CTNNA1

gene
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Also known as CAP102

Summary

CTNNA1 (catenin alpha 1, HGNC:2509) is a protein-coding gene on chromosome 5q31.2, encoding Catenin alpha-1 (P35221). Associates with the cytoplasmic domain of a variety of cadherins. It is haploinsufficient (ClinGen: sufficient evidence).

This gene encodes a member of the catenin family of proteins that play an important role in cell adhesion process by connecting cadherins located on the plasma membrane to the actin filaments inside the cell. The encoded mechanosensing protein contains three vinculin homology domains and undergoes conformational changes in response to cytoskeletal tension, resulting in the reconfiguration of cadherin-actin filament connections. Certain mutations in this gene cause butterfly-shaped pigment dystrophy.

Source: NCBI Gene 1495 — RefSeq curated summary.

At a glance

  • Gene–disease (curated): CTNNA1-related diffuse gastric and lobular breast cancer syndrome (Definitive, ClinGen) — +3 more curated relationships
  • GWAS associations: 6
  • Clinical variants (ClinVar): 3,635 total — 190 pathogenic, 43 likely-pathogenic
  • Phenotypes (HPO): 8
  • Druggable target: yes
  • Cancer driver (intOGen): activating (oncogene-like) across 2 cancer types
  • Dosage sensitivity (ClinGen): haploinsufficiency sufficient evidence, triplosensitivity no evidence
  • MANE Select transcript: NM_001903

Identifiers

Gene identifiers

FieldValue
HGNC IDHGNC:2509
Approved symbolCTNNA1
Namecatenin alpha 1
Location5q31.2
Locus typegene with protein product
StatusApproved
AliasesCAP102
Ensembl geneENSG00000044115
Ensembl biotypeprotein_coding
OMIM116805
Entrez1495

Gene structure

Transcript identifiers

Ensembl transcripts: 91 — 74 protein_coding, 7 retained_intron, 5 protein_coding_CDS_not_defined, 5 nonsense_mediated_decay

ENST00000302763, ENST00000517533, ENST00000517534, ENST00000517656, ENST00000517904, ENST00000517980, ENST00000518263, ENST00000518381, ENST00000518585, ENST00000518825, ENST00000518910, ENST00000518919, ENST00000519113, ENST00000519116, ENST00000519309, ENST00000519489, ENST00000519634, ENST00000519768, ENST00000520158, ENST00000520260, ENST00000520339, ENST00000520400, ENST00000520520, ENST00000520522, ENST00000520865, ENST00000521368, ENST00000521387, ENST00000521640, ENST00000521683, ENST00000521724, ENST00000521941, ENST00000522013, ENST00000522052, ENST00000522227, ENST00000522730, ENST00000522792, ENST00000523275, ENST00000523298, ENST00000523685, ENST00000523912, ENST00000524127, ENST00000524292, ENST00000540387, ENST00000627109, ENST00000889697, ENST00000889698, ENST00000889699, ENST00000889700, ENST00000889701, ENST00000889702, ENST00000889703, ENST00000889704, ENST00000889705, ENST00000889706, ENST00000889707, ENST00000889708, ENST00000889709, ENST00000889710, ENST00000889711, ENST00000889712, ENST00000889713, ENST00000889714, ENST00000889715, ENST00000889716, ENST00000889717, ENST00000889718, ENST00000930309, ENST00000930310, ENST00000930311, ENST00000930312, ENST00000930313, ENST00000930314, ENST00000965845, ENST00000965846, ENST00000965847, ENST00000965848, ENST00000965849, ENST00000965850, ENST00000965851, ENST00000965852, ENST00000965853, ENST00000965854, ENST00000965855, ENST00000965856, ENST00000965857, ENST00000965858, ENST00000965859, ENST00000965860, ENST00000965861, ENST00000965862, ENST00000965863

RefSeq mRNA: 37 — MANE Select: NM_001903 NM_001290307, NM_001290309, NM_001290310, NM_001290312, NM_001323982, NM_001323983, NM_001323984, NM_001323985, NM_001323986, NM_001323987, NM_001323988, NM_001323989, NM_001323990, NM_001323991, NM_001323992, NM_001323993, NM_001323994, NM_001323995, NM_001323996, NM_001323997, NM_001323998, NM_001323999, NM_001324000, NM_001324001, NM_001324002, NM_001324003, NM_001324004, NM_001324005, NM_001324006, NM_001324007, NM_001324008, NM_001324009, NM_001324010, NM_001324011, NM_001324012, NM_001324013, NM_001903

CCDS: CCDS34243, CCDS75315, CCDS78064

Canonical transcript exons

ENST00000302763 — 18 exons

ExonStartEnd
ENSE00002108433138753425138753510
ENSE00002108708138933802138935034
ENSE00003475022138887490138887642
ENSE00003480945138781923138782029
ENSE00003515286138930473138930654
ENSE00003527073138886212138886292
ENSE00003572213138812183138812302
ENSE00003576257138917742138917898
ENSE00003596703138925256138925407
ENSE00003600527138783177138783372
ENSE00003601387138932578138932712
ENSE00003613458138904349138904441
ENSE00003614555138827515138827718
ENSE00003615885138929246138929356
ENSE00003620126138930830138930935
ENSE00003648114138924510138924710
ENSE00003666705138824530138824799
ENSE00003784019138810038138810204

Expression profiles

Bgee: expression breadth ubiquitous, 305 present calls, max score 99.38.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 143.4330 / max 1817.1032, expressed in 1815 samples.

FANTOM5 promoters (5 alternative TSS)

Promoter IDTPM avgSamples expressed
58801125.68281815
5880215.64241681
588052.0566150
588030.02988
588040.02145

Top tissues by expression

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

TissueAnatomy IDExpression scoreQuality
colonic epitheliumUBERON:000039799.38gold quality
calcaneal tendonUBERON:000370199.34gold quality
amniotic fluidUBERON:000017399.17gold quality
nasal cavity epitheliumUBERON:000538499.13gold quality
peripheral nervous systemUBERON:000001099.11gold quality
nerveUBERON:000102199.11gold quality
tibial nerveUBERON:000132399.11gold quality
corpus callosumUBERON:000233699.11gold quality
middle frontal gyrusUBERON:000270299.09gold quality
pharyngeal mucosaUBERON:000035599.06gold quality
bronchial epithelial cellCL:000232899.02gold quality
lower esophagus mucosaUBERON:003583499.00gold quality
adrenal tissueUBERON:001830398.99gold quality
ventricular zoneUBERON:000305398.98gold quality
epithelium of bronchusUBERON:000203198.97gold quality
bronchusUBERON:000218598.97gold quality
tendonUBERON:000004398.96gold quality
epithelium of nasopharynxUBERON:000195198.95gold quality
oral cavityUBERON:000016798.94gold quality
esophagus mucosaUBERON:000246998.94gold quality
nasopharynxUBERON:000172898.93gold quality
sural nerveUBERON:001548898.90gold quality
esophagusUBERON:000104398.85gold quality
nasal cavity mucosaUBERON:000182698.84gold quality
upper lobe of left lungUBERON:000895298.84gold quality
right lungUBERON:000216798.83gold quality
popliteal arteryUBERON:000225098.81gold quality
tibial arteryUBERON:000761098.81gold quality
upper lobe of lungUBERON:000894898.81gold quality
islet of LangerhansUBERON:000000698.79gold quality

Single-cell (SCXA)

Detected in 4 experiment(s), a significant marker in 3.

ExperimentMarker?Max mean expression
E-HCAD-11yes22.64
E-MTAB-5061yes6.23
E-MTAB-6058no517.23
E-ANND-3no0.00

Regulation

Is transcription factor: no

Upstream regulators (CollecTRI, top): CEBPA, EGR1, RCOR2

miRNA regulators (miRDB)

73 targeting CTNNA1, 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-9-5P100.0072.282361
HSA-MIR-450A-1-3P100.0069.331837
HSA-MIR-4262100.0073.263931
HSA-MIR-428299.9975.366408
HSA-MIR-181A-5P99.9972.962995
HSA-MIR-181B-5P99.9972.972996
HSA-MIR-181C-5P99.9972.952996
HSA-MIR-181D-5P99.9973.042997
HSA-MIR-433-3P99.9869.371203
HSA-MIR-569699.9872.364487
HSA-MIR-314899.9775.066478
HSA-MIR-141-3P99.9472.792421
HSA-MIR-200A-3P99.9472.682420
HSA-MIR-4760-3P99.9370.502385
HSA-MIR-4753-3P99.9071.033786
HSA-MIR-548E-5P99.8972.734486
HSA-MIR-612499.8769.783551
HSA-MIR-579-3P99.8671.663628
HSA-MIR-450399.8571.451869
HSA-MIR-664B-3P99.8471.653590
HSA-MIR-430799.8270.453374
HSA-MIR-6739-5P99.8067.872806
HSA-MIR-139-5P99.8069.501399
HSA-MIR-4668-5P99.7970.583782
HSA-MIR-548AG99.7769.251492
HSA-MIR-6733-5P99.7467.942759
HSA-MIR-471999.7372.103329
HSA-MIR-548AI99.6969.241494
HSA-MIR-548BA99.6969.141514
HSA-MIR-570-5P99.6969.241494

Functional genomics

ClinGen dosage: haploinsufficiency 3 (sufficient evidence), triplosensitivity 0 (no evidence). ClinGen Gene Dosage Map

Literature-anchored findings (GeneRIF, showing 40)

  • Abnormal E-cadherin and alpha-catenin and beta-catenin in pancreatic carcinoma tissues. Abnormal E-cadherin and alpha-catenin with differentiation, lymph node and liver metastases. Aberrant beta-catenin with lymph node and liver metastases. (PMID:12532469)
  • Pancreatic cancer likely occurs in case of the inactivation of E-cadherin and alpha-catenin genes and abnormal expression of proteins (PMID:14599963)
  • alpha-catenin has a role in cell growth control in three-dimensional culture (PMID:14755240)
  • Allelic imbalance occurs at two distinct regions of which one includes the CTNNA1 gene in ovarian cancer. (PMID:15297182)
  • Our results suggest that alpha-catenin links CCR5 and CXCR4 to the cytoskeleton and is involved in the organization of these receptors at the membrane, thereby possibly affecting HIV-1 infection. (PMID:15541354)
  • ubiquitin-independent degradation of alpha-catenin regulates beta-catenin signaling and maintenance of the differentiated phenotype of articular chondrocytes (PMID:15695815)
  • Loss of expression in squamous cell carcinoma of the floor of the mouth correlated significantly with poor prognosis (PMID:15916880)
  • Downregulation of alpha-catenin expression is common in gastric carcinoma (PMID:15948257)
  • These results indicate that the interaction of alpha-catenin and actin functions in the assembly of desmosomes in epithelial cells. (PMID:16273278)
  • Cdc42 regulates AJ permeability by controlling the binding of alpha-catenin with beta-catenin and the consequent interaction of the VE-cadherin/catenin complex with the actin cytoskeleton. (PMID:16322481)
  • Direct attachment of alpha-catenin to F-actin is required to promote cadherin-mediated contact formation and strong cell-cell adhesive states. (PMID:16798615)
  • The expression of alpha-catenin was significantly lower in the invasive group than in the non-invasive group of pituitary adenoma. (PMID:16927799)
  • we explored the implication of three proteins (E-cadherin, a- and b-catenins) that form the cadherin-catenin complex, a receptorial structure strictly involved in tumoral vascular invasion and embolization in this biologic event (PMID:17576040)
  • The previously reported characteristics of this mutation, E-cadherin (V832M) do not apply to human epithelial cells expressing this mutant protein. (PMID:17668349)
  • prognostic and chemosensitivity marker for invasive bladder cancer (PMID:17760743)
  • removal of N-glycans on E-cadherin resulted in elevated tyrosine phosphorylation level of beta-catenin and reduced beta- and alpha-catenins at adherens junctions (PMID:17979184)
  • These results suggest induction of SRF-mediated transcription by alpha(E)-catenin either downstream of RhoA or via a parallel pathway. (PMID:18078809)
  • Rsults suggest that the lower epithelial alpha-catenin, E-cadherin and (or) ZO-1 expression in patients with atopic asthma contributes to a defective airway epithelial barrier and a higher influx of eosinophils in the epithelium. (PMID:18418437)
  • This study reveals for the first time that alpha-catenin is a key regulator of beta-catenin transcriptional activity and that the status of alpha-catenin expression in tumor tissues might have prognostic value for Src targeted therapy (PMID:18566211)
  • The mean values of the percentage of positive cells for the tested proteins between E-AD vs. AD did not demonstrate any statistically significant difference except for alpha-catenin. (PMID:19124205)
  • loss of alpha-catenin alone drastically reduces the adhesive force between individual cadherin pairs on adjoining cells, explain the global loss of cell adhesion in human breast cancer cells (PMID:19458087)
  • increased E-cadherin and alpha-catenin expression and reduced Wnt signaling might be involved in the mechanisms of tumor suppressor function of BCSC-1. (PMID:19656157)
  • This study identifies the E-cadherin/catenin complex as a discriminative, partly polyamine-regulated feature of IL-4/IL-13-exposed alternatively activated macrophages (PMID:19726720)
  • Loss of alpha-catenin resulted in increased in vitro tumorigenic characteristics (increased soft agarose colony formation, clonogenic survival after suspension, and survival in suspension). (PMID:19745064)
  • 4 biallelic inactivating alpha-catenin mutations were found among 55 human breast cancer cell lines. All caused premature termination. Loss of alpha-catenin protein expression was associated with the lobular subtype in primary breast cancers. (PMID:19763817)
  • an interaction of CAR and alpha-catenin mediates the impact of CAR on cell proliferation, migration, invasion, and morphology. (PMID:19773761)
  • Methylation and inactivation of CTNNA1 is associated with advanced myeloid malignancies. (PMID:19826047)
  • results show that the association of alpha-catenin with the cadherin-catenin complex is required for efficient leukocyte transendothelial migration (PMID:19918298)
  • The EGFR-ERK-CK2-mediated phosphorylation of alpha-catenin promotes beta-catenin transactivation and tumor cell invasion. (PMID:19941816)
  • Data show that actin bundle formation and subsequent linkage between actin bundles and VE-cadherin through alpha- and beta-catenins are important for the stabilization of VE-cadherin at the cell-cell contacts in cAMP-Epac-Rap1 signal-activated cells. (PMID:20032304)
  • An evolutionarily conserved PTEN-C/EBPalpha-CTNNA1 axis controls myeloid development and transformation. (PMID:20371743)
  • The E-cadherin-catenin complex is the factor indicative of metastasis and disease progression in gastric cancer. (PMID:20529814)
  • The study objective was to assess changes in the expressions of E-cadherin and alpha-, beta- and gamma-catenin proteins in pancreatic duct carcinoma in correlation with clinicopathological parameters, lymph node involvement and distant metastases. (PMID:20529828)
  • Data show that E-cadherin and alpha-catenin were predominantly expressed in the cell membranes, whereas beta- and gamma-catenin were found both in the cell membrane and cytoplasm. (PMID:20933443)
  • These results suggest that JNK affects the association of alpha-catenin with the adherens junction complex and regulates adherens junctions. (PMID:21030692)
  • study presents evidence that in the cadherin-catenin complex alpha-catenin contributes to the binding strength of another catenin, p120, to the same complex; data suggest alpha-catenin-p120 contact within the cadherin-catenin complex can regulate cadherin trafficking (PMID:21937720)
  • Report loss of CTNNA1 as lobular carcinoma in situ of the breast progresses to more invasive lesions. (PMID:22080244)
  • Data demonstrate that the expression of alpha-E-catenin is increased by Sec6 siRNAs, and E-cadherin and beta-catenin localize mainly at the cell-cell contact region in HSC3 cells, which were transfected with Sec6 siRNA. (PMID:22381337)
  • A discrete trimeric complex of beta-catenin, alpha-catenin and the tumor suppressor APC, forms in the cytoplasm in response to Wnt signaling. (PMID:22469663)
  • binding studies suggest that vinculin must be in an activated state to bind to alpha-catenin and that this interaction is stabilized by the formation of a ternary alpha-catenin-vinculin-F-actin complex, which can be formed via the F-actin binding domain (PMID:22493458)

Cross-species orthologs

5 orthologs

OrganismSymbolGene ID
danio_rerioctnna1ENSDARG00000102441
mus_musculusCtnna1ENSMUSG00000037815
rattus_norvegicusCtnna1ENSRNOG00000005796
drosophila_melanogasteralpha-CatFBGN0010215
caenorhabditis_elegansWBGENE00001978

Paralogs (4): VCL (ENSG00000035403), CTNNA2 (ENSG00000066032), CTNNAL1 (ENSG00000119326), CTNNA3 (ENSG00000183230)

Protein

Protein identifiers

Catenin alpha-1P35221 (reviewed: P35221)

Alternative names: Alpha E-catenin, Cadherin-associated protein, Renal carcinoma antigen NY-REN-13

All UniProt accessions (30): A0A087WZL6, A0A384MDY0, P35221, E5RFG3, E5RFK9, E5RFM3, E5RFM5, E5RG03, E5RGD2, E5RGG4, E5RGS1, E5RGU3, E5RGY6, E5RGY7, E5RHJ5, E5RHR7, E5RHV7, E5RHY5, E5RIB1, E5RIE0, E5RIT8, E5RJ41, E5RJ43, E5RJC9, E5RJL0, E5RJP7, E5RJZ2, G3XAM7, H0YB54, H0YBB8

UniProt curated annotations — full annotation on UniProt →

Function. Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation. May play a crucial role in cell differentiation.

Subunit / interactions. Monomer and homodimer; the monomer preferentially binds to CTNNB1 and the homodimer to actin. Component of an cadherin:catenin adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1, alpha-catenin/CTNNA1 and p120 catenin/CTNND1. Possible component of an E-cadherin/ catenin adhesion complex together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-catenin/JUP; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Binds AFDN and F-actin. Interacts with ARHGAP21. Interacts with AJUBA. Interacts with LIMA1. Interacts with vinculin/VCL. Interacts with TJP2/ZO2 (via N-terminus). Interacts with TJP1/ZO1 (via N-terminus).

Subcellular location. Cytoplasm. Cytoskeleton. Cell junction. Adherens junction. Cell membrane. Nucleus Cell membrane.

Tissue specificity. Ubiquitously expressed in normal tissues. Abundantly expressed in brain and cerebellum, also expressed in the placenta, liver, lung, colon, heart, pancreas, stomach and thymus.

Post-translational modifications. Sumoylated. Phosphorylation seems to contribute to the strength of cell-cell adhesion rather than to the basic capacity for cell-cell adhesion.

Disease relevance. Germline CTNNA1 truncating mutations have been detected in patients with hereditary diffuse gastric cancer (HDGC) and may play a role in disease susceptibility. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. Macular dystrophy, patterned, 2 (MDPT2) [MIM:608970] A form of retinal patterned dystrophy, a heterogeneous group of macular disorders caused by abnormal accumulation of lipofuscin in the retinal pigment epithelium. Lipofuscin distribution can show various shapes that define different types of macular dystrophy, including reticular (fishnet-like) dystrophy, macroreticular (spider-shaped) dystrophy and butterfly-shaped pigment dystrophy. MDPT2 is an autosomal dominant form characterized by bilateral accumulation of pigment in the macular area that resembles the wings of a butterfly. The disease is caused by variants affecting the gene represented in this entry.

Miscellaneous. Expressed at high levels in the nervous system. Lacks the beta-catenin interaction domain.

Similarity. Belongs to the vinculin/alpha-catenin family.

Isoforms (3)

UniProt IDNamesCanonical?
P35221-11, CTNNA1ayes
P35221-22
P35221-33, CTNNA1b

RefSeq proteins (37): NP_001277236, NP_001277238, NP_001277239, NP_001277241, NP_001310911, NP_001310912, NP_001310913, NP_001310914, NP_001310915, NP_001310916, NP_001310917, NP_001310918, NP_001310919, NP_001310920, NP_001310921, NP_001310922, NP_001310923, NP_001310924, NP_001310925, NP_001310926, NP_001310927, NP_001310928, NP_001310929, NP_001310930, NP_001310931, NP_001310932, NP_001310933, NP_001310934, NP_001310935, NP_001310936, NP_001310937, NP_001310938, NP_001310939, NP_001310940, NP_001310941, NP_001310942, NP_001894* (*=MANE)

Domains & families (InterPro)

IDNameType
IPR000633Vinculin_CSConserved_site
IPR001033Alpha_cateninFamily
IPR006077Vinculin/cateninFamily
IPR036723Alpha-catenin/vinculin-like_sfHomologous_superfamily

Pfam: PF01044

UniProt features (78 total): helix 22, sequence conflict 14, modified residue 12, sequence variant 6, turn 5, region of interest 4, mutagenesis site 4, strand 3, cross-link 2, splice variant 2, compositionally biased region 2, initiator methionine 1, chain 1

Structure

Experimental structures (PDB)

10 structures.

PDBMethodResolution (Å)
6V2OX-RAY DIFFRACTION1.27
6V2PX-RAY DIFFRACTION1.3
9BL4X-RAY DIFFRACTION1.75
9BL3X-RAY DIFFRACTION2
9BL2X-RAY DIFFRACTION2.1
1H6GX-RAY DIFFRACTION2.2
4EHPX-RAY DIFFRACTION2.66
7UTJELECTRON MICROSCOPY2.77
6UPVELECTRON MICROSCOPY3.2
4IGGX-RAY DIFFRACTION3.66

Predicted structure (AlphaFold)

ModelpLDDTFraction very-high
AF-P35221-F183.010.55

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 (14): 268, 295, 297, 634, 641, 645, 652, 655, 658, 851, 57, 797, 2, 264

Mutagenesis-validated functional residues (4):

PositionPhenotype
641abolishes phosphorylation by ck2. no effect on phosphorylation by ck1.
641enhances phosphorylation by ck1.
652–658abolishes phosphorylation by ck1. no effect on phosphorylation by ck2.
652abolishes phosphorylation by ck1.

Function

Pathways and Gene Ontology

Reactome pathways

11 pathways

IDPathway
R-HSA-418990Adherens junctions interactions
R-HSA-5218920VEGFR2 mediated vascular permeability
R-HSA-525793Myogenesis
R-HSA-5626467RHO GTPases activate IQGAPs
R-HSA-9762292Regulation of CDH11 function
R-HSA-9764302Regulation of CDH19 Expression and Function
R-HSA-9764561Regulation of CDH1 Function
R-HSA-9766229Degradation of CDH1
R-HSA-9833576CDH11 homotypic and heterotypic interactions
R-HSA-9958810SRC activates STAT3 in a quantitative manner, through Cadherin-11 (CDH11), RAC1 and gp130 (IL6ST)
R-HSA-9958825Activation of STAT3 by cadherin engagement

MSigDB gene sets: 476 (showing top): GOBP_RESPONSE_TO_NITROGEN_COMPOUND, GOBP_NEGATIVE_REGULATION_OF_CELL_DEVELOPMENT, WANG_CLIM2_TARGETS_UP, GOBP_ESTABLISHMENT_OR_MAINTENANCE_OF_CELL_POLARITY, KAAB_FAILED_HEART_ATRIUM_DN, BASSO_B_LYMPHOCYTE_NETWORK, GOCC_SECRETORY_GRANULE, GOBP_APICAL_JUNCTION_ASSEMBLY, GOBP_REGENERATION, GOBP_EXTRINSIC_APOPTOTIC_SIGNALING_PATHWAY, MITSIADES_RESPONSE_TO_APLIDIN_DN, WEIGEL_OXIDATIVE_STRESS_BY_TBH_AND_H2O2, GOBP_NEUROGENESIS, KEGG_TIGHT_JUNCTION, GOBP_RESPONSE_TO_AXON_INJURY

GO Biological Process (29): ovarian follicle development (GO:0001541), cell adhesion (GO:0007155), establishment or maintenance of cell polarity (GO:0007163), smoothened signaling pathway (GO:0007224), integrin-mediated signaling pathway (GO:0007229), neuroblast proliferation (GO:0007405), negative regulation of neuroblast proliferation (GO:0007406), intracellular protein localization (GO:0008104), male gonad development (GO:0008584), gap junction assembly (GO:0016264), cell migration (GO:0016477), axon regeneration (GO:0031103), odontogenesis of dentin-containing tooth (GO:0042475), apical junction assembly (GO:0043297), response to estrogen (GO:0043627), positive regulation of smoothened signaling pathway (GO:0045880), cellular response to indole-3-methanol (GO:0071681), epithelial cell-cell adhesion (GO:0090136), extrinsic apoptotic signaling pathway in absence of ligand (GO:0097192), cell-cell adhesion (GO:0098609), negative regulation of protein localization to nucleus (GO:1900181), negative regulation of cell motility (GO:2000146), negative regulation of integrin-mediated signaling pathway (GO:2001045), negative regulation of extrinsic apoptotic signaling pathway in absence of ligand (GO:2001240), positive regulation of extrinsic apoptotic signaling pathway in absence of ligand (GO:2001241), apoptotic process (GO:0006915), regulation of cell population proliferation (GO:0042127), negative regulation of apoptotic process (GO:0043066), cell motility (GO:0048870)

GO Molecular Function (11): RNA binding (GO:0003723), structural molecule activity (GO:0005198), beta-catenin binding (GO:0008013), vinculin binding (GO:0017166), identical protein binding (GO:0042802), gamma-catenin binding (GO:0045295), cadherin binding (GO:0045296), actin filament binding (GO:0051015), protein binding (GO:0005515), cytoskeletal protein binding (GO:0008092), protein-containing complex binding (GO:0044877)

GO Cellular Component (23): acrosomal vesicle (GO:0001669), nucleus (GO:0005634), Golgi apparatus (GO:0005794), cytosol (GO:0005829), plasma membrane (GO:0005886), cell-cell junction (GO:0005911), adherens junction (GO:0005912), zonula adherens (GO:0005915), focal adhesion (GO:0005925), intercalated disc (GO:0014704), actin cytoskeleton (GO:0015629), catenin complex (GO:0016342), flotillin complex (GO:0016600), lamellipodium (GO:0030027), cell junction (GO:0030054), sperm midpiece (GO:0097225), sperm principal piece (GO:0097228), sperm head-tail coupling apparatus (GO:0120212), cytoplasm (GO:0005737), cytoskeleton (GO:0005856), membrane (GO:0016020), anchoring junction (GO:0070161), plasma membrane protein complex (GO:0098797)

Reactome top-level categories

Rollup of top-11 pathways:

CategoryPathways
Cell-cell junction organization1
VEGFA-VEGFR2 Pathway1
Developmental Biology1
RHO GTPase Effectors1
Regulation of CDH11 Expression and Function1
Regulation of Expression and Function of Type II Classical Cadherins1
Regulation of CDH1 Expression and Function1
Regulation of CDH1 Function1
Regulation of CDH11 function1
Activation of STAT3 by cadherin engagement1
Adherens junctions interactions1

GO top-level categories

Rollup of top GO terms by namespace:

CategoryTerms
cellular anatomical structure6
protein binding4
cellular process2
cell surface receptor signaling pathway2
cell-cell junction assembly2
binding2
intracellular membrane-bounded organelle2
cytoplasm2
plasma membrane protein complex2
sperm flagellum2
female gonad development1
anatomical structure development1
generation of neurons1
neural precursor cell proliferation1
neuroblast proliferation1
negative regulation of neurogenesis1
regulation of neuroblast proliferation1
negative regulation of neural precursor cell proliferation1
macromolecule localization1
gonad development1
development of primary male sexual characteristics1
cell motility1
neuron projection regeneration1
response to axon injury1
axon development1
odontogenesis1
response to hormone1
smoothened signaling pathway1
regulation of smoothened signaling pathway1
positive regulation of signal transduction1
response to indole-3-methanol1
cellular response to alcohol1
cellular response to nitrogen compound1
cell-cell adhesion1
signal transduction in absence of ligand1
extrinsic apoptotic signaling pathway1
cell adhesion1
nucleic acid binding1
molecular_function1
cytoskeletal protein binding1

Protein interactions and networks

STRING

2252 interactions, top by confidence (×1000):

Protein AProtein BPartner UniProtScore
CTNNA1CTNNB1P35222997
CTNNA1CDH1P12830979
CTNNA1CDH17Q12864964
CTNNA1CTNND1O60716964
CTNNA1CDH2P19022801
CTNNA1TJP1Q07157761
CTNNA1LRRTM2O43300730
CTNNA1CDH6P55285720
CTNNA1IQGAP1P46940702
CTNNA1CDH15P55291695
CTNNA1LRATD2Q96KN1693
CTNNA1CDH3P22223692
CTNNA1AFDNP55196691
CTNNA1LIMA1Q9UHB6669
CTNNA1CTNND2Q9UQB3657

IntAct

364 interactions, top by confidence:

ABTypeScore
CTNNB1CTNNA1psi-mi:“MI:0915”(physical association)0.890
CDH1CTNNA1psi-mi:“MI:0914”(association)0.800
CDH1CTNNA1psi-mi:“MI:0915”(physical association)0.800
CTNNA1CDH1psi-mi:“MI:0914”(association)0.800
CTNNBIP1APCpsi-mi:“MI:0914”(association)0.740
CDH1CTNND1psi-mi:“MI:0914”(association)0.730
EGFRCTNNA1psi-mi:“MI:2364”(proximity)0.730
CTNNA1EGFRpsi-mi:“MI:2364”(proximity)0.730
CFTRESYT2psi-mi:“MI:2364”(proximity)0.710
CFTRESYT2psi-mi:“MI:0914”(association)0.710
VCPUBXN8psi-mi:“MI:0914”(association)0.690
TAX1BP3ARVCFpsi-mi:“MI:0914”(association)0.690
CTNNA1JUPpsi-mi:“MI:2364”(proximity)0.640
CTNNA1APCpsi-mi:“MI:2364”(proximity)0.640
CTNNA1CTNNA1psi-mi:“MI:0407”(direct interaction)0.620
CTNNB1JUPpsi-mi:“MI:0914”(association)0.610
CTNNA1NFKBIApsi-mi:“MI:0915”(physical association)0.580

BioGRID (512): CTNNA1 (Affinity Capture-MS), CTNNA1 (Affinity Capture-MS), CTNNA1 (Affinity Capture-MS), CTNNA1 (Biochemical Activity), CTNNA1 (Affinity Capture-MS), CTNNA1 (Affinity Capture-MS), CTNNA1 (Affinity Capture-MS), CTNNA1 (Affinity Capture-MS), CTNNA1 (Affinity Capture-RNA), CTNNB1 (Co-fractionation), DMD (Co-fractionation), JUP (Co-fractionation), CTNNA1 (Affinity Capture-MS), CTNNA1 (Reconstituted Complex), CTNNA1 (Proximity Label-MS)

ESM2 similar proteins: A0A3B6UES5, A0A3G2LGI8, D3ZHV2, G8JYB2, O46037, O60437, P0CE94, P0CE95, P11533, P12003, P18206, P19826, P26039, P26231, P26234, P30427, P33338, P35220, P35221, P54939, P85972, P90947, Q02328, Q03001, Q04615, Q15149, Q17162, Q3MHM6, Q54K81, Q54MH2, Q59I72, Q64727, Q6ZWR6, Q71LX4, Q8MSU4, Q91ZU6, Q95XZ0, Q9ERE8, Q9H1K6, Q9MBF8

Diamond homologs: A4IGI7, B7ZC77, P26231, P26232, P30997, P35220, P35221, P90947, Q04615, Q3MHM6, Q59I72, Q5R416, Q61301, Q65CL1, Q6GLP0, Q9PVF8, Q9UI47, O88327, Q5RC06, Q9UBT7, A0A3B6UES5, O46037, P12003, P18206, P19826, P26234, P85972, Q17162, Q54MH2, Q64727

SIGNOR signaling

5 interactions.

AEffectBMechanism
PTPN11down-regulatesCTNNA1dephosphorylation
CSNK2A1down-regulatesCTNNA1phosphorylation
CTNNA1down-regulatesYAP1binding
CDH1up-regulatesCTNNA1binding
CDH11unknownCTNNA1binding

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 171 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
Adherens junctions interactions917.9×1e-06
Signaling by high-kinase activity BRAF mutants717.8×3e-05
MAP2K and MAPK activation716.0×5e-05
Signaling by RAF1 mutants715.6×5e-05
Signaling by moderate kinase activity BRAF mutants714.2×5e-05
Paradoxical activation of RAF signaling by kinase inactive BRAF714.2×5e-05
Signaling downstream of RAS mutants714.2×5e-05
RHO GTPases activate IQGAPs513.8×1e-03

GO biological processes:

GO termPartnersFoldFDR
adherens junction organization724.1×6e-06
cell-cell adhesion mediated by cadherin822.2×2e-06
calcium-dependent cell-cell adhesion516.3×2e-03
cell-cell junction assembly515.0×3e-03
regulation of neuron projection development514.6×3e-03
cell morphogenesis1010.6×1e-05
canonical Wnt signaling pathway1010.3×1e-05
MAPK cascade99.3×1e-04

Disease & clinical

Cancer significance

From intOGen — cancer-driver classification: activating (oncogene-like) across 2 cancer types — CEAD, COADREAD.

Clinical variants and AI predictions

ClinVar

3635 variants total. Per-class counts are floors (≥ shown; pagination cap):

ClassificationCount (floor)
Pathogenic190
Likely pathogenic43
Uncertain significance1738
Likely benign1065
Benign80

Top pathogenic / likely-pathogenic (30)

Variant IDHGVSClassification
1000045NM_001903.5(CTNNA1):c.2181_2184del (p.Asp728fs)Pathogenic
1000847NM_001903.5(CTNNA1):c.100dup (p.Thr34fs)Pathogenic
1011394NM_001903.5(CTNNA1):c.919del (p.Glu307fs)Pathogenic
1013834NM_001903.5(CTNNA1):c.1548del (p.Asn517fs)Pathogenic
1020564NM_001903.5(CTNNA1):c.648del (p.Asn217fs)Pathogenic
1021478NM_001903.5(CTNNA1):c.511C>T (p.Gln171Ter)Pathogenic
1022142NM_001903.5(CTNNA1):c.1033C>T (p.Gln345Ter)Pathogenic
1025313NM_001903.5(CTNNA1):c.229del (p.Asp77fs)Pathogenic
1035877NM_001903.5(CTNNA1):c.737dup (p.Gln247fs)Pathogenic
1038840NM_001903.5(CTNNA1):c.1969C>T (p.Gln657Ter)Pathogenic
1042674NM_001903.5(CTNNA1):c.1479del (p.Lys493fs)Pathogenic
1046228NM_001903.5(CTNNA1):c.1544C>G (p.Ser515Ter)Pathogenic
1051089NM_001903.5(CTNNA1):c.292C>T (p.Arg98Ter)Pathogenic
1059771NM_001903.5(CTNNA1):c.616C>T (p.Gln206Ter)Pathogenic
1064101NC_000005.9:g.(?138253421)(138253597_?)delPathogenic
1352946NM_001903.5(CTNNA1):c.199C>T (p.Gln67Ter)Pathogenic
1356510NM_001903.5(CTNNA1):c.479dup (p.Ile161fs)Pathogenic
1366961NM_001903.5(CTNNA1):c.2320C>T (p.Gln774Ter)Pathogenic
1373875NM_001903.5(CTNNA1):c.313A>T (p.Lys105Ter)Pathogenic
1393445NM_001903.5(CTNNA1):c.1461dup (p.Lys488Ter)Pathogenic
1405949NM_001903.5(CTNNA1):c.1441del (p.Gln481fs)Pathogenic
1416783NM_001903.5(CTNNA1):c.86del (p.Leu29fs)Pathogenic
1425345NM_001903.5(CTNNA1):c.68dup (p.Ala24fs)Pathogenic
1429789NM_001903.5(CTNNA1):c.1387C>T (p.Gln463Ter)Pathogenic
1435131NM_001903.5(CTNNA1):c.1117A>T (p.Lys373Ter)Pathogenic
1441992NC_000005.9:g.(?138117614)(138119071_?)delPathogenic
1469682NM_001903.5(CTNNA1):c.2186_2187del (p.Phe729fs)Pathogenic
1472837NM_001903.5(CTNNA1):c.151_152del (p.Lys51fs)Pathogenic
1475146NM_001903.5(CTNNA1):c.531T>G (p.Tyr177Ter)Pathogenic
1479337NM_001903.5(CTNNA1):c.1674dup (p.Glu559fs)Pathogenic

SpliceAI

3969 predictions. Top by Δscore:

VariantEffectΔscore
5:138781921:A:AGacceptor_gain1.0000
5:138781922:G:GAacceptor_gain1.0000
5:138781922:GA:Gacceptor_gain1.0000
5:138781922:GAA:Gacceptor_gain1.0000
5:138781922:GAAA:Gacceptor_gain1.0000
5:138781922:GAAAT:Gacceptor_gain1.0000
5:138782027:CAG:Cdonor_gain1.0000
5:138782027:CAGGT:Cdonor_loss1.0000
5:138782030:G:GAdonor_loss1.0000
5:138782030:G:GGdonor_gain1.0000
5:138782031:T:Adonor_loss1.0000
5:138783371:AG:Adonor_gain1.0000
5:138783372:GG:Gdonor_gain1.0000
5:138783373:G:GAdonor_loss1.0000
5:138783373:G:GGdonor_gain1.0000
5:138810031:A:AGacceptor_gain1.0000
5:138810033:A:AGacceptor_gain1.0000
5:138810036:A:AGacceptor_gain1.0000
5:138810036:A:Gacceptor_loss1.0000
5:138810036:AG:Aacceptor_gain1.0000
5:138810036:AGGT:Aacceptor_gain1.0000
5:138810037:G:GTacceptor_gain1.0000
5:138810037:GG:Gacceptor_gain1.0000
5:138810037:GGT:Gacceptor_gain1.0000
5:138810037:GGTG:Gacceptor_gain1.0000
5:138810037:GGTGA:Gacceptor_gain1.0000
5:138810200:AAGTT:Adonor_gain1.0000
5:138810202:GTT:Gdonor_gain1.0000
5:138810203:TT:Tdonor_gain1.0000
5:138810205:G:GGdonor_gain1.0000

AlphaMissense

5999 scored. Top likely-pathogenic:

VariantProtein changeam_pathogenicity
5:138781961:T:AW13R1.000
5:138781961:T:CW13R1.000
5:138781983:T:CI20T1.000
5:138781983:T:GI20S1.000
5:138781989:C:TT22I1.000
5:138781998:T:AV25D1.000
5:138782007:T:CL28P1.000
5:138782010:T:CL29S1.000
5:138782010:T:GL29W1.000
5:138782019:T:AL32H1.000
5:138782019:T:CL32P1.000
5:138782022:T:AV33D1.000
5:138783187:T:AL39H1.000
5:138783187:T:CL39P1.000
5:138783265:T:AV65D1.000
5:138783273:G:CA68P1.000
5:138783286:T:CF72S1.000
5:138783297:G:AG76R1.000
5:138783297:G:CG76R1.000
5:138783297:G:TG76W1.000
5:138783298:G:AG76E1.000
5:138810067:T:CF111L1.000
5:138810068:T:CF111S1.000
5:138810068:T:GF111C1.000
5:138810069:C:AF111L1.000
5:138810069:C:GF111L1.000
5:138810118:G:CA128P1.000
5:138810119:C:AA128D1.000
5:138810131:T:AL132H1.000
5:138810131:T:CL132P1.000

dbSNP variants (sampled 300 via entrez): RS1000014476 (5:138814764 T>G), RS1000048609 (5:138814401 G>A), RS1000081336 (5:138852019 G>A), RS1000132696 (5:138870732 A>G), RS1000138614 (5:138802277 C>T), RS1000140136 (5:138873394 A>G), RS1000171708 (5:138779593 C>T), RS1000175958 (5:138900243 G>A,T), RS1000185378 (5:138871019 G>A,C), RS1000197839 (5:138865419 C>T), RS1000241753 (5:138752555 G>C), RS1000281973 (5:138758131 C>A,T), RS1000287975 (5:138769986 A>T), RS1000292215 (5:138825951 T>C), RS1000295856 (5:138928144 C>G,T)

Disease associations

OMIM: gene MIM:116805 | disease phenotypes: MIM:608970, MIM:601228, MIM:120435, MIM:123100, MIM:114500, MIM:181500, MIM:135700

GenCC curated gene-disease

DiseaseClassificationInheritance
patterned macular dystrophy 2DefinitiveAutosomal dominant
CTNNA1-related diffuse gastric and lobular breast cancer syndromeDefinitiveAutosomal dominant
patterned macular dystrophySupportiveAutosomal dominant
hereditary nonpolyposis colon cancerNo Known Disease RelationshipUnknown

ClinGen Gene-Disease Validity (2)

Expert-panel classifications — Definitive > Strong > Moderate > Limited > Disputed > Refuted.

DiseaseClassificationInheritance
CTNNA1-related diffuse gastric and lobular breast cancer syndromeDefinitiveAD
hereditary nonpolyposis colon cancerNo Known Disease RelationshipAD

Mondo (13): hereditary neoplastic syndrome (MONDO:0015356), patterned macular dystrophy 2 (MONDO:0012162), hereditary diffuse gastric adenocarcinoma (MONDO:0007648), inherited retinal dystrophy (MONDO:0019118), polyposis syndrome, hereditary mixed, 1 (MONDO:0042486), hereditary nonpolyposis colon cancer (MONDO:0018630), craniosynostosis (MONDO:0015469), colorectal cancer (MONDO:0005575), schizophrenia (MONDO:0005090), CTNNA1-related diffuse gastric and lobular breast cancer syndrome (MONDO:0100256), congenital fibrosis of extraocular muscles (MONDO:0007614), hereditary breast ovarian cancer syndrome (MONDO:0003582), patterned macular dystrophy (MONDO:0020381)

Orphanet (11): Inherited cancer-predisposing syndrome (Orphanet:140162), Butterfly-shaped pigment dystrophy (Orphanet:99001), Hereditary diffuse gastric cancer (Orphanet:26106), OBSOLETE: Inherited retinal disorder (Orphanet:71862), Hereditary mixed polyposis syndrome (Orphanet:157794), Hereditary nonpolyposis colon cancer (Orphanet:443909), Craniosynostosis (Orphanet:1531), Congenital fibrosis of extraocular muscles (Orphanet:45358), Hereditary breast and/or ovarian cancer syndrome (Orphanet:145), NON RARE IN EUROPE: Colorectal cancer (Orphanet:466667), NON RARE IN EUROPE: Schizophrenia (Orphanet:3140)

HPO phenotypes

8 total (10 of 8 shown, HPO-id order):

HPOTerm
HP:0000006Autosomal dominant inheritance
HP:0003596Middle age onset
HP:0003621Juvenile onset
HP:0007663Reduced visual acuity
HP:0007963Pattern dystrophy of the retina
HP:0008001Foveal hyperpigmentation
HP:0011462Young adult onset
HP:0011510Drusen
HP:0000556Retinal dystrophy
HP:0100753Schizophrenia

GWAS associations

6 associations (top):

StudyTraitp-value
GCST002539_60Schizophrenia5.000000e-09
GCST007325_152General risk tolerance (MTAG)6.000000e-12
GCST007325_42General risk tolerance (MTAG)5.000000e-08
GCST010725_68Malaria4.000000e-07
GCST010725_7Malaria2.000000e-06
GCST012490_297Femur bone mineral density x serum urate levels interaction8.000000e-10

EFO canonical traits (2, from GWAS)

EFO IDTrait name
EFO:0008579risk-taking behaviour
EFO:0004531urate measurement

MeSH disease descriptors (5)

DescriptorNameTree numbers
D003398CraniosynostosesC05.116.099.370.894.232; C05.660.207.240; C05.660.906.364; C16.131.621.207.240; C16.131.621.906.364
D061325Hereditary Breast and Ovarian Cancer SyndromeC04.588.180.483; C04.588.322.455.431; C04.700.517; C12.050.351.500.056.630.705.431; C12.050.351.937.418.685.431; C12.100.250.056.630.705.431; C12.900.418.685.431; C16.320.700.517; C17.800.090.500.483; C19.344.410.431; C19.391.630.705.431
D009386Neoplastic Syndromes, HereditaryC04.700; C16.320.700
D058499Retinal DystrophiesC11.768.585.658
C580012congenital fibrosis of the extraocular muscles (supp.)

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (1): CHEMBL4295748 (SINGLE PROTEIN)

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
7.28Kd52.44nMCHEMBL5653589
7.28ED5052.77nMCHEMBL5653589

PubChem BioAssay actives

1 with measured affinity, of 3 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
4-methyl-3-[(2-methyl-6-pyridin-3-ylpyrazolo[3,4-d]pyrimidin-4-yl)amino]-N-[3-(trifluoromethyl)phenyl]benzamide2148169: Binding affinity to human CTNNA1 incubated for 45 mins by Kinobead based pull down assaykd0.0524uM

CTD chemical–gene interactions

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

ChemicalActions (top 5)PubMed papers
bisphenol Aaffects expression, affects cotreatment, increases methylation, increases expression4
Benzo(a)pyreneincreases expression, decreases expression, decreases methylation4
Tetrachlorodibenzodioxindecreases reaction, increases expression3
Cadmium Chlorideincreases abundance, increases expression, decreases expression3
sodium bichromatedecreases expression2
ochratoxin Aincreases expression2
methacrylaldehydeaffects cotreatment, increases expression, increases oxidation, increases abundance2
Acroleinaffects cotreatment, increases expression, increases oxidation, increases abundance2
Methotrexateincreases expression, decreases expression2
Ozoneincreases oxidation, increases abundance, affects cotreatment, increases expression2
Plant Extractsaffects cotreatment, increases expression2
Quercetindecreases phosphorylation, increases expression2
Tobacco Smoke Pollutionincreases expression, affects expression2
FR900359increases phosphorylation1
geldanamycinincreases expression1
alpha-pineneaffects cotreatment, increases expression, increases oxidation, increases abundance1
bis(tri-n-butyltin)oxideincreases expression1
deoxynivalenoldecreases expression1
tributyltinincreases expression1
sodium arseniteincreases expression1
cobaltous chlorideincreases expression1
manganese chloridedecreases expression1
coumarinincreases phosphorylation1
methylmercury IIincreases expression1
di-n-butylphosphoric acidaffects expression1
taraxasterolincreases expression1
K 7174increases expression1
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamideincreases expression1
ICG 001increases expression1
bisphenol Bincreases expression1

ChEMBL screening assays

2 unique, capped per target: 2 binding

Representative assays (with source publication via chembl_document):

Assay IDTypeDescriptionSource paper
CHEMBL4119001BindingBinding affinity to CTNNA1 in human NCI-H358 cells at 1 uM by mass spectrometry based pull down assayStudies of TAK1-centered polypharmacology with novel covalent TAK1 inhibitors. — Bioorg Med Chem

Cellosaurus cell lines

4 cell lines: 3 cancer cell line, 1 transformed cell line

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

CellosaurusNameCategorySex
CVCL_1Y05DLD-1/alpha-cat cellCancer cell lineMale
CVCL_D9CLUbigene HEK293 CTNNA1 KOTransformed cell lineFemale
CVCL_SK10HAP1 CTNNA1 (-) 1Cancer cell lineMale
CVCL_XN00HAP1 CTNNA1 (-) 2Cancer cell lineMale

Clinical trials (associated diseases)

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

TrialPhaseStatusTitle
NCT00722436PHASE4TERMINATEDTranexamic Acid for Craniofacial Surgery
NCT02188576PHASE4COMPLETEDThe Efficacy and Population Pharmacokinetics of Tranexamic Acid for Craniosynostosis Surgery
NCT00114829PHASE4UNKNOWNPreoperative Assessment of Colon Tumor
NCT00114842PHASE4COMPLETEDMagnetic Resonance (MR) Colonography With Fecal Tagging
NCT00114946PHASE4TERMINATEDA Study to Compare Two Avastin-Based Treatment Regimens for the Treatment of Metastatic Colorectal Cancer
NCT00122720PHASE4COMPLETEDThe Effect of Darbepoetin Upon Rehabilitation for Colorectal Cancer Surgery
NCT00129870PHASE4TERMINATEDCONCEPT: Comparison of Oxaliplatin vs Conventional Methods With Calcium/Magnesium in First-Line Metastatic Colorectal Cancer
NCT00138060PHASE4COMPLETEDToxicity/Benefit Ratio Optimization of Chemotherapy in Colorectal Cancer (CRC) Patients by Determination of Individual Genotypic Determinants
NCT00216424PHASE4TERMINATEDCapecitabine (Xeloda) and Radiation for Patients With Rectosigmoid Carcinoma
NCT00327093PHASE4TERMINATEDElaboration of a Model for Predicting Efficacy of Monoclonal Antibodies (Cetuximab and Bevacizumab) in Patients With Colorectal Cancer and Liver Metastases
NCT00332943PHASE4COMPLETEDMR Colonography With Fecal Tagging. Barium vs. BariumFerumoxsil
NCT00441311PHASE4COMPLETEDDissemination of Colorectal Cancer Screening to Primary Care Physicians
NCT00460837PHASE4WITHDRAWNComparison of Bowel Preparation in Virtual Colonoscopy (VC) - Patient Experience
NCT00473980PHASE4COMPLETEDPreoperative Non-steroidal Anti-inflammatory Drugs(NSAID) to Colorectal Cancer Patients
NCT00488904PHASE4COMPLETEDOmega-3 Fatty Acids and Postoperative Complications After Colorectal Surgery
NCT00496678PHASE4COMPLETEDTrial of Patient Navigation-Activation
NCT00502671PHASE4COMPLETEDA Study of Xeloda (Capecitabine) as Adjuvant Monotherapy in Patients With Colon Cancer.
NCT00559676PHASE4COMPLETEDStudy of Biomarkers in Patients Undergoing Chemotherapy for Metastatic Colorectal Cancer
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