PNMT

gene
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Summary

PNMT (phenylethanolamine N-methyltransferase, HGNC:9160) is a protein-coding gene on chromosome 17q12, encoding Phenylethanolamine N-methyltransferase (P11086). Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor.

The product of this gene catalyzes the last step of the catecholamine biosynthesis pathway, which methylates norepinephrine to form epinephrine (adrenaline). The enzyme also has beta-carboline 2N-methyltransferase activity. This gene is thought to play a key step in regulating epinephrine production. Alternatively spliced transcript variants have been found for this gene.

Source: NCBI Gene 5409 — RefSeq curated summary.

At a glance

  • GWAS associations: 13
  • Clinical variants (ClinVar): 56 total
  • Druggable target: yes — 1 molecules with ChEMBL bioactivity
  • MANE Select transcript: NM_002686

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:9160
Approved symbolPNMT
Namephenylethanolamine N-methyltransferase
Location17q12
Locus typegene with protein product
StatusApproved
Ensembl geneENSG00000141744
Ensembl biotypeprotein_coding
OMIM171190
Entrez5409

Gene structure

Transcript identifiers

Ensembl transcripts: 3 — 3 protein_coding

ENST00000269582, ENST00000394246, ENST00000581428

RefSeq mRNA: 1 — MANE Select: NM_002686 NM_002686

CCDS: CCDS11343

Canonical transcript exons

ENST00000269582 — 3 exons

ExonStartEnd
ENSE000009507013966845339668677
ENSE000009507033966995139670475
ENSE000036634933966962939669836

Expression profiles

Bgee: expression breadth ubiquitous, 182 present calls, max score 94.20.

FANTOM5 (CAGE): breadth broad, TPM avg 1.3771 / max 215.1365, expressed in 262 samples.

FANTOM5 promoters (11 alternative TSS)

Promoter IDTPM avgSamples expressed
1606150.353147
1606110.264085
1606160.195586
1606090.162674
1606080.114554
1606130.103536
1606070.059030
1606120.045617
1606100.029611
1606140.025815

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
male germ line stem cell (sensu Vertebrata) in testisCL:0000089 ∩ UBERON:000047394.20silver quality
nucleus accumbensUBERON:000188291.22gold quality
caudate nucleusUBERON:000187390.12gold quality
putamenUBERON:000187489.41gold quality
right atrium auricular regionUBERON:000663187.07gold quality
hindlimb stylopod muscleUBERON:000425286.76gold quality
cardiac atriumUBERON:000208185.84gold quality
gastrocnemiusUBERON:000138885.77gold quality
right lungUBERON:000216785.22gold quality
skeletal muscle tissue of rectus abdominisUBERON:000451185.12silver quality
apex of heartUBERON:000209884.84gold quality
substantia nigraUBERON:000203884.42gold quality
muscle of legUBERON:000138384.14gold quality
medial globus pallidusUBERON:000247783.82gold quality
hypothalamusUBERON:000189883.69gold quality
pituitary glandUBERON:000000783.35gold quality
adenohypophysisUBERON:000219683.12gold quality
midbrainUBERON:000189183.07gold quality
amygdalaUBERON:000187682.73gold quality
muscle organUBERON:000163082.62gold quality
triceps brachiiUBERON:000150982.48gold quality
dorsal motor nucleus of vagus nerveUBERON:000287081.97gold quality
globus pallidusUBERON:000187581.83gold quality
primordial germ cell in gonadCL:0000670 ∩ UBERON:000099181.75gold quality
cervix squamous epitheliumUBERON:000692281.50gold quality
buccal mucosa cellCL:000233680.62silver quality
heart left ventricleUBERON:000208480.54gold quality
cingulate cortexUBERON:000302780.53gold quality
anterior cingulate cortexUBERON:000983580.32gold quality
cardiac ventricleUBERON:000208280.22gold quality

Single-cell (SCXA)

Detected in 3 experiment(s), a significant marker in 3.

ExperimentMarker?Max mean expression
E-MTAB-10042yes174.37
E-MTAB-7407yes151.44
E-ANND-3no0.00

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): EGR1, HIF1A, MAZ, NR3C1, PITX2, SP1, TFAP2A, TFAP2B

Literature-anchored findings (GeneRIF, showing 25)

  • Human PNMT has been crystallized in complex with an inhibitor and the cofactor product S-adenosyl-L-homocysteine and diffraction data measured from a cryocooled crystal extend to a resolution of 2.3 A. (PMID:11807261)
  • pharmacologic and biochemical evidence of beta-carboline 2N-methyltransferase activity (PMID:11900856)
  • Association between the phenylethanolamine N-methyltransferase gene and multiple sclerosis. (PMID:11958827)
  • homozygosity/heterozygosity of the phenylethanolamine N-methyltransferase gene polymorphism was highly predictive of significant weight loss with sibutramine during the first 3 months of obesity treatment (PMID:12634439)
  • genetic variants of PNMT may play a role in the development of essential hypertension. (PMID:14553966)
  • Oncogenomic recombination hotspot around the PPP1R1B-STARD3-TCAP-PNMT-PERLD1-ERBB2-C17orf37-GRB7 amplicon at human chromosome 17q12 is closely linked to evolutionary recombination hotspot around the GSDML-GSDM locus. (PMID:15010812)
  • Presence of local PNMT transcription in human heart after transplantation. (PMID:15848714)
  • disulfide-linked dimers are as active as the monomeric enzyme indicating that the crystal structure of the protein is a valid target for inhibitor design. (PMID:15893506)
  • Nicotinic stimuli appear to regulate expression of the epinephrine-synthesizing gene PNMT through a previously uncharacterized regulatory element. (PMID:15968085)
  • Results suggest that PNMT catalyzes transfer of methyl to ligand amines only when “anchor” interactions, such as those identified for the beta-hydroxyls of p-octopamine and cis-AT, are present. (PMID:16363801)
  • the differences in PNMT expression between normotensives and hypertensives are not determined by the polymorphisms in this gene, but rather by the interplay of gene expression regulators, which may vary among individuals (PMID:17645789)
  • We examined the correlation between reward dependence (RD) trait, and 5 polymorphisms in genes of norepinephrine pathways. We found that rs3764351 in PNMT was significantly associated with reward dependence trait. (PMID:18702937)
  • Haplotypes of the phenylethanolamine N-methyltransferase (PNMT), catechol-O-methyltransferase (COMT) have functionally important effects on alcohol-induced cardiovascular symptoms by affecting blood catecholamine levels. (PMID:18715275)
  • The crystal structures illustrate the adaptability of the PNMT substrate binding site in accepting multi-fused ring systems, such as substituted norbornene, as well as noradrenochrome, the oxidation product of noradrenaline. (PMID:19570037)
  • the reaction takes place via an SN2 mechanism with methyl transfer being rate-limiting (PMID:19733262)
  • PNMT G-390A polymorphism is possibly associated with essential hypertension risk in male Chinese Han population. (PMID:19952402)
  • In Caucasians, phenylethanolamine N-methyltransferase single nucleotide polymorphisms are associated with the development of acute kidney injury, disease severity, and in-hospital mortality. (PMID:20090367)
  • PNMT variants in cis may interact with nuclear factors in trans to govern adrenergic activity. (PMID:20204374)
  • The 2-SNP AA haplotype in the PNMT promoter is associated with decreased risk of essential hypertension in Han Chinese. (PMID:21866188)
  • initial velocity studies on human PNMT in the absence and presence of product and dead end inhibitors. (PMID:24018397)
  • PNMT underexpression is associated with malignant pheochromocytoma and paraganglioma. (PMID:27007161)
  • Epistasis between phenylethanolamine N-methyltransferase and beta2-adrenergic receptor influences extracellular epinephrine level and associates with the susceptibility to allergic asthma. (PMID:31855300)
  • The effect of transcutaneous electrical nerve stimulation (TENS) on pain control and phenylethanolamine-N-methyltransferase (PNMT) gene expression after cesarean section. (PMID:34933717)
  • Overexpression of miR-375 and L-type Amino Acid Transporter 1 in Pheochromocytoma and Their Molecular and Functional Implications. (PMID:35269556)
  • Composite paraganglioma-ganglioneuroma with atypical catecholamine profile and phenylethanolamine N-methyltransferase expression: a case report and literature review. (PMID:37952980)

Cross-species orthologs

6 orthologs

OrganismSymbolGene ID
danio_reriopnmtENSDARG00000116039
mus_musculusPnmtENSMUSG00000038216
rattus_norvegicusPnmtENSRNOG00000046057
caenorhabditis_elegansWBGENE00011573
caenorhabditis_elegansWBGENE00015124
caenorhabditis_elegansWBGENE00018340

Paralogs (2): NNMT (ENSG00000166741), INMT (ENSG00000241644)

Protein

Protein identifiers

Phenylethanolamine N-methyltransferaseP11086 (reviewed: P11086)

Alternative names: Noradrenaline N-methyltransferase

All UniProt accessions (3): A8MT87, P11086, J3QRI3

UniProt curated annotations — full annotation on UniProt →

Function. Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L-methionine as the methyl donor. Other substrates include phenylethanolamine and octopamine. Also methylates normetanephrine.

Activity regulation. Inhibited by methyl methanethiosulfonate, phenylglyoxal, tetranitromethane and diethyl pyrocarbonate. Inhibited by 4-oxo-1,4-dihydro-quinoline-3,7-dicarboxylic acid, 4-(benzo[d][1,3]dioxol-5-ylamino)-4-oxobutanoic acid and 1,4-diaminonaphthalene-2,6-disulfonic acid.

Pathway. Catecholamine biosynthesis; (R)-adrenaline biosynthesis; (R)-adrenaline from (R)-noradrenaline: step 1/1.

Similarity. Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.

RefSeq proteins (1): NP_002677* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR000940NNMT_TEMT_transFamily
IPR025820NNMT/PNMT/TEMT_CSConserved_site
IPR029063SAM-dependent_MTases_sfHomologous_superfamily
IPR053384SAM-dep_methyltransferaseFamily

Pfam: PF01234

Enzyme classification (BRENDA):

  • EC 2.1.1.28 — phenylethanolamine N-methyltransferase (BRENDA: 11 organisms, 48 substrates, 244 inhibitors, 71 Km, 22 kcat entries)

Substrate kinetics (BRENDA)

20 substrates with measured Km, best-characterized 15. Km ranges are aggregated across organisms/conditions.

SubstrateKm (mM)Measurements
S-ADENOSYL-L-METHIONINE0.0012–0.04523
PHENYLETHANOLAMINE0.07–2.0518
L-NOREPINEPHRINE0.015–0.1014
3,4-DICHLOROPHENYLETHANOLAMINE0.0008–0.00163
3-TRIFLUOROMETHYLPHENYLETHANOLAMINE0.0005–0.0553
3,4-DICHLOROPHENYLETHYLENEDIAMINE0.012–0.01312
ANTI-9-AMINO-6-(TRIFLUOROMETHYL)BENZONORBORNENE0.0015–0.0252
D-NOREPINEPHRINE0.0297–0.1092
OCTOPAMINE0.00552
2-HYDROXYPHENYLETHANOLAMINE0.6761
3,4-DIHYDROXYPHENYLETHANOLAMINE0.0131
3-CHLORO-4-HYDROXYPHENYLETHANOLAMINE0.00241
3-HYDROXYPHENYLETHANOLAMINE0.0891
3-METHOXY-4-HYDROXY-PHENYLETHANOLAMINE0.3661
4-AMINOMETHYL-1,2,3,4-TETRAHYDROISOQUINOLINE0.0471

Catalyzed reactions (Rhea), 4 shown:

  • phenylethanolamine + S-adenosyl-L-methionine = N-methylphenylethanolamine + S-adenosyl-L-homocysteine + H(+) (RHEA:12176)
  • (R)-noradrenaline + S-adenosyl-L-methionine = (R)-adrenaline + S-adenosyl-L-homocysteine + H(+) (RHEA:25269)
  • (R)-octopamine + S-adenosyl-L-methionine = (R)-synephrine + S-adenosyl-L-homocysteine + H(+) (RHEA:70519)
  • (R)-normetanephrine + S-adenosyl-L-methionine = (R)-metanephrine + S-adenosyl-L-homocysteine + H(+) (RHEA:70683)

UniProt features (53 total): helix 12, strand 11, binding site 10, sequence variant 9, mutagenesis site 5, turn 2, initiator methionine 1, chain 1, modified residue 1, sequence conflict 1

Structure

Experimental structures (PDB)

44 structures, top 30 by resolution.

PDBMethodResolution (Å)
4MIKX-RAY DIFFRACTION1.95
2G72X-RAY DIFFRACTION2
3KQSX-RAY DIFFRACTION2
7TWUX-RAY DIFFRACTION2.1
2G8NX-RAY DIFFRACTION2.15
2AN3X-RAY DIFFRACTION2.2
2AN4X-RAY DIFFRACTION2.2
2G71X-RAY DIFFRACTION2.2
3KQYX-RAY DIFFRACTION2.2
4MQ4X-RAY DIFFRACTION2.2
2OBFX-RAY DIFFRACTION2.3
3HCCX-RAY DIFFRACTION2.3
3KQVX-RAY DIFFRACTION2.3
3KR1X-RAY DIFFRACTION2.3
3KR2X-RAY DIFFRACTION2.3
3HCDX-RAY DIFFRACTION2.39
3KQTX-RAY DIFFRACTION2.4
1HNNX-RAY DIFFRACTION2.4
1YZ3X-RAY DIFFRACTION2.4
2G70X-RAY DIFFRACTION2.4
3HCAX-RAY DIFFRACTION2.4
3HCBX-RAY DIFFRACTION2.4
3KPUX-RAY DIFFRACTION2.4
3KPVX-RAY DIFFRACTION2.4
3KPWX-RAY DIFFRACTION2.4
3KPYX-RAY DIFFRACTION2.4
3KQMX-RAY DIFFRACTION2.4
3KQOX-RAY DIFFRACTION2.4
3KQPX-RAY DIFFRACTION2.4
4DM3X-RAY DIFFRACTION2.4

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-P11086-F194.640.92

Functional residue map

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

Ligand- & substrate-binding residues (10): 219; 267; 35; 40; 79–80; 85; 101; 106; 158–159; 181

Post-translational modifications (1): 7

Mutagenesis-validated functional residues (5):

PositionPhenotype
35strongly increases km for phenylethanolamine and s-adenosyl-l-methionine.
185strongly reduced enzyme activity towards phenylethanolamine. increases affinity for s-adenosyl-l-methionine.
185strongly reduced enzyme activity towards phenylethanolamine. decreases affinity for phenylethanolamine and s-adenosyl-l-
219reduced enzyme activity towards phenylethanolamine. decreases affinity for phenylethanolamine 6-fold. decreases affinity
267strongly reduced enzyme activity towards phenylethanolamine. decreases affinity for phenylethanolamine 200-fold. decreas

Function

Pathways and Gene Ontology

Reactome pathways

1 pathways

IDPathway
R-HSA-209905Catecholamine biosynthesis

MSigDB gene sets: 117 (showing top): GSE45365_CD8A_DC_VS_CD11B_DC_IFNAR_KO_MCMV_INFECTION_UP, GOBP_PHENOL_CONTAINING_COMPOUND_METABOLIC_PROCESS, GOBP_PHENOL_CONTAINING_COMPOUND_BIOSYNTHETIC_PROCESS, GCM_RING1, GCM_FCGR2B, MORF_PML, MORF_PDPK1, GOBP_METHYLATION, MORF_MT4, GCM_BECN1, KEGG_TYROSINE_METABOLISM, WANG_HCP_PROSTATE_CANCER, MORF_ORC1L, MORF_MYST2, MORF_RBM8A

GO Biological Process (3): methylation (GO:0032259), epinephrine biosynthetic process (GO:0042418), catecholamine biosynthetic process (GO:0042423)

GO Molecular Function (5): phenylethanolamine N-methyltransferase activity (GO:0004603), protein binding (GO:0005515), methyltransferase activity (GO:0008168), S-adenosylmethionine-dependent methyltransferase activity (GO:0008757), transferase activity (GO:0016740)

GO Cellular Component (1): cytosol (GO:0005829)

Reactome top-level categories

Rollup of top-1 pathways:

CategoryPathways
Metabolism of amine-derived hormones1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
metabolic process1
epinephrine metabolic process1
catecholamine biosynthetic process1
catecholamine metabolic process1
catechol-containing compound biosynthetic process1
biogenic amine biosynthetic process1
N-methyltransferase activity1
S-adenosylmethionine-dependent methyltransferase activity1
binding1
transferase activity, transferring one-carbon groups1
methyltransferase activity1
catalytic activity1
cytoplasm1
cellular anatomical structure1

Protein interactions and networks

STRING

536 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
PNMTTHP07101948
PNMTDBHP09172901
PNMTDDCP20711732
PNMTCRHP06850720
PNMTPENKP01210685
PNMTPAHP00439679
PNMTCOMTP21964670
PNMTPOMCP01189666
PNMTAOC1P19801666
PNMTTOMTQ8WZ04638
PNMTCHGBP05060609
PNMTMAOAP21397591
PNMTMAOBP27338591
PNMTNPYP01303583
PNMTSDHDO14521529

IntAct

10 interactions, top by confidence:

ABTypeScore
PNMTLNX1psi-mi:“MI:0915”(physical association)0.560
PNMTKLHL8psi-mi:“MI:0915”(physical association)0.560
ESR1PGK2psi-mi:“MI:0914”(association)0.530
PNMTTERF1psi-mi:“MI:0915”(physical association)0.370
PNMTTERF2IPpsi-mi:“MI:0915”(physical association)0.370
PNMTKLHL8psi-mi:“MI:0915”(physical association)0.000
PNMTLNX1psi-mi:“MI:0915”(physical association)0.000

BioGRID (13): PNMT (Affinity Capture-MS), PNMT (Negative Genetic), PNMT (Positive Genetic), PNMT (Positive Genetic), RPS6KA4 (Positive Genetic), PNMT (Positive Genetic), UCK2 (Positive Genetic), RELA (Positive Genetic), PNMT (Two-hybrid), KLHL8 (Two-hybrid), PNMT (Affinity Capture-MS), PNMT (Two-hybrid), PNMT (Two-hybrid)

ESM2 similar proteins: A0A5F8AH41, A0AVI4, A0JMH2, A1Y9I9, A5WVX1, B0X4N1, B4P925, D3ZX08, O55171, O88512, O95050, O97972, P0DPD7, P0DPE0, P0DPE1, P10937, P10938, P11086, P40935, P40936, Q06AU9, Q08DK0, Q14CH7, Q32PE2, Q32Q92, Q3SZG9, Q3URQ7, Q568P9, Q5E9L5, Q5JTZ9, Q5RCH4, Q5RFR7, Q6NTR1, Q6NZB1, Q7QIL2, Q7TMC8, Q80YU0, Q8HY87, Q8K304, Q8NFF5

Diamond homologs: A0A5F8AH41, O55239, O95050, O97972, P10937, P10938, P11086, P40261, P40935, P40936, Q06AU9, Q06AV1, Q5RFR7

SIGNOR signaling

2 interactions.

AEffectBMechanism
PNMT“up-regulates quantity”adrenaline“chemical modification”
PNMT“down-regulates quantity”noradrenaline“chemical modification”

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance48
Likely benign4
Benign2

Top pathogenic / likely-pathogenic (0)

SpliceAI

386 predictions. Top by Δscore:

VariantEffectΔscore
17:39669617:T:Aacceptor_gain1.0000
17:39669625:CCA:Cacceptor_loss1.0000
17:39669626:CAGG:Cacceptor_loss1.0000
17:39669627:A:AGacceptor_gain1.0000
17:39669627:A:Gacceptor_loss1.0000
17:39669628:G:GCacceptor_gain1.0000
17:39669628:GGT:Gacceptor_gain1.0000
17:39669772:G:GTdonor_gain1.0000
17:39669831:C:Tdonor_gain1.0000
17:39669834:GGG:Gdonor_gain1.0000
17:39669835:GG:Gdonor_gain1.0000
17:39669835:GGG:Gdonor_gain1.0000
17:39669835:GGGTA:Gdonor_loss1.0000
17:39669836:GG:Gdonor_gain1.0000
17:39669837:G:GAdonor_loss1.0000
17:39669837:G:GGdonor_gain1.0000
17:39669838:T:Gdonor_loss1.0000
17:39669947:ACAG:Aacceptor_gain1.0000
17:39669947:ACAGG:Aacceptor_gain1.0000
17:39668676:CGG:Cdonor_loss0.9900
17:39668678:G:Cdonor_loss0.9900
17:39668679:T:Gdonor_loss0.9900
17:39669622:T:Aacceptor_gain0.9900
17:39669627:AG:Aacceptor_gain0.9900
17:39669627:AGGT:Aacceptor_gain0.9900
17:39669628:GG:Gacceptor_gain0.9900
17:39669628:GGTG:Gacceptor_gain0.9900
17:39669628:GGTGA:Gacceptor_gain0.9900
17:39669736:G:GTdonor_gain0.9900
17:39669797:GCAT:Gdonor_gain0.9900

AlphaMissense

1820 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
17:39670102:A:CS188R0.994
17:39670104:C:AS188R0.994
17:39670104:C:GS188R0.994
17:39668563:T:CF30L0.992
17:39668565:C:AF30L0.992
17:39668565:C:GF30L0.992
17:39670084:T:CF182L0.983
17:39670086:C:AF182L0.983
17:39670086:C:GF182L0.983
17:39669793:T:AW123R0.982
17:39669793:T:CW123R0.982
17:39669706:T:CF94L0.981
17:39669708:T:AF94L0.981
17:39669708:T:GF94L0.981
17:39669725:C:AT100K0.980
17:39670089:C:GC183W0.980
17:39669744:C:AN106K0.978
17:39669744:C:GN106K0.978
17:39669728:A:TD101V0.975
17:39668564:T:CF30S0.974
17:39668564:T:GF30C0.974
17:39668641:T:AW56R0.974
17:39668641:T:CW56R0.974
17:39668643:G:CW56C0.974
17:39668643:G:TW56C0.974
17:39669691:A:CS89R0.974
17:39669693:T:AS89R0.974
17:39669693:T:GS89R0.974
17:39669763:T:AW113R0.974
17:39669763:T:CW113R0.974

dbSNP variants (sampled 300 via entrez): RS1000060686 (17:39669165 C>T), RS1000303052 (17:39666412 C>T), RS1000681701 (17:39667490 G>C), RS1001040040 (17:39670577 A>C,G), RS1002355862 (17:39668602 C>T), RS1002463115 (17:39667464 C>G,T), RS1002976726 (17:39667353 G>A), RS1004599803 (17:39667307 G>A), RS1004717498 (17:39668390 C>A,G,T), RS1005548956 (17:39668492 G>A), RS1006562326 (17:39670027 C>G,T), RS1006732991 (17:39670723 G>C), RS1007111530 (17:39666989 A>AC), RS1007451551 (17:39668340 A>G,T), RS1007547213 (17:39670653 G>A)

Disease associations

OMIM: gene MIM:171190 | disease phenotypes:

GenCC curated gene-disease

Mondo (0):

Orphanet (0):

HPO phenotypes

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

GWAS associations

13 associations (top):

StudyTraitp-value
GCST000624_15Ulcerative colitis3.000000e-08
GCST000964_1Ulcerative colitis5.000000e-11
GCST003119_9Urinary metabolites4.000000e-26
GCST003589_1Bronchial hyperresponsiveness in asthma3.000000e-20
GCST007235_3Pancreatic ductal adenocarcinoma1.000000e-06
GCST007564_21Asthma or allergic disease (pleiotropy)4.000000e-17
GCST008757_30Alcohol consumption1.000000e-09
GCST008916_10Asthma5.000000e-09
GCST008916_21Asthma2.000000e-62
GCST008916_45Asthma3.000000e-10
GCST008916_86Asthma2.000000e-14
GCST009798_16Asthma8.000000e-27
GCST010002_123Refractive error1.000000e-24

EFO canonical traits (1, from GWAS)

EFO IDTrait name
EFO:0005116urinary metabolite measurement

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL4617 (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: 1,522 (via chembl_molecule»patent_compound — counts attach to the compound, not the gene–compound relationship, so off-target/promiscuous molecules can dominate).

MoleculeNamePhasePatents
CHEMBL1088977ADEMETIONINE31,522

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

PharmGKB variants

3 variants.

VariantGenesLevelScore#Clin annotsDrugs
rs876493PNMT0.000
rs2934965PNMT0.000
rs2941523PNMT0.000

GtoPdb / IUPHAR curated pharmacology

(IUPHAR/BPS Guide to Pharmacology — expert-curated)

Target class: enzyme — Catecholamine turnover

Most potent curated ligand interactions (1 total), top 1:

LigandActionAffinityParameter
LY134046Inhibition7.6pKi

Binding affinities (BindingDB)

26 measured of 26 human assays (28 total across all organisms); most potent 26 below. Values come from heterogeneous assays and are not directly comparable.

LigandMeasureValue
3-(hydroxymethyl)-N-(2,2,2-trifluoroethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI23 nM
3-(hydroxymethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI52 nM
N-(4-chlorophenyl)-3-(hydroxymethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI63 nM
3-(fluoromethyl)-N-(2,2,2-trifluoroethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI130 nM
3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI150 nM
3-(fluoromethyl)-N-(3,3,3-trifluoropropyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI220 nM
N-(4-chlorophenyl)-3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI270 nM
7-methanesulfonyl-1,2,3,4-tetrahydroisoquinolineKI790 nM
3-(fluoromethyl)-7-methanesulfonyl-1,2,3,4-tetrahydroisoquinolineKI1100 nM
((+/-)-3-Fluoromethyl-7-(3,3,3-trifluoropropylsulfonyl)-1,2,3,4-tetrahydroisoquinolineKI1300 nM
N-ethyl-3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI1400 nM
3-(fluoromethyl)-7-[(2,2,2-trifluoroethane)sulfonyl]-1,2,3,4-tetrahydroisoquinolineKI1400 nM
3-(fluoromethyl)-N-propyl-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI1700 nM
3-(fluoromethyl)-7-(propane-1-sulfonyl)-1,2,3,4-tetrahydroisoquinolineKI2400 nM
3-(fluoromethyl)-N-methyl-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI3700 nM
3-(fluoromethyl)-N-(2-methoxyethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamideKI5100 nM
7-(trichloromethane)sulfonyl-1,2,3,4-tetrahydroisoquinolineKI6300 nM
7-(prop-2-ene-1-sulfonyl)-1,2,3,4-tetrahydroisoquinolineKI9000 nM
((+/-)-7-Ethylsulfonyl-3-fluoromethyl-1,2,3,4-tetrahydroisoquinolineKI14000 nM
7-(butane-1-sulfonyl)-3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinolineKI18000 nM
7-(benzenesulfonyl)-1,2,3,4-tetrahydroisoquinolineKI23000 nM
7-{[(4-chlorophenyl)methane]sulfonyl}-3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinolineKI32000 nM
((+/-)-3-Fluoromethyl-7-(4,4,4-trifluorobutylsulfonyl)-1,2,3,4-tetrahydroisoquinolineKI67000 nM
3-(fluoromethyl)-7-[(3-methoxypropane)sulfonyl]-1,2,3,4-tetrahydroisoquinolineKI72000 nM
3-Fluoromethyl-1,2,3,4-tetrahydro-isoquinoline-7-sulfonic acid adamantan-1-ylamideKI88000 nM
1,2,3,4-tetrahydroisoquinolineKI4.7e+07 nM

ChEMBL bioactivities

250 potent at pChembl≥5 of 305 total, top 50 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChemblTypeValueUnitMolecule
9.00Ki1nMCHEMBL290890
8.89Ki1.3nMCHEMBL286497
8.85Ki1.4nMCHEMBL176112
8.81Ki1.55nMCHEMBL287837
8.74Ki1.8nMCHEMBL355581
8.68Ki2.1nMCHEMBL4764318
8.52Ki3nMCHEMBL541797
8.52IC503nMCHEMBL287837
8.52Ki3nMCHEMBL287837
8.51Ki3.1nMCHEMBL287837
8.49Ki3.2nMCHEMBL4751862
8.48Ki3.3nMCHEMBL4782649
8.46Ki3.5nMCHEMBL4760727
8.42Ki3.8nMCHEMBL4800292
8.41Ki3.9nMCHEMBL4754656
8.31Ki4.9nMCHEMBL337144
8.00IC5010nMCHEMBL287837
8.00Ki10nMCHEMBL38681
7.92Ki12nMCHEMBL41487
7.80Ki16nMCHEMBL57966
7.77Ki17nMCHEMBL200375
7.77Ki17nMCHEMBL59441
7.77Ki17nMCHEMBL177621
7.75Ki18nMCHEMBL4749263
7.72Ki19nMCHEMBL287837
7.70Ki20nMCHEMBL356439
7.64Ki23nMCHEMBL366785
7.58Ki26.5nMCHEMBL287837
7.55Ki28nMCHEMBL175519
7.55IC5028nMCHEMBL175519
7.54Ki29nMCHEMBL149023
7.52Ki30nMCHEMBL146188
7.46Ki35nMCHEMBL177621
7.42Ki38nMCHEMBL4740168
7.41Ki39nMCHEMBL176112
7.40Ki40nMCHEMBL26828
7.40Ki40nMCHEMBL459366
7.34Ki46nMCHEMBL290890
7.34Ki46nMCHEMBL4795252
7.33Ki47nMCHEMBL59441
7.30Ki50nMCHEMBL459366
7.28Ki52nMCHEMBL41647
7.28Ki52nMCHEMBL149816
7.25Ki56nMCHEMBL281864
7.24Ki57nMCHEMBL4796664
7.23Ki59nMCHEMBL149535
7.21Ki61nMCHEMBL425522
7.20Ki63nMCHEMBL176112
7.17Ki67nMCHEMBL206892
7.16Ki70nMCHEMBL275595

PubChem BioAssay actives

193 with measured affinity, of 6100 total; 50 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

CompoundAssayTypeValueUnit
N-(4-chlorophenyl)-3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide298194: Inhibition of human PNMT K57A mutantki0.0010uM
N-(4-chlorophenyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide298194: Inhibition of human PNMT K57A mutantki0.0013uM
N-(4-chlorophenyl)-3-(hydroxymethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide298194: Inhibition of human PNMT K57A mutantki0.0014uM
7,8-dichloro-1,2,3,4-tetrahydroisoquinoline282848: Binding affinity to human wild type his-tagged PNMTki0.0015uM
4-[[3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinolin-7-yl]sulfonyl]thiomorpholine298194: Inhibition of human PNMT K57A mutantki0.0018uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[3-(1,2,3,4-tetrahydroisoquinolin-3-ylmethylamino)propylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0021uM
7,8-dichloro-1,2,3,4-tetrahydroisoquinoline;hydrochloride155332: Binding affinity for phenylethanolamine N-methyl-transferase was determined.ki0.0030uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[2-[(7-chloro-1,2,3,4-tetrahydroisoquinolin-3-yl)methylamino]ethylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0032uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[3-[(7-chloro-1,2,3,4-tetrahydroisoquinolin-3-yl)methylamino]propylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0033uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[3-[(7-nitro-1,2,3,4-tetrahydroisoquinolin-3-yl)methylamino]propylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0035uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[2-[(7-nitro-1,2,3,4-tetrahydroisoquinolin-3-yl)methylamino]ethylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0038uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[4-(1,2,3,4-tetrahydroisoquinolin-3-ylmethylamino)butylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0039uM
[(3R)-7-bromo-1,2,3,4-tetrahydroisoquinolin-3-yl]methanol239072: Inhibitory binding affinity for phenylethanolamine N-methyl-transferase (PNMT)ki0.0049uM
8,9-dichloro-2,3,4,5-tetrahydro-1H-2-benzazepine239072: Inhibitory binding affinity for phenylethanolamine N-methyl-transferase (PNMT)ki0.0100uM
(3S)-3-methyl-7-nitro-1,2,3,4-tetrahydroisoquinoline313557: Inhibition of human PNMT by radiochemical assayki0.0160uM
3-(fluoromethyl)-N-(3,3,3-trifluoropropyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide298194: Inhibition of human PNMT K57A mutantki0.0170uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[6-(1,2,3,4-tetrahydroisoquinolin-3-ylmethylamino)hexylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0180uM
6,7,8-trichloro-1,2,3,4-tetrahydroisoquinoline155335: Dissociation constant(Ki) of compound was determined to measure Phenylethanolamine N-methyl-transferase inhibitory potencyki0.0200uM
3-(hydroxymethyl)-N-(2,2,2-trifluoroethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide1796978: Radiochemical Assay of PNMT Inhibitors from Article 10.1021/jm060466d: “Comparison of the binding of 3-fluoromethyl-7-sulfonyl-1,2,3,4-tetrahydroisoquinolines with their isosteric sulfonamides to the active site of phenylethanolamine N-methyltransferase.”ki0.0230uM
3-(hydroxymethyl)-N-(3,3,3-trifluoropropyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide239080: In vitro binding affinity against human phenylethanolamine N-Methyltransferaseki0.0280uM
7-chloro-1,2,3,4-tetrahydroisoquinoline155334: Dissociation constant(Ki) of compound was determined to measure PNMT-inhibitory potencyki0.0290uM
8-chloro-1,2,3,4-tetrahydroisoquinoline155333: Dissociation constant(Ki) of compound was determined to measure PNMT-inhibitory potencyki0.0300uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[2-(1,2,3,4-tetrahydroisoquinolin-3-ylmethylamino)ethylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0380uM
N-[3-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]propyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0460uM
3-(hydroxymethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide1796978: Radiochemical Assay of PNMT Inhibitors from Article 10.1021/jm060466d: “Comparison of the binding of 3-fluoromethyl-7-sulfonyl-1,2,3,4-tetrahydroisoquinolines with their isosteric sulfonamides to the active site of phenylethanolamine N-methyltransferase.”ki0.0520uM
5,6,7,8-tetrachloro-1,2,3,4-tetrahydroisoquinoline155335: Dissociation constant(Ki) of compound was determined to measure Phenylethanolamine N-methyl-transferase inhibitory potencyki0.0520uM
7-bromo-1,2,3,4-tetrahydroisoquinoline293029: Binding affinity to human PNMTki0.0560uM
(2R,3R,4S,5S)-2-(6-aminopurin-9-yl)-5-[5-(1,2,3,4-tetrahydroisoquinolin-3-ylmethylamino)pentylsulfanylmethyl]oxolane-3,4-diol1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0570uM
5,7,8-trichloro-1,2,3,4-tetrahydroisoquinoline155334: Dissociation constant(Ki) of compound was determined to measure PNMT-inhibitory potencyki0.0590uM
(3R)-3-(fluoromethyl)-N-(2,2,2-trifluoroethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide239480: In vitro binding affinity against recombinant human Phenylethanolamine N-methyl-transferase expressed in Escherichia coli using [methyl-3H]-AdoMetki0.0610uM
3-(difluoromethyl)-7-(trifluoromethyl)-1,2,3,4-tetrahydroisoquinoline264506: Binding affinity to human PNMTki0.0670uM
3-(fluoromethyl)-7-iodo-1,2,3,4-tetrahydroisoquinoline239072: Inhibitory binding affinity for phenylethanolamine N-methyl-transferase (PNMT)ki0.0700uM
N-[3-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]propyl]-7-nitro-1,2,3,4-tetrahydroisoquinoline-3-carboxamide1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0700uM
N-[2-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]ethyl]-7-chloro-1,2,3,4-tetrahydroisoquinoline-3-carboxamide1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0710uM
(3R)-3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide239480: In vitro binding affinity against recombinant human Phenylethanolamine N-methyl-transferase expressed in Escherichia coli using [methyl-3H]-AdoMetki0.0720uM
3-methyl-7-nitro-1,2,3,4-tetrahydroisoquinoline257555: Inhibitory activity against human PNMTki0.0720uM
N-[2-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]ethyl]-7-nitro-1,2,3,4-tetrahydroisoquinoline-3-carboxamide1700192: Competitive inhibition of C-terminal hexahistidine tag in human recombinant PNMT expressed in Escherichia coli assessed as inhibition constant using PEA as substrate in presence of 100 uM AdoMet as co-substrate by Sigma-plot analysiski0.0860uM
1-(2,3-dichlorophenyl)ethanamine239072: Inhibitory binding affinity for phenylethanolamine N-methyl-transferase (PNMT)ki0.0900uM
7-bromo-3-(difluoromethyl)-1,2,3,4-tetrahydroisoquinoline264506: Binding affinity to human PNMTki0.0940uM
(3R)-3-(fluoromethyl)-N-(3,3,3-trifluoropropyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide239480: In vitro binding affinity against recombinant human Phenylethanolamine N-methyl-transferase expressed in Escherichia coli using [methyl-3H]-AdoMetki0.0990uM
7,8-dichloro-2-[4-(7,8-dichloro-3,4-dihydro-1H-isoquinolin-2-yl)butyl]-3,4-dihydro-1H-isoquinoline;dihydrochloride155323: Inhibition of rabbit adrenal phenylethanolamine N-methyl-transferaseic500.1000uM
(3R)-N-(4-chlorophenyl)-3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide239480: In vitro binding affinity against recombinant human Phenylethanolamine N-methyl-transferase expressed in Escherichia coli using [methyl-3H]-AdoMetki0.1100uM
3-(fluoromethyl)-N-(2,2,2-trifluoroethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide1796978: Radiochemical Assay of PNMT Inhibitors from Article 10.1021/jm060466d: “Comparison of the binding of 3-fluoromethyl-7-sulfonyl-1,2,3,4-tetrahydroisoquinolines with their isosteric sulfonamides to the active site of phenylethanolamine N-methyltransferase.”ki0.1300uM
3-(fluoromethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide1796978: Radiochemical Assay of PNMT Inhibitors from Article 10.1021/jm060466d: “Comparison of the binding of 3-fluoromethyl-7-sulfonyl-1,2,3,4-tetrahydroisoquinolines with their isosteric sulfonamides to the active site of phenylethanolamine N-methyltransferase.”ki0.1500uM
N-ethyl-3-(hydroxymethyl)-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide239080: In vitro binding affinity against human phenylethanolamine N-Methyltransferaseki0.1700uM
3-(difluoromethyl)-7-nitro-1,2,3,4-tetrahydroisoquinoline264506: Binding affinity to human PNMTki0.1700uM
3-(hydroxymethyl)-N-propyl-1,2,3,4-tetrahydroisoquinoline-7-sulfonamide239080: In vitro binding affinity against human phenylethanolamine N-Methyltransferaseki0.1900uM
3-(difluoromethyl)-7-iodo-1,2,3,4-tetrahydroisoquinoline264506: Binding affinity to human PNMTki0.2000uM
7-bromo-1,2,3,4-tetrahydrobenzo[h]isoquinoline293029: Binding affinity to human PNMTki0.2200uM
(7-thiomorpholin-4-ylsulfonyl-1,2,3,4-tetrahydroisoquinolin-3-yl)methanol239080: In vitro binding affinity against human phenylethanolamine N-Methyltransferaseki0.2300uM

CTD chemical–gene interactions

12 total (human), top 12 by PubMed support.

ChemicalActions (top 5)PubMed papers
Benzo(a)pyrenedecreases expression, increases methylation2
MT19c compounddecreases expression1
Bortezomibdecreases expression1
Panobinostataffects cotreatment, affects expression1
Cisplatinaffects cotreatment, affects expression1
Dexamethasoneincreases expression1
Formaldehydedecreases expression1
Nicotineincreases expression1
Phenobarbitaldecreases expression1
Tretinoindecreases expression1
Triclosandecreases expression1
Valproic Acidincreases methylation1

ChEMBL screening assays

72 unique, capped per target: 65 binding, 5 functional, 2 admet

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL1024773BindingBinding affinity to wild type human PNMT by liquid scintillation spectrometry in presence of [3H]AdoMetTime-dependent inactivation of human phenylethanolamine N-methyltransferase by 7-isothiocyanatotetrahydroisoquinoline. — Bioorg Med Chem Lett
CHEMBL4416337ADMETInhibition of human PNMT expressed in Escherichia coli at 10 uM assessed as reduction in SAH level using DL-normetanephrine as substrate in presence of SAM incubated for 45 mins by LC-MS/MS analysis relative to controlHigh-Affinity Alkynyl Bisubstrate Inhibitors of Nicotinamide N-Methyltransferase (NNMT). — J Med Chem
CHEMBL759758FunctionalAbility to inhibit rabbit adrenal phenylethanolamine N-methyl-transferase norepinephrine to epinephrine (E13), in vitro, at 10 e-4 M compound concentration.Tetrahydrothiadiazoloisoquinolines: synthesis and inhibition of phenylethanolamine-N-methyltransferase. — J Med Chem

Cellosaurus cell lines

3 cell lines: 3 cancer cell line

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

CellosaurusNameCategorySex
CVCL_D1PWAbcam K-562 PNMT KOCancer cell lineFemale
CVCL_D2LIAbcam Raji PNMT KOCancer cell lineMale
CVCL_WQ33Abcam Jurkat PNMT KOCancer 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.