TMOD3

gene
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Also known as UTMOD

Summary

TMOD3 (tropomodulin 3, HGNC:11873) is a protein-coding gene on chromosome 15q21.2, encoding Tropomodulin-3 (Q9NYL9). Blocks the elongation and depolymerization of the actin filaments at the pointed end.

Enables cadherin binding activity involved in cell-cell adhesion. Predicted to be involved in actin filament organization; muscle contraction; and myofibril assembly. Predicted to act upstream of or within actin cytoskeleton organization; erythrocyte development; and positive regulation of mitotic cell cycle phase transition. Located in adherens junction.

Source: NCBI Gene 29766 — RefSeq curated summary.

At a glance

  • Clinical variants (ClinVar): 60 total
  • MANE Select transcript: NM_014547

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:11873
Approved symbolTMOD3
Nametropomodulin 3
Location15q21.2
Locus typegene with protein product
StatusApproved
AliasesUTMOD
Ensembl geneENSG00000138594
Ensembl biotypeprotein_coding
OMIM605112
Entrez29766

Gene structure

Transcript identifiers

Ensembl transcripts: 21 — 12 protein_coding, 7 protein_coding_CDS_not_defined, 2 nonsense_mediated_decay

ENST00000308580, ENST00000558300, ENST00000558455, ENST00000558666, ENST00000558714, ENST00000559202, ENST00000560549, ENST00000560725, ENST00000561136, ENST00000561408, ENST00000561438, ENST00000871168, ENST00000871169, ENST00000871170, ENST00000871171, ENST00000871172, ENST00000871173, ENST00000871174, ENST00000924675, ENST00000924676, ENST00000961498

RefSeq mRNA: 1 — MANE Select: NM_014547 NM_014547

CCDS: CCDS10145

Canonical transcript exons

ENST00000308580 — 10 exons

ExonStartEnd
ENSE000009314045186921751869373
ENSE000011028215189381551893945
ENSE000011707485186281151863010
ENSE000012431385190877651915725
ENSE000016372995189641951896526
ENSE000016548625190015551900298
ENSE000025401975182965351829836
ENSE000034797805190189251902036
ENSE000036494485188905651889145
ENSE000036767645188758951887711

Expression profiles

Bgee: expression breadth ubiquitous, 268 present calls, max score 97.62.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 49.0555 / max 642.6341, expressed in 1819 samples.

FANTOM5 promoters (9 alternative TSS)

Promoter IDTPM avgSamples expressed
14668342.26961817
1466843.18001347
1466822.45641342
1466900.3872136
1466850.3428143
1466910.186954
1466960.113444
1466950.093937
1466860.02524

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
amniotic fluidUBERON:000017397.62gold quality
esophagus squamous epitheliumUBERON:000692096.60gold quality
oral cavityUBERON:000016796.21gold quality
buccal mucosa cellCL:000233695.76gold quality
gingivaUBERON:000182895.03gold quality
lower lobe of lungUBERON:000894994.95gold quality
lower esophagus mucosaUBERON:003583494.76gold quality
gingival epitheliumUBERON:000194994.63gold quality
colonic epitheliumUBERON:000039794.23gold quality
skin of hipUBERON:000155493.65gold quality
calcaneal tendonUBERON:000370193.34gold quality
epithelium of esophagusUBERON:000197693.13gold quality
mucosa of sigmoid colonUBERON:000499392.77gold quality
pharyngeal mucosaUBERON:000035592.60gold quality
esophagus mucosaUBERON:000246992.45gold quality
penisUBERON:000098992.41gold quality
colonic mucosaUBERON:000031791.92gold quality
tendon of biceps brachiiUBERON:000818891.51gold quality
tonsilUBERON:000237291.15gold quality
tendonUBERON:000004391.10gold quality
spermCL:000001991.08gold quality
visceral pleuraUBERON:000240190.34gold quality
monocyteCL:000057690.10gold quality
upper leg skinUBERON:000426290.07gold quality
jejunal mucosaUBERON:000039989.85gold quality
stromal cell of endometriumCL:000225589.57gold quality
mononuclear cellCL:000084289.36gold quality
leukocyteCL:000073889.26gold quality
palpebral conjunctivaUBERON:000181289.08gold quality
parietal pleuraUBERON:000240089.05gold quality

Single-cell (SCXA)

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

ExperimentMarker?Max mean expression
E-ANND-3yes13.29
E-GEOD-130148yes5.75

Regulation

Is transcription factor: no

miRNA regulators (miRDB)

170 targeting TMOD3, 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-3163100.0077.238605
HSA-MIR-200B-3P100.0073.312693
HSA-MIR-200C-3P100.0073.352685
HSA-MIR-429100.0073.442698
HSA-MIR-5692A100.0074.406850
HSA-MIR-29A-3P100.0073.111835
HSA-MIR-29B-3P100.0073.181833
HSA-MIR-29C-3P100.0073.151833
HSA-MIR-3613-3P100.0076.367965
HSA-MIR-3646100.0073.565283
HSA-MIR-340-5P100.0072.504437
HSA-MIR-4510100.0066.602050
HSA-MIR-6127100.0066.762188
HSA-MIR-6129100.0066.462080
HSA-MIR-6130100.0066.692012
HSA-MIR-6133100.0066.482064
HSA-LET-7A-3P100.0074.033932
HSA-LET-7B-3P100.0074.083913
HSA-MIR-98-3P100.0074.083907
HSA-MIR-4795-3P100.0074.624024
HSA-MIR-6758-5P100.0066.211470
HSA-MIR-6856-5P100.0065.471298
HSA-MIR-428299.9975.366408
HSA-MIR-548C-3P99.9974.017587
HSA-MIR-366299.9973.825684
HSA-MIR-318599.9968.121959
HSA-MIR-806899.9873.852376
HSA-MIR-499A-5P99.9870.791323
HSA-MIR-4482-3P99.9872.503147
HSA-MIR-548N99.9871.944170

Literature-anchored findings (GeneRIF, showing 10)

  • capping of actin filament pointed ends by Tmod3 inhibits cell migration and reveal a novel control mechanism for regulation of actin filaments in lamellipodia. (PMID:12707310)
  • levels of TM1, TM2 and TM3 are reduced in human transitional cell carcinoma cells, but significantly upregulated by inhibition of the mitogen-activated protein kinase-signaling pathway (PMID:15095301)
  • the Tmod3 isoform may regulate actin dynamics differently in cells than the previously described tropomodulin isoforms (PMID:17012745)
  • findings show that the pointed-end capping protein Tmod3 contributes to epithelial cell shape within confluent monolayers of polarized epithelial cells (PMID:17928307)
  • investigation of biomarkers for early diagnosis of endometriosis: Data suggest that TMOD3, tropomyosin 3, and stomatin-like protein 2 are autoantigens present in blood of women with endometriosis; immunodominant epitopes were identified. (PMID:22158085)
  • study has identified several new proteins like RHOC, DLG5, UGDH, TMOD3 in addition to known chemoresistance associated proteins in non-small cell lung carcinoma. (PMID:26898345)
  • TMOD3 expression was found to be elevated in liver cancer cells and tissues. In the in vitro experiments, liver cancer cell proliferation, invasion and migration were inhibited by TMOD3 knockdown and promoted by ectopic expression of TMOD3. TMOD3 overexpression activated MAPK/ERK signaling and increased the levels of other targets of this pathway. (PMID:30864730)
  • These findings reveal that Tmod3 enhances aggressive behavior of hepatocellular carcinoma (HCC) both in vitro and in vivo by interacting with EFGR and by activating the PI3K-AKT signaling pathway. (PMID:31313392)
  • Tropomodulins Control the Balance between Protrusive and Contractile Structures by Stabilizing Actin-Tropomyosin Filaments. (PMID:32037094)
  • Clinicopathological Characteristics, Prognosis, and Correlated Tumor Cell Function of Tropomodulin-3 in Pancreatic Adenocarcinoma. (PMID:37563820)

Cross-species orthologs

5 orthologs

OrganismSymbolGene ID
danio_reriotmod2ENSDARG00000002571
mus_musculusTmod3ENSMUSG00000058587
rattus_norvegicusTmod3ENSRNOG00000032436
drosophila_melanogastertmodFBGN0082582
caenorhabditis_elegansunc-94WBGENE00006823

Paralogs (6): TMOD2 (ENSG00000128872), TMOD1 (ENSG00000136842), TMOD4 (ENSG00000163157), LMOD3 (ENSG00000163380), LMOD1 (ENSG00000163431), LMOD2 (ENSG00000170807)

Protein

Protein identifiers

Tropomodulin-3Q9NYL9 (reviewed: Q9NYL9)

Alternative names: Ubiquitous tropomodulin

All UniProt accessions (4): Q9NYL9, H0YKU1, H0YNJ8, H0YNU8

UniProt curated annotations — full annotation on UniProt →

Function. Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton.

Subunit / interactions. Binds to the N-terminus of tropomyosin and to actin. Interacts with FLII.

Subcellular location. Cytoplasm. Cytoskeleton.

Tissue specificity. Ubiquitous.

Similarity. Belongs to the tropomodulin family.

RefSeq proteins (1): NP_055362* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR004934TMODFamily
IPR032675LRR_dom_sfHomologous_superfamily

Pfam: PF03250

UniProt features (3 total): chain 1, modified residue 1, sequence conflict 1

Structure

Experimental structures (PDB)

0 structures.

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-Q9NYL9-F182.100.48

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 (1): 25

Function

Pathways and Gene Ontology

Reactome pathways

3 pathways

IDPathway
R-HSA-390522Striated Muscle Contraction
R-HSA-9013418RHOBTB2 GTPase cycle
R-HSA-9696264RND3 GTPase cycle

MSigDB gene sets: 289 (showing top): GOBP_MYELOID_CELL_DIFFERENTIATION, GOBP_NEGATIVE_REGULATION_OF_PROTEIN_CONTAINING_COMPLEX_ASSEMBLY, RRAGTTGT_UNKNOWN, RODRIGUES_THYROID_CARCINOMA_ANAPLASTIC_UP, GOBP_REGULATION_OF_PROTEIN_POLYMERIZATION, GOBP_MYELOID_CELL_HOMEOSTASIS, GOBP_MYELOID_CELL_DEVELOPMENT, GOBP_NEGATIVE_REGULATION_OF_PROTEIN_POLYMERIZATION, GOBP_ERYTHROCYTE_HOMEOSTASIS, GOBP_CELL_CYCLE_PHASE_TRANSITION, GOBP_POSITIVE_REGULATION_OF_MITOTIC_CELL_CYCLE, GOBP_STRIATED_MUSCLE_CELL_DIFFERENTIATION, AP4_Q6, GOBP_NEGATIVE_REGULATION_OF_ACTIN_FILAMENT_DEPOLYMERIZATION, GOBP_REGULATION_OF_CELLULAR_COMPONENT_BIOGENESIS

GO Biological Process (9): muscle contraction (GO:0006936), actin filament organization (GO:0007015), myofibril assembly (GO:0030239), mitotic cell cycle phase transition (GO:0044772), erythrocyte development (GO:0048821), pointed-end actin filament capping (GO:0051694), positive regulation of mitotic cell cycle phase transition (GO:1901992), actin cytoskeleton organization (GO:0030036), cell-cell adhesion (GO:0098609)

GO Molecular Function (4): actin binding (GO:0003779), tropomyosin binding (GO:0005523), cadherin binding involved in cell-cell adhesion (GO:0098641), protein binding (GO:0005515)

GO Cellular Component (5): cytoskeleton (GO:0005856), striated muscle thin filament (GO:0005865), adherens junction (GO:0005912), myofibril (GO:0030016), cytoplasm (GO:0005737)

Reactome top-level categories

Rollup of top-3 pathways:

CategoryPathways
Muscle contraction1
RHOBTB GTPase Cycle1
RHO GTPase cycle1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
supramolecular fiber organization2
cytoskeletal protein binding2
muscle system process1
actin cytoskeleton organization1
cellular component assembly involved in morphogenesis1
actomyosin structure organization1
striated muscle cell development1
membraneless organelle assembly1
mitotic cell cycle1
cell cycle phase transition1
mitotic cell cycle process1
erythrocyte differentiation1
myeloid cell development1
actin filament capping1
mitotic cell cycle phase transition1
positive regulation of mitotic cell cycle1
positive regulation of cell cycle phase transition1
regulation of mitotic cell cycle phase transition1
cytoskeleton organization1
actin filament-based process1
cell adhesion1
cadherin binding1
cell-cell adhesion1
cell-cell adhesion mediator activity1
binding1
intracellular membraneless organelle1
actin cytoskeleton1
sarcomere1
myofilament1
cell-cell junction1
contractile muscle fiber1
intracellular anatomical structure1
cellular anatomical structure1

Protein interactions and networks

STRING

1180 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
TMOD3ADD1P35611955
TMOD3ADD2P35612945
TMOD3ADD3Q9UEY8939
TMOD3NEBP20929917
TMOD3CGNL1Q0VF96906
TMOD3DMTNQ08495894
TMOD3CARMIL2Q6F5E8847
TMOD3EPB41P11171821
TMOD3ANK1P16157801
TMOD3CAPZA2P47755798
TMOD3CAPZA1P52907796
TMOD3CYP19A1P11511735
TMOD3MYPNQ86TC9724
TMOD3ANK2Q01484708
TMOD3ANK3Q12955693

IntAct

178 interactions, top by confidence:

ABTypeScore
PRPF3PRPF4psi-mi:“MI:0914”(association)0.730
CFTRESYT2psi-mi:“MI:0914”(association)0.710
DAPK1MYO1Bpsi-mi:“MI:0914”(association)0.530
LIN9MYBL1psi-mi:“MI:0914”(association)0.530
TWF1MYO1Cpsi-mi:“MI:0914”(association)0.530
SSH1GSNpsi-mi:“MI:0914”(association)0.530
DBN1SVILpsi-mi:“MI:0914”(association)0.530
CFTRPLEKHG3psi-mi:“MI:0914”(association)0.480
FOSMYO1Cpsi-mi:“MI:2364”(proximity)0.480
TMOD3CSNK2A1psi-mi:“MI:0217”(phosphorylation reaction)0.440
Tubgcp3psi-mi:“MI:0915”(physical association)0.400
Cbx1FLOT1psi-mi:“MI:0915”(physical association)0.400
Cdk1psi-mi:“MI:0915”(physical association)0.400
Poc1bpsi-mi:“MI:0915”(physical association)0.400
Pafah1b1EDIL3psi-mi:“MI:0915”(physical association)0.400
ErhBCLAF3psi-mi:“MI:0915”(physical association)0.400
Stag2PPP1R12Apsi-mi:“MI:0915”(physical association)0.400

BioGRID (362): TMOD3 (Affinity Capture-MS), TMOD3 (Affinity Capture-MS), TMOD3 (Affinity Capture-MS), ATP6V1B2 (Co-fractionation), MCFD2 (Co-fractionation), PAM16 (Co-fractionation), RUVBL2 (Co-fractionation), SMARCC1 (Co-fractionation), SMARCC2 (Co-fractionation), SNRPD1 (Co-fractionation), TMOD3 (Co-fractionation), TMOD3 (Co-fractionation), TMOD3 (Co-fractionation), TMOD3 (Co-fractionation), TMOD3 (Co-fractionation)

ESM2 similar proteins: A0A1L8G016, A1A5Q0, B3DH20, D3Z8X7, D4A1F2, E1BTG2, F1MF74, F1RA39, O14730, O60308, O88978, O94851, O95801, P51432, P70566, Q1RMR5, Q1RMT7, Q28FY0, Q2YDM7, Q3UHZ5, Q3UM18, Q4KLT3, Q4R3F0, Q4R8L2, Q5BJT6, Q5EA11, Q5ZJD3, Q6AZN0, Q6P5Q4, Q7Z569, Q80V31, Q863A4, Q863A5, Q863A6, Q863A7, Q86X45, Q8BML1, Q8CCP0, Q8R368, Q8R3H9

Diamond homologs: A0A0G2K0D3, A0JNC0, A1A5Q0, E1BTG2, E7F7X0, E9QA62, O01479, P28289, P29536, P49813, P70566, P70567, Q0VAK6, Q0VC48, Q3UHZ5, Q6P5Q4, Q8BVA4, Q9JHJ0, Q9JKK7, Q9JLH8, Q9NYL9, Q9NZQ9, Q9NZR1

SIGNOR signaling

0 interactions.

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 187 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
RHO GTPases activate PAKs628.6×4e-05
Signaling by RAS mutants518.6×2e-03
RHO GTPases activate IQGAPs515.2×3e-03
Sensory processing of sound513.5×3e-03
Signaling by FGFR1 in disease512.8×3e-03
Signaling by RAF1 mutants512.2×4e-03
Signaling by moderate kinase activity BRAF mutants511.1×4e-03
Paradoxical activation of RAF signaling by kinase inactive BRAF511.1×4e-03

GO biological processes:

GO termPartnersFoldFDR
barbed-end actin filament capping631.7×2e-05
actin filament-based movement526.4×5e-04
actin polymerization or depolymerization525.2×5e-04
platelet aggregation511.1×1e-02
actin filament organization129.4×8e-06
cellular response to type II interferon68.2×1e-02
actin cytoskeleton organization115.7×1e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

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

ClassificationCount (floor)
Pathogenic0
Likely pathogenic0
Uncertain significance43
Likely benign0
Benign0

Top pathogenic / likely-pathogenic (0)

SpliceAI

2545 predictions. Top by Δscore:

VariantEffectΔscore
15:51829834:CAGG:Cdonor_loss1.0000
15:51829835:AGG:Adonor_loss1.0000
15:51829837:G:Cdonor_loss1.0000
15:51835055:T:Gdonor_gain1.0000
15:51862806:CATA:Cacceptor_loss1.0000
15:51862808:TAGC:Tacceptor_loss1.0000
15:51862809:A:AGacceptor_gain1.0000
15:51862809:A:Cacceptor_loss1.0000
15:51862810:G:GCacceptor_loss1.0000
15:51862810:G:GGacceptor_gain1.0000
15:51863010:GGTA:Gdonor_loss1.0000
15:51863011:GTA:Gdonor_loss1.0000
15:51863012:T:Adonor_loss1.0000
15:51869372:AGGT:Adonor_loss1.0000
15:51869374:G:GAdonor_loss1.0000
15:51869374:G:GGdonor_gain1.0000
15:51869375:T:Gdonor_loss1.0000
15:51887584:TACA:Tacceptor_loss1.0000
15:51887586:CAGG:Cacceptor_loss1.0000
15:51887587:A:AGacceptor_gain1.0000
15:51887588:G:Aacceptor_loss1.0000
15:51887588:G:GGacceptor_gain1.0000
15:51887711:GG:Gdonor_loss1.0000
15:51887713:T:Gdonor_loss1.0000
15:51887729:T:Gdonor_gain1.0000
15:51889050:TTATA:Tacceptor_loss1.0000
15:51889051:TATA:Tacceptor_loss1.0000
15:51889052:ATAG:Aacceptor_loss1.0000
15:51889053:TA:Tacceptor_loss1.0000
15:51889054:A:ACacceptor_loss1.0000

AlphaMissense

2341 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
15:51900214:C:AN265K0.999
15:51900214:C:GN265K0.999
15:51896506:A:CS239R0.998
15:51896508:C:AS239R0.998
15:51896508:C:GS239R0.998
15:51900213:A:TN265I0.995
15:51869296:T:CL69P0.994
15:51896522:C:AA244D0.994
15:51900209:T:CS264P0.994
15:51901976:T:CF322L0.994
15:51901978:T:AF322L0.994
15:51901978:T:GF322L0.994
15:51900298:G:CQ293H0.993
15:51900298:G:TQ293H0.993
15:51902012:G:CA334P0.993
15:51908778:C:AR343S0.993
15:51869319:G:CA77P0.992
15:51896519:T:AV243D0.992
15:51900212:A:TN265Y0.992
15:51900215:T:CF266L0.992
15:51900217:T:AF266L0.992
15:51900217:T:GF266L0.992
15:51901977:T:CF322S0.992
15:51893932:T:CL205S0.991
15:51893939:T:AN207K0.991
15:51893939:T:GN207K0.991
15:51901995:G:CR328P0.991
15:51862979:T:CL32P0.990
15:51887673:T:CL123S0.990
15:51893936:T:AN206K0.990

dbSNP variants (sampled 300 via entrez): RS1000063084 (15:51862492 A>G), RS1000074884 (15:51832575 T>G), RS1000087447 (15:51909772 A>G), RS1000092852 (15:51892312 A>G), RS1000118425 (15:51877156 A>G), RS1000184533 (15:51880199 A>G), RS1000198182 (15:51861855 C>G,T), RS1000222442 (15:51885341 G>C), RS1000224434 (15:51900986 C>T), RS1000252743 (15:51843423 A>G,T), RS1000290989 (15:51856946 G>A,T), RS1000294377 (15:51849899 A>G), RS1000299360 (15:51901343 A>G), RS1000374896 (15:51850137 T>C), RS1000399712 (15:51856054 G>A)

Disease associations

OMIM: gene MIM:605112 | 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: no

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

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
bisphenol Adecreases expression, decreases methylation, increases expression3
Air Pollutantsaffects expression, increases abundance, decreases expression2
Benzo(a)pyreneaffects methylation, decreases expression2
Phenylmercuric Acetateaffects cotreatment, increases expression2
aristolochic acid Idecreases expression1
FR900359increases phosphorylation1
bisphenol Fincreases expression1
geldanamycinincreases expression1
triphenyl phosphateaffects expression1
pyrogallol 1,3-dimethyl etheraffects cotreatment, decreases expression, affects localization, increases expression1
bufalindecreases expression1
potassium chromate(VI)decreases expression1
cupric oxideincreases expression1
di-n-butylphosphoric acidaffects expression1
perfluorooctane sulfonic aciddecreases expression1
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamideaffects cotreatment, increases expression1
bisphenol Bincreases expression1
dorsomorphinaffects cotreatment, increases expression1
bisphenol Sincreases expression1
bisphenol AFincreases expression1
Acetaminophenincreases expression1
Caffeineaffects phosphorylation1
Dichlorodiphenyl Dichloroethylenedecreases expression1
Doxorubicindecreases expression1
Enzyme Inhibitorsdecreases activity, increases O-linked glycosylation1
Furaldehydeaffects cotreatment, increases expression1
Haloperidoldecreases expression1
Ozoneaffects expression, increases abundance1
Phenobarbitalaffects expression1
Rotenoneincreases expression1

Cellosaurus cell lines

1 cell lines: 1 cancer cell line

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

CellosaurusNameCategorySex
CVCL_B2IVAbcam HeLa TMOD3 KOCancer cell lineFemale

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.