV22D0.999
14:77458257:A:TN23I0.999
14:77458263:G:CW25S0.999
14:77458266:A:GH26R0.999
14:77458267:C:AH26Q0.999

dbSNP variants (sampled 300 via entrez): RS1000084027 (14:77461006 A>C,G), RS1000438011 (14:77467066 G>A), RS1000486366 (14:77469461 A>G,T), RS1000715392 (14:77458137 G>C), RS1001529122 (14:77460545 T>C), RS1002563391 (14:77468924 T>G), RS1002616016 (14:77462314 A>G,T), RS1002663980 (14:77464694 G>A), RS1003204456 (14:77459173 C>G,T), RS1003903692 (14:77458954 T>C), RS1004012445 (14:77461531 CG>C,CGG), RS1004182366 (14:77467140 T>G), RS1004669579 (14:77468962 C>T), RS1004683929 (14:77462946 T>A,C,G), RS1004906979 (14:77457700 C>A)

Disease associations

OMIM: gene MIM:608466 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

0 associations (top):

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL3309113 (SINGLE PROTEIN)

PharmGKB: 1 entry (VIP=true, CPIC=false)

ChEMBL bioactivities

1 potent at pChembl≥5 of 3 total, top 1 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
6.52IC50300nMCHEMBL4536929

PubChem BioAssay actives

1 with measured affinity, of 4 total; 1 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
1-[[1-(4-fluorophenyl)pyrrole-2-carbonyl]amino]-3-[3-(trifluoromethyl)phenyl]thiourea2100615: Inhibition of human recombinant Aha1 expressed in Escherichia coli BL21 (DE3)ic500.3000uM

CTD chemical–gene interactions

54 total (human), top 30 by PubMed support.

ChemicalActions (top 5)PubMed papers
sodium arseniteincreases reaction, affects cotreatment, increases abundance, increases expression, affects binding4
Tobacco Smoke Pollutionincreases expression3
Cyclosporineincreases expression2
Cadmium Chlorideincreases expression2
aristolochic acid Iincreases expression1
3-((6-(2-methoxyphenyl)pyrimidin-4-yl)amino)phenyl)methane sulfonamidedecreases expression1
bisphenol Aincreases expression1
2-methyl-4-isothiazolin-3-oneincreases expression1
manganese chlorideincreases abundance, increases expression, affects cotreatment1
cupric oxideincreases phosphorylation1
celastrolincreases expression1
microcystin RRincreases expression1
di-n-butylphosphoric acidaffects expression1
4-phenylbutyric acidincreases expression1
azoxystrobinincreases expression1
CGP 52608affects binding, increases reaction1
chloropicrinincreases expression1
geduninincreases expression1
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamideaffects cotreatment, decreases expression1
ICG 001increases expression1
abrinedecreases expression1
(4-amino-1,4-dihydro-3-(2-pyridyl)-5-thioxo-1,2,4-triazole)copper(II)increases expression1
LDN 193189affects cotreatment, decreases expression1
picoxystrobinincreases expression1
PCI 5002affects cotreatment, increases expression1
bisphenol AFincreases expression1
Temozolomideincreases expression1
Acetaminophenaffects response to substance1
Air Pollutantsincreases abundance, increases expression1
Antimycin Aincreases expression1

ChEMBL screening assays

3 unique, capped per target: 3 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL3379288BindingBinding affinity to Aha1 (unknown origin) using FITC-labeled compound up to 5 uM by fluorescence polarization assayPotential C-terminal-domain inhibitors of heat shock protein 90 derived from a C-terminal peptide helix. — Bioorg Med Chem

Cellosaurus cell lines

4 cell lines: 4 cancer cell line

First 10 cell lines (id-ordered, not curated):

CellosaurusNameCategorySex
CVCL_E1PVHAP1 AHSA1 (-) 2Cancer cell lineMale
CVCL_E1PWHAP1 AHSA1 (-) 3Cancer cell lineMale
CVCL_E1PXHAP1 AHSA1 (-) 4Cancer cell lineMale
CVCL_XL14HAP1 AHSA1 (-) 1Cancer cell lineMale

Clinical trials (associated diseases)

0 trials via MONDO — disease-level, not drug-specific.

No linked Atlas pages yet — the cross-entity mesh grows as the corpus expands.