CTNND1 encodes p120-catenin, an armadillo-repeat protein that binds cadherin cytoplasmic tails and controls cadherin surface stability. At adherens junctions it supports persistent cell-cell adhesion by protecting cadherins from turnover while allowing regulated junction remodeling. Cadherin-free long p120 products can restrain RhoA activation; cadherin engagement and phosphorylation modulate this regulation. Cytoplasmic and nuclear pools interact with signaling proteins and the transcription factor Kaiso. Alternative translation starts and splicing generate products with different N- and C-terminal sequences and distinct patterns of nuclear accumulation and effects on cell morphology.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000122 negative regulation of transcription by RNA polymerase II | IMP PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | KEEP AS NON CORE | Summary: p120 dampens LPP3-dependent transcription. Reason: Knockdown and reexpression alter LEF-1 reporter output in confluent human endothelial cells (Figure 3). This is contextual upstream regulation. Supporting Evidence: |
| GO:0002042 cell migration involved in sprouting angiogenesis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cadherin turnover contributes to endothelial collective migration. Reason: The literal mouse Ctnnd1 donor and PMID:33972531 support this inherited context. Human endothelial live imaging and cadherin-binding-site mutants connect p120 occupancy to junction turnover during collective migration. The source also relates this mechanism to mouse vascular studies; it does not make p120 a cell-surface trans-cell adhesion molecule. This vascular output is contextual to its cadherin-stabilizing activity. |
| GO:0005102 signaling receptor binding | IPI PMID:19332538 Density-enhanced phosphatase 1 regulates phosphorylation of ... | MODIFY | Summary: DEP1 association is protein phosphatase binding. Reason: The source examines DEP1/PTPRJ substrate trapping and phosphorylation in epithelial cells, including association with p120. The demonstrated intracellular protein-phosphatase partner class supports the more informative protein phosphatase binding term. The original receptor-binding term does not require extracellular binding or agonism. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10207085 The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ ... | MODIFY | Summary: p120 binds the DNA-binding transcription factor Kaiso. Reason: The original abstract reports p120-bait two-hybrid identification and specific mammalian coimmunoprecipitation of Kaiso. The verified partner is ZBTB33, a DNA-binding transcription factor, supporting the narrower binding class without assigning DNA-binding activity to p120. Full original Methods were not recovered. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: PMID:10207085 Kaiso specifically coprecipitated with a variety of p120-specific monoclonal antibodies |
| GO:0005515 protein binding | IPI PMID:12370829 The transmembrane receptor protein tyrosine phosphatase DEP1... | MODIFY | Summary: DEP1 substrate trapping supports protein phosphatase binding. Reason: The source explicitly reports interaction of the DEP1 catalytic-domain substrate-trapping mutant with p120 and cell-contact colocalization. Literal MINT records agree with the pair. These data support the binding class at the tested substrate-trapping and cellular scope, without making p120 a phosphatase catalyst. Proposed replacements: protein phosphatase binding Supporting Evidence: PMID:12370829 GST-fusion proteins containing the DEP1 catalytic domain with a substrate-trapping D/A mutation were found to interact with p120(ctn) |
| GO:0005515 protein binding | IPI PMID:12475979 Hepatocyte growth factor receptor tyrosine kinase met is a s... | MODIFY | Summary: The DEP1 partner supports protein phosphatase binding. Reason: The curated p120βPTPRJ pair is preserved in the literal pulldown record from this source. Its title emphasizes MET, but that does not contradict an additional p120 assay. The partner is a protein tyrosine phosphatase; full target Methods were not independently recovered, so the original experimental assignment is retained with curator deference. Proposed replacements: protein phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | MODIFY | Summary: p120 associates with the receptor kinase EGFR. Reason: The literal source record joins human p120 and EGFR in a coimmunoprecipitation interaction. The verified receptor class supports receptor tyrosine kinase binding, with the co-complex and phosphotyrosine-network assay limits retained. This does not imply receptor activation or purified binary binding. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16354688 A family of human zinc finger proteins that bind methylated ... | UNDECIDED | Summary: The source-specific p120βKaiso experiment remains unresolved. Reason: The accessible abstract addresses Kaiso-family DNA binding and repression, but does not establish the particular p120 interaction cited here; the available literal interaction set supplies no matching pair. Independent positive p120βKaiso evidence is preserved in other rows. Incomplete original access leaves this experimental source assertion undecided, without a negative binding or wrong-gene inference. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17047063 E-cadherin regulates human Nanos1, which interacts with p120... | KEEP AS NON CORE | Summary: The source reports positive p120βNANOS1 association. Reason: The abstract explicitly identifies the N-terminal NANOS1 region as interacting with p120 and reports effects on p120 distribution and protrusions. This positive pair is retained under the project binding policy. The experiment does not establish that p120 performs NANOS1 RNA regulation. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18343367 P120-catenin is a novel desmoglein 3 interacting partner: id... | MODIFY | Summary: Cadherin binding captures the measured partner. Reason: The original abstract and accessible publisher Methods/Results report p120 coimmunoprecipitation with desmoglein-3 and reduced association after deletion of its intracellular anchor region. The verified partner is a cadherin, supporting the specific binding class at cellular complex scope. The complete original was not recovered; the observed free surface desmoglein pool is distinct from mature desmosomes. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19604117 CagA associates with c-Met, E-cadherin, and p120-catenin in ... | KEEP AS NON CORE | Summary: CagA joins a p120-containing infection-associated complex. Reason: The source reports a CagAβMETβE-cadherinβp120 complex in infected gastric epithelial cells; its perturbation indicates that the CagAβp120 association is mediated through MET. Positive physical association is retained without converting this into purified direct CagA binding or a general pathogen-response function. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19604117 CagA associates with c-Met, E-cadherin, and p120-catenin in ... | MODIFY | Summary: MET association supports receptor tyrosine kinase binding. Reason: The source reports increased METβp120 interaction during infection and literal coimmunoprecipitation records preserve the pair. MET is a receptor tyrosine kinase. The refinement describes partner class at the cellular complex scope, not p120 kinase or receptor activity. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19604117 CagA associates with c-Met, E-cadherin, and p120-catenin in ... | MODIFY | Summary: The infection-associated pair is E-cadherin binding. Reason: The source explicitly reports E-cadherinβp120 interaction and its modulation during infection, corroborated by literal coimmunoprecipitation records. Cadherin binding is more informative than generic binding; the complex assay does not establish every pair as an isolated binary contact. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | MODIFY | Summary: The measured partner supports phosphatase binding. Reason: Reciprocal co-IP, far-Western and LPP3 C-terminal pulldown assays support the specific binding class (Figures 7β9). Proposed replacements: phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21357690 RET modulates cell adhesion via its cleavage by caspase in s... | MODIFY | Summary: The N-cadherin pair supports cadherin binding. Reason: The actual human SH-SY5Y experiments examine N-cadherin/p120 association in the RET cleavage context, including RET708Stop. The positive coimmunoprecipitation is retained as cadherin binding, without treating a cleavage-fragment perturbation or the broader mouse neuronal experiments as equivalent conditions. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22846708 FERM-containing protein FRMD5 is a p120-catenin interacting ... | KEEP AS NON CORE | Summary: p120 positively associates with FRMD5. Reason: The abstract and literal records support a p120-containing complex through the FRMD5 C-terminal region; the tested FRMD5 fragment spans residues 355β570. The partner name or FERM annotation does not by itself establish an adaptor function performed by p120, so the positive interaction remains contextual. Supporting Evidence: PMID:22846708 formed a molecular complex with p120-catenin through its C-terminal region |
| GO:0005515 protein binding | IPI PMID:23990464 Binding between the junctional proteins afadin and PLEKHA7 a... | UNDECIDED | Summary: The cited PLEKHA7 pair requires source-specific verification. Reason: The literal partner UniProtKB:Q3UIL6 is reviewed mouse Plekha7, not an unidentified human accession. The original IPI supporting entity is preserved: a non-human partner can occur in a valid interaction experiment. The accessible abstract establishes afadinβPLEKHA7 biology and mentions p120, but the exact p120βPLEKHA7 assay, constructs and species pairing were not recovered, and no matching literal pair was resolved. UNDECIDED reflects that unresolved target experiment, not evidence against binding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24189400 Perturbation of the mutated EGFR interactome identifies vuln... | MODIFY | Summary: The EGFR interactome contains a p120 association. Reason: The human airway epithelial interactome study identifies CTNND1 among catenin associations of wild-type EGFR. The literal tandem-affinity record supports receptor tyrosine kinase binding at a tagged co-complex scope. It does not establish a purified binary interface or generalize every mutant receptor network to wild type. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24424122 Rescue of wild-type E-cadherin expression from nonsense-muta... | MODIFY | Summary: The E-cadherin proximity result supports cadherin binding. Reason: The literal source record uses proximity ligation for E-cadherin and p120 in the suppressor-tRNA rescue context. Cadherin binding is biologically established and a more informative partner class. The original assay is retained as proximity evidence with curator deference, not redescribed as a purified binding experiment. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | MODIFY | Summary: The membrane interaction assay supports EGFR binding. Reason: The literal source record preserves the EGFRβp120 membrane two-hybrid pair. EGFR supplies the receptor tyrosine kinase partner class. The reporter and tagged-construct conditions are retained; no native stoichiometry or receptor activation by p120 is inferred. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28051089 Cadherin 26 is an alpha integrin-binding epithelial receptor... | KEEP AS NON CORE | Summary: The three reported partners belong to a cadherin-containing association. Reason: The actual CDH26 study reports alpha-catenin, beta-catenin and p120 association in transfected HEK cells. All three original partner identities are retained. Co-complex evidence does not establish each isolated binary interaction or a single specific activity covering this heterogeneous partner set. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: The screen supports a p120βEGFR receptor-kinase association. Reason: The literal MYTH record contains p120 Cub and EGFR Nub constructs. The main study distinguishes these membrane two-hybrid assays from its affinity-purification networks. Receptor tyrosine kinase binding is the appropriate partner class, without inferring an untagged physiological complex from the screen alone. Proposed replacements: receptor tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The source identifies E-cadherin as the p120 partner. Reason: The exact human E-cadherinβp120 coimmunoprecipitation record supports the cadherin class. The source is a proteome-scale screen and the literal record is a spoke-expanded association; its target panel was not separately read. Curator-supported binding is retained without claiming purified binary contact. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The source identifies N-cadherin as the p120 partner. Reason: The exact human N-cadherinβp120 coimmunoprecipitation record supports cadherin binding. Its spoke-expanded screen context and uninspected target panel remain explicit; the refinement does not assign all product variants the same affinity. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The source identifies the DNA-binding factor Kaiso as partner. Reason: The literal human ZBTB33βp120 coimmunoprecipitation record and official Kaiso function support DNA-binding transcription factor binding. This screen-specific positive is retained with curator deference for its uninspected target panel. It does not establish p120 as a DNA-binding transcription factor. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:34591612 A protein interaction landscape of breast cancer. | MODIFY | Summary: The CDH1 pair supports cadherin binding. Reason: The interaction set contains both a wild-type CDH1 pair and separately marked CDH1 mutant records. Cadherin binding is supported while those experimental conditions remain distinct. The source is a breast-cancer interaction screen; purified binary binding and mutation-independent equivalence are not inferred. Proposed replacements: cadherin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:37207277 Using brain cell-type-specific protein interactomes to inter... | MODIFY | Summary: p120 associates with the GTPase-activating protein SYNGAP1. Reason: The positive anti-bait coimmunoprecipitation records identify SYNGAP1, a reviewed Ras/Rap GTPase-activating protein, supporting the more informative GAP-binding class. The neuronal IP-MS study includes nonstoichiometric associations; its exact target table and validation panel were not independently inspected. This refinement retains curator-grounded association without claiming a purified binary interface or GAP catalysis by p120. Proposed replacements: GTPase activating protein binding Supporting Evidence: |
| GO:0005634 nucleus | EXP PMID:11896187 Specific sequences in p120ctn determine subcellular distribu... | ACCEPT | Summary: Several tested p120 products enter the nucleus. Reason: The original human-cell experiments test sequenced constructs derived from AF062341 and directly image nuclear p120. Accumulation varies with translation start and C-terminal exon B. The positive gene-level location is supported without assuming equal distribution of all 32 products or assigning an unreported isoform. Supporting Evidence: |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Nuclear localization is supported by the actual PAINT placement. Reason: The exact target lies below PTN000822184 in the recovered PTHR10372 tree. The nuclear IBD is on that path with the seeded donor set; direct human p120 localization experiments support the inherited location. Target self-evidence is valid grounding, and the assertion remains gene-level rather than an all-product localization claim. |
| GO:0005634 nucleus | IDA PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | ACCEPT | Summary: Nuclear p120 localization is directly observed. Reason: Figure 7 documents density-dependent nuclear p120 localization. This positive cellular-location observation supports the nuclear annotation without requiring a separately demonstrated nuclear activity; it does not imply exclusive localization or equivalent nuclear access by all products. Supporting Evidence: |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: The curated nuclear mapping is biologically appropriate. Reason: The original UniProt nuclear-location mapping agrees with direct localization of selected human p120 products. Nuclear entry depends on product and cellular context; this broad annotation does not claim all 32 products are nuclear. |
| GO:0005737 cytoplasm | EXP PMID:11896187 Specific sequences in p120ctn determine subcellular distribu... | ACCEPT | Summary: p120 occupies cytoplasmic pools. Reason: Human-cell imaging supports cytoplasmic p120, including the tested historical 4A and 1AB constructs. Punctate and other cytoplasmic pools justify the broad location; they are not all identified as free cytosol or generalized to every product. Supporting Evidence: |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: Cytoplasmic localization is conserved and directly observed. Reason: The cytoplasmic IBD lies on the genuine target ancestral path and has the seeded donor set. Direct human imaging and mouse functional experiments support cytoplasmic pools. The broad location covers soluble and other cytoplasmic distributions without collapsing them all to cytosol. |
| GO:0005737 cytoplasm | IDA PMID:17047063 E-cadherin regulates human Nanos1, which interacts with p120... | ACCEPT | Summary: NANOS1 expression redistributes p120 into the cytoplasm. Reason: The source abstract explicitly reports p120 cytoplasmic translocation after conditional human NANOS1 expression in DLD1 cells. Retain this observed location without assigning NANOS1 RNA-binding activity or its full migratory phenotype to p120. Supporting Evidence: PMID:17047063 It induced cytoplasmic translocation of p120ctn |
| GO:0005737 cytoplasm | IDA PMID:21998202 RPTPΞΌ tyrosine phosphatase promotes adipogenic differentiati... | ACCEPT | Summary: A functional cytoplasmic p120 pool is supported. Reason: Fractionation and phosphorylation-dependent GLUT4-trafficking effects support cytoplasmic activity. Target experiments use mouse p120 in 3T3-L1 cells; retention uses conserved function, not a claimed human assay. Supporting Evidence: |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt mapping retains the observed cytoplasmic pool. Reason: Direct imaging of selected human constructs and conserved cellular experiments support the curated broad cytoplasmic location. It is not restricted to free cytosol or inferred solely from lack of a signal peptide. |
| GO:0005829 cytosol | IMP PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | ACCEPT | Summary: Cytosolic p120 accompanies the junctional pool. Reason: Figure 7 shows cytosolic p120 at higher cell density. Supporting Evidence: |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited plasma-membrane location is supported. Reason: The plasma-membrane IBD occurs on the reconstructed target path with the seeded donors. Independent cadherin association and imaging place p120 at the cytoplasmic face of the membrane. This does not imply a transmembrane segment or extracellular ligand-binding role. |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: HPA directly supports plasma-membrane localization. Reason: The current Human Protein Atlas entry reports an enhanced main plasma-membrane location and supporting antibody annotations in A-431, U-251MG and U2OS cells. The annotation text was inspected; image pixels were not independently reassessed. This agrees with established junctional p120 biology. Supporting Evidence: GO_REF:0000052 |
| GO:0005886 plasma membrane | IDA PMID:17115030 The armadillo protein p0071 regulates Rho signalling during ... | ACCEPT | Summary: The curated membrane observation is retained with a source-access limit. Reason: The accessible abstract foregrounds p0071 cytokinesis, while the p120-specific location experiment remains uninspected. A title naming another family member is not grounds for rejecting the curator. Established p120 membrane localization supports retention with explicit curator deference; no p0071 cytokinetic mechanism is transferred. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The membrane vocabulary mapping agrees with p120 localization. Reason: The UniProt cell-membrane mapping is consistent with cadherin-associated p120 at the cytoplasmic membrane face. It does not classify p120 as an integral membrane or extracellular adhesion protein. |
| GO:0005886 plasma membrane | IMP PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | ACCEPT | Summary: p120 occupies the cytoplasmic face of the cell membrane. Reason: Figures 7β10 support membrane recruitment and partner association; p120 itself is not transmembrane. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-419002 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The modeled cadherin complex contains p120 through its intracellular cadherin association. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-419002 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5357477 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The VE-cadherin phosphorylation reaction includes membrane-localized p120 in its cadherin context; PAK/SRC perform the phosphorylation. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-5357477 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8876497 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The InlA-bound E-cadherin complex contains p120 at the host plasma membrane; InlA binding is attributed to the extracellular cadherin domain. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-8876497 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8876948 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The InlA-associated phosphorylation model retains p120 in a membrane complex; SRC performs the kinase reaction. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-8876948 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-8876993 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The model records the membrane cadherin complex and displacement of p120 as CBLL1 binds, rather than p120 ubiquitin-ligase activity. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-8876993 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9761421 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: CDH11 association explicitly places p120 with the membrane cadherin complex. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9761421 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9761474 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The AMOT-2/CDH11 assembly contains p120 through the cadherin complex; no direct AMOT-2βp120 interface is inferred. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9761474 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9762246 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The ANGPTL4/CDH11 event retains p120 in its membrane complex; extracellular ANGPTL4 binding is performed by CDH11. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9762246 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9762282 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The model releases beta-catenin from the CDH11 complex and preserves the p120 membrane context, without transferring beta-catenin transcriptional output. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9762282 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9817325 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The event explicitly models CDH1 association with p120 at the basolateral membrane; product-dependent binding differences remain relevant. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9817325 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9934294 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The membrane cadherin complex includes p120 while alpha-catenin recruits vinculin; that separate binding activity is not assigned to p120. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9934294 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9934410 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The trans-dimer model contains membrane-associated p120, while cadherin extracellular domains execute trans-cell binding. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9934410 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9934411 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The cis-cluster model contains membrane cadherin-associated p120; cluster membership does not make p120 an extracellular adhesion molecule. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9934411 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9934486 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The model includes p120 in the membrane complex while alpha-catenin recruits F-actin; this location assertion does not establish p120 actin binding. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9934486 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9934751 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The phosphorylation model contains membrane-associated p120 and distinguishes the kinases from their cadherin/catenin substrates. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9934751 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9934755 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The CBLL1 event places p120 in the membrane cadherin context and records competition/displacement, not p120 ubiquitin-ligase activity. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9934755 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9958889 | ACCEPT | Summary: The Reactome assembly supports plasma-membrane localization. Reason: The SRC event retains the membrane cadherin/catenin context; SRC supplies catalysis, whereas p120 is a complex component/substrate context. The literal event-to-complex-to-O60716 path is present in the captured model; retention concerns location, not every activity in the event. Supporting Evidence: Reactome:R-HSA-9958889 |
| GO:0005911 cell-cell junction | IDA PMID:12370829 The transmembrane receptor protein tyrosine phosphatase DEP1... | ACCEPT | Summary: DEP1 and p120 colocalize at cell-cell contacts. Reason: The source explicitly reports p120 colocalization with DEP1 at A549 cell-cell contacts. This is a direct positive junctional observation in the accessible abstract, independent of any claim about catalytic inhibition. Supporting Evidence: |
| GO:0005911 cell-cell junction | IDA PMID:18343367 P120-catenin is a novel desmoglein 3 interacting partner: id... | ACCEPT | Summary: p120 localizes to cell-cell contacts. Reason: The accessible DSG3 study and curated record support p120 at cell-cell contacts, consistent with independent cadherin studies. The full original remains incompletely accessed. Its free surface desmoglein pool is distinguished from desmosomal incorporation, so retention uses broad junctional biology and curator deference. Supporting Evidence: |
| GO:0005912 adherens junction | IBA GO_REF:0000033 | ACCEPT | Summary: Junctional localization is conserved. Reason: The genuine current PTHR10372 tree places the exact 968-aa target below PTN000822184, and the literal adherens-junction IBD on that path has the seeded donor set. Direct mammalian imaging and cadherin-complex studies support the inherited junctional location, with no target-specific loss established. Target self-evidence is legitimate, and donor number is not the rationale for acceptance. This phylogenetic assertion does not establish equal localization of every splice product. Supporting Evidence: GO_REF:0000033 |
| GO:0005912 adherens junction | IDA PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | ACCEPT | Summary: p120 is an adherens-junction component. Reason: Junctional recruitment and staining support this location (Figures 5 and 7). Supporting Evidence: |
| GO:0005912 adherens junction | IEA GO_REF:0000120 | ACCEPT | Summary: The rule and location mapping support adherens junctions. Reason: The target matches branch 9 of the actual ARBA00028426 condition sets, and the UniProt location premise independently maps to adherens junction. Direct imaging and cadherin-complex experiments corroborate this location. Both original electronic premises are retained. Supporting Evidence: GO_REF:0000120 |
| GO:0005912 adherens junction | ISS GO_REF:0000024 | ACCEPT | Summary: The ortholog transfer supports adherens junctions. Reason: The mouse P30999 ortholog transfer agrees with direct p120 junctional imaging, human cadherin-24 complexes and conserved cadherin binding. No target-specific divergence from this location is established. Nuclear and other cytoplasmic pools remain compatible with the annotation. Supporting Evidence: GO_REF:0000024 |
| GO:0010829 negative regulation of D-glucose transmembrane transport | IDA PMID:21998202 RPTPΞΌ tyrosine phosphatase promotes adipogenic differentiati... | KEEP AS NON CORE | Summary: p120 reduces GLUT4 surface delivery. Reason: Overexpressed mouse p120 inhibits insulin-stimulated GLUT4 trafficking; active RPTPmu partially reverses this. Reduced glucose transport is the physiological inference from transporter availability, not a directly measured flux. Supporting Evidence: |
| GO:0016342 catenin complex | IDA PMID:28051089 Cadherin 26 is an alpha integrin-binding epithelial receptor... | ACCEPT | Summary: p120 associates with a cadherinβcatenin complex. Reason: The actual CDH26 experiments recover p120 together with alpha- and beta-catenin in the cadherin-associated assembly in HEK cells. This supports the broad complex annotation without establishing a native stoichiometry or isolated pairwise interfaces among every component. Supporting Evidence: |
| GO:0019212 phosphatase inhibitor activity | IDA PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | MARK AS OVER ANNOTATED | Summary: The cited inhibition concerns LPP3-driven signaling rather than measured phosphatase catalysis. Reason: The original human endothelial experiments demonstrate p120βLPP3 association and suppression of Ξ²-catenin/LEF1 signaling. The main Methods and Results measure reporter activity, protein association, localization and cellular outcomes, not LPP3 lipid-substrate turnover with and without p120. Phosphatase-defective LPP3 retains signaling activity, which separates the reporter endpoint from catalysis but does not disprove possible catalytic inhibition. The phosphatase-inhibitor assignment exceeds the demonstrated source-specific mechanism; the positive phosphatase-binding assertion is retained separately. Supporting Evidence: |
| GO:0019902 phosphatase binding | IPI PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | KEEP AS NON CORE | Summary: LPP3 is a supported phosphatase partner. Reason: Figures 7β9 establish binding; this contextual association does not establish inhibition of catalysis. Supporting Evidence: |
| GO:0030496 midbody | IDA PMID:15166316 Dissection of the mammalian midbody proteome reveals conserv... | UNDECIDED | Summary: The specific midbody-screen target remains unverified. Reason: The accessible source describes purified mammalian midbodies and a proteomic/RNAi strategy, but the exact CTNND1 target entry was not independently recovered. General family cytokinesis biology cannot substitute for this source-specific location result. The curated positive remains undecided, without a negative midbody claim. Supporting Evidence: |
| GO:0044331 cell-cell adhesion mediated by cadherin | IMP PMID:14610055 A core function for p120-catenin in cadherin turnover. | ACCEPT | Summary: p120 stabilizes cadherin-dependent adhesion. Reason: PMID:14610055 measures cadherin loss and impaired cell-cell adhesion after p120 depletion, with restoration by murine p120 rescue in human A431 cells. Pulse-chase/surface biotinylation places the effect after normal cadherin arrival at the surface. Together with actual cadherin binding, this identifies work performed by p120 in cadherin-dependent adhesion through receptor retention; it does not make p120 itself the extracellular trans-cell ligand. Supporting Evidence: |
| GO:0045296 cadherin binding | HDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by... | ACCEPT | Summary: Cadherin binding is retained with the proximity-screen limit. Reason: This source uses E-cadherin BioID proximity proteomics, whose labeling range can include neighboring proteins. Its precise p120 table entry was not independently read. Cadherin binding is nevertheless directly established by targeted p120 studies, supporting curator deference for the existing annotation while preserving the source-method distinction. Supporting Evidence: PMID:20371349 Single-residue mutations within the JMD(core)-binding site of p120 abolished its interaction with E- and N-cadherins |
| GO:0045296 cadherin binding | IBA GO_REF:0000033 | ACCEPT | Summary: Cadherin binding is an inherited activity. Reason: The literal cadherin-binding IBD lies on the genuine target path and matches the seeded source set. Targeted association, mutation and structural evidence corroborate the inherited activity. Target self-evidence is valid grounding; no target-specific loss is established. Supporting Evidence: GO_REF:0000033 |
| GO:0045296 cadherin binding | IEA GO_REF:0000117 | ACCEPT | Summary: The matched rule supports cadherin binding. Reason: The target matches branch 2 of ARBA00092450. Cadherin binding is independently demonstrated by targeted assays and a deposited p120βcadherin-tail structure, supporting this electronic assertion without inferring equal affinity across all products. Supporting Evidence: GO_REF:0000117 |
| GO:0045296 cadherin binding | IPI PMID:10725230 ARVCF localizes to the nucleus and adherens junction and is ... | ACCEPT | Summary: p120 associates with E-cadherin. Reason: The recovered original contains p120/E-cadherin coimmunoprecipitation despite its ARVCF title focus. Figure 5 uses endogenous canine MDCK proteins with human ARVCF; separate human p120 constructs are described elsewhere. The positive cadherin-binding assertion is retained with this cellular/species scope, not described as a purified human pair. Supporting Evidence: |
| GO:0045296 cadherin binding | IPI PMID:12734196 Characterization of cadherin-24, a novel alternatively splic... | ACCEPT | Summary: p120 associates with long cadherin-24. Reason: The recovered PMID:12734196 original expresses the human cadherin-24 long form in A431D cells and recovers p120 in its cellular cadherin complex. Official Q86UP0-1 is the long product. The evidence supports cadherin binding at controlled co-immunoprecipitation scope; it does not require p120 to carry cadherin-24 extracellular adhesion activity or prove direct purified pairwise contact. Supporting Evidence: |
| GO:0045296 cadherin binding | IPI PMID:12734196 Characterization of cadherin-24, a novel alternatively splic... | ACCEPT | Summary: p120 associates with short cadherin-24. Reason: The original separately tests the human cadherin-24 short product and recovers a p120-containing complex. Q86UP0-2 remains distinct from the long-form source. Shared p120 association does not imply identical affinities or equal extracellular adhesive activity of the cadherins. Supporting Evidence: |
| GO:0050821 protein stabilization | IMP PMID:14610055 A core function for p120-catenin in cadherin turnover. | ACCEPT | Summary: p120 protects cadherin surface stability. Reason: Depletion/rescue, pulse-chase and surface-biotinylation experiments establish cadherin stabilization. Initial synthesis/delivery remain largely unchanged while degradation accelerates after surface arrival. Internalization versus post-endocytic sorting remains unresolved; the evidence does not assign p120 protease inhibition or folding-chaperone activity. Supporting Evidence: |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | KEEP AS NON CORE | Summary: p120 peptides were detected in the parotid exosome fraction. Reason: Publisher Table S2 identifies CTNND1/old IPI00182469.2, supported by two peptide entries in Table S1. Both peptides occur in multiple current official products, so historical 1AB labeling does not establish a unique product. This positive fraction-localization result does not establish secretion machinery or an exosome-biogenesis function. Supporting Evidence: |
| GO:0070161 anchoring junction | EXP PMID:18343367 P120-catenin is a novel desmoglein 3 interacting partner: id... | ACCEPT | Summary: p120 associates with anchoring junctions. Reason: Cadherin complexes and independent adherens-junction observations establish the broad anchoring-junction location. The partially accessible DSG3 source distinguishes its p120-associated free surface pool from desmosomes. The experimental assertion is retained with curator deference and that compartment limit. Supporting Evidence: |
| GO:0070161 anchoring junction | IEA GO_REF:0000044 | ACCEPT | Summary: The curated location mapping is appropriate. Reason: The UniProt cell-junction mapping agrees with p120 in cadherin-associated anchoring junctions. This broad location does not establish every junction type or every product, nor does the DSG3 source establish p120 as a mature-desmosome component. Supporting Evidence: GO_REF:0000044 |
| GO:0098609 cell-cell adhesion | IBA GO_REF:0000033 | ACCEPT | Summary: p120 contributes to conserved cell-cell adhesion. Reason: The actual ancestral placement and cadherin stabilization experiments support conserved adhesion participation. p120 performs intracellular binding and retention that sustains adhesive contacts; cadherins perform extracellular trans-cell binding. Supporting Evidence: GO_REF:0000033 |
| GO:0098609 cell-cell adhesion | IEA GO_REF:0000002 | ACCEPT | Summary: The family mapping agrees with performed adhesion biology. Reason: The literal IPR028435 membership agrees with the experimentally established cadherin-binding and retention role. This is positive adhesion-process participation through an intracellular component; it does not assign p120 cadherin extracellular binding. Supporting Evidence: GO_REF:0000002 |
| GO:0098632 cell-cell adhesion mediator activity | ISS GO_REF:0000024 | MODIFY | Summary: Cadherin binding captures the measured partner. Reason: The mouse Ctnnd1 donor and GO-CAM link are preserved. Actual human HUVEC imaging and VE-cadherin binding-site mutants place p120 on the intracellular tail, with dissociation preceding junctional trafficking. GO:0098632 requires cell-surface binding to an extracellular component of another cell. Cadherin binding captures the supported p120 activity without transferring the cadherin trans-cell role or rejecting its angiogenic contribution. Proposed replacements: cadherin binding Supporting Evidence: GO_REF:0000024 |
| GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels | IDA PMID:18602475 Regulation of AMPA receptor trafficking by delta-catenin. | UNDECIDED | Summary: The CTNND1-specific receptor-trafficking assertion is unresolved. Reason: The accessible abstract and publisher sections emphasize delta-catenin/GRIP/GluR2. Complete original experiments were unrecovered, so CTNND1 participation cannot be adjudicated; the title does not justify a wrong-paralog verdict. Supporting Evidence: |
| GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels | IEP PMID:18602475 Regulation of AMPA receptor trafficking by delta-catenin. | UNDECIDED | Summary: The expression-supported CTNND1 assertion is unresolved. Reason: The available delta-catenin-focused material does not expose the CTNND1-specific expression evidence. Preserve the original IEP assertion without inferring misattribution from the abstract. Supporting Evidence: |
| GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels | IMP PMID:18602475 Regulation of AMPA receptor trafficking by delta-catenin. | UNDECIDED | Summary: The CTNND1-specific perturbation evidence is unresolved. Reason: Complete original Methods and Results were inaccessible. The delta-catenin-focused abstract does not show whether CTNND1 was also tested, so it cannot justify rejection of the experimental assertion. Supporting Evidence: |
| GO:0140311 protein sequestering activity | IDA PMID:21998202 RPTPΞΌ tyrosine phosphatase promotes adipogenic differentiati... | UNDECIDED | Summary: The specific protein-sequestering mechanism remains unresolved. Reason: GO:0140311 requires binding the protein being sequestered. GO-CAM 613aae0000000885 specifies SLC2A4/GLUT4 as the input, while the cited mouse p120 experiments in 3T3-L1 cells establish reduced GLUT4 surface trafficking and its recovery upon RPTPΞΌ coexpression. The paper discusses Rho/Rac regulation but does not establish a p120βGLUT4 sequestration interface or show that GDP-dissociation inhibition mediates this trafficking effect. The independently supported Rho GDI activity therefore does not resolve or replace this source-specific sequestration assertion. Genuine mechanistic uncertainty remains despite access to the relevant main passages; no absence of binding is inferred. Supporting Evidence: |
| GO:0150107 positive regulation of protein localization to cell-cell junction | IMP PMID:18343367 P120-catenin is a novel desmoglein 3 interacting partner: id... | ACCEPT | Summary: p120 promotes junctional retention of cadherins. Reason: The curated IMP and accessible DSG3 experiments support retention at the plasma membrane through p120 association. The deletion perturbs DSG3βs intracellular p120-association region, not CTNND1 itself; reduced surface colocalization and accelerated turnover are therefore evidence for the cadherin-side interaction requirement. The established junctional stabilization role supports retention with curator deference to the unavailable complete original assay. This does not imply initial secretory transport or p120 incorporation into mature desmosomes. Supporting Evidence: |
| GO:1902532 negative regulation of intracellular signal transduction | IMP PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | KEEP AS NON CORE | Summary: p120 limits the LPP3 signaling response. Reason: Figure 3 supports a density-dependent negative effect; it is not universal inhibition of intracellular signaling. Supporting Evidence: |
| GO:1905554 negative regulation of blood vessel branching | IMP PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | MARK AS OVER ANNOTATED | Summary: A negative branching role is not established at this source scope. Reason: Branching experiments do not isolate p120 as a negative regulator; depletion also disrupts junctions. Retain that distinction from transcriptional inhibition. Supporting Evidence: |
| GO:0005094 Rho GDP-dissociation inhibitor activity | ISS PMID:17194753 Specific phosphorylation of p120-catenin regulatory domain d... | NEW | Summary: Long human p120 products are inferred to inhibit Rho GDP dissociation. Reason: Purified mouse p120 directly inhibits Rho GDP release in two original studies, with binding, truncation and regulatory-site tests. The independent later direct binding/GDP assays strengthen the activity evidence and address the earlier co-purifying-factor caveat. The paper-cited 911-aa mouse sequence aligns across its full length to a human long product with 887 identical paired residues and conserved tested regulatory positions/basic motif. This supports an explicit human sequence inference, not a human IDA or equal activity of all 32 products. Historical mouse 1B does not identify current human 1B; the best matching current human sequence is O60716-8. No additional Rho process annotation is proposed. Supporting Evidence: PMID:10980705 p120 selectively inhibits RhoA activity in vitro and in vivo file:human/CTNND1/CTNND1-bioinformatics/RESULTS.md |
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Download this section (compressed HTML)Q: Which exact human p120 products retain Rho GDP-dissociation inhibition, and how do initiation sites, exon B and phosphorylation alter that activity?
Q: Does p120 binding directly inhibit LPP3 phosphatase catalysis, or mainly change its localization and downstream beta-catenin/LEF1 signaling?
Q: Does the GLUT4-linked GO-CAM sequestration activity have a demonstrated p120βGLUT4 physical interface, as distinct from Rho/Rac-dependent trafficking regulation?
Q: Can the original p120 target assays be resolved for the Kaiso-family, PLEKHA7, AMPA-trafficking and midbody-screen sources?
Q: Should the inherited extracellular adhesion-mediator activity be reconciled with the intracellular cadherin-tail role recorded in the endothelial source and GO-CAM?
Experiment: Compare sequence-verified human start/splice products in matched cadherin-tail binding and surface-turnover assays.
Hypothesis: Product-specific terminal sequences regulate localization and turnover control even when the shared armadillo interface retains cadherin binding.
Experiment: Measure purified LPP3 substrate turnover with and without defined p120 constructs separately from LEF1 reporters.
Hypothesis: The signaling effect may occur without direct inhibition of phosphatase chemistry.
Experiment: Measure intrinsic and GEF-stimulated RhoA GDP release using purified, sequence-verified human p120 start/splice products, with and without cadherin tails and controlled phosphorylation. Include the mapped mouse construct, no-p120 and inactive-truncation controls.
Hypothesis: Retention of the mapped regulatory regions predicts Rho GDP-dissociation inhibition in a subset of long human products, modulated by cadherin occupancy and phosphorylation.
What is not known β curated, literature-grounded statements of the open unknowns (the inverse of core functions).
Gap: The capacity of individual human p120 start/splice products to inhibit RhoA GDP dissociation, and its quantitative dependence on cadherin occupancy and phosphorylation, remains unresolved.
OPEN BIOLOGY RESIDUAL_SUBGAP
What is known: Direct mouse GDP-release assays and conserved regulatory sequences support the human Rho GDI inference. Reconstruction of all 32 human products establishes their sequences, not their individual activities; the historical mouse assay name does not identify an equivalent human splice product.
Significance: Product-specific activity would distinguish junctional cadherin stabilization from the regulation of a cadherin-free Rho-inhibitory pool.
What would resolve it: Measure intrinsic and GEF-stimulated RhoA GDP release with purified, sequence-verified human start/splice products, with matched phosphorylation states and cadherin-tail competition.
Provenance (the field's own admissions):
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