HSPBP1

gene
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Also known as FES1

Summary

HSPBP1 (HSPA (Hsp70) binding protein 1, HGNC:24989) is a protein-coding gene on chromosome 19q13.42, encoding Hsp70-binding protein 1 (Q9NZL4). Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding.

Enables molecular sequestering activity and ubiquitin protein ligase binding activity. Involved in positive regulation of proteasomal ubiquitin-dependent protein catabolic process and positive regulation of protein ubiquitination. Is active in extracellular space.

Source: NCBI Gene 23640 — RefSeq curated summary.

At a glance

  • GWAS associations: 1
  • Clinical variants (ClinVar): 78 total — 2 pathogenic
  • Druggable target: yes — 1 molecules with ChEMBL bioactivity
  • MANE Select transcript: NM_012267

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:24989
Approved symbolHSPBP1
NameHSPA (Hsp70) binding protein 1
Location19q13.42
Locus typegene with protein product
StatusApproved
AliasesFES1
Ensembl geneENSG00000133265
Ensembl biotypeprotein_coding
OMIM612939
Entrez23640

Gene structure

Transcript identifiers

Ensembl transcripts: 24 — 24 protein_coding

ENST00000255631, ENST00000433386, ENST00000585698, ENST00000585927, ENST00000587551, ENST00000587922, ENST00000587959, ENST00000588971, ENST00000593263, ENST00000874509, ENST00000874510, ENST00000874511, ENST00000874512, ENST00000874513, ENST00000874514, ENST00000874515, ENST00000874516, ENST00000933732, ENST00000933733, ENST00000933734, ENST00000933735, ENST00000933736, ENST00000957929, ENST00000957930

RefSeq mRNA: 3 — MANE Select: NM_012267 NM_001130106, NM_001297600, NM_012267

CCDS: CCDS33111

Canonical transcript exons

ENST00000433386 — 8 exons

ExonStartEnd
ENSE000006998175527764255277846
ENSE000011754785526527855265389
ENSE000011754865526588655265982
ENSE000011754935526613155266286
ENSE000011755005527439855274622
ENSE000011792795527939955279702
ENSE000028358145528003555280110
ENSE000029516415526222355262682

Expression profiles

Bgee: expression breadth ubiquitous, 270 present calls, max score 96.74.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 32.4712 / max 134.6519, expressed in 1811 samples.

FANTOM5 promoters (4 alternative TSS)

Promoter IDTPM avgSamples expressed
18277031.01111808
1827690.6902226
1827720.4765232
1827710.2934143

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
nucleus accumbensUBERON:000188296.74gold quality
right uterine tubeUBERON:000130296.38gold quality
caudate nucleusUBERON:000187396.15gold quality
putamenUBERON:000187496.01gold quality
right frontal lobeUBERON:000281095.09gold quality
apex of heartUBERON:000209894.12gold quality
cingulate cortexUBERON:000302793.97gold quality
anterior cingulate cortexUBERON:000983593.79gold quality
amygdalaUBERON:000187693.74gold quality
mucosa of transverse colonUBERON:000499193.59gold quality
Brodmann (1909) area 9UBERON:001354093.31gold quality
prefrontal cortexUBERON:000045193.29gold quality
dorsolateral prefrontal cortexUBERON:000983493.04gold quality
olfactory segment of nasal mucosaUBERON:000538692.27gold quality
neocortexUBERON:000195091.96gold quality
lower esophagus mucosaUBERON:003583491.96gold quality
telencephalonUBERON:000189391.92gold quality
frontal cortexUBERON:000187091.78gold quality
frontal lobeUBERON:001652591.75gold quality
hypothalamusUBERON:000189891.55gold quality
forebrainUBERON:000189091.46gold quality
lower esophagusUBERON:001347391.37gold quality
lower esophagus muscularis layerUBERON:003583391.37gold quality
right atrium auricular regionUBERON:000663191.30gold quality
hindlimb stylopod muscleUBERON:000425291.24gold quality
epithelium of bronchusUBERON:000203191.19gold quality
gastrocnemiusUBERON:000138891.10gold quality
cerebral cortexUBERON:000095691.06gold quality
heart left ventricleUBERON:000208491.01gold quality
bronchusUBERON:000218590.97gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

ExperimentMarker?Max mean expression
E-ANND-3yes8.15
E-HCAD-5no2.24

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

23 targeting HSPBP1, 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-12118100.0065.881270
HSA-MIR-188-3P100.0068.761240
HSA-MIR-607799.9968.042299
HSA-MIR-3173-3P99.9866.491217
HSA-MIR-6891-5P99.9866.531372
HSA-MIR-6825-5P99.9669.813431
HSA-MIR-4728-5P99.8569.394718
HSA-MIR-76599.8468.242442
HSA-MIR-3156-3P99.7666.72939
HSA-MIR-11181-3P99.7566.382205
HSA-MIR-451699.6167.783390
HSA-MIR-1260A99.6166.671098
HSA-MIR-1260B99.6166.671098
HSA-MIR-3682-3P99.5867.63865
HSA-MIR-391199.3866.951087
HSA-MIR-127699.3668.181642
HSA-MIR-570399.1067.092053
HSA-MIR-313898.4167.53744
HSA-MIR-615-5P98.1063.76591
HSA-MIR-4800-5P97.2265.91324
HSA-MIR-10398-5P97.1264.941051
HSA-MIR-4693-3P95.2365.92735
HSA-MIR-542-5P87.4760.4276

Literature-anchored findings (GeneRIF, showing 25)

  • Results report cooperative interactions involving Hsp70, Hsp40, and TPR1 that enhance Hsp70-dependent folding of chemically denatured substrates. (PMID:14503850)
  • Detection of hsp70 may be used as the screening marker for diagnosis of polycyclic aromatic hydrocarbons (PAHs)-related lung cancer related lung cancer, and may supplement the diagnostic value of conventional cytology. (PMID:14761400)
  • HspBP1 interferes with the CHIP-induced degradation of immature forms of the cystic fibrosis transmembrane conductance regulator (CFTR) and stimulates CFTR maturation. (PMID:15215316)
  • BAG2 binds to the carboxyl terminus of Hsp70-interacting protein (CHIP) and provides a cochaperone-dependent regulatory mechanism for preventing unregulated ubiquitylation of misfolded proteins by CHIP (PMID:16169850)
  • The results demonstrate that Hsp70 and HspBP1 are not coordinately regulated but provide evidence that an increase in the ratio of HspBP1 to Hsp70 correlates with apoptosis, in a similar way to reducing the amount of Hsp70. (PMID:16677834)
  • Stress-induced heat shock protein 70 (Hsp70) effectively protects cells against ultraviol ray-induced apoptosis in melanocytes bu penetrating mitchondrial and lysosomal membranes. (PMID:16950797)
  • Here, we report that upon the formation of huntingtin aggregates; endogenous cytosolic huntingtin, Hsc70/Hsp70 (heat shock protein and cognate protein of 70kDa) and syntaxin 1A become aggregate-centered. (PMID:17208201)
  • that HspBP1, by antagonizing the prosurvival activity of Hsp70, sensitizes tumor cells to cathepsin-mediated cell death. (PMID:17855353)
  • Association between endogenous LAP2alpha and Hsp70 in non-transfected cells was confirmed by co-immunoprecipitation. (PMID:18261988)
  • The two chaperones, HSP72 and HSPBP1, interact both physically and functionally, leading to the activation of th EGFR-ERK1/2 signalling pathway. (PMID:18986301)
  • Results indicate that low HspBP1 expression could be a marker of tumor aggressiveness. (PMID:18987994)
  • Our data suggest that HIP may prevent inclusion formation by facilitating the constitutive HSC70 refolding cycle and possibly by preventing aggregation. (PMID:19183265)
  • HspBP1 may play a role in tumor (dys)regulation of chaperone proteins (PMID:19659607)
  • High gene expression of HspBP1 is associated with leukemia. (PMID:20694586)
  • shown that HspBP1 binds Tag7 in the conditioned medium of tumor CSML0 cells, thereby preventing formation of the cytotoxic Tag7-Hsp70 complex (PMID:22037021)
  • BAG-1M and HspBP1 had differential impacts on the dynamic composition of steroid receptor folding complexes (PMID:24454860)
  • Oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1. (PMID:24898092)
  • our results clearly show that HspBP1 acts as an endogenous negative regulator of HIV-1 gene-expression and replication by suppressing NF-kappaB-mediated activation of viral transcription. (PMID:26538602)
  • downregulation of Hsp70 and HspBP1 represents a unique feature of patients with preterm prelabor rupture of membranes (PMID:28497897)
  • Findings indicate a critical role of HspBP1 in differential CHIP/Hsp70 activities in neuronal and glial cells and the greater neuronal vulnerability to misfolded proteins in neurodegenerative diseases. (PMID:28847953)
  • Circulating HspBp1 is associated with progression of HIV infection and can be used as a new marker to predict the prognosis and management of HIV infection (PMID:30786116)
  • The Co-Chaperone HspBP1 Is a Novel Component of Stress Granules that Regulates Their Formation. (PMID:32235396)
  • HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I. (PMID:33713958)
  • HspBP1 is a dual function regulatory protein that controls both DNA repair and apoptosis in breast cancer cells. (PMID:35387978)
  • The cochaperone HspBP1 binds to and inhibits Hsp70 activity. (PMID:9830037)

Cross-species orthologs

4 orthologs

OrganismSymbolGene ID
danio_reriohspbp1ENSDARG00000102937
mus_musculusHspbp1ENSMUSG00000063802
rattus_norvegicusHspbp1ENSRNOG00000017795
drosophila_melanogasterCG10973FBGN0036306

Paralogs (1): SIL1 (ENSG00000120725)

Protein

Protein identifiers

Hsp70-binding protein 1Q9NZL4 (reviewed: Q9NZL4)

Alternative names: Heat shock protein-binding protein 1, Hsp70-binding protein 2, Hsp70-interacting protein 1, Hsp70-interacting protein 2

All UniProt accessions (7): Q9NZL4, K7EKM6, K7EL16, K7EMM7, K7EN20, K7EQQ0, K7ERT9

UniProt curated annotations — full annotation on UniProt →

Function. Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.

Subunit / interactions. Interacts with the ATP-binding domain of HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with PGLYRP1; this interaction blocks the cytotoxic activity of the PGLYRP1-HSPA1A complex.

Tissue specificity. Ubiquitous.

Isoforms (3)

UniProt IDNamesCanonical?
Q9NZL4-11yes
Q9NZL4-22
Q9NZL4-33

RefSeq proteins (3): NP_001123578, NP_001284529, NP_036399* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR011989ARM-likeHomologous_superfamily
IPR013918Nucleotide_exch_fac_Fes1Domain
IPR016024ARM-type_foldHomologous_superfamily
IPR050693SIL1/FES1/HPBP1Family

Pfam: PF08609

UniProt features (36 total): helix 20, repeat 4, splice variant 3, sequence variant 2, modified residue 2, chain 1, sequence conflict 1, turn 1, region of interest 1, compositionally biased region 1

Structure

Experimental structures (PDB)

3 structures.

PDBMethodResolution (Å)
1XQRX-RAY DIFFRACTION2.1
8X87X-RAY DIFFRACTION2.2
1XQSX-RAY DIFFRACTION2.9

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9NZL4-F184.360.68

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 (2): 351, 356

Function

Pathways and Gene Ontology

Reactome pathways

0 pathways

MSigDB gene sets: 151 (showing top): GOBP_REGULATION_OF_PROTEASOMAL_UBIQUITIN_DEPENDENT_PROTEIN_CATABOLIC_PROCESS, STARK_PREFRONTAL_CORTEX_22Q11_DELETION_DN, GRAESSMANN_APOPTOSIS_BY_DOXORUBICIN_DN, GRAESSMANN_RESPONSE_TO_MC_AND_DOXORUBICIN_DN, GOBP_POSITIVE_REGULATION_OF_PROTEIN_CATABOLIC_PROCESS, GOBP_MACROMOLECULE_CATABOLIC_PROCESS, GOBP_PROTEIN_MATURATION, GOBP_REGULATION_OF_CATABOLIC_PROCESS, GOBP_POSITIVE_REGULATION_OF_CATABOLIC_PROCESS, HOSHIDA_LIVER_CANCER_LATE_RECURRENCE_DN, GOBP_REGULATION_OF_PROTEIN_CATABOLIC_PROCESS, GOBP_POST_TRANSLATIONAL_PROTEIN_MODIFICATION, GOBP_PROTEIN_FOLDING, MORI_PRE_BI_LYMPHOCYTE_UP, CYTAGCAAY_UNKNOWN

GO Biological Process (3): protein folding (GO:0006457), positive regulation of protein ubiquitination (GO:0031398), positive regulation of proteasomal ubiquitin-dependent protein catabolic process (GO:0032436)

GO Molecular Function (5): adenyl-nucleotide exchange factor activity (GO:0000774), enzyme inhibitor activity (GO:0004857), ubiquitin protein ligase binding (GO:0031625), molecular sequestering activity (GO:0140313), protein binding (GO:0005515)

GO Cellular Component (2): obsolete extracellular space (GO:0005615), endoplasmic reticulum (GO:0005783)

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
cellular process1
protein maturation1
protein ubiquitination1
regulation of protein ubiquitination1
positive regulation of protein modification by small protein conjugation or removal1
regulation of proteasomal ubiquitin-dependent protein catabolic process1
proteasome-mediated ubiquitin-dependent protein catabolic process1
positive regulation of proteasomal protein catabolic process1
positive regulation of ubiquitin-dependent protein catabolic process1
ATP binding1
ADP binding1
ATPase regulator activity1
catalytic activity1
enzyme regulator activity1
molecular function inhibitor activity1
ubiquitin-like protein ligase binding1
molecular_function1
binding1
cytoplasm1
endomembrane system1
intracellular membrane-bounded organelle1

Protein interactions and networks

STRING

4104 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
HSPBP1HSPA4P34932997
HSPBP1HSPA8P11142984
HSPBP1DNAJB1P25685942
HSPBP1STUB1Q9UNE7897
HSPBP1HSP90AB1P08238890
HSPBP1HSP90AA1P07900854
HSPBP1UBE2D1P51668837
HSPBP1STIP1P31948782
HSPBP1BRSK1Q8TDC3760
HSPBP1GRPEL1Q9HAV7755
HSPBP1TRIM21P19474745
HSPBP1BAG1Q99933740
HSPBP1DNAJA1P31689683
HSPBP1HYOU1Q9Y4L1667
HSPBP1HSPA1AP08107629

IntAct

124 interactions, top by confidence:

ABTypeScore
CSNK2BCSNK2A2psi-mi:“MI:0914”(association)0.960
HSPA8HSPBP1psi-mi:“MI:0915”(physical association)0.930
HSPBP1HSPA8psi-mi:“MI:0915”(physical association)0.930
HSPBP1HSPA2psi-mi:“MI:0915”(physical association)0.920
HSPA2HSPBP1psi-mi:“MI:0915”(physical association)0.920
MED4MED19psi-mi:“MI:0914”(association)0.900
HSPA8BAG2psi-mi:“MI:2364”(proximity)0.860
GMNNMCIDASpsi-mi:“MI:0914”(association)0.770
HSPA8GAKpsi-mi:“MI:0914”(association)0.760
CFTRESYT2psi-mi:“MI:2364”(proximity)0.710
CFTRESYT2psi-mi:“MI:0914”(association)0.710
VCPUBXN8psi-mi:“MI:0914”(association)0.690
HSPBP1NOTCH2NLApsi-mi:“MI:0915”(physical association)0.670
NOTCH2NLAHSPBP1psi-mi:“MI:0915”(physical association)0.670
HSF1KPNA3psi-mi:“MI:0914”(association)0.640
HMCESHSPA8psi-mi:“MI:0914”(association)0.640

BioGRID (256): HSPBP1 (Two-hybrid), HSPBP1 (Two-hybrid), NOTCH2NL (Two-hybrid), HSPA8 (Affinity Capture-MS), HSPA6 (Affinity Capture-MS), EDRF1 (Affinity Capture-MS), NT5C2 (Affinity Capture-MS), ELF2 (Affinity Capture-MS), HSPBP1 (Two-hybrid), HSPBP1 (Two-hybrid), ACTR2 (Co-fractionation), HSPBP1 (Co-fractionation), HSPBP1 (Co-fractionation), HSPBP1 (Co-fractionation), HSPBP1 (Co-fractionation)

ESM2 similar proteins: A5A779, A6NLP5, A8E7I5, C5IJB0, F1MX48, I3L5V6, M0RDU0, O35465, O95801, P23610, P36915, P36916, P97452, Q00558, Q08602, Q0P5H9, Q14137, Q14318, Q17QX2, Q2TBQ9, Q2YD98, Q3B7U9, Q3SZV0, Q4R588, Q4R8D2, Q5EA80, Q5NVK5, Q5R8E2, Q5RA07, Q5TM59, Q66H45, Q68G30, Q6AY79, Q6IMX7, Q6P597, Q6P9Z4, Q6SZW1, Q7YR35, Q810A3, Q8C3I8

Diamond homologs: A1DLW4, A2R4I6, A3LUY1, O43030, P0CN68, P0CN69, P38260, Q0CH70, Q0V4C4, Q1E3S4, Q2GXZ7, Q2U9E2, Q4I624, Q4P7F2, Q4R588, Q4WDH3, Q59NN8, Q5AYT7, Q6BLA1, Q6C239, Q6CNM7, Q6FM01, Q6IMX7, Q6NUA7, Q75B89, Q99P31, Q9C239, Q9NZL4, Q08199, Q32KV6, Q6BTV5, Q6CKV0, Q6P6S4, Q9EPK6, Q9H173, Q9VBV5

SIGNOR signaling

0 interactions.

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 113 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
Attenuation phase525.5×2e-04
Cellular response to heat stress524.6×2e-04
Dengue Virus Genome Translation and Replication519.8×4e-04
Aggrephagy618.6×1e-04
HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand716.9×4e-05
Regulation of HSF1-mediated heat shock response915.7×3e-06
Autophagy611.1×1e-03
The role of GTSE1 in G2/M progression after G2 checkpoint510.1×5e-03

GO biological processes:

GO termPartnersFoldFDR
protein refolding637.1×9e-06
cellular response to heat620.4×2e-04
response to unfolded protein514.9×3e-03
protein folding99.2×2e-04

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic2
Likely pathogenic0
Uncertain significance59
Likely benign5
Benign2

Top pathogenic / likely-pathogenic (2)

Variant IDHGVSClassification
564606GRCh37/hg19 19q13.42-13.43(chr19:54196216-58759679)x3Pathogenic
59116GRCh38/hg38 19q13.33-13.43(chr19:47908540-58539965)x3Pathogenic

SpliceAI

1400 predictions. Top by Δscore:

VariantEffectΔscore
19:55265286:C:CAdonor_gain1.0000
19:55265385:CCAGG:Cacceptor_gain1.0000
19:55265386:CAGGC:Cacceptor_gain1.0000
19:55265388:GG:Gacceptor_gain1.0000
19:55265390:C:CCacceptor_gain1.0000
19:55266284:GACC:Gacceptor_loss1.0000
19:55266285:ACC:Aacceptor_loss1.0000
19:55266286:CCT:Cacceptor_loss1.0000
19:55266287:C:CAacceptor_loss1.0000
19:55274393:CTCA:Cdonor_loss1.0000
19:55274394:TCA:Tdonor_loss1.0000
19:55274395:CA:Cdonor_loss1.0000
19:55274396:A:ACdonor_gain1.0000
19:55274396:A:ATdonor_loss1.0000
19:55274397:C:CCdonor_gain1.0000
19:55274397:C:CGdonor_loss1.0000
19:55274397:CAG:Cdonor_gain1.0000
19:55274397:CAGG:Cdonor_gain1.0000
19:55274629:C:CTacceptor_gain1.0000
19:55274631:C:CTacceptor_gain1.0000
19:55277637:GGTAC:Gdonor_loss1.0000
19:55277638:GTACC:Gdonor_loss1.0000
19:55277639:TACCT:Tdonor_loss1.0000
19:55277640:AC:Adonor_loss1.0000
19:55277641:CCTGC:Cdonor_loss1.0000
19:55277842:CGCCT:Cacceptor_gain1.0000
19:55277845:CT:Cacceptor_gain1.0000
19:55277847:C:CCacceptor_gain1.0000
19:55277848:T:Cacceptor_loss1.0000
19:55277855:C:CTacceptor_gain1.0000

AlphaMissense

0 scored. Top likely-pathogenic:

dbSNP variants (sampled 300 via entrez): RS1000144911 (19:55280969 G>A,T), RS1000229684 (19:55269832 C>T), RS1000419104 (19:55270285 T>A), RS1000434554 (19:55263713 C>G,T), RS1000619537 (19:55268804 G>A), RS1000709305 (19:55275018 A>C), RS1000751749 (19:55269072 A>G,T), RS1000819574 (19:55270741 TCCACACATC>T), RS1000823688 (19:55274304 T>C), RS1000876135 (19:55274465 C>G,T), RS1001022531 (19:55278967 C>G), RS1001061472 (19:55279493 G>A), RS1001496914 (19:55276719 G>C), RS1001547872 (19:55276917 C>A,T), RS1001554938 (19:55279892 T>C)

Disease associations

OMIM: gene MIM:612939 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

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

GWAS associations

1 associations (top):

StudyTraitp-value
GCST010653_3Thyroid stimulating hormone levels1.000000e-08

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL5724653 (SINGLE PROTEIN)

Molecules with ChEMBL bioactivity

1 molecules (phase ≥1), by development phase (incl. off-target/promiscuous compounds). Patent mentions across the top 20 by phase: 1,538 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

MoleculeNamePhasePatents
CHEMBL1232461MOLIBRESIB21,538

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

ChEMBL bioactivities

2 potent at pChembl≥5 of 2 total, top 2 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
6.56Kd273nMMOLIBRESIB
6.16IC50690nMMOLIBRESIB

PubChem BioAssay actives

2 with measured affinity, of 7 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
2-[(4S)-6-(4-chlorophenyl)-8-methoxy-1-methyl-4H-[1,2,4]triazolo[4,3-a][1,4]benzodiazepin-4-yl]-N-ethylacetamide2179230: Binding affinity against HSPBP1 (unknown origin) assessed as apparent dissociation constant incubated for 1 hr by colloidal coomassie staining based LC-MS/MS analysiskd0.2730uM

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
sodium arsenitedecreases expression, increases expression2
Air Pollutantsaffects cotreatment, increases abundance, increases oxidation, increases expression2
Smokedecreases expression, increases abundance, increases expression2
aristolochic acid Iincreases expression1
GSK-J4decreases expression1
bisphenol Faffects cotreatment, increases expression1
alpha-pineneincreases oxidation, increases abundance, affects cotreatment1
bisphenol Aaffects expression1
beta-lapachonedecreases expression1
methacrylaldehydeaffects cotreatment, increases oxidation, increases abundance1
di-n-butylphosphoric acidaffects expression1
K 7174decreases expression1
(+)-JQ1 compounddecreases expression1
Acetaminophendecreases expression1
Acroleinincreases oxidation, increases abundance, affects cotreatment1
Atrazinedecreases expression1
Benzo(a)pyreneincreases methylation1
Caffeineincreases phosphorylation1
Dexamethasoneaffects cotreatment, increases expression1
Doxorubicindecreases expression1
Enzyme Inhibitorsdecreases activity, increases O-linked glycosylation1
Indomethacinaffects cotreatment, increases expression1
Isoniaziddecreases expression1
Ivermectindecreases expression1
Ozoneincreases oxidation, increases abundance, affects cotreatment1
Tobacco Smoke Pollutiondecreases expression1
Valproic Acidincreases methylation1
1-Methyl-3-isobutylxanthineaffects cotreatment, increases expression1
Aflatoxin B1increases methylation1
Okadaic Acidincreases expression1

ChEMBL screening assays

7 unique, capped per target: 7 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL5697673BindingInhibition of HSPBP1 (unknown origin) assessed as fold change at 10 uM incubated for 1 hr by colloidal coomassie staining based LC-MS/MS analysisInhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia. — Nature

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.