Oncofusion

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Proteinmoderate confidence 3 of 5: One strong study, or several smaller consistent ones.Q5d-interactome3

CTNNB1 (beta-catenin) — the Wnt link inside DotCom, and the one piece of KMT2A biology that is not chromatin

also called CTNNB1 · beta-catenin · Catenin beta-1 · b-catenin

Beta-catenin is the main switch of the Wnt signalling pathway, and it was found sitting inside the complex that places the H3K79 mark the KMT2A fusion depends on. That is the only published thread connecting the fusion's chromatin machinery to a classical signalling pathway.

The same thing, for a scientist

CTNNB1 (P35222, 781 aa) was identified as a component of **DotCom**, the DOT1L complex, alongside the Wnt-pathway proteins TRRAP and SKP1 and the four MLLT-family KMT2A fusion partners. The authors used that composition to predict and then confirm a role for Dot1 in Wnt/Wingless signalling: Dot1 knockdown in *Drosophila* reduced expression of a subset of Wingless targets, as did loss of the fly homologues of the Dot1-associated H3K79 regulators. This is the only entry in the graph's interactome that connects the fusion's methyltransferase machinery to a signalling pathway rather than to another chromatin factor, which is why it is worth a node even though CTNNB1 does not bind KMT2A::AFF1 and shows no KMT2A-selective dependency (difference +0.013; mean -0.247 across 1,208 lines, 12.3% depleted).

What it looks like
loading AF-P35222-F1…
AlphaFold AF-P35222-F1 ↗
colourshape

This is a prediction, not a measurement. No one has seen this protein in this shape. The colours say how much the software trusts itself, and that is worth reading before anything else — the orange stretches are places the model is effectively saying this part has no fixed shape.

very high (90+)confident (70–90)low (50–70)very low (<50)
I have never read one of these pictures before

A protein is one long chain of amino acids that folds up. The ribbon traces that chain from one end to the other; it is not a wire, it is a simplification of where the backbone runs. Drag to rotate, scroll to zoom.

Domains are the stretches of chain that do a particular job, and they are what the coloured blocks above the picture mark out. Click one and the view flies to it. In this project the important question about any domain is usually whether the fusion still has it — the labels say lost where it does not.

Anything in yellow sticks is a bound small molecule, which is usually the drug.

Go deeper
The finding, at its correct strength

DotCom's composition — DOT1L with ENL, AF9, AF17, AF10, TRRAP, SKP1 and beta-catenin — was determined by affinity purification with MudPIT 1. TRRAP, SKP1 and beta-catenin are all Wnt-pathway-associated, and the authors treated that as a prediction to be tested rather than a conclusion: knocking down Dot1 in Drosophila reduced expression of a subset of Wingless targets, and knocking down the fly homologues of the Dot1-associated H3K79 regulators did the same 1.

So the claim is (i) beta-catenin co-purifies with DOT1L, and (ii) Dot1 function is required for a subset of Wnt/Wingless target gene expression in flies. Those are both well supported. What is not supported is any statement that beta-catenin contacts DOT1L directly, that the complex is the route by which Wnt signalling operates in mammals, or that any of this has been shown in leukemia.

Method: affinity purification + MudPIT for composition; Drosophila RNAi with expression readouts for function 1. Shown for: wild-type DOT1L complex, in HeLa cells and flies. Which part of the fusion: none. CTNNB1 is not a member of the KMT2A::AFF1 interactome.

Why a signalling link is worth recording even as a negative

Almost every entry in this graph's interactome is a chromatin protein, a scaffold or an elongation factor. That homogeneity is itself a risk: a graph that only contains chromatin will only generate chromatin hypotheses, and the therapeutic record of chromatin targets in this disease is mixed at best — DOT1L inhibition underperformed, and menin inhibition works but already has a described resistance mechanism.

Beta-catenin is the one documented handle that runs out of the chromatin machinery into a signalling pathway with its own drug landscape. The honest statement of its status is: the link is real at the level of complex composition, functional at the level of fly genetics, untested in KMT2A-rearranged leukemia, and invisible in the dependency data 2.

CTNNB1 mean gene effect is -0.247 with 12.3% of lines depleted and a KMT2A-rearranged minus other-leukemia difference of +0.013 — no selectivity at all. It is a dependency in a minority of cancer lines, typically those with Wnt-pathway lesions, and KMT2A-rearranged lines are not among them.

Facts and figures
uniprotP35222
gene symbolCTNNB1
length AA781
protein nameCatenin beta-1
alphafold IDAF-P35222-F1
accession resolutionUniProt query gene_exact:CTNNB1 AND organism_id:9606 AND reviewed:true; primary gene name read back as CTNNB1 and length 781 confirmed
complexDotCom (DOT1L complex), as a Wnt-pathway-associated component alongside TRRAP and SKP1
interaction evidence classaffinity purification + MudPIT co-purification; Drosophila genetics for function
shown for fusionfalse
contact on kmt2a aff1none
pathwayWnt/beta-catenin
druggabilityBeta-catenin has an active drug-discovery landscape (tankyrase inhibitors, beta-catenin/TCF disruptors, CBP/beta-catenin modulators), unlike most entries in this interactome. Nothing in the KMT2A literature currently justifies applying it here.
subnuclear localizationUNPUBLISHED - a bounded absence, not NOT APPLICABLE. Beta-catenin demonstrably enters the nucleus and acts there as a TCF/LEF co-activator, so a subnuclear address is a meaningful question, and nobody has answered it. UniProt P35222 carries nine location values and not one has a subnuclear qualifier. The bounded query (CTNNB1 OR beta-catenin)[tiab] AND (MLL OR KMT2A)[tiab] AND (nuclear OR localization OR localisation)[tiab] returns 8 records on 2026-09-21, querytranslation confirmed, and none reports a subnuclear compartment - they report nuclear-versus-cytoplasmic partitioning and pathway activity.
localization shown for fusionPARTIAL, and for the wrong fusion. Wnt/beta-catenin pathway ACTIVATION - which is nuclear beta-catenin by definition of the assay - is established as required in MURINE MLL-AF9 (KMT2A::MLLT3) leukaemia stem cells [E_q89_ctnnb1_loc2] and as elevated in BET-inhibitor-resistant MLL-AF9 LSCs [E_q89_ctnnb1_loc3]. NOTHING in KMT2A::AFF1, nothing in B-lineage, and no direct imaging of beta-catenin's compartment in any KMT2A-rearranged cell - the pathway readouts are transcriptional and genetic. This entry's existing position is that CTNNB1 does not bind KMT2A::AFF1 and is in the graph as a DotCom component and the one signalling thread; the localisation dimension does not change that and should not be read as strengthening the interaction claim.
essentiality
{
  "depmap_common_essential": false,
  "chronos_mean": -0.2473,
  "n_lines": 1208,
  "fraction_lines_depleted": 0.1233,
  "chronos_mean_kmt2a_rearranged": -0.1065,
  "chronos_mean_other_leukemia": -0.1199,
  "kmt2a_selectivity_difference": 0.0134,
  "n_kmt2a_rearranged_lines": 11,
  "n_other_leukemia_lines": 43,
  "benchmark_men1_difference": -0.8656
}
localization
{
  "THE_COMPARTMENT_IS_THE_MECHANISM": "For beta-catenin, localisation is not a descriptive fact about the protein, it IS the signalling event. UniProt P35222 fetched 2026-09-21 states the switch in its note: 'CYTOPLASMIC when it is un-stable (highly phosphorylated) or bound to CDH1. TRANSLOCATES TO THE NUCLEUS WHEN IT IS STABILIZED (low level of phosphorylation)... The MAJORITY of CTNNB1 is localized to the CELL MEMBRANE.' So the resting answer is membrane, the destruction-complex answer is cytoplasmic-and-doomed, and the signalling answer is nuclear - three compartments for three states of one protein [E_q89_ctnnb1_loc1].",
  "subcellular_full_list": "Nine location values. Cytoplasm (5 ECO:0000269); Nucleus (9 ECO:0000269); Cell junction, adherens junction (2 ECO:0000269); Cell membrane (2 ECO:0000269); Cytoplasm/cytoskeleton, Cell junction, Synapse and Cytoplasm/cytoskeleton/cilium basal body all by similarity (ECO:0000250); and Cytoplasm/cytoskeleton/microtubule organizing center/centrosome plus Cytoplasm/cytoskeleton/spindle pole with NO evidence at all. Regulated translocation partners named in the note: GLIS2 and MUC1 promote nuclear translocation, EMD (emerin) INHIBITS it, FAM53B promotes it, SNAIL1 promotes it by similarity [E_q89_ctnnb1_loc1].",
  "subnuclear": "UNPUBLISHED. Nuclear beta-catenin is reported as nuclear, never as belonging to a named subnuclear compartment - no nucleolar, speckle, PML-body or nuclear-matrix assignment exists in UniProt or in the bounded literature this beat searched. For a protein whose entire disease relevance is a nucleocytoplasmic switch, that the nuclear destination has no internal address is a real gap rather than a technicality.",
  "system_note": "None of UniProt's attributions is haematopoietic. The disease-relevant localisation work is murine MLL-AF9 LSC biology [E_q89_ctnnb1_loc2][E_q89_ctnnb1_loc3]."
}
cell type
{
  "in_this_disease": "THE LEUKAEMIA STEM CELL, AND SPECIFICALLY THE GMP-DERIVED ONE. In mouse AML driven by the fusion oncoprotein MLL-AF9, Wnt/beta-catenin signalling is REQUIRED for self-renewal of LSCs derived either from haematopoietic stem cells or from the more differentiated GRANULOCYTE-MACROPHAGE PROGENITOR - and because the pathway is normally active in HSCs but NOT in GMPs, the authors read this as REACTIVATION of beta-catenin signalling being required for an oncogene to transform a committed progenitor. Beta-catenin is not absolutely required for self-renewal of adult HSCs [E_q89_ctnnb1_loc2].",
  "why_a_cell_type_and_not_just_a_pathway": "The GMP-versus-HSC contrast is a statement about WHICH CELL needs the nuclear pool. In an HSC the pathway is already on; in a GMP it has to be switched back on, and switching it on means moving beta-catenin into the nucleus. So this is a localisation requirement indexed to a cell type, which is rare in this graph.",
  "fusion_named_precisely": "MLL-AF9 = KMT2A::MLLT3, MOUSE, myeloid. NOT the index fusion KMT2A::AFF1 and not B-lineage. The companion oncogene arm of the same study is Hoxa9 plus Meis1a."
}
cell state
{
  "SELF_RENEWAL": "See cell-state-stem-like-self-renewal. Wnt/beta-catenin is required for LSC self-renewal in murine MLL-AF9 AML and for the reacquisition of self-renewal by a committed progenitor [E_q89_ctnnb1_loc2].",
  "DRUG_RESISTANCE": "A second, independent state. BET-inhibitor resistance in murine MLL-AF9 leukaemia emerges FROM LEUKAEMIA STEM CELLS and is in part a consequence of INCREASED Wnt/beta-catenin signalling, in human and mouse leukaemia cells; negatively regulating the pathway restores I-BET sensitivity in vitro and in vivo. In the resistant clones chromatin-bound BRD4 is globally reduced while Myc expression is unaltered [E_q89_ctnnb1_loc3].",
  "the_localisation_reading": "Both states are states of beta-catenin's DISTRIBUTION, because Wnt pathway activity is operationally nuclear beta-catenin. A graph that records 'Wnt signalling is required' and not 'beta-catenin must be nuclear' has recorded the same fact with the mechanism removed."
}
localization bounded absence
{
  "date": "2026-09-21",
  "tool": "NCBI esearch db=pubmed",
  "queries": [
    {
      "query": "(CTNNB1[tiab] OR beta-catenin[tiab]) AND (MLL[tiab] OR KMT2A[tiab]) AND (nuclear[tiab] OR localization[tiab] OR localisation[tiab])",
      "querytranslation": "(\"CTNNB1\"[Title/Abstract] OR \"beta-catenin\"[Title/Abstract]) AND (\"MLL\"[Title/Abstract] OR \"KMT2A\"[Title/Abstract]) AND (\"nuclear\"[Title/Abstract] OR \"localization\"[Title/Abstract] OR \"localisation\"[Title/Abstract])",
      "count": 8
    },
    {
      "query": "beta-catenin[tiab] AND (\"MLL-AF9\"[tiab] OR \"MLL-ENL\"[tiab] OR \"MLL-AF4\"[tiab] OR \"MLL-GAS7\"[tiab])",
      "querytranslation": "\"beta-catenin\"[Title/Abstract] AND (\"MLL-AF9\"[Title/Abstract] OR \"MLL-ENL\"[Title/Abstract] OR \"MLL-AF4\"[Title/Abstract] OR \"MLL-GAS7\"[Title/Abstract])",
      "count": 8,
      "note": "Named-fusion form run separately per rule 94, one tag per term. The literature is MLL-AF9-dominated; MLL-AF4 appears in the query and not in the answers this beat screened."
    }
  ],
  "reading": "Eight records either way and none is a subnuclear localisation study or a beta-catenin imaging experiment in a KMT2A-rearranged cell. The pathway literature in this disease is transcriptional and genetic, and it substitutes for the imaging that was never done.",
  "absence_class": "measured-not-reported"
}
How this could bite us back
  • Wnt/beta-catenin is required for intestinal crypt homeostasis and haematopoietic stem-cell maintenance; systemic beta-catenin inhibition has a well-documented toxicity profile that would be hard to justify without a KMT2A-specific rationale, which does not currently exist.
  • If DOT1L-containing and AF4/P-TEFb-containing assemblies are mutually exclusive, a beta-catenin route would be relevant to AF9/ENL-type fusions rather than to the t(4;11) disease this project targets.
Still open
  1. Is H3K79 methylation required for Wnt target expression in human haematopoietic cells, or is that a Drosophila-specific result?
  2. Wnt/beta-catenin is required for leukemic stem-cell self-renewal in several models. Is it required in KMT2A::AFF1 infant B-ALL, where the cell of origin may be a fetal-liver progenitor with different Wnt dependence?
  3. Does beta-catenin co-purify with DOT1L in a KMT2A-rearranged leukemia line, or only in HeLa? The complex has never been re-purified from the disease context.
  4. Where is beta-catenin in a KMT2A-rearranged blast? Every result in this disease is a pathway readout; no one has fractionated or imaged the protein in a fusion-positive cell, and the epithelial membrane pool that dominates the UniProt record may not exist in a blast at all.
  5. Nuclear beta-catenin has no subnuclear address anywhere in the literature. For a co-activator that works with TCF/LEF at enhancers, does it concentrate at transcription-factory-like clusters, and does that change in the BET-inhibitor-resistant state where chromatin-bound BRD4 falls?
  6. Is Wnt/beta-catenin required in KMT2A::AFF1 B-lineage disease as it is in murine MLL-AF9 myeloid disease? The requirement is one of the better-evidenced LSC dependencies in the myeloid arm and has never been tested in the index fusion.
Every source behind this entry (5)
  1. E1strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    The DOT1L complex DotCom contains the known Wnt pathway modifiers TRRAP, Skp1 and beta-catenin alongside DOT1L and the MLL partners ENL, AF9/MLLT3, AF17/MLLT6 and AF10/MLLT10; knockdown of Dot1 in Drosophila decreased expression of a subset of Wingless target genes, as did loss of the Drosophila homologues of the Dot1-associated proteins regulating H3K79.

    Linking H3K79 trimethylation to Wnt signaling through a novel Dot1-containing complex (DotCom). · Mohan M, Herz HM, Takahashi YH, Lin C, Lai KC, Zhang Y, Washburn MP, Florens L, Shilatifard A · Genes & Development 2010
    PMID 20203130DOI
    What this evidence cannot show

    Abstract read in full; not full text. Composition is from co-purification, so beta-catenin's presence in the complex does not establish a direct DOT1L-beta-catenin contact. The functional Wnt result is in Drosophila, not in human cells and not in leukemia. Beta-catenin is an abundant and famously sticky protein, which is a known source of false positives in affinity purifications.

    Evidence that argues against this (1)
    • The in vitro reconstitution of defined minimal complexes found that DOT1 forms a stable complex with AF9 and does NOT interact with AF9-AF4-P-TEFb complexes. If the DOT1L assembly and the AF4/P-TEFb assembly are mutually exclusive, then whatever DotCom contributes through beta-catenin is contributed to AF9-type fusions rather than to AFF1-type ones, and KMT2A::AFF1 may not engage this axis at all. Biswas D et al. 2011
  2. E2strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.dataset

    CTNNB1 has DepMap mean gene effect -0.2473 across 1,208 lines with 12.3% of lines depleted, mean -0.1065 in 11 KMT2A-rearranged leukemia lines against -0.1199 in 43 other leukemia lines (difference +0.013), against -0.866 for MEN1 in the same lines.

    DepMap CRISPR (Chronos) gene effect via the Open Targets Platform GraphQL API, with KMT2A-rearrangement status from Cellosaurus; per-gene recomputation for this beat · Broad Institute DepMap; Cellosaurus; Open Targets Platform; analysis run by this project · Database and derived analysis 2026
    What this evidence cannot show

    DepMap release version not stated by the API. CTNNB1 dependency in DepMap is concentrated in Wnt-driven colorectal and hepatic lines; a leukemia-only comparison therefore samples the part of the panel where CTNNB1 does least, and says little about whether Wnt signalling matters to leukemic stem-cell self-renewal, which is a self-renewal phenotype rather than a proliferation one.

    Evidence that argues against this (1)
    • −0.1065 in eleven index lines against −0.1199 in 43 comparators is a difference of 0.013 — no effect. The entry records a null and the dossier should not be read as if CTNNB1 had been placed in the interactome by dependency. Oncofusion knowledge graph (internal analysis) 2026
  3. E_q89_ctnnb1_loc1established confidence 5 of 5: Multiple independent lines of evidence; treated as settled in the field.database

    UniProt P35222 (CTNB1_HUMAN, primary gene CTNNB1, 781 aa, read back 2026-09-21) carries NINE subcellular location values - Cytoplasm, Nucleus, Cytoplasm/cytoskeleton, Cell junction/adherens junction, Cell junction, Cell membrane, Cytoplasm/cytoskeleton/MTOC/centrosome, Cytoplasm/cytoskeleton/spindle pole and Synapse and cilium basal body - of which Nucleus has nine ECO:0000269 attributions and Cytoplasm five, while the centrosome and spindle-pole values carry NO evidence at all. Its note states the switch: cytoplasmic when unstable (highly phosphorylated) or bound to CDH1; translocates to the nucleus when stabilised (low phosphorylation); the MAJORITY of CTNNB1 is at the cell membrane. Named regulators of translocation: GLIS2, MUC1 and FAM53B promote nuclear entry, EMD inhibits it, SNAIL1 promotes it by similarity. NO subnuclear qualifier appears on any value.

    What this evidence cannot show

    A curated composite across many cell types and decades, none haematopoietic among the rows examined. Two of the nine values have no evidence of any kind and should not be quoted. The statement that most CTNNB1 is at the cell membrane is uncoded and is cell-type-dependent - it is true of an epithelium with adherens junctions and its applicability to a haematopoietic blast is untested.

    Evidence that argues against this (1)
    • Importing this record wholesale into a leukaemia graph would import an epithelial cell's beta-catenin, and the entry should say so. 'The majority of CTNNB1 is localized to the cell membrane' is a statement about cells with E-cadherin adherens junctions; a haematopoietic blast does not have them, and CDH1 - the partner UniProt names for the cytoplasmic-bound pool - is an epithelial cadherin. So the membrane pool that dominates the UniProt record may be largely absent from the cell type this graph cares about, which would change the interpretation of every beta-catenin measurement in leukaemia: a given amount of nuclear beta-catenin represents a much larger fraction of the total in a blast than in an epithelial cell. Nobody has measured the partition in a KMT2A-rearranged blast, and until someone does, the UniProt baseline is the wrong prior rather than a conservative one. Wang Y et al. 2010
  4. E_q89_ctnnb1_loc2strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    In MOUSE AML induced by the fusion oncoprotein MLL-AF9 (KMT2A::MLLT3), the Wnt/beta-catenin signalling pathway is REQUIRED for self-renewal of leukaemia stem cells derived either from haematopoietic stem cells or from the more differentiated GRANULOCYTE-MACROPHAGE PROGENITOR. Because the pathway is normally active in HSCs but NOT in GMPs, the authors conclude that REACTIVATION of beta-catenin signalling is required for transformation of progenitor cells by certain oncogenes. Beta-catenin is not absolutely required for self-renewal of adult HSCs, which the authors read as a therapeutic window. The companion model in the same study is Hoxa9 plus Meis1a co-expression.

    The Wnt/beta-catenin pathway is required for the development of leukemia stem cells in AML. · Wang Y, Krivtsov AV, Sinha AU, North TE, Goessling W, Feng Z, Zon LI, Armstrong SA · Science 2010
    PMID 20339075DOI
    What this evidence cannot show

    MURINE, MYELOID, and the fusion is MLL-AF9 = KMT2A::MLLT3, NOT the index fusion KMT2A::AFF1 - stated in the claim's first clause per rule 73 because generalising murine MLL-AF9 myeloid results to infant B-lineage KMT2A::AFF1 is this project's commonest documented synthesis failure. The readout is pathway activity and self-renewal, not beta-catenin imaging; 'nuclear beta-catenin' is inferred from pathway activation rather than measured as a compartment. Abstract read in full, full text not read.

    Evidence that argues against this (1)
    • The therapeutic window this paper proposes - beta-catenin needed by the LSC and not by the normal HSC - is the load-bearing claim and it is the one most exposed. 'Not ABSOLUTELY required' is the authors' own hedge, and beta-catenin's roles outside haematopoiesis are extensive: intestinal crypt renewal, hair follicle, bone. A systemic Wnt inhibitor in an infant is a different proposition from one in an adult, and this graph's ELOVL1 entry makes the parallel point from the other direction - a vulnerability inherited from a developmental programme is shared with the developing tissue. Separately, the GMP-reactivation reading depends on the pathway being OFF in normal GMPs, which is a statement about a mouse progenitor population defined by surface markers; the human equivalence is assumed, not shown. Fong CY et al. 2015
  5. E_q89_ctnnb1_loc3strong confidence 4 of 5: Replicated in peer-reviewed work by more than one group.paper

    BET-INHIBITOR RESISTANCE IN MLL-AF9 LEUKAEMIA IS PARTLY A Wnt/beta-CATENIN STATE. Primary mouse haematopoietic stem and progenitor cells immortalised with MLL-AF9 gave single-cell clones resistant in vitro and in vivo to I-BET, cross-resistant to JQ1 and to genetic BET knockdown; resistance is not mediated by drug efflux or metabolism and emerges FROM LEUKAEMIA STEM CELLS ex vivo and in vivo. Chromatin-bound BRD4 is globally REDUCED in resistant cells while Myc expression is unaltered. Resistance in human and mouse leukaemia cells is in part a consequence of INCREASED Wnt/beta-catenin signalling, and negative regulation of the pathway restores I-BET sensitivity in vitro and in vivo.

    BET inhibitor resistance emerges from leukaemia stem cells. · Fong CY, Gilan O, Lam EY, Rubin AF, Ftouni S, Tyler D, Stanley K, Sinha D, Yeh P, Morison J, Giotopoulos G, Lugo D, Jeffrey P, Lee SC, Carpenter C, Gregory R, Ramsay RG, Lane SW, Abdel-Wahab O, Kouzarides T, Johnstone RW, Dawson SJ, Huntly BJ, Prinjha RK, Papenfuss AT, Dawson MA · Nature 2015
    PMID 26367796DOI
    What this evidence cannot show

    MLL-AF9 = KMT2A::MLLT3, murine primary HSPCs plus human leukaemia cells for the Wnt arm; not the index fusion, not B-lineage. Again a pathway-activity readout rather than a beta-catenin compartment measurement. Abstract read in full, full text not read. 'In part a consequence' is the authors' hedge and is retained here.

    Evidence that argues against this (1)
    • This result and the previous one agree so readily that the agreement deserves suspicion, and the sharpest objection is that Wnt/beta-catenin activation may be a generic LSC-state marker rather than a mechanism specific to anything. Both papers locate the beta-catenin requirement in the LSC compartment; stemness programmes across tissues run on Wnt; and 'resistance emerges from stem cells and stem cells use Wnt' can be true without beta-catenin being a useful target in this disease. What argues against the generic reading is the reversibility - negative regulation of the pathway RESTORED I-BET sensitivity in vivo, which is an intervention result rather than a correlation - and the globally reduced chromatin-bound BRD4 with unaltered Myc, which says the resistant state has rewired transcription rather than simply become more stem-like. The residual gap is the same one this whole entry is about: nobody has looked at where beta-catenin actually IS in a resistant clone versus a sensitive one. UniProt Consortium 2026
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