Alpha-E-catenin is a cytoplasmic adhesion protein that couples cadherinβcatenin complexes to the actin cortex at adherens junctions. Its N-terminal region associates with beta-catenin or plakoglobin, while actin binding, force-dependent conformational changes and recruitment of vinculin and other cytoskeletal partners stabilize junctional linkage. Cytosolic alpha-catenin can oligomerize and influence actin organization, and cytoplasmic and nuclear pools are also found outside junctions. The shorter CTNNA1b product lacks the N-terminal beta-catenin-binding region.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001541 ovarian follicle development | IEA GO_REF:0000107 | UNDECIDED | Summary: The inherited ovarian-development role remains unresolved. Reason: The rat Ctnna1 IEP source PMID:10864803 reports alpha-catenin localization and changing abundance during follicular development and hormonal treatment. These observations establish ovarian context, but the full experiments needed to evaluate its developmental contribution remain unavailable. The specific inherited process assertion remains unresolved. |
| GO:0001669 acrosomal vesicle | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the contextual acrosomal localization. Reason: The rat source PMID:16755864 explicitly reports alpha-catenin in acrosomes and late spermatids as well as myoid cells. The literal experimental donor supports this conserved localization transfer. The annotation is not invalid because epithelial junctions are the better characterized site of CTNNA1 action, but sperm localization is outside the compact junctional core. The complete original was not recovered. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | KEEP AS NON CORE | Summary: Retain RNA contact detected by the mRNA-interactome screen. Reason: UV crosslinking followed by stringent oligo(dT) capture identifies CTNNA1 in the HeLa mRNA interactome (Table S1, Excel row 28). Its ion-count adjusted p value is 0.0030253; the DESeq value is 0.236597. The paper admits proteins significant by either method, so this is qualifying RNA-contact evidence. Transcript specificity, an RNA-regulatory mechanism and isoform-specific activity remain unestablished; the interaction is retained as non-core. Supporting Evidence: |
| GO:0005198 structural molecule activity | IEA GO_REF:0000002 | MODIFY | Summary: Specify the junctional membraneβcytoskeleton anchoring activity. Reason: The InterPro structural assignment is sound but broad. AlphaE-catenin couples membrane-associated cadherinβcatenin complexes to F-actin under load. The force-dependent reconstitution reconciles the earlier failure of an unloaded complex to bind F-actin simultaneously. The more precise term includes binding to membrane-associated proteins and does not require direct lipid binding. The family mapping supplies broad structural support; the primary experiments establish the refinement. Proposed replacements: cytoskeletal protein-membrane anchor activity Supporting Evidence: GO_REF:0000002 PMID:25359979 the minimal cadherin-catenin complex formed stable bonds with an actin filament under force |
| GO:0005515 protein binding | IPI PMID:12477722 Comprehensive proteomic analysis of breast cancer cell membr... | UNDECIDED | Summary: The original LRATD2 association remains unresolved. Reason: The positive IPI names human LRATD2 (Q96KN1; historical BCMP101/FAM84B), not FERMT2. The available complete abstract and inspected current interaction exports do not resolve the CTNNA1βLRATD2 assay. The source-specific assertion remains undecided because no independently inspected target-pair result resolves it; missing access or a missing export record is not evidence of nonbinding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16212417 Biosensor-based micro-affinity purification for the proteomi... | MODIFY | Summary: Specify association with E-cadherin. Reason: GST-E-cadherin intracellular-domain affinity capture from enriched SW480 lysates identifies the cadherin-associated alpha-catenin assembly. The two literal records preserve residues 736β882, SPR/pull-down methods and spoke expansion. GO:0045296 specifies the measured cadherin partner class of this positive interaction; beta-catenin is a known intermediary, not a substitute for the recorded E-cadherin partner. The assay does not resolve an isolated alpha-cateninβcadherin interface. The PMID:8834786 excerpt corroborates rat N-cadherin complex association, separately from this human E-cadherin assay and without resolving a direct interface. Proposed replacements: cadherin binding Supporting Evidence: PMID:8834786 Both complexes are composed of N-cadherin and alpha-catenin |
| GO:0005515 protein binding | IPI PMID:17052462 Crystal structure of a beta-catenin/BCL9/Tcf4 complex. | MODIFY | Summary: Specify beta-catenin binding. Reason: The source abstract explicitly distinguishes beta-catenin mutations that impair BCL9 binding without impairing alpha-catenin binding. The curated CTNNA1βCTNNB1 interaction agrees with extensive independent beta-catenin-binding evidence. Full target assay details were not recovered, so the refinement preserves curator deference and does not present the BCL9/Tcf crystal complex as a CTNNA1 structure. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:7890674 the amino-terminal half independently binds alpha-catenin |
| GO:0005515 protein binding | IPI PMID:17057644 A distinct PAR complex associates physically with VE-cadheri... | KEEP AS NON CORE | Summary: Retain the PAR-3 association in the cadherin complex. Reason: The MINT record identifies anti-bait co-immunoprecipitation of PARD3 and CTNNA1 in CHO cells, with a Figure 1B locator. The abstract establishes a VE-cadherin-associated PAR complex; it does not establish that CTNNA1 binds a particular PAR-3 PDZ domain. The positive association remains non-core without transferring polarity-complex catalysis or a purified binary interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17098867 Pleiotrophin disrupts calcium-dependent homophilic cell-cell... | MODIFY | Summary: Specify beta-catenin binding in the pleiotrophin response experiment. Reason: The inspected source describes disruption of the alpha-/beta-catenin association during pleiotrophin-dependent remodeling of calcium-dependent adhesion. The positive pair supports beta-catenin binding despite context-dependent dissociation. It does not make CTNNA1 a pleiotrophin receptor or kinase. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:7890674 the amino-terminal half independently binds alpha-catenin |
| GO:0005515 protein binding | IPI PMID:18093941 EPLIN mediates linkage of the cadherin catenin complex to F-... | MODIFY | Summary: Specify binding to mouse EPLIN-alpha, a cytoskeletal protein. Reason: Q9ERG0-2 is mouse Lima1/EPLIN-alpha, not ABI1. PMID:18093941 Methods and Figure 1B describe purified recombinant human alpha-E-catenin binding mouse EPLIN-alpha; DLD-1 co-immunoprecipitation separately supports endogenous EPLIN association. This supports the cytoskeletal-partner class despite the missing exact pair in inspected current exports. The partner isoform remains in WITH/FROM; no target isoform or isoform-exclusive activity is inferred. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18093941 EPLIN mediates linkage of the cadherin catenin complex to F-... | MODIFY | Summary: Specify binding to the actin-associated protein EPLIN. Reason: Human LIMA1/EPLIN co-immunoprecipitates with alpha-catenin in DLD-1 cells in Figure 1A. Separate purified-protein assays use mouse EPLIN-alpha. The cytoskeletal partner class is supported without equating these species-specific assays or transferring EPLIN actin-bundling activity to CTNNA1. Proposed replacements: cytoskeletal protein binding Supporting Evidence: PMID:18093941 an actin-binding protein, couples with alpha-catenin and, in turn, links the cadherin-catenin complex to F-actin |
| GO:0005515 protein binding | IPI PMID:19016843 Molecular basis of actin reorganization promoted by binding ... | MODIFY | Summary: Specify the E-cadherin-associated interaction. Reason: The literal MINT-7010191/EBI-8501008 record identifies alpha-catenin association with GST-tagged E-cadherin residues 732β882 in a pull-down with spoke expansion. This supports the cadherin partner-class refinement. The complete abstract describes EspB effects on alpha-catenin oligomerization and actin organization; the original full Methods remain unavailable, so the assay record supplies the target-specific evidence without establishing a direct binary interface. The PMID:8834786 excerpt corroborates rat N-cadherin complex association, separately from this human E-cadherin assay and without resolving a direct interface. Proposed replacements: cadherin binding Supporting Evidence: PMID:8834786 Both complexes are composed of N-cadherin and alpha-catenin |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | MODIFY | Summary: Specify gamma-catenin binding. Reason: The exact interaction record pairs human CTNNA1 with JUP in the source two-hybrid pooling screen and cites Supplementary Table S1. JUP is plakoglobin/gamma-catenin, for which independent direct association is well established. The partner-specific refinement does not imply that CTNNA1 is a MAP kinase or that this screen measured a native complex stoichiometry. Proposed replacements: gamma-catenin binding Supporting Evidence: PMID:7890674 Plakoglobin, also known as gamma-catenin, directly binds to both APC and alpha-catenin |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | KEEP AS NON CORE | Summary: Retain the screened APC interaction as a contextual association. Reason: The literal source record reports CTNNA1βAPC in a two-hybrid pooling assay. This positive result is retained separately from the earlier biochemical finding that APC association can be bridged by beta-catenin. Assay context and construct differences are not grounds to delete the experiment. No APC enzymatic, Wnt-transcriptional or microtubule-regulatory activity is assigned to CTNNA1 from this interaction alone. APC association is retained on the same complex-association basis as cadherin association. No supported narrower APC partner-class term has been established for this interaction; generic retention reflects that specificity limit, not a rule excluding indirect associations. Supporting Evidence: PMID:7890674 alpha-Catenin cannot directly bind APC but associates with it by binding to beta-catenin |
| GO:0005515 protein binding | IPI PMID:22750944 Centralspindlin and Ξ±-catenin regulate Rho signalling at the... | MODIFY | Summary: Specify E-cadherin-associated binding at the zonula adherens. Reason: PMID:22750944 Results/Figures 5β6 identify alpha-catenin and ECT2 in E-cadherin immunocomplexes. MgcRacGAP depletion reduces the alpha-cateninβECT2 association while retaining the E-cadherinβalpha-catenin association. Cadherin binding preserves the measured partner class of this junctional assembly; the evidence is co-immunoprecipitation and does not resolve the cadherin-contacting subunit. Proposed replacements: cadherin binding Supporting Evidence: PMID:22750944 We therefore conclude that Ξ±-catenin serves as a cortical anchor for centralspindlin at the zonula adherens, to thereby support the Ect2-Rho signalling pathway. |
| GO:0005515 protein binding | IPI PMID:22750944 Centralspindlin and Ξ±-catenin regulate Rho signalling at the... | KEEP AS NON CORE | Summary: Retain association with the centralspindlin component RACGAP1. Reason: The inspected study supports alpha-catenin association with MgcRacGAP/RACGAP1 and a junctional anchoring role for centralspindlin. Alpha-catenin depletion reduces junctional ECT2 and Rho signaling, while its N-terminal constructs associate with the assembly. The positive interaction is retained without assigning RhoGAP catalysis to CTNNA1. Supporting Evidence: PMID:22750944 We therefore conclude that Ξ±-catenin serves as a cortical anchor for centralspindlin at the zonula adherens, to thereby support the Ect2-Rho signalling pathway. |
| GO:0005515 protein binding | IPI PMID:22750944 Centralspindlin and Ξ±-catenin regulate Rho signalling at the... | KEEP AS NON CORE | Summary: Retain the ECT2-containing junctional association. Reason: The original study identifies an alpha-catenin-dependent cortical platform for centralspindlin and ECT2. MgcRacGAP contributes to ECT2 recruitment, so complex association should not be restated as an independently purified CTNNA1βECT2 interface. The interaction is positive and contextual; it does not show that CTNNA1 itself catalyzes nucleotide exchange. Supporting Evidence: PMID:22750944 We therefore conclude that Ξ±-catenin serves as a cortical anchor for centralspindlin at the zonula adherens, to thereby support the Ect2-Rho signalling pathway. |
| GO:0005515 protein binding | IPI PMID:23292143 Dimer asymmetry defines Ξ±-catenin interactions. | MODIFY | Summary: Specify vinculin binding. Reason: The original structural/biochemical work uses human alpha-catenin residues 82β906 and vinculin head residues 1β840 and supports their direct association. This is more informative than generic binding. The literal P18206-2 supporting entity remains unchanged; fragment assemblies and sequential 2:1/2:2 complexes do not establish an isoform-exclusive or invariant full-length native stoichiometry. Proposed replacements: vinculin binding Supporting Evidence: PMID:9700171 All these results indicate that Ξ±E-catenin can directly bind to the head domain of vinculin at the 326β509 domain. |
| GO:0005515 protein binding | IPI PMID:24509793 Ξ±-catenin acts as a tumour suppressor in E-cadherin-negative... | KEEP AS NON CORE | Summary: Retain the IΞΊBΞ± interaction in E-cadherin-negative breast cells. Reason: The original study supports alpha-catenin association with IΞΊBΞ± in the specified basal-like breast cancer context and links it to altered IΞΊBΞ± stability/NF-ΞΊB signaling. This is a positive cellular association, not a purified binary-binding assay. The context differs from cadherin anchoring but is not a reason to remove the interaction. Supporting Evidence: PMID:24509793 Mechanistically, Ξ±-catenin interacts with the IΞΊBΞ± protein, and stabilizes IΞΊBΞ± by inhibiting its ubiquitylation and its association with the proteasome. |
| GO:0005515 protein binding | IPI PMID:24509793 Ξ±-catenin acts as a tumour suppressor in E-cadherin-negative... | MODIFY | Summary: Specify beta-catenin binding in the breast-cell study. Reason: The original Figure 3h experiment supports association of alpha-catenin with beta-catenin by co-immunoprecipitation in the study context. The partner-specific term is justified while preserving the distinction between cellular co-association and an independently purified binary interface. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:7890674 the amino-terminal half independently binds alpha-catenin |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: Specify gamma-catenin binding with the proximity-assay limit. Reason: The exact CTNNA1βJUP record is a positive endogenous proximity-ligation assay in HeLa cells. Plakoglobin is gamma-catenin, and independent biochemical evidence establishes the partner interaction. The source-specific refinement retains the positive proximity result without claiming that proximity alone resolves a direct interface. Proposed replacements: gamma-catenin binding Supporting Evidence: PMID:7890674 Plakoglobin, also known as gamma-catenin, directly binds to both APC and alpha-catenin |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | KEEP AS NON CORE | Summary: Retain the endogenous APC proximity result. Reason: The literal source record reports CTNNA1βAPC proximity ligation in HeLa cells. This detects a local molecular association and is not a purified binary-binding measurement. The positive result is retained as non-core rather than discarded for being generic or used to infer a separate CTNNA1 signaling activity. APC association is retained on the same complex-association basis as cadherin association. No supported narrower APC partner-class term has been established for this interaction; generic retention reflects that specificity limit, not a rule excluding indirect associations. Supporting Evidence: PMID:7890674 alpha-Catenin cannot directly bind APC but associates with it by binding to beta-catenin |
| GO:0005515 protein binding | IPI PMID:25764135 Alpha-catenin-dependent recruitment of the centrosomal prote... | MODIFY | Summary: Specify binding to the microtubule-associated protein CAP350. Reason: The inspected original reports the alpha-cateninβCAP350 interaction in two-hybrid, tagged co-immunoprecipitation and endogenous junctional-complex experiments. CAP350 is a cytoskeletal partner, and alpha-catenin recruits it to adherens junctions. Microtubule co-sedimentation of alpha-catenin is CAP350-dependent in these experiments; this is not evidence that alpha-catenin alone has CAP350 microtubule-binding activity. Proposed replacements: cytoskeletal protein binding Supporting Evidence: PMID:25764135 A two-hybrid screen for centrosomal protein partners revealed a consistent high-confidence interaction of CAP350 with the adhesion protein Ξ±-catenin. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | KEEP AS NON CORE | Summary: Retain APC co-association from quantitative interaction proteomics. Reason: The exact source record is an anti-tag immunoprecipitation/mass-spectrometry interaction from a HeLa line with tagged APC and a spoke expansion. It supports complex association with CTNNA1, consistent with an indirect beta-catenin-linked assembly. The original target table was not independently recovered; curated positive support is retained without a native pairwise or fixed-stoichiometry claim. APC association is retained on the same complex-association basis as cadherin association. No supported narrower APC partner-class term has been established for this interaction; generic retention reflects that specificity limit, not a rule excluding indirect associations. Supporting Evidence: PMID:7890674 alpha-Catenin cannot directly bind APC but associates with it by binding to beta-catenin |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | MODIFY | Summary: Specify beta-catenin binding from the quantitative interactome. Reason: The literal record identifies tagged beta-catenin and CTNNA1 in a HeLa affinity-purification experiment. The known beta-catenin-binding class is retained with the source assay limit: co-association and spoke expansion do not alone establish a direct interface, and the target table was not independently read. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:7890674 the amino-terminal half independently binds alpha-catenin |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | KEEP AS NON CORE | Summary: Retain the NHERF2-containing affinity-purified association. Reason: The exact Q15599βCTNNA1 record is tandem-affinity purification in HEK293T with spoke expansion and a Supplementary Data File 2 locator. It is positive complex-association evidence. The presence of PDZ domains in NHERF2 does not establish that this experiment measured binding to one of those domains; that separate fragmentomics question is assessed under its own source. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28051089 Cadherin 26 is an alpha integrin-binding epithelial receptor... | MODIFY | Summary: Specify the cadherin- and beta-catenin-associated interactions. Reason: PMID:28051089 Results/Figure 3f shows CDH26 co-immunoprecipitating with alpha-catenin, with beta-catenin co-immunoprecipitation as a positive control. The two proposed classes retain these demonstrated partners, while the original multi-partner tuple also preserves p120-catenin. The experiment uses cell lysates and supports a cadherin-associated catenin complex; CDH26 cell aggregation and integrin activity are not assigned to alpha-catenin. Proposed replacements: cadherin binding beta-catenin binding Supporting Evidence: PMID:28051089 In vitro, CDH26 promotes calcium-dependent cellular adhesion of cells lacking endogenous CDHs by a mechanism involving homotypic binding and interaction with catenin family members (alpha, beta, and p120), as assessed by biochemical assays. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: Specify beta-catenin binding in BioPlex. Reason: The exact record pairs beta-catenin bait with CTNNA1 in the 293T BioPlex affinity-purification screen and carries a spoke-expansion flag. It corroborates a well-established partner interaction. The target-specific supplemental entry was not independently read, so this is curator-grounded class refinement rather than a claim that the screen independently proved a binary interface. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:7890674 the amino-terminal half independently binds alpha-catenin |
| GO:0005515 protein binding | IPI PMID:34591612 A protein interaction landscape of breast cancer. | MODIFY | Summary: Specify the E-cadherin-associated interaction in breast-cell lines. Reason: The two current MINT records identify alpha-catenin in immunopurifications of C-terminally tagged, residue-243-mutant CDH1 in MCF10A and MDA-MB-231 cells. Cadherin binding specifies this measured partner class while retaining the mutant-construct, cell-line and spoke-expansion scope. This is evidence for a cadherin-associated assembly, not an isolated interface or a claim that every wild-type or mutant cadherin behaves identically. The PMID:8834786 excerpt corroborates rat N-cadherin complex association, separately from this human E-cadherin assay and without resolving a direct interface. Proposed replacements: cadherin binding Supporting Evidence: PMID:8834786 Both complexes are composed of N-cadherin and alpha-catenin |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | MODIFY | Summary: Specify beta-catenin binding in the endogenous-tagging resource. Reason: OpenCell uses endogenous tagging, localization and IP-MS to describe human protein associations. Its positive curated CTNNA1βCTNNB1 pair agrees with established beta-catenin-binding biology, but the target-specific table and full operative assay were not independently inspected. The annotation is refined with curator deference, without assuming isoform discrimination or a direct interface from the screen. Proposed replacements: beta-catenin binding Supporting Evidence: PMID:7890674 the amino-terminal half independently binds alpha-catenin |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | MODIFY | Summary: Specify association with the protein kinase BRAF. Reason: Tagged CTNNA1 associates with residue-600-mutant BRAF in curated complementation, pull-down and BRET records from human cell hosts. Protein kinase binding specifies that experimentally tested partner class. The mutation-strength descriptions differ between records, and the full target Results/Methods remain uninspected; the refinement is restricted to the mutant-construct assay context and does not establish a wild-type comparison or CTNNA1 kinase activity. Proposed replacements: protein kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports GRID2IP_1, GRID2IP_2 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports MPDZ_10, MPDZ_12, MPDZ_5 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports DLG4_1, DLG4_2, DLG4_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports APBA1_1, APBA1_2 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports TJP1_2, TJP1_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports DLG1_1, DLG1_2, DLG1_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports IL16_1, IL16_3, IL16_4 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports SCRIB_1, SCRIB_2, SCRIB_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports NHERF2_2 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports DLG2_2, DLG2_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports NHERF3_1, NHERF3_3, NHERF3_4 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports FRMPD2_1, FRMPD2_2, FRMPD2_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports MAGI2_2, MAGI2_3, MAGI2_4, MAGI2_5, MAGI2_6 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports NHERF4_2, NHERF4_4 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports LNX2_2, LNX2_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports Inadl_1, Inadl_10, Inadl_2, Inadl_3, Inadl_4, Inadl_5, Inadl_6, Inadl_8, Inadl_9 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports LNX1_1, LNX1_2, LNX1_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports PARD3_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | MODIFY | Summary: Specify weak in vitro binding to DLG3 PDZ2, while retaining the unresolved PDZ1/3 records. Reason: The original Dataset 1 separately measures the native CTNNA1 C-terminal decapeptide with DLG3 PDZ2 above the stated threshold (normalized BI 0.0611; pKd 3.564). This supports the gene-level PDZ-domain-binding refinement. It is a single weak DAPF measurement with no orthogonal fluorescence-polarization result, not a physiological full-length complex demonstration. The two literal curated records concern PDZ1 and PDZ3 and remain below threshold; the PDZ2 result does not repair or replace their fragment identities. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports MAGI1_1, MAGI1_2 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports APBA2_1, APBA2_2 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports GRIP2_3, GRIP2_4, GRIP2_5, GRIP2_6, GRIP2_7 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports DFNB31_1, DFNB31_2, DFNB31_3 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: The positive fragment-binding record remains unresolved against the measured affinity limits. Reason: For the CTNNA1 terminal decapeptide, Dataset 1 reports GRIP1_2, GRIP1_3, GRIP1_4, GRIP1_5, GRIP1_7 below the 0.05 DAPF detection threshold, with composite pKd zero. These are censored measurements, not demonstrated nonbinding. The positive IntAct assertion remains unreconciled with the quantitative result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment... | MODIFY | Summary: Specify gamma-catenin association in HaloMS. Reason: The literal records pair CTNNA1 with JUP/plakoglobin in the source in vitro HaloMS interaction set (Table S13), with spoke expansion. The inspected methods use wheat-germ-produced bait and cellular lysate for the human benchmark; this is complex-association evidence, not an all-purified binary assay. The gamma-catenin partner class is supported independently and by the curated positive record. Proposed replacements: gamma-catenin binding Supporting Evidence: PMID:7890674 Plakoglobin, also known as gamma-catenin, directly binds to both APC and alpha-catenin |
| GO:0005515 protein binding | IPI PMID:38884001 Mapping adipocyte interactome networks by HaloTag-enrichment... | MODIFY | Summary: Specify association with the cytoskeletal protein EPLIN. Reason: The exact HaloMS record pairs CTNNA1 with LIMA1/EPLIN in Table S13 and has a spoke-expansion flag. The source supports an in vitro association with a cytoskeletal partner, independently established by the earlier EPLIN study. The screening association is not presented as a separately validated purified pair or as a new adipocyte-specific catalytic function. Proposed replacements: cytoskeletal protein binding Supporting Evidence: PMID:18093941 an actin-binding protein, couples with alpha-catenin and, in turn, links the cadherin-catenin complex to F-actin |
| GO:0005634 nucleus | EXP PMID:16184169 ARHGAP10 is necessary for alpha-catenin recruitment at adher... | KEEP AS NON CORE | Summary: Retain the context-specific nuclear localization. Reason: Original Figure 2a includes alpha-catenin staining in human epithelial cells, with nuclear-region signal visible in Caco-2 cells. The experimental localization is retained with curator deference as a nonexclusive pool. The prose nuclear/perinuclear statement concerns ARHGAP10; it is not used to assign alpha-catenin a general nuclear function. Supporting Evidence: |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain a nonexclusive nuclear pool. Reason: The literal UniProt subcellular-location mapping supports nucleus in addition to membrane/junctional and cytoplasmic locations. CTNNA1 is not restricted to adherens junctions. This broad localization is retained as contextual without inferring a DNA-binding transcription factor activity or universal localization of all three products. Supporting Evidence: GO_REF:0000044 file:human/CTNNA1/CTNNA1-uniprot.txt |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Retain broad cytoplasmic localization. Reason: The UniProt vocabulary mapping agrees with the soluble and junction-associated cytoplasmic pools of alpha-catenin. Cytoplasm is broader than cytosol, and the source mapping is not itself a fractionation experiment warranting narrowing every product to one subcompartment. Supporting Evidence: GO_REF:0000044 file:human/CTNNA1/CTNNA1-uniprot.txt |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | ACCEPT | Summary: Retain the conserved cytoplasmic localization. Reason: The exact zebrafish donor Q9PVF8 carries experimental cytoplasmic localization from PMID:10456847, whose abstract describes cytoplasmic maternal catenin complexes and free catenins. The curator-mediated transfer is compatible with independently established human cytoplasmic pools; it does not establish identical developmental deployment or isoform behavior. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-375140 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-375140 event (CDO binds promyogenic cadherins) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-375140 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-448958 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-448958 event (Nuclear translocation of p38 MAPK) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-448958 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9817325 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9817325 event (CDH1 associates with CTNND1) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9817325 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9817330 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9817330 event (CDH1:CTNNB1 complex binds CTNNA1) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9817330 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934294 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9934294 event (CDH1-associated CTNNA1 binds VCL) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9934294 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934410 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9934410 event (CDH1 forms homotypic trans-dimers) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9934410 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934411 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9934411 event (CDH1 forms cis-clusters) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9934411 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934486 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9934486 event (CDH1-associated CTNNA1 binds F-actin) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9934486 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9934751 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9934751 event (CDH1 is phosphorylated on tyrosine residues) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9934751 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9958889 | ACCEPT | Summary: Retain the cytosolic CTNNA1 component in this Reactome event. Reason: The actual R-HSA-9958889 event (SRC phosphorylates CDH1) has an explicit component/member path to CTNNA1 physical entity R-HSA-191697 and UniProt P35221. That entity is located in cytosol and can be included in a plasma-membrane-associated cadherin complex. The localization assertion does not assign the event's kinase, translocation or extracellular adhesion chemistry to CTNNA1. Supporting Evidence: Reactome:R-HSA-9958889 |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | ACCEPT | Summary: Retain cytoskeletal association. Reason: The UniProt subcellular-location mapping is consistent with direct F-actin association and junctional anchoring experiments. The broad cytoskeleton term captures this physical association without asserting that every free CTNNA1 molecule is a constitutive cytoskeletal filament component. |
| GO:0005886 plasma membrane | EXP PMID:21708131 Bidirectional transcription from human LRRTM2/CTNNA1 and LRR... | ACCEPT | Summary: Retain plasma-membrane localization with explicit source-access restraint. Reason: The official record attributes peripheral cytoplasmic-side membrane localization of the short CTNNA1b product to PMID:21708131. The accessible abstract confirms N-terminally truncated products, but its complete localization experiment was not recovered; the gene-level positive annotation is retained with curator deference. Current isoform 3 lacks residues 1β370, including the beta-catenin-binding region, so beta-catenin-mediated recruitment is not an established explanation for that short product. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: Retain HPA-supported plasma-membrane localization. Reason: The current HPA cell-expression records include plasma-membrane and cell-junction staining in several human cell lines, with additional nonexclusive intracellular pools. This supports the source localization at its actual resolution. The antibody/line records are gene-level evidence and do not distinguish the three official products. Supporting Evidence: GO_REF:0000052 |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Retain membrane association from the combined mappings. Reason: The literal combined-method annotation includes both UniProt subcellular-location mapping and mouse Ctnna1 similarity support. The reviewed target and PMID:1924379 cadherin-colocalization evidence support membrane association. This is peripheral association with junctional complexes, not an integral-membrane topology claim. |
| GO:0005886 plasma membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Retain the curator-mediated mouse-to-human membrane localization. Reason: The exact P26231 mouse Ctnna1 source is distinct from alphaN-catenin. Its experimental membrane-localization support and the human cadherin-associated literature agree. Source-specific developmental experiments do not imply equal localization of every alternative human product. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-419002 | ACCEPT | Summary: Retain membrane-associated CTNNA1 in the modeled complex. Reason: The actual R-HSA-419002 event (Interaction of cadherin with Beta/gamma catenin, alpha catenin and p120 catenin) contains CTNNA1 through physical entity R-HSA-191735 and reference P35221. This is the membrane-associated component representation; it is distinct from cytosolic entity R-HSA-191697 used in other events. Component membership supports the localization, not the catalytic or regulatory activity performed by another event participant. Supporting Evidence: Reactome:R-HSA-419002 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5357477 | ACCEPT | Summary: Retain membrane-associated CTNNA1 in the modeled complex. Reason: The actual R-HSA-5357477 event (PAK1-3 phosphorylates VE-cadherin) contains CTNNA1 through physical entity R-HSA-191735 and reference P35221. This is the membrane-associated component representation; it is distinct from cytosolic entity R-HSA-191697 used in other events. Component membership supports the localization, not the catalytic or regulatory activity performed by another event participant. Supporting Evidence: Reactome:R-HSA-5357477 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5672304 | ACCEPT | Summary: Retain membrane-associated CTNNA1 in the modeled complex. Reason: The actual R-HSA-5672304 event (IQGAP1 binds CDH1:CTTNB1:CTTNA1 and MEN1) contains CTNNA1 through physical entity R-HSA-191735 and reference P35221. This is the membrane-associated component representation; it is distinct from cytosolic entity R-HSA-191697 used in other events. Component membership supports the localization, not the catalytic or regulatory activity performed by another event participant. Supporting Evidence: Reactome:R-HSA-5672304 |
| GO:0005911 cell-cell junction | IDA PMID:10460003 Cadherin and catenin expression in normal human bronchial ep... | ACCEPT | Summary: Retain cell-junction localization in human airway epithelium. Reason: The original abstract explicitly reports alpha-catenin staining in normal human bronchial epithelial cells and comparisons with lung tumors. The curated junction-localization annotation is consistent with that target evidence and extensive independent junction experiments. Full image panels were not recovered, so a finer junction subtype is not claimed from this source alone. Supporting Evidence: |
| GO:0005911 cell-cell junction | IDA PMID:7650039 Identification of plakoglobin domains required for associati... | ACCEPT | Summary: Retain cell-junction localization from the plakoglobin experiment. Reason: The source explicitly uses human HT-1080 cells, immunofluorescence and co-immunoprecipitation to map plakoglobin association with N-cadherin and alpha-catenin. The positive junction-localization assertion is retained at the original source resolution rather than narrowed solely from the preferred core location. Supporting Evidence: |
| GO:0005911 cell-cell junction | IEA GO_REF:0000120 | ACCEPT | Summary: Retain the electronic cell-junction assertion. Reason: The actual ARBA00028427 target branch matches the three listed CTNNA1 FunFam features and excludes fungi. The combined source also carries a rat Ctnna1 junction annotation from hepatic stellate-cell work; its abstract reports alpha-catenin at contacts in human/rat cultures. These are compatible with the established junctional role. The source objects remain distinct from experimental proof of a particular human product. Supporting Evidence: GO_REF:0000120 |
| GO:0005912 adherens junction | IBA GO_REF:0000033 | ACCEPT | Summary: Retain the ancestral adherens-junction placement. Reason: The actual PTHR18914 tree places human CTNNA1 below the Eumetazoa root PTN001052343 carrying this IBD. The exact donor annotations and target path are present with no target-path loss record. Human junctional experiments support the placement; neither donor count nor the separate Dictyostelium family classification undermines this transfer. Supporting Evidence: GO_REF:0000033 |
| GO:0005912 adherens junction | IEA GO_REF:0000120 | ACCEPT | Summary: Retain adherens-junction localization from the combined mapping. Reason: The exact UniProt-location and rodent experimental donor inputs converge on adherens-junction association. The conserved alpha-catenin role and human partner/localization experiments support the transfer. This does not imply that all expression or tumor phenotypes in the donor papers independently demonstrate junction assembly. Supporting Evidence: GO_REF:0000120 |
| GO:0005915 zonula adherens | IEA GO_REF:0000107 | ACCEPT | Summary: Retain zonula-adherens localization. Reason: PMID:11025210 explicitly describes mouse alpha/beta-catenin in the zonula-adherens complex, distinct from the more apical tight junction. This matches the mouse Ctnna1 donor localization and the established human epithelial junctional location. |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | UNDECIDED | Summary: The source-specific focal-adhesion localization remains unresolved. Reason: The original study describes focal-adhesion fractionation and its cytoskeletal/cytosolic contamination limits, but the target-specific supplemental entry was not independently verified. No saved independent CTNNA1 observation establishes this compartment. The HDA assertion is therefore undecided; this access limit does not show absence from focal adhesions, and the established adherens-junction role neither proves nor excludes that additional pool. Supporting Evidence: |
| GO:0007155 cell adhesion | IEA GO_REF:0000002 | ACCEPT | Summary: Retain the conserved cell-adhesion function. Reason: The alpha-catenin InterPro family assignment is compatible with performed cadherinβactin coupling and junction stabilization. CTNNA1 supplies structural linkage used in adhesion; this is participation rather than mere expression or disease association. More specific cell-cell adhesion is represented in the compact core without a redundant new annotation. |
| GO:0007155 cell adhesion | NAS PMID:8323564 Cloning of the human alpha-catenin cDNA and its aberrant mRN... | ACCEPT | Summary: Retain the historical cell-adhesion attribution. Reason: The human cloning study describes alpha-catenin in the cadherinβcatenin adhesion complex and identifies abnormal transcripts in a deficient cancer line. Its NAS assertion is coherent with direct later junctional/force experiments. The cloning paper alone is not represented as a complete mechanistic adhesion assay. |
| GO:0008013 beta-catenin binding | IBA GO_REF:0000033 | ACCEPT | Summary: Retain inherited beta-catenin binding. Reason: The actual ancestral IBD at PTN001052343 lies on the human CTNNA1 path and is grounded in exact experimental descendant annotations. CTNNA1 itself in the donor set is legitimate experimental grounding, not circularity. Binding is directly established in the junctional complex literature; current isoform 3 lacks the mapped N-terminal interface, so this is not a claim of equal activity for all products. Supporting Evidence: GO_REF:0000033 |
| GO:0008013 beta-catenin binding | IEA GO_REF:0000107 | ACCEPT | Summary: Retain beta-catenin binding from the rat orthology transfer. Reason: The rat Ctnna1 IPI donor points to PMID:12960056. Its abstract verifies epididymal catenin localization, but the specific alpha/beta-catenin interaction experiment remains uninspected. The molecular function is retained with curator deference and independent structural/biochemical support; the donor tissue context does not assign an epididymal function to human CTNNA1. |
| GO:0008013 beta-catenin binding | IPI PMID:7650039 Identification of plakoglobin domains required for associati... | ACCEPT | Summary: Retain the curated beta-catenin interaction. Reason: The paper directly studies catenin/cadherin complexes and maps the plakoglobin alpha-catenin interface in human cells. The precise beta-catenin panel behind this IPI was not recovered in full, but the partner interaction is independently well established. The positive source-specific assertion is retained with curator deference rather than judged absent from the abstract. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IPI PMID:7890674 The APC protein and E-cadherin form similar but independent ... | ACCEPT | Summary: Retain direct beta-catenin binding. Reason: The original abstract explicitly distinguishes direct beta-cateninβalpha-catenin binding from alpha-catenin association with APC through beta-catenin. This supports the stated molecular interaction without requiring alpha-catenin to be a direct APC-binding protein. Supporting Evidence: |
| GO:0008092 cytoskeletal protein binding | IEA GO_REF:0000117 | ACCEPT | Summary: Retain the broader cytoskeletal-protein-binding assertion. Reason: The actual ARBA00029239 target branch matches CTNNA1 alpha-catenin FunFam features. CTNNA1 associates with multiple cytoskeletal proteins, including actin, vinculin, EPLIN and CAP350. Restricting this source to F-actin would discard genuine partner breadth; the existing specific actin and vinculin assertions remain separately informative. |
| GO:0008584 male gonad development | IEA GO_REF:0000107 | UNDECIDED | Summary: The inherited male-gonad-development role remains unresolved. Reason: PMID:7507830 reports developmental redistribution of rat alpha-catenin to the Sertoli-cell junctional region, explicitly distinct from Sertoli-germ-cell contacts. The positive IEP evidence establishes expression and localization during maturation. The full results needed to assess the inferred male-gonad-development contribution remain unavailable, so the transfer remains unresolved. |
| GO:0014704 intercalated disc | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the contextual intercalated-disc location. Reason: PMID:17535849 explicitly reports alphaE-catenin at intercalated discs despite focusing on alphaT-catenin. This supports the matched mouse Ctnna1 localization transfer as a cardiac context outside the epithelial junctional core; alphaT-catenin-specific plakophilin binding is not inferred for CTNNA1. |
| GO:0015629 actin cytoskeleton | IEA GO_REF:0000002 | ACCEPT | Summary: Retain actin-cytoskeleton association. Reason: The alpha-catenin family mapping agrees with direct actin binding and force-dependent junctional linkage. The location is biologically sound, without equating all CTNNA1 forms with a permanently incorporated actin-filament subunit. |
| GO:0016264 gap junction assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the contextual gap-junction assembly contribution. Reason: The abstract of PMID:12577316 reports catenin/ZO-1/Cx43 association and inhibition of Cx43 membrane redistribution after intracellular anti-alpha-catenin antiserum delivery during a rat cardiomyocyte calcium switch. This supports a contextual organizational contribution to gap-junction assembly. Detailed controls and figures remain uninspected, and the interpretation retains curator deference at that experimental scope. |
| GO:0016342 catenin complex | IBA GO_REF:0000033 | ACCEPT | Summary: Retain inherited catenin-complex membership. Reason: The actual root IBD, target path and experimental donor set support catenin-complex membership. Direct human complex studies corroborate the transfer. Presence of target experimental evidence among the PAINT donors is expected, and complex membership does not require a single invariant stoichiometry across all junctional states. Supporting Evidence: GO_REF:0000033 |
| GO:0016342 catenin complex | IDA PMID:28051089 Cadherin 26 is an alpha integrin-binding epithelial receptor... | ACCEPT | Summary: Retain the CDH26-associated catenin complex. Reason: The inspected original supports alpha-catenin association with CDH26 and beta-catenin in an adhesion-associated assembly. This is appropriate catenin-complex membership. It does not show that every component binds every other component directly or that the complex has one fixed composition in all tissues. Supporting Evidence: |
| GO:0016342 catenin complex | IDA PMID:7650039 Identification of plakoglobin domains required for associati... | ACCEPT | Summary: Retain catenin-complex membership from the plakoglobin study. Reason: The source explicitly maps alpha-catenin association with plakoglobin and N-cadherin using human-cell immunofluorescence and co-immunoprecipitation. The complex assertion is sound even though the full original figures were not recovered. No full-length native stoichiometry is inferred. Supporting Evidence: |
| GO:0016477 cell migration | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain conserved cell-migration involvement as contextual. Reason: The actual PTN001052343 migration IBD is on the human target path and is grounded in experimental descendant evidence; it is not rejected for the number or identity of donors. Alpha-catenin organization of junctional/cortical assemblies can contribute to migration. This broader context is retained outside the compact adhesion core. Supporting Evidence: GO_REF:0000033 |
| GO:0016600 flotillin complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the curated flotillin-complex association. Reason: Both donor identifiers resolve to mouse Ctnna1 P26231, whose exact-term IDA comes from PMID:24046456. Original Results and Figure 1 caption place alpha-catenin in cadherin/flotillin co-immunoprecipitation experiments in C2C12 cells. The term permits associated proteins, so the complex assertion is retained with curator deference. Blot pixels were not independently inspected, and direct binary flotillin binding is not claimed. |
| GO:0017166 vinculin binding | IPI PMID:9700171 alpha-Catenin-vinculin interaction functions to organize the... | ACCEPT | Summary: Retain vinculin binding. Reason: The original studies mouse alphaE-catenin/vinculin constructs in human DLD-1 cells, chicken gizzard pull-down material and mouse F9 rescue. Together with direct binding to the vinculin head, the source supports this molecular function. It is not described as an all-human purified-protein experiment. Supporting Evidence: |
| GO:0030027 lamellipodium | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the contextual lamellipodium localization. Reason: The mouse Ctnna1 donor cites PMID:14657280. Its abstract describes lamellipodium extension and cadherin-catenin complex recruitment, but does not identify the alpha-catenin-specific localization panel. The positive donor localization is retained with curator deference; the precise target image remains unverified. |
| GO:0030054 cell junction | IDA GO_REF:0000052 | ACCEPT | Summary: Retain the HPA cell-junction localization at its measured resolution. Reason: The actual HPA antibody and cell-line records include cell-junction staining together with plasma-membrane and intracellular pools. The broad junction label is supported by this source; narrowing this particular image-derived assertion to a named junction subtype would exceed the recorded resolution. The data are not isoform-exclusive. Supporting Evidence: GO_REF:0000052 |
| GO:0031103 axon regeneration | IEA GO_REF:0000107 | UNDECIDED | Summary: The inherited axon-regeneration role remains unresolved. Reason: PMID:12387456 reports alpha-catenin immunoreactivity associated with mossy-fiber sprouting in restricted regions of pilocarpine-treated rat hippocampus. Other sprouting regions lack the same expression change. The association is positive, but the inaccessible full study leaves the specific axon-regeneration contribution unresolved. |
| GO:0042475 odontogenesis of dentin-containing tooth | IEA GO_REF:0000107 | UNDECIDED | Summary: The inherited tooth-development role remains unresolved. Reason: PMID:10681393 reports alpha-catenin in rat ameloblasts throughout incisor amelogenesis. The tooth-development term includes an enamel-covered dentin-containing tooth, so this is relevant developmental context. The full experiments remain unavailable and the observed expression does not settle the specific performed developmental role. |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | MODIFY | Summary: Specify alpha-catenin homodimerization. Reason: The mouse-source identical-protein-binding transfer is biologically consistent with alpha-catenin dimerization, independently demonstrated in recombinant and structural studies. Homodimerization names the activity more precisely. The source species and construct limits remain separate from the human structural corroboration, and no equal oligomerization of all alternative products is assumed. Proposed replacements: protein homodimerization activity Supporting Evidence: GO_REF:0000107 PMID:23292143 Ξ±-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions |
| GO:0042802 identical protein binding | IPI PMID:23292143 Dimer asymmetry defines Ξ±-catenin interactions. | MODIFY | Summary: Specify protein homodimerization. Reason: The source directly examines human alpha-catenin residues 82β906 and shows an asymmetric dimer under its structural/biochemical conditions. Homodimerization is more informative than identical-protein binding. The truncated crystallographic construct is not automatically equivalent to every full-length product or every cellular oligomeric state. Proposed replacements: protein homodimerization activity Supporting Evidence: PMID:23292143 Ξ±-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions |
| GO:0043297 apical junction assembly | NAS PMID:9700171 alpha-Catenin-vinculin interaction functions to organize the... | ACCEPT | Summary: Retain apical-junction assembly participation. Reason: The original alphaE-catenin/vinculin experiments directly connect the junctional interaction to assembly of the apical junctional complex, including construct/rescue experiments. Alpha-catenin supplies organizational linkage used by the junction, rather than being only a downstream expression marker. The mixed species and construct scopes are retained in the source account. Supporting Evidence: |
| GO:0043627 response to estrogen | IEA GO_REF:0000107 | UNDECIDED | Summary: The inherited estrogen-response assertion remains unresolved. Reason: PMID:10864803 reports decreased alpha-catenin abundance after diethylstilbestrol in rat granulosa cells. Expression changes can support a response term, but the full experimental and regulatory context needed to adjudicate this particular estrogen-response inference remains unavailable. Retain the transfer as unresolved. |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain contextual association with protein complexes. Reason: The rat IPI source PMID:8834786 describes two separable N-cadherin/alpha-catenin complexes containing beta-catenin or plakoglobin in cultured cardiomyocytes. Retain the broad complex-binding assertion as non-core; the more informative junctional anchoring and specific partner activities describe the principal molecular role. Detailed source methods and figures remain uninspected. |
| GO:0045295 gamma-catenin binding | IPI PMID:7650039 Identification of plakoglobin domains required for associati... | ACCEPT | Summary: Retain gamma-catenin binding. Reason: The source maps the alpha-catenin-binding region to the first plakoglobin armadillo repeat using human-cell co-immunoprecipitation and deletion constructs. This directly supports the partner class. The original abstract is available; complete figure/Methods access was not obtained, so exact construct endpoints beyond that description are not inferred. Supporting Evidence: |
| GO:0045295 gamma-catenin binding | IPI PMID:7890674 The APC protein and E-cadherin form similar but independent ... | ACCEPT | Summary: Retain direct gamma-catenin binding. Reason: The original abstract explicitly reports that plakoglobin directly binds alpha-catenin and distinguishes the APC-containing complex from the cadherin complex. The molecular function is supported without assigning APC or beta-catenin activities to CTNNA1. Supporting Evidence: |
| GO:0045296 cadherin binding | HDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by... | KEEP AS NON CORE | Summary: Retain the curated cadherin-associated interaction. Reason: The E-cadherin BioID study identifies a cadherin-centered protein neighborhood. Its available introduction/discussion and proximity method do not independently resolve the CTNNA1 target assay or a physical interface. The existing HDA assertion is retained with curator deference because alpha-catenin association with cadherin complexes is independently established by the co-immunoprecipitation and reconstitution literature; the BioID experiment alone is not treated as proof of direct contact. This is retained as a contextual cadherin-complex association rather than a separate direct cadherin-contact activity. The core describes beta-catenin recruitment and cytoskeletal anchoring explicitly; non-core status here does not make the junctional assembly biologically peripheral. Supporting Evidence: |
| GO:0045296 cadherin binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: Retain the family-based cadherin-binding assertion. Reason: The alpha-catenin family annotation is consistent with alpha-catenin participation in stable cadherin-associated complexes. Reconstitution and cellular interaction studies establish recruitment through beta-catenin or plakoglobin. Retain the existing cadherin partner-class assertion at that complex-association scope; it does not identify a separate alpha-catenin interface on the isolated cadherin tail. This is retained as a contextual cadherin-complex association rather than a separate direct cadherin-contact activity. The core describes beta-catenin recruitment and cytoskeletal anchoring explicitly; non-core status here does not make the junctional assembly biologically peripheral. |
| GO:0045296 cadherin binding | IPI PMID:12734196 Characterization of cadherin-24, a novel alternatively splic... | KEEP AS NON CORE | Summary: Retain association with cadherin-24 isoform 1. Reason: Both human cadherin-24 splice products co-immunoprecipitate alpha-catenin in transfected A431D cells in PMID:12734196. This supports the existing cadherin partner-class assertion for Q86UP0-1. The source tests NP-40 cell lysates, so the demonstrated association may be mediated within the catenin complex; the partner isoform does not specify a CTNNA1 isoform. This is retained as a contextual cadherin-complex association rather than a separate direct cadherin-contact activity. The core describes beta-catenin recruitment and cytoskeletal anchoring explicitly; non-core status here does not make the junctional assembly biologically peripheral. Supporting Evidence: |
| GO:0045296 cadherin binding | IPI PMID:12734196 Characterization of cadherin-24, a novel alternatively splic... | KEEP AS NON CORE | Summary: Retain association with cadherin-24 isoform 2. Reason: PMID:12734196 reports alpha-catenin in immunoprecipitates of the second human cadherin-24 splice product in A431D cells. Retain the positive association with Q86UP0-2, separately from Q86UP0-1. The two products share this observed catenin-complex association; the experiment does not establish an isolated binary interface or different CTNNA1 activities for the two partners. This is retained as a contextual cadherin-complex association rather than a separate direct cadherin-contact activity. The core describes beta-catenin recruitment and cytoskeletal anchoring explicitly; non-core status here does not make the junctional assembly biologically peripheral. Supporting Evidence: |
| GO:0045296 cadherin binding | IPI PMID:7650039 Identification of plakoglobin domains required for associati... | KEEP AS NON CORE | Summary: Retain N-cadherin-associated binding. Reason: The complete PMID:7650039 abstract reports human HT-1080 co-immunoprecipitation and maps distinct plakoglobin regions for alpha-catenin and N-cadherin association. This supports the curated N-cadherin-associated catenin assembly, retained with curator deference for the unrecovered full target panel. Substitution of beta-catenin binding would change the source premise: plakoglobin, not beta-catenin, is the intermediary directly mapped in this experiment. This is retained as a contextual cadherin-complex association rather than a separate direct cadherin-contact activity. The core describes beta-catenin recruitment and cytoskeletal anchoring explicitly; non-core status here does not make the junctional assembly biologically peripheral. Supporting Evidence: |
| GO:0051015 actin filament binding | IBA GO_REF:0000033 | ACCEPT | Summary: Retain inherited F-actin binding. Reason: The actual ancestral IBD and target path support actin-filament binding, with exact experimental donor matches and no target-specific loss record. Direct biochemical and force-dependent experiments independently establish the function. The transfer does not imply that unloaded cadherin-bound monomer and free alpha-catenin dimer have identical affinities. Supporting Evidence: GO_REF:0000033 |
| GO:0051015 actin filament binding | IEA GO_REF:0000120 | ACCEPT | Summary: Retain the orthology-based F-actin-binding assertion. Reason: Experimental donor annotations support the transfer, and biochemical alpha-catenin assays independently establish actin-filament binding. This conserved activity is accepted with curator deference for donor experiments whose complete target-specific assays were not recovered. |
| GO:0070161 anchoring junction | EXP PMID:12417594 The LIM protein Ajuba is recruited to cadherin-dependent cel... | ACCEPT | Summary: Retain anchoring-junction localization from the Ajuba study. Reason: The original abstract explicitly places the alpha-cateninβAjuba association in cadherin-dependent cell junctions and shows alpha-catenin-dependent Ajuba recruitment. Anchoring-junction localization is supported. The source does not require a new nuclear or transcriptional function merely because Ajuba can shuttle to the nucleus. Supporting Evidence: |
| GO:0070161 anchoring junction | EXP PMID:16184169 ARHGAP10 is necessary for alpha-catenin recruitment at adher... | ACCEPT | Summary: Retain anchoring-junction localization from the ARHGAP10 study. Reason: The original abstract directly reports alpha-catenin at cell-cell contacts and describes its recruitment by the ARHGAP10-associated machinery. This is positive junction evidence at the sourceβs resolution; ARHGAP10 GAP catalysis and the pathogen uptake endpoint are distinct from the localization assertion. Supporting Evidence: |
| GO:0070161 anchoring junction | IEA GO_REF:0000044 | ACCEPT | Summary: Retain the mapped anchoring-junction location. Reason: The UniProt subcellular-location mapping agrees with the alpha-catenin-containing cadherin adhesion apparatus. The broad location is valid without narrowing every source mapping or every alternative product to a single junction subtype. Supporting Evidence: GO_REF:0000044 file:human/CTNNA1/CTNNA1-uniprot.txt |
| GO:0071681 cellular response to indole-3-methanol | IDA PMID:10868478 Suppression of breast cancer invasion and migration by indol... | MARK AS OVER ANNOTATED | Summary: Alpha-catenin abundance increases after indole-3-carbinol exposure, but its contribution to the cellular response remains unresolved. Reason: The term permits expression changes, and GO guidance allows some response annotations from expression patterns. The original study reports increased alpha-catenin abundance after 24-hour indole-3-carbinol treatment of human MCF-7 and MDA-MB-468 cells, alongside altered invasion, migration and other adhesion proteins. It proposes a joint E-cadherin/catenin mechanism but does not distinguish a performed alpha-catenin contribution from a downstream abundance readout. Retain this as source-specific overannotation of participation, while preserving the positive expression result; neither direct compound sensing nor a particular intervention assay is required by the term. Supporting Evidence: PMID:10868478 I3C significantly caused a dose-dependent increase in E-cadherin, three major catenins (alpha, beta, and gamma-catenin) and BRCA1 expression |
| GO:0098609 cell-cell adhesion | IBA GO_REF:0000033 | ACCEPT | Summary: Retain conserved cell-cell adhesion participation. Reason: The actual PAINT root IBD lies on the human CTNNA1 lineage and is grounded in experimental descendant evidence. The target performs structural coupling in cadherin-mediated adhesion, directly supported by junction and force experiments. The phylogenetic transfer is compatible with the core function and is not undermined by a short donor list or target self-evidence. Supporting Evidence: GO_REF:0000033 |
| GO:0098797 plasma membrane protein complex | IEA GO_REF:0000117 | MODIFY | Summary: Specify the catenin complex within the membrane-associated assembly. Reason: The actual ARBA00028841 target branch matches CTNNA1 family features and predicts a broad plasma-membrane protein complex. The demonstrated cadherinβcatenin machinery permits the more informative catenin-complex description for this source. This refines an existing assertion rather than proposing a redundant new complex annotation, and does not imply integral membrane topology. Proposed replacements: catenin complex |
| GO:1900181 negative regulation of protein localization to nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain contextual restraint of nuclear signaling-effector accumulation. Reason: The two donor identifiers resolve to one mouse Ctnna1 experiment from PMID:21145499. In the original study reproduced in its coauthorβs thesis, Ctnna1 knockdown in Eph4 cells increases nuclear TAZ/YAP and TGF-beta-dependent SMAD2/3 accumulation. This supports the transferred regulatory role, without assigning intrinsic nuclear transport or kinase activity to alpha-catenin. |
| GO:1900181 negative regulation of protein localization to nucleus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the curator-mediated nuclear-localization regulation transfer. Reason: The exact mouse Ctnna1 IMP from PMID:21145499 supports increased nuclear Hippo/TGF-beta effector accumulation after Ctnna1 knockdown. The original experiment was recovered in the coauthorβs thesis reproduction, including the relevant figure. This is the same mouse evidence underlying the separate electronic transfer, not an independent experiment or proof of intrinsic nuclear transport. |
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Download this section (compressed HTML)Q: How were below-quantification CTNNA1-tail/PDZ measurements represented as positive fragment interactions in the curated records, and can those records be reconciled with original Dataset 1 values? DLG3 PDZ2 is a distinct weak positive and does not resolve PDZ1/PDZ3.
Q: What mechanism recruits the 536-aa CTNNA1b product to membranes despite loss of residues 1β370, including the beta-catenin-binding region, and which functions of the longer products does it retain?
Q: Do the rodent expression-derived developmental/hormonal annotations reflect a demonstrated alpha-catenin contribution to the process, or only changes in abundance? Full source experiments are needed for the five unresolved transfers.
Q: How should the deeper alpha-catenin/vinculin relationship be represented across the separate current PANTHER families, given direct Dictyostelium alpha-catenin-like biology? Family classification alone does not settle orthology or ancestral cellular setting.
Q: Does CTNNA1 bind wild-type BRAF under the same conditions as the residue-600-mutant constructs in PMID:35512704, and how do the differing curated mutation-strength features relate to the original measurements?
Experiment: Measure CTNNA1-tail binding to DLG3 PDZ1/2/3 with replicated affinity assays and matched domain constructs, then test full-length cellular association and the dependence on the terminal decapeptide.
Experiment: Compare the three official CTNNA1 products in matched-expression localization and junctional rescue assays, with direct measurement of partner association and force-dependent actin coupling.
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