APC is a large, multidomain tumor suppressor that coordinates beta-catenin turnover and cytoskeletal organization. Its central repeats bind beta-catenin and its SAMP motifs engage AXIN in the cytoplasmic destruction complex, helping recruit and present beta-catenin to kinases and ubiquitination machinery. Its C-terminal regions bind microtubules, associate with microtubule-end proteins and directly recruit actin monomers to nucleate filaments. These activities contribute to cell polarity, migration and accurate mitosis. APC also binds regulatory partners, including Asef-family nucleotide-exchange factors, whose autoinhibition it can relieve. APC occupies cytoplasmic, cortical, junctional and nuclear pools; truncating variants disrupt several of these separable functions and underlie familial adenomatous polyposis and many sporadic colorectal cancers.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000281 mitotic cytokinesis | IMP PMID:17570218 APC inactivation associates with abnormal mitosis completion... | ACCEPT | Summary: Mitotic cytokinesis fits the established APC function or location. Reason: PMID17570218 compares APC-mutant human tissue and mouse models and uses video microscopy of cytokinesis. Retain APC involvement in mitotic division; division defects do not assign APC contractile-motor chemistry. Supporting Evidence: |
| GO:0000776 kinetochore | IDA PMID:11283619 A role for the Adenomatous Polyposis Coli protein in chromos... | ACCEPT | Summary: Kinetochore fits the established APC function or location. Reason: PMID11283619 explicitly places APC at kinetochore-embedded microtubule ends and associates it with Bub proteins. This supports the kinetochore location, separately from the unverified centrosome row. Supporting Evidence: |
| GO:0001708 cell fate specification | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cell fate specification is supported but secondary to APCβs principal activities. Reason: Retain the PAINT ancestral-function inference. Cell-fate effects are developmental outputs of APC-mediated Wnt regulation, rather than a separate molecular activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0003170 heart valve development | ISS GO_REF:0000024 | UNDECIDED | Summary: Source-local evidence remains unresolved for heart valve development. Reason: The ISS donor and its anatomical assay have not been traced sufficiently to adjudicate this specific heart-development assertion; do not reject it from its specificity alone. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:A0A0R4IWH7 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0003203 endocardial cushion morphogenesis | ISS GO_REF:0000024 | UNDECIDED | Summary: Source-local evidence remains unresolved for endocardial cushion morphogenesis. Reason: The ISS donor and its anatomical assay have not been traced sufficiently to adjudicate this specific heart-development assertion; do not reject it from its specificity alone. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:A0A0R4IWH7 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0005515 protein binding | IPI PMID:10811618 Structural basis of the Axin-adenomatous polyposis coli inte... | MODIFY | Summary: APC SAMP3 binds the isolated RGS-like domain of AXIN. Reason: The original source directly resolves APC binding to the isolated AXIN RGS-like domain using SAMP3 pull-downs, an unbound GST control and the crystal complex. The official 1EMU record maps the APC peptide to human P25054 and identifies the AXIN component as human. GO:0019904 captures this experimentally defined domain-specific interaction; it does not substitute beta-catenin binding or assign APC a G-protein-regulatory activity. The normal publication cache is abstract-only; targeted original Results, figure legends and binding Methods were read separately. Proposed replacements: protein domain specific binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10947987 Asef, a link between the tumor suppressor APC and G-protein ... | MODIFY | Summary: Refine this source-specific assertion to guanyl nucleotide exchange factor activator activity. Reason: PMID10947987 reports APC binding to Asef and increasing its exchange activity; the inspected original indexed binding Results include GST and translation controls. APC activates the GEF rather than catalyzing nucleotide exchange itself. The original partner and isoform identifiers are preserved; the current read does not establish that every listed modern isoform was independently assayed, and reagent species is not inferred from the human annotation. Proposed replacements: guanyl nucleotide exchange factor activator activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10947987 Asef, a link between the tumor suppressor APC and G-protein ... | MODIFY | Summary: Refine this source-specific assertion to guanyl nucleotide exchange factor activator activity. Reason: PMID10947987 reports APC binding to Asef and increasing its exchange activity; the inspected original indexed binding Results include GST and translation controls. APC activates the GEF rather than catalyzing nucleotide exchange itself. The original partner and isoform identifiers are preserved; the current read does not establish that every listed modern isoform was independently assayed, and reagent species is not inferred from the human annotation. Proposed replacements: guanyl nucleotide exchange factor activator activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11283619 A role for the Adenomatous Polyposis Coli protein in chromos... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID11283619 reports APC in a complex with Bub1 and Bub3 at mitotic kinetochores. The original Bub3 association is retained as non-core; association does not make APC a checkpoint kinase. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11389840 Siah-1 mediates a novel beta-catenin degradation pathway lin... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID11389840 explicitly reports the APC C terminus interacting with Siah1 during beta-catenin turnover. Retain the interaction without assigning APC the ligase activity of its partner. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11425858 Synergistic activation of the Wnt signaling pathway by Dvl a... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The available abstract describes a DVL/CKIepsilon/AXIN ternary complex; its APC target interaction has not been located. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:11425858 Synergistic activation of the Wnt signaling pathway by Dvl a... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The available abstract describes a DVL/CKIepsilon/AXIN ternary complex; its APC target interaction has not been located. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:11943150 Involvement of the telomeric protein Pin2/TRF1 in the regula... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 11943150 abstract assays Pin2/TRF1βEB1; target APCβEB1 result has not been read. This does not establish a wrong-paper attribution. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:11972058 Association and regulation of casein kinase 2 activity by ad... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: The actual PMID11972058 binding Results include CK2alpha-prime, which associates less strongly than CK2alpha. Preserve this source-specific binding assertion as non-core; the inhibitory fragment assay does not establish inhibition of every CK2 isoform separately. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11972058 Association and regulation of casein kinase 2 activity by ad... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: The actual PMID11972058 binding Results show APC association with CK2alpha and the holoenzyme. Retain the non-core binding record separately from this sourceβs specific kinase-inhibitor refinement; APC is not the kinase. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15161933 Comprehensive proteomic analysis of interphase and mitotic 1... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 15161933 abstract describes a 14-3-3-zeta proteomic screen but does not identify the APC target record. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:15327768 Mechanism of phosphorylation-dependent binding of APC to bet... | MODIFY | Summary: Refine this source-specific assertion to beta-catenin binding. Reason: This source directly characterizes an APCβbeta-catenin interaction, rather than merely listing a proteomic candidate. Refine the generic interaction to beta-catenin binding while preserving its original experimental reference, partner and qualifier. Existing beta-catenin-binding rows are corroborating records, not grounds to invent another row. Proposed replacements: beta-catenin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15327768 Mechanism of phosphorylation-dependent binding of APC to bet... | MODIFY | Summary: Refine this source-specific assertion to beta-catenin binding. Reason: This source directly characterizes an APCβbeta-catenin interaction, rather than merely listing a proteomic candidate. Refine the generic interaction to beta-catenin binding while preserving its original experimental reference, partner and qualifier. Existing beta-catenin-binding rows are corroborating records, not grounds to invent another row. Proposed replacements: beta-catenin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15327769 Crystal structure of a beta-catenin/APC complex reveals a cr... | MODIFY | Summary: Refine this source-specific assertion to beta-catenin binding. Reason: This source directly characterizes an APCβbeta-catenin interaction, rather than merely listing a proteomic candidate. Refine the generic interaction to beta-catenin binding while preserving its original experimental reference, partner and qualifier. Existing beta-catenin-binding rows are corroborating records, not grounds to invent another row. Proposed replacements: beta-catenin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16212417 Biosensor-based micro-affinity purification for the proteomi... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The source uses an APC beta-catenin-binding fragment for micro-affinity purification, but the recovered APCβbeta-catenin target result has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:16293619 Thermodynamics of beta-catenin-ligand interactions: the role... | MODIFY | Summary: Refine this source-specific assertion to beta-catenin binding. Reason: This source directly characterizes an APCβbeta-catenin interaction, rather than merely listing a proteomic candidate. Refine the generic interaction to beta-catenin binding while preserving its original experimental reference, partner and qualifier. Existing beta-catenin-binding rows are corroborating records, not grounds to invent another row. Proposed replacements: beta-catenin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16611247 Human scribble, a novel tumor suppressor identified as a tar... | MODIFY | Summary: Refine this source-specific assertion to PDZ domain binding. Reason: 16611247 explicitly reports APC C-terminal motif binding to SCRIB PDZ1/4 in its complete abstract. Same-source specific binding only; no autonomous scaffold/catalytic activity, no transfer of this refinement to unread screen rows72/73. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16753179 The third 20 amino acid repeat is the tightest binding site ... | MODIFY | Summary: Refine this source-specific assertion to beta-catenin binding. Reason: This source directly characterizes an APCβbeta-catenin interaction, rather than merely listing a proteomic candidate. Refine the generic interaction to beta-catenin binding while preserving its original experimental reference, partner and qualifier. Existing beta-catenin-binding rows are corroborating records, not grounds to invent another row. Proposed replacements: beta-catenin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17145773 Asef2 functions as a Cdc42 exchange factor and is stimulated... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The inspected Asef2 activation assay does not adjudicate this separate original partner/isoform-specific binding record. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:17145773 Asef2 functions as a Cdc42 exchange factor and is stimulated... | MODIFY | Summary: Refine this source-specific assertion to guanyl nucleotide exchange factor activator activity. Reason: PMID17145773 Fig4β5 document APCβAsef2 association and increased Asef2-mediated GDP exchange with purified MBP-APC ARM compared with MBP/control. The ARM205β885 construct was amplified from pancreatic tumor-cell cDNA; endogenous association was tested in human SW480 and Panc04-03 cells. This is a source-local GEF-activator mechanism, not APC exchange catalysis. The source partner/isoform remains intact; a separate modern isoform-specific assay is not inferred. Proposed replacements: guanyl nucleotide exchange factor activator activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17145773 Asef2 functions as a Cdc42 exchange factor and is stimulated... | MODIFY | Summary: Refine this source-specific assertion to guanyl nucleotide exchange factor activator activity. Reason: PMID17145773 Fig4β5 document APCβAsef2 association and increased Asef2-mediated GDP exchange with purified MBP-APC ARM compared with MBP/control. The ARM205β885 construct was amplified from pancreatic tumor-cell cDNA; endogenous association was tested in human SW480 and Panc04-03 cells. This is a source-local GEF-activator mechanism, not APC exchange catalysis. The source partner/isoform remains intact; a separate modern isoform-specific assay is not inferred. Proposed replacements: guanyl nucleotide exchange factor activator activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17145773 Asef2 functions as a Cdc42 exchange factor and is stimulated... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The inspected Asef2 activation assay does not adjudicate this separate original partner/isoform-specific binding record. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:17218255 Modeling of a human circadian mutation yields insights into ... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The available abstract centers on PER2/CKI clock regulation; the APC target assay has not been located. A different focus is not proof of misattribution. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:17240990 Energetics of peptide recognition by the second PDZ domain o... | MODIFY | Summary: Refine this source-specific assertion to PDZ domain binding. Reason: The original abstract explicitly reports that the APC C-terminal segment binds the second PDZ domain of human PTP1E, although less tightly than an earlier SPR estimate. This is a source-specific domain-binding result, so refine to PDZ domain binding. Weak affinity does not negate binding; the abstract does not establish all APC construct/species details or a physiological phosphatase-regulatory role. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17318191 Bcr-Abl stabilizes beta-catenin in chronic myeloid leukemia ... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 17318191 abstract and targeted original Fig4/Results concern Bcr-Abl/AXIN/GSK3 and beta-catenin; no APC-specific binding assay was identified in this bounded read. Do not borrow other beta-catenin papers to refine its IPI. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:17510365 Wilms tumor suppressor WTX negatively regulates WNT/beta-cat... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID17510365 tandem-affinity/MS experiments place APC, AXIN1 and WTX in the same destruction-complex network. Retain the reported association as non-core; a purified APCβAXIN1 interface is not inferred from this particular coassembly result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17510365 Wilms tumor suppressor WTX negatively regulates WNT/beta-cat... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The abstract establishes the WTX-containing complex, but this particular APCβbeta-catenin pair assay has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:17510365 Wilms tumor suppressor WTX negatively regulates WNT/beta-cat... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID17510365 explicitly identifies APC in the WTX/AMER1 complex by tandem-affinity purification and MS. Retain the sourceβs experimental association without converting every complex member into a direct binary interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17588722 Htid-1, the human homolog of the Drosophila melanogaster l(2... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID17588722 reports endogenous APC association with Tid50/Tid48 and maps GST binding to the APC N-terminal armadillo region. This supports the non-core DNAJA3/Tid interaction; APC does not acquire chaperone catalysis. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17599059 Identification and characterization of Asef2, a guanine-nucl... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID17599059 maps Asef2 interaction to its ABR/SH3 region, with cellular activation by tumor-truncated APC. Retain this pair as non-core rather than borrowing the separate purified APC-ARM activation assay from PMID17145773 as this sourceβs provenance. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17599059 Identification and characterization of Asef2, a guanine-nucl... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID17599059 reports Asef2βAPC association and cellular effects of tumor-truncated APC. Preserve the originally annotated Asef2 isoform, while not claiming that its modern isoform identity was independently reconstructed from the available abstract. Retain the interaction as non-core. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17925383 AMER1 regulates the distribution of the tumor suppressor APC... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID17925383 reports AMER1 binding the APC armadillo region and recruiting APC to the plasma membrane. This establishes the pair; the lipid-binding function of AMER1 is not assigned to APC. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18281465 Trabid, a new positive regulator of Wnt-induced transcriptio... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: The original abstract directly reports that Trabid binds APC and deubiquitylates it. Retain this experimentally reported interaction as non-core; APC is the bound deubiquitylation substrate here, not the deubiquitinase. The abstract does not by itself reconstruct the complete binding assay or support an additional specific APC molecular activity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18502210 The armadillo repeat domain of the APC tumor suppressor prot... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: Original PMID18502210 Results2.1 identify Striatin among proteins associated with FLAG-human APCarm in HEK293T cells by MS, compared with empty tag. Retain the actual association as non-core; no new catalytic role is inferred. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18502210 The armadillo repeat domain of the APC tumor suppressor prot... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: Original PMID18502210 Results2.1 identify SG2NA/STRN3 in the FLAG-human APCarm experiment, not just a family-level analogy to Striatin. Retain the reported non-core association with its original partner. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18502210 The armadillo repeat domain of the APC tumor suppressor prot... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: Original PMID18502210 Results2.1 identify zinedin/STRN4 in the FLAG-human APCarm experiment. Retain the measured non-core association; the other family members are not being used as substitutes for this target result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19116273 Activated protein C ligation of ApoER2 (LRP8) causes Dab1-de... | REMOVE | Summary: The assay uses activated protein C, not the APC tumor suppressor. Reason: Actual source Methods/SPR and its APC-V5/coagulation context identify activated protein C (PROC), not adenomatous polyposis coli. The ApoER2/LRP8 assertion is misattributed to APC. This conclusion rests on the inspected experimental protein identity, not on a title or abstract mismatch; it does not assert that APC could never associate with LRP8. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19131971 The Axin1 scaffold protein promotes formation of a degradati... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 19131971 abstract describes the AXIN1βMYC complex; the APC-specific pair record has not been read. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:19632184 An EB1-binding motif acts as a microtubule tip localization ... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID19632184 identifies an APC SxIP motif recognized by EB1 in microtubule-tip targeting. The real EB1 interaction is retained as non-core; the separate APC plus-end annotation captures its functional context without inventing another row. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20224554 Binding of APC and dishevelled mediates Wnt5a-regulated foca... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: Original PMID20224554 Results/Fig2 test recombinant Dvl1 association with the APC armadillo region, including a dose-response binding experiment. Preserve this non-core pair and its assay scope; mixed host species are not used to infer construct identity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20224554 Binding of APC and dishevelled mediates Wnt5a-regulated foca... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: Original PMID20224554 Results/Fig2 identify endogenous Dvl2βAPC coassociation in HeLaS3 cells, with additional experiments in other hosts. Retain the actual non-core association without describing it as the purified Dvl1 assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20224554 Binding of APC and dishevelled mediates Wnt5a-regulated foca... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The sourceβs Dvl1/Dvl2 experiments do not establish the separate originally listed P54792 partner result. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 20936779 abstract describes the MAPK interactome, not the APCβJUP target row. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 20936779 abstract describes the MAPK interactome, not the APCβCTNNA1 target row. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:20936779 A human MAP kinase interactome. | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 20936779 abstract describes the MAPK interactome, not the APCβERBIN target row. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:21311754 Rho GTPase Cdc42 is a direct interacting partner of Adenomat... | MODIFY | Summary: Refine this source-specific assertion to small GTPase binding. Reason: The actual source assays a human APC fragment against active versus GDP-state Cdc42 and corroborates interaction in cells. Small-GTPase binding is the appropriate refinement of this paperβs own interaction result. The in-vitro APC fragment was translated, not purified full-length APC; no GEF/GAP catalysis is implied. Proposed replacements: small GTPase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21858148 Molecular basis for the recognition of adenomatous polyposis... | MODIFY | Summary: Refine this source-specific assertion to PDZ domain binding. Reason: 21858148 actual Results/Fig1β3 compare APC-C11/C4 with purified DLG1 PDZ1/2/3 by pull-down, ITC and structures. Same-source specific binding only; no autonomous scaffold/catalytic activity, no transfer of this refinement to unread screen rows72/73. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22000517 Crystal structures of the armadillo repeat domain of adenoma... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: The original abstract reports the crystal structure of the APC armadillo domain in complex with the tyrosine-rich region of Sam68, together with mutation and phosphorylation tests of complex formation. This establishes the reported interaction more directly than a screen-level prediction. Retain it as a non-core association; APC does not thereby acquire RNA-binding or splicing catalysis, and complete reagent provenance is not inferred from the abstract. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22056988 Nuclear PKM2 regulates Ξ²-catenin transactivation upon EGFR a... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The available abstract describes PKM2βbeta-catenin nuclear signaling; the APC target pair experiment has not been located. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:22128170 Amer2 protein is a novel negative regulator of Wnt/Ξ²-catenin... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID22128170 reports direct AMER2βAPC association and membrane recruitment. Retain the interaction as non-core; AMER2βs lipid-binding and developmental contexts are not new APC activities. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22682247 Wnt signaling through inhibition of Ξ²-catenin degradation in... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID22682247 examines an intact endogenous AXIN1/APC destruction-complex context. Retain the reported AXIN1 association as non-core, without settling the competing disassembly models or claiming every contact is direct. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22682247 Wnt signaling through inhibition of Ξ²-catenin degradation in... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The intact AXIN1-complex model is clear, but the source-specific APCβbeta-catenin interaction experiment has not been adjudicated. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:23185543 Structure of the human discs large 1 PDZ2- adenomatous polyp... | MODIFY | Summary: Refine this source-specific assertion to PDZ domain binding. Reason: 23185543 actual Methods/Fig1 and deposited4G69 show the human APC C-terminal peptide bound to human DLG1 PDZ2. Same-source specific binding only; no autonomous scaffold/catalytic activity, no transfer of this refinement to unread screen rows72/73. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24251807 Adenomatous polyposis coli (APC) membrane recruitment 3, a m... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 24251807 abstract establishes AMER3 binding to APC and to AMER1; its statement about AMER1βAPC is background and does not identify the experimental APCβAMER1 pair in this paper. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:24251807 Adenomatous polyposis coli (APC) membrane recruitment 3, a m... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID24251807 explicitly reports AMER3 binding the APC armadillo domain. This supports its own non-core pair, distinct from the uninspected AMER1 pair cited to the same paper. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The publication profiles endogenous proximity-ligation interactions; the individual APC pair and antibody controls have not been examined. Proximity is not automatically a direct interface. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The publication profiles endogenous proximity-ligation interactions; the individual APC pair and antibody controls have not been examined. Proximity is not automatically a direct interface. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The publication profiles endogenous proximity-ligation interactions; the individual APC pair and antibody controls have not been examined. Proximity is not automatically a direct interface. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The publication profiles endogenous proximity-ligation interactions; the individual APC pair and antibody controls have not been examined. Proximity is not automatically a direct interface. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The quantitative HeLa interactome supplies a candidate association, but the individual APC pull-down/stoichiometry record has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 30126976 abstract describes PDZ-domain screens and selected validations but does not expose the target APCβDLG1 assay. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:30126976 Proteome-wide analysis of phospho-regulated PDZ domain inter... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: 30126976 abstract describes PDZ-domain screens and selected validations but does not expose the target APCβSCRIB assay. Retain the original source object. The unresolved point is the source-local target assay or table and its controls. |
| GO:0005515 protein binding | IPI PMID:31413325 HENA, heterogeneous network-based data set for Alzheimer's d... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The integrated Alzheimer network is accessible as general context; the original APC interaction experiment behind this record has not been traced. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The kinase interaction-network abstract does not adjudicate this APC target pair. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: BioPlex reports large 293T/HCT116 association networks; this APC target experiment and construct have not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: BioPlex reports large 293T/HCT116 association networks; this APC target experiment and construct have not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: BioPlex reports large 293T/HCT116 association networks; this APC target experiment and construct have not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The OpenCell study combines imaging and interaction data; the specific APC pair record remains uninspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The OpenCell study combines imaging and interaction data; the specific APC pair record remains uninspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The OpenCell study combines imaging and interaction data; the specific APC pair record remains uninspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36115835 Quantitative fragmentomics allow affinity mapping of interac... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The fragmentomics study measures PDZ-domain/motif interactions, but the individual APC peptideβpartner affinity record has not been read. Other APC PDZ structures cannot supply this row with new experimental provenance. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:36950384 Protein interaction studies in human induced neurons indicat... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The human induced-neuron network provides context, but its individual APCβbeta-catenin result has not been inspected. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:39009827 Proteome-scale characterisation of motif-based interactome r... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The motif-rewiring study examines disease-associated variants; the exact APC construct and target-binding result have not been read. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The multimodal U2OS map does not in its abstract expose this individual APC interaction assay. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The multimodal U2OS map does not in its abstract expose this individual APC interaction assay. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | UNDECIDED | Summary: Source-local evidence remains unresolved for protein binding. Reason: The multimodal U2OS map does not in its abstract expose this individual APC interaction assay. The original evidence and partner identifiers are preserved; neither a different abstract emphasis nor another paper supplies the missing source-local assay. |
| GO:0005515 protein binding | IPI PMID:8638125 Binding of APC to the human homolog of the Drosophila discs ... | MODIFY | Summary: Refine this source-specific assertion to PDZ domain binding. Reason: 8638125 complete abstract maps the interaction to APC C-terminus and the DLG homology repeat region; DHR is the PDZ-domain terminology, also recognized by the current GO term synonyms. Same-source specific binding only; no autonomous scaffold/catalytic activity, no transfer of this refinement to unread screen rows72/73. Proposed replacements: PDZ domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:8638126 Binding of GSK3beta to the APC-beta-catenin complex and regu... | MODIFY | Summary: Refine this source-specific assertion to beta-catenin binding. Reason: This source directly characterizes an APCβbeta-catenin interaction, rather than merely listing a proteomic candidate. Refine the generic interaction to beta-catenin binding while preserving its original experimental reference, partner and qualifier. Existing beta-catenin-binding rows are corroborating records, not grounds to invent another row. Proposed replacements: beta-catenin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9601641 Downregulation of beta-catenin by human Axin and its associa... | KEEP AS NON CORE | Summary: Protein binding is supported but secondary to APCβs principal activities. Reason: PMID9601641 explicitly reports human AXIN binding APC in vitro and endogenous complex association. Retain the real pair as non-core; kinase and destruction-complex functions are represented by separate supported annotations. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9707618 A novel frizzled gene identified in human esophageal carcino... | MODIFY | Summary: Refine this source-specific assertion to beta-catenin binding. Reason: This source directly characterizes an APCβbeta-catenin interaction, rather than merely listing a proteomic candidate. Refine the generic interaction to beta-catenin binding while preserving its original experimental reference, partner and qualifier. Existing beta-catenin-binding rows are corroborating records, not grounds to invent another row. Proposed replacements: beta-catenin binding Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:11035805 Adenomatous polyposis coli protein contains two nuclear expo... | ACCEPT | Summary: Nucleus fits the established APC function or location. Reason: PMID11035805 identifies two APC nuclear-export signals; mutating them accumulates full-length APC in the nucleus. This directly supports a shuttling nuclear APC pool. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:12072559 Subcellular distribution of Wnt pathway proteins in normal a... | ACCEPT | Summary: Nucleus fits the established APC function or location. Reason: PMID12072559 confocal imaging of human colon crypts, polyps and carcinomas detects nuclear APC. Retain the source-specific human-tissue location. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:12955080 Nuclear accumulation of full-length and truncated adenomatou... | ACCEPT | Summary: Nucleus fits the established APC function or location. Reason: PMID12955080 detects APC nuclear accumulation in proliferating carcinoma cells, including truncated and full-length forms. Retain this regulated nuclear pool. Supporting Evidence: |
| GO:0005634 nucleus | IEA GO_REF:0000117 | ACCEPT | Summary: Nucleus fits the established APC function or location. Reason: Independent NES-mutant experiments and human-colon microscopy establish nuclear APC, supporting the broad electronic inference. Nuclear location alone does not establish an autonomous transcription-factor activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00026330 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3361751 | KEEP AS NON CORE | Summary: Nucleoplasm is supported but secondary to APCβs principal activities. Reason: The Reactome promoter-exchange model places APC in a nuclear context, while its summary acknowledges unresolved recruitment details. Retain this modeled location as non-core rather than claiming a fully established molecular handoff. Supporting Evidence: Reactome:R-HSA-3361751 |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-3364042 | KEEP AS NON CORE | Summary: Nucleoplasm is supported but secondary to APCβs principal activities. Reason: The Reactome promoter-exchange model places APC in a nuclear context, while its summary acknowledges unresolved recruitment details. Retain this modeled location as non-core rather than claiming a fully established molecular handoff. Supporting Evidence: Reactome:R-HSA-3364042 |
| GO:0005737 cytoplasm | EXP PMID:10947987 Asef, a link between the tumor suppressor APC and G-protein ... | ACCEPT | Summary: Cytoplasm fits the established APC function or location. Reason: PMID10947987 reports APC/Asef colocalization in cytoplasmic and membrane-associated regions in the stated mammalian tissues/cells. This is consistent with APC cytoplasmic complexes; construct and host species remain distinct. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:11035805 Adenomatous polyposis coli protein contains two nuclear expo... | ACCEPT | Summary: Cytoplasm fits the established APC function or location. Reason: PMID11035805 nuclear-export experiments demonstrate APC shuttling between the cytoplasm and nucleus, directly supporting a cytoplasmic pool. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:12955080 Nuclear accumulation of full-length and truncated adenomatou... | ACCEPT | Summary: Cytoplasm fits the established APC function or location. Reason: PMID12955080 relates cytoplasmic versus nuclear APC distribution to the proliferative state of carcinoma cells. Preserve the cytoplasmic location alongside nuclear annotations. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:20937854 ErbB2 receptor controls microtubule capture by recruiting AC... | ACCEPT | Summary: Cytoplasm fits the established APC function or location. Reason: PMID20937854 reports relocalization of APC toward plasma membrane and ruffles during cortical microtubule capture. The cytoplasmic APC pool is coherent with this redistribution; the upstream ErbB2/ACF7 enzymes are separate. Supporting Evidence: |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Cytoplasm fits the established APC function or location. Reason: Experimental APC shuttling and distinct cytoplasmic destruction-complex/microtubule pools support this broad electronic cytoplasmic location. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00026971 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. UniProtKB-SubCell:SL-0086 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0005813 centrosome | IDA PMID:11283619 A role for the Adenomatous Polyposis Coli protein in chromos... | UNDECIDED | Summary: Source-local evidence remains unresolved for centrosome. Reason: The accessible mitotic source supports kinetochore localization but the exact centrosome-localization experiment has not been located. Dynein accumulation at centrosomes in another study is not direct APC localization evidence. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195251 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Assembly of the destruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195251 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195275 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Phosphorylation of APC component of the destruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195275 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195280 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Dissociation of beta-catenin from Axin and association of beta catenin with phospho-(20 aa) APC in the detruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195280 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195283 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Phosphorylation of phospho- (Ser45, Thr41) beta-catenin at Ser37 by GSK-3. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195283 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195287 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Phosphorylation of phospho-(Ser45 ) at Thr 41 by GSK-3. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195287 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195300 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Phosphorylation of phospho-(Ser45,Thr41,Ser37) at Ser33 by GSK-3. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195300 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195304 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Association of beta-catenin with the destruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195304 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-195318 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Phosphorylation of beta-catenin at Ser45 by CK1 alpha. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-195318 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-201685 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Beta-catenin is released from the destruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-201685 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-202947 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Caspase mediated cleavage of APC. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-202947 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130279 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Association of beta-catenin with the RBX1:SCF(beta-TrCP1) ubiquitin ligase complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-2130279 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130282 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Degradation of ubiquitinated beta catenin by the proteasome. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-2130282 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2130286 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Multi-ubiquitination of phospho-beta-catenin by RBX1:SCF(beta-TrCP1). The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-2130286 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4791278 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with APC truncation mutants have impaired AXIN binding. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-4791278 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4827388 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with CTNNB1 S45 mutants aren't phosphorylated by CK1alpha. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-4827388 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4839634 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with CTNNB1 S33 mutants aren't phosphorylated by GSK3beta. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-4839634 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4839635 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with CTNNB1 S37 mutants aren't phosphorylated by GSK3beta. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-4839635 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4839638 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with CTNNB1 T41 mutants aren't phosphorylated by GSK3beta. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-4839638 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4839734 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with AXIN mutants destabilize the destruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-4839734 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4839746 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Truncated AMER1 mutants destabilize the destruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-4839746 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5229343 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with AXIN is phosphorylated in the destruction complex. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-5229343 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5246693 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with APC is K63-polyubiquitinated. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-5246693 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5246696 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with APC truncation mutants are not K63 polyubiquitinated. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-5246696 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5339713 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Misspliced GSK3beta mutants stabilize beta-catenin levels. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-5339713 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6781905 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with ZRANB1 binds APC. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. Supporting Evidence: Reactome:R-HSA-6781905 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-209060 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Human APC is further phosphorylated by Murine GSK3beta. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. This mixed-species model includes human APC with murine kinases; it is not an all-human reconstitution. Supporting Evidence: Reactome:R-NUL-209060 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-209065 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Human APC is further phosphorylated by Murine CKIepsilon. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. This mixed-species model includes human APC with murine kinases; it is not an all-human reconstitution. Supporting Evidence: Reactome:R-NUL-209065 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-209132 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Human APC is initially phosphorylated by Murine CKIepsilon. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. This mixed-species model includes human APC with murine kinases; it is not an all-human reconstitution. Supporting Evidence: Reactome:R-NUL-209132 |
| GO:0005829 cytosol | TAS Reactome:R-NUL-209144 | ACCEPT | Summary: Cytosol fits the established APC function or location. Reason: Retain the curated cytosolic APC assertion associated with Human APC is finally phosphorylated by Murine GSK3beta. The recovered summary describes the reaction, rather than a new localization measurement; independent APC cytoplasmic-complex evidence supports this broad compartment. This mixed-species model includes human APC with murine kinases; it is not an all-human reconstitution. Supporting Evidence: Reactome:R-NUL-209144 |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | ACCEPT | Summary: Cytoskeleton fits the established APC function or location. Reason: The cytoskeletal location agrees with direct APC microtubule binding and stabilization. The UniProt-derived mapping is corroborated by experiments without claiming its complete historical derivation was reconstructed. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0090 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0005874 microtubule | IDA PMID:28057765 Insulin signaling regulates a functional interaction between... | ACCEPT | Summary: Microtubule fits the established APC function or location. Reason: PMID28057765 examines APC associated with the microtubule/dynein transport system. Human APC fragments are assayed with nonhuman components in the stated contexts; this supports microtubule association, not APC motor catalysis. Supporting Evidence: |
| GO:0005881 cytoplasmic microtubule | IBA GO_REF:0000033 | ACCEPT | Summary: Cytoplasmic microtubule fits the established APC function or location. Reason: The PAINT cellular-component inference agrees with experimental APC microtubule binding/stabilization. The full ancestral tree/MSA was not reconstructed; donor count or APC self-inclusion is not evidence of a defect. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0005886 plasma membrane | EXP PMID:10947987 Asef, a link between the tumor suppressor APC and G-protein ... | ACCEPT | Summary: Plasma membrane fits the established APC function or location. Reason: PMID10947987 reports APC/Asef colocalization in membrane-associated regions. This supports a cortical pool, without treating host species as construct identity or inferring direct APC lipid binding. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | UNDECIDED | Summary: Source-local evidence remains unresolved for plasma membrane. Reason: The specific Human Protein Atlas plasma-membrane image and antibody validation have not been inspected. Other studies support cortical APC, but do not validate this particular image-based source. |
| GO:0005886 plasma membrane | IDA PMID:16611247 Human scribble, a novel tumor suppressor identified as a tar... | ACCEPT | Summary: Plasma membrane fits the established APC function or location. Reason: PMID16611247 links APCβSCRIB association with APC recruitment at cell junctions. Retain the plasma-membrane-associated pool without assigning APC the transmembrane topology of an adhesion receptor. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:20937854 ErbB2 receptor controls microtubule capture by recruiting AC... | ACCEPT | Summary: Plasma membrane fits the established APC function or location. Reason: PMID20937854 explicitly reports APC relocalization to plasma membrane and ruffles during cortical microtubule capture. Supporting Evidence: |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Plasma membrane fits the established APC function or location. Reason: Experimentally observed APC recruitment by membrane-associated partners supports the UniProt-derived plasma-membrane location. It does not establish that APC directly binds membrane lipid. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0039 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0005912 adherens junction | IDA PMID:16611247 Human scribble, a novel tumor suppressor identified as a tar... | ACCEPT | Summary: Adherens junction fits the established APC function or location. Reason: PMID16611247 connects APC binding SCRIB PDZ domains with APC recruitment at adherens junctions. This supports the location independently of direct cadherin binding. Supporting Evidence: |
| GO:0005912 adherens junction | IEA GO_REF:0000044 | ACCEPT | Summary: Adherens junction fits the established APC function or location. Reason: APC recruitment to junctional complexes supports the UniProt-derived adherens-junction annotation; the existing experimental NOT cadherin binding is compatible with this indirect localization. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0009 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0005923 bicellular tight junction | IDA PMID:18502210 The armadillo repeat domain of the APC tumor suppressor prot... | ACCEPT | Summary: Bicellular tight junction fits the established APC function or location. Reason: PMID18502210 explicitly reports APC/Striatin colocalization in epithelial tight junctions. Preserve this junctional APC pool and distinguish it from the separate neurite-outgrowth experiments. Supporting Evidence: |
| GO:0006974 DNA damage response | IDA PMID:14728717 N-methyl-N'-nitro-N-nitrosoguanidine-induced senescence-like... | UNDECIDED | Summary: Source-local evidence remains unresolved for DNA damage response. Reason: The accessible full-text passages show APC-expression changes during MNNG-induced senescence. A direct APC role in the response is not established by those passages; retain uncertainty pending examination of a functional APC perturbation. Do not describe APC as a DNA-repair enzyme. |
| GO:0007026 negative regulation of microtubule depolymerization | IBA GO_REF:0000033 | ACCEPT | Summary: Negative regulation of microtubule depolymerization fits the established APC function or location. Reason: Direct microtubule association and stabilization are established APC functions. Preserve experimental and PAINT records without treating a short ancestral donor list as weak evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0007026 negative regulation of microtubule depolymerization | IDA PMID:11166179 Binding of the adenomatous polyposis coli protein to microtu... | ACCEPT | Summary: Negative regulation of microtubule depolymerization fits the established APC function or location. Reason: PMID11166179 explicitly reports that APC binding increases microtubule stability in vivo and in vitro, supporting negative regulation of depolymerization. Supporting Evidence: |
| GO:0007026 negative regulation of microtubule depolymerization | IMP PMID:17192415 Lack of adenomatous polyposis coli protein correlates with a... | ACCEPT | Summary: Negative regulation of microtubule depolymerization fits the established APC function or location. Reason: PMID17192415 connects APC depletion with reduced microtubule stability, fewer protrusions and impaired migration. Retain the existing stabilization process, corroborated independently by direct binding assays. Supporting Evidence: |
| GO:0007094 mitotic spindle assembly checkpoint signaling | IMP PMID:17227893 Loss of APC induces polyploidy as a result of a combination ... | ACCEPT | Summary: Mitotic spindle assembly checkpoint signaling fits the established APC function or location. Reason: Human U2OS APC depletion reduces kinetochore tension, checkpoint recruitment and the mitotic delay; the actual body supports APC participation in chromosome-spindle checkpoint regulation. Supporting Evidence: |
| GO:0007155 cell adhesion | NAS PMID:8259518 Association of the APC gene product with beta-catenin. | KEEP AS NON CORE | Summary: Cell adhesion is supported but secondary to APCβs principal activities. Reason: Retain the curatorβs non-traceable-author-statement adhesion association as a contextual function. Beta-catenin association alone is not a complete adhesion mechanism; APCβs direct cytoskeletal and junctional roles provide broader biological context. Supporting Evidence: |
| GO:0007389 pattern specification process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Pattern specification process is supported but secondary to APCβs principal activities. Reason: Retain the phylogenetic inference of developmental function, while distinguishing patterning or nervous-system outputs from APCβs core binding/scaffolding and cytoskeletal activities. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0007399 nervous system development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Nervous system development is supported but secondary to APCβs principal activities. Reason: Retain the phylogenetic inference of developmental function, while distinguishing patterning or nervous-system outputs from APCβs core binding/scaffolding and cytoskeletal activities. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0008013 beta-catenin binding | EXP PMID:15327768 Mechanism of phosphorylation-dependent binding of APC to bet... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: Beta-catenin binding is a central APC activity supported by direct binding and structural studies. Preserve the original source and evidence, including the explicitly nonhuman beta-catenin partner where present, without claiming every study used only human proteins. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IBA GO_REF:0000033 | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: Beta-catenin binding is a central APC activity supported by direct binding and structural studies. Preserve the original source and evidence, including the explicitly nonhuman beta-catenin partner where present, without claiming every study used only human proteins. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0008013 beta-catenin binding | IDA PMID:7806582 E-cadherin and APC compete for the interaction with beta-cat... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: Beta-catenin binding is a central APC activity supported by direct binding and structural studies. Preserve the original source and evidence, including the explicitly nonhuman beta-catenin partner where present, without claiming every study used only human proteins. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IEA GO_REF:0000120 | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: Beta-catenin binding is a central APC activity supported by direct binding and structural studies. Preserve the original source and evidence, including the explicitly nonhuman beta-catenin partner where present, without claiming every study used only human proteins. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00093020 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009224 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009232 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009240 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR026818 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0008013 beta-catenin binding | IPI PMID:10773885 Regulation and function of the interaction between the APC t... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: PMID10773885 distinguishes APC binding regions and their interactions with EB1, beta-catenin and microtubules. Preserve the curatorβs beta-catenin pair and existing specific activity, without claiming every molecular interface in the study was independently reconstructed. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IPI PMID:11533658 Pin1 regulates turnover and subcellular localization of beta... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: PMID11533658 explicitly describes Pin1 inhibiting the APCβbeta-catenin interaction. Preserve this specific binding annotation; the isomerase activity belongs to Pin1. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IPI PMID:15327768 Mechanism of phosphorylation-dependent binding of APC to bet... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: Beta-catenin binding is a central APC activity supported by direct binding and structural studies. Preserve the original source and evidence, including the explicitly nonhuman beta-catenin partner where present, without claiming every study used only human proteins. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IPI PMID:16753179 The third 20 amino acid repeat is the tightest binding site ... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: Beta-catenin binding is a central APC activity supported by direct binding and structural studies. Preserve the original source and evidence, including the explicitly nonhuman beta-catenin partner where present, without claiming every study used only human proteins. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IPI PMID:7890674 The APC protein and E-cadherin form similar but independent ... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: PMID7890674 reports purified-protein and two-hybrid APCβbeta-catenin association, distinct from its negative APCβE-cadherin tests. Supporting Evidence: |
| GO:0008013 beta-catenin binding | IPI PMID:9707618 A novel frizzled gene identified in human esophageal carcino... | ACCEPT | Summary: Beta-catenin binding fits the established APC function or location. Reason: PMID9707618 reports increased APCβbeta-catenin complex formation after FzE3 manipulations. Retain the specific binding activity while distinguishing cellular association from purified binary affinity. Supporting Evidence: |
| GO:0008017 microtubule binding | IBA GO_REF:0000033 | ACCEPT | Summary: Microtubule binding fits the established APC function or location. Reason: APC directly binds microtubules through its C-terminal region. This is a core activity supported by experiments and consistent PAINT/InterPro inferences. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0008017 microtubule binding | IDA PMID:11166179 Binding of the adenomatous polyposis coli protein to microtu... | ACCEPT | Summary: Microtubule binding fits the established APC function or location. Reason: APC directly binds microtubules through its C-terminal region. This is a core activity supported by experiments and consistent PAINT/InterPro inferences. Supporting Evidence: |
| GO:0008017 microtubule binding | IDA PMID:16188939 The adenomatous polyposis coli protein (APC) exists in two d... | ACCEPT | Summary: Microtubule binding fits the established APC function or location. Reason: APC directly binds microtubules through its C-terminal region. This is a core activity supported by experiments and consistent PAINT/InterPro inferences. Supporting Evidence: |
| GO:0008017 microtubule binding | IEA GO_REF:0000120 | ACCEPT | Summary: Microtubule binding fits the established APC function or location. Reason: APC directly binds microtubules through its C-terminal region. This is a core activity supported by experiments and consistent PAINT/InterPro inferences. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00043642 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009234 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0008285 negative regulation of cell population proliferation | IDA PMID:8521819 The tumour suppressor gene product APC blocks cell cycle pro... | KEEP AS NON CORE | Summary: Negative regulation of cell population proliferation is supported but secondary to APCβs principal activities. Reason: Reduced proliferation is a well-supported downstream consequence of APC-mediated signaling and cell-cycle regulation. Retain the process annotation as non-core, without proposing a separate catalytic activity. Supporting Evidence: |
| GO:0008285 negative regulation of cell population proliferation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Negative regulation of cell population proliferation is supported but secondary to APCβs principal activities. Reason: Reduced proliferation is a well-supported downstream consequence of APC-mediated signaling and cell-cycle regulation. Retain the process annotation as non-core, without proposing a separate catalytic activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00027539 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0008286 insulin receptor signaling pathway | IMP PMID:28057765 Insulin signaling regulates a functional interaction between... | KEEP AS NON CORE | Summary: Insulin receptor signaling pathway is supported but secondary to APCβs principal activities. Reason: The source links insulin/GSK3-dependent dynein redistribution to APC in experiments with mixed-species reagents and mouse-colon physiology. Retain this signaling context as non-core; APC is not asserted to be the insulin receptor or dynein motor. Supporting Evidence: |
| GO:0015630 microtubule cytoskeleton | IEA GO_REF:0000117 | ACCEPT | Summary: Microtubule cytoskeleton fits the established APC function or location. Reason: APC directly associates with microtubules and their end-binding partners, supporting the electronic microtubule-cytoskeleton component annotation. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00029268 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0016055 Wnt signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: Wnt signaling pathway fits the established APC function or location. Reason: APC organizes beta-catenin-regulatory complexes, supporting the broad InterPro-derived Wnt-process assignment without assigning APC kinase chemistry. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR009223 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009224 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009232 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009234 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. InterPro:IPR009240 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0016328 lateral plasma membrane | IDA PMID:12072559 Subcellular distribution of Wnt pathway proteins in normal a... | ACCEPT | Summary: Lateral plasma membrane fits the established APC function or location. Reason: PMID12072559 directly detects APC and AXIN at lateral borders of human colon cells by tissue microscopy. Supporting Evidence: |
| GO:0016342 catenin complex | IBA GO_REF:0000033 | UNDECIDED | Summary: Membership in the specifically defined cadherin-associated catenin complex remains unresolved. Reason: GO:0016342 specifically describes the cadherin-associated catenin adhesion complex, not every APCβbeta-catenin assembly. The PAINT node PTN000288612 and its target-to-node inheritance for that exact complex have not been reconstructed. Preserve this IBA as uncertain; target beta-catenin binding and destruction-complex membership do not establish the narrower adhesion assembly, and neither donor count nor self-inclusion is a failure argument. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0016342 catenin complex | IDA PMID:7806582 E-cadherin and APC compete for the interaction with beta-cat... | UNDECIDED | Summary: Membership in the specifically defined cadherin-associated catenin complex remains unresolved. Reason: The current GO:0016342 definition concerns the E-cadherin/catenin actin-linkage complex. PMID7806582 explicitly distinguishes alternative APC-containing and E-cadherin-containing catenin complexes in its available abstract. The full source-local assay behind this exact IDA compartment mapping has not been inspected, so preserve uncertainty rather than treating any beta-catenin complex as sufficient. The separate NOT direct cadherin-binding result does not prove that indirect membership is impossible. Supporting Evidence: |
| GO:0016342 catenin complex | IEA GO_REF:0000117 | UNDECIDED | Summary: Membership in the specifically defined cadherin-associated catenin complex remains unresolved. Reason: The current GO:0016342 definition is the cadherin-associated catenin adhesion assembly. The exact ARBA00086680 rule premise and target mapping to that assembly have not been reconstructed. APC beta-catenin binding and cytoplasmic destruction-complex membership alone cannot validate this narrower electronic complex assertion; retain uncertainty without declaring the rule or interaction false. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00086680 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0016477 cell migration | IBA GO_REF:0000033 | ACCEPT | Summary: Cell migration fits the established APC function or location. Reason: APC coordinates microtubule and actin organization during cell migration. The experiments and PAINT assignment support this direct cytoskeletal participation rather than only a secondary disease phenotype. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0016477 cell migration | IMP PMID:19151759 Asef2 and Neurabin2 cooperatively regulate actin cytoskeleta... | ACCEPT | Summary: Cell migration fits the established APC function or location. Reason: PMID19151759 connects APC/Asef2/Neurabin2 accumulation at lamellipodia and membrane ruffles with HGF-induced HeLa migration. APC contributes structural/regulatory work; it is not the GTPase exchange enzyme. Supporting Evidence: |
| GO:0019887 protein kinase regulator activity | IDA PMID:11972058 Association and regulation of casein kinase 2 activity by ad... | MODIFY | Summary: Refine this source-specific assertion to protein serine/threonine kinase inhibitor activity. Reason: PMID11972058 reports dose-dependent CK2 inhibition by C-terminal APC fragments, supporting the serine/threonine-kinase inhibitor refinement. The original Methods explicitly derive the APC2086β2843,2086β2394,2226β2560 and2518β2843 fragments from a human fetal-fibroblast cDNA library. The pig-brain full-length APC preparation is a separate assay; this review does not describe purified full-length human APC or assign APC kinase catalysis. Proposed replacements: protein serine/threonine kinase inhibitor activity Supporting Evidence: |
| GO:0019901 protein kinase binding | IDA PMID:24130866 Large extent of disorder in Adenomatous Polyposis Coli offer... | ACCEPT | Summary: Protein kinase binding fits the established APC function or location. Reason: PMID24130866 examines the disordered APC mutation-cluster region and CK1 accessibility in vitro. Preserve the existing kinase-binding annotation as a scaffold/substrate interaction; phosphorylation does not make APC a kinase. Supporting Evidence: |
| GO:0019901 protein kinase binding | IPI PMID:8638126 Binding of GSK3beta to the APC-beta-catenin complex and regu... | ACCEPT | Summary: Protein kinase binding fits the established APC function or location. Reason: PMID8638126 places APC in a GSK3beta-containing regulatory complex and tests phosphorylation-sensitive beta-catenin binding. Retain kinase association without assigning kinase catalysis to APC. Supporting Evidence: |
| GO:0030027 lamellipodium | IDA PMID:19151759 Asef2 and Neurabin2 cooperatively regulate actin cytoskeleta... | ACCEPT | Summary: Lamellipodium fits the established APC function or location. Reason: PMID19151759 explicitly places APC with Asef2/Neurabin2 in lamellipodia after HGF treatment of HeLa cells. Supporting Evidence: |
| GO:0030027 lamellipodium | IEA GO_REF:0000044 | ACCEPT | Summary: Lamellipodium fits the established APC function or location. Reason: The UniProt-derived lamellipodial location is consistent with directly observed APC accumulation in HGF-induced protrusions. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0291 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0030054 cell junction | IEA GO_REF:0000117 | ACCEPT | Summary: Cell junction fits the established APC function or location. Reason: APC localization at adherens and tight junctions supports this broader electronic cell-junction component assertion. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00028333 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0030178 negative regulation of Wnt signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: Negative regulation of Wnt signaling pathway fits the established APC function or location. Reason: APC-mediated beta-catenin recruitment and turnover support the InterPro-derived negative-Wnt-regulation process. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR026818 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0030335 positive regulation of cell migration | IMP PMID:17192415 Lack of adenomatous polyposis coli protein correlates with a... | ACCEPT | Summary: Positive regulation of cell migration fits the established APC function or location. Reason: PMID17192415 reports decreased migration after APC loss, alongside reduced microtubule stability and protrusions. Retain positive regulation of migration in that source context. Supporting Evidence: |
| GO:0030877 beta-catenin destruction complex | IBA GO_REF:0000033 | ACCEPT | Summary: Beta-catenin destruction complex fits the established APC function or location. Reason: APC is a component of the beta-catenin destruction complex. Actual all-human biochemical reconstitution independently supports complex membership and substrate recruitment; APC is not the kinase or ubiquitin-transfer enzyme. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. Supporting Evidence: |
| GO:0030877 beta-catenin destruction complex | IDA PMID:16188939 The adenomatous polyposis coli protein (APC) exists in two d... | ACCEPT | Summary: Beta-catenin destruction complex fits the established APC function or location. Reason: APC is a component of the beta-catenin destruction complex. Actual all-human biochemical reconstitution independently supports complex membership and substrate recruitment; APC is not the kinase or ubiquitin-transfer enzyme. |
| GO:0030877 beta-catenin destruction complex | IDA PMID:8638126 Binding of GSK3beta to the APC-beta-catenin complex and regu... | ACCEPT | Summary: Beta-catenin destruction complex fits the established APC function or location. Reason: APC is a component of the beta-catenin destruction complex. Actual all-human biochemical reconstitution independently supports complex membership and substrate recruitment; APC is not the kinase or ubiquitin-transfer enzyme. |
| GO:0030877 beta-catenin destruction complex | IDA PMID:9601641 Downregulation of beta-catenin by human Axin and its associa... | ACCEPT | Summary: Beta-catenin destruction complex fits the established APC function or location. Reason: APC is a component of the beta-catenin destruction complex. Actual all-human biochemical reconstitution independently supports complex membership and substrate recruitment; APC is not the kinase or ubiquitin-transfer enzyme. |
| GO:0030877 beta-catenin destruction complex | NAS PMID:9601641 Downregulation of beta-catenin by human Axin and its associa... | ACCEPT | Summary: Beta-catenin destruction complex fits the established APC function or location. Reason: APC is a component of the beta-catenin destruction complex. Actual all-human biochemical reconstitution independently supports complex membership and substrate recruitment; APC is not the kinase or ubiquitin-transfer enzyme. |
| GO:0031256 leading edge membrane | IEA GO_REF:0000117 | ACCEPT | Summary: Leading edge membrane fits the established APC function or location. Reason: Observed APC accumulation in protrusive cortical regions supports the electronic leading-edge-membrane annotation; no direct lipid-binding chemistry is inferred. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00086462 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0031274 positive regulation of pseudopodium assembly | IMP PMID:17192415 Lack of adenomatous polyposis coli protein correlates with a... | ACCEPT | Summary: Positive regulation of pseudopodium assembly fits the established APC function or location. Reason: PMID17192415 directly links APC loss to disappearance of protrusions, alongside microtubule and migration defects. Retain the existing regulation of pseudopodium assembly. Supporting Evidence: |
| GO:0031625 ubiquitin protein ligase binding | IDA PMID:18076571 Putative tumor suppressor EDD interacts with and up-regulate... | KEEP AS NON CORE | Summary: Ubiquitin protein ligase binding is supported but secondary to APCβs principal activities. Reason: Retain the observed EDD/UBR5 ligase interaction as a regulatory association. It does not establish that APC is an E3 ligase or that the EDD experiment tested the later SCF-beta-TrCP interface. Supporting Evidence: |
| GO:0032587 ruffle membrane | IDA PMID:19151759 Asef2 and Neurabin2 cooperatively regulate actin cytoskeleta... | ACCEPT | Summary: Ruffle membrane fits the established APC function or location. Reason: PMID19151759 explicitly reports APC accumulation with Asef2/Neurabin2 in membrane ruffles after HGF stimulation. Supporting Evidence: |
| GO:0032587 ruffle membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Ruffle membrane fits the established APC function or location. Reason: The experimentally observed ruffle-associated APC pool supports the UniProt-derived ruffle-membrane location. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0301 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0032886 regulation of microtubule-based process | IMP PMID:20937854 ErbB2 receptor controls microtubule capture by recruiting AC... | ACCEPT | Summary: Regulation of microtubule-based process fits the established APC function or location. Reason: PMID20937854 describes APC relocalization in cortical microtubule capture downstream of ErbB2/ACF7 signaling. Retain regulation of the microtubule process without transferring the upstream enzymesβ chemistry. Supporting Evidence: |
| GO:0043065 positive regulation of apoptotic process | IMP PMID:17227893 Loss of APC induces polyploidy as a result of a combination ... | KEEP AS NON CORE | Summary: Positive regulation of apoptotic process is supported but secondary to APCβs principal activities. Reason: The actual human-cell experiments connect APC loss with reduced apoptosis under basal/mitotic-stress conditions. Apoptosis is retained as a downstream non-core effect, with staurosporine controls distinguished from the APC mechanism. Supporting Evidence: |
| GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process | NAS PMID:9601641 Downregulation of beta-catenin by human Axin and its associa... | ACCEPT | Summary: Proteasome-mediated ubiquitin-dependent protein catabolic process fits the established APC function or location. Reason: APC recruits and organizes beta-catenin for proteasomal destruction, rather than merely being consumed as the proteasome substrate. Its scaffold performs work in substrate processing, so involvement in this process is justified. |
| GO:0045295 gamma-catenin binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Gamma-catenin binding is supported but secondary to APCβs principal activities. Reason: Plakoglobin binding is supported but is secondary to APCβs better-established beta-catenin regulatory and cytoskeletal functions. Preserve the specific binding activity without making it a separate dominant core function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. |
| GO:0045295 gamma-catenin binding | IPI PMID:7890674 The APC protein and E-cadherin form similar but independent ... | KEEP AS NON CORE | Summary: Gamma-catenin binding is supported but secondary to APCβs principal activities. Reason: Plakoglobin binding is supported but is secondary to APCβs better-established beta-catenin regulatory and cytoskeletal functions. Preserve the specific binding activity without making it a separate dominant core function. Supporting Evidence: |
| GO:0045296 cadherin binding | IDA NOT PMID:7890674 The APC protein and E-cadherin form similar but independent ... | ACCEPT | Summary: Preserve the tested negative cadherin-binding assertion. Reason: Preserve the experimental NOT cadherin-binding assertion. Purified-protein/two-hybrid tests distinguish APC binding beta-catenin/plakoglobin from E-cadherin association under the tested conditions; junctional localization does not reverse this negative result. Supporting Evidence: |
| GO:0045732 positive regulation of protein catabolic process | IC PMID:16188939 The adenomatous polyposis coli protein (APC) exists in two d... | ACCEPT | Summary: Positive regulation of protein catabolic process fits the established APC function or location. Reason: APC promotes beta-catenin turnover through its scaffold and recruitment functions. These are active contributions to protein catabolism, not an assertion that APC is the protease or ubiquitin-transfer catalyst. |
| GO:0045732 positive regulation of protein catabolic process | IGI PMID:12952940 Wnt-5a inhibits the canonical Wnt pathway by promoting GSK-3... | ACCEPT | Summary: Positive regulation of protein catabolic process fits the established APC function or location. Reason: APC promotes beta-catenin turnover through its scaffold and recruitment functions. These are active contributions to protein catabolism, not an assertion that APC is the protease or ubiquitin-transfer catalyst. |
| GO:0045732 positive regulation of protein catabolic process | IGI PMID:12952940 Wnt-5a inhibits the canonical Wnt pathway by promoting GSK-3... | ACCEPT | Summary: Positive regulation of protein catabolic process fits the established APC function or location. Reason: APC promotes beta-catenin turnover through its scaffold and recruitment functions. These are active contributions to protein catabolism, not an assertion that APC is the protease or ubiquitin-transfer catalyst. |
| GO:0045736 negative regulation of cyclin-dependent protein serine/threonine kinase activity | IDA PMID:8521819 The tumour suppressor gene product APC blocks cell cycle pro... | KEEP AS NON CORE | Summary: Negative regulation of cyclin-dependent protein serine/threonine kinase activity is supported but secondary to APCβs principal activities. Reason: The source links APC to reduced cyclin/CDK activity as part of cell-cycle control. Retain this downstream regulation, without equating it to direct CDK-inhibitor molecular activity. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:18076571 Putative tumor suppressor EDD interacts with and up-regulate... | KEEP AS NON CORE | Summary: Perinuclear region of cytoplasm is supported but secondary to APCβs principal activities. Reason: Retain the sourceβs perinuclear APC localization in its regulatory context; it is not the principal compartment selected for the core functional model. Supporting Evidence: |
| GO:0051010 microtubule plus-end binding | IDA PMID:19632184 An EB1-binding motif acts as a microtubule tip localization ... | ACCEPT | Summary: Microtubule plus-end binding fits the established APC function or location. Reason: PMID19632184 identifies APC as an SxIP-containing EB1 partner in microtubule-tip targeting. Retain microtubule plus-end binding in that adaptor-mediated context, distinct from direct basic-region binding along microtubules. Supporting Evidence: |
| GO:0051988 regulation of attachment of spindle microtubules to kinetochore | IMP PMID:17227893 Loss of APC induces polyploidy as a result of a combination ... | ACCEPT | Summary: Regulation of attachment of spindle microtubules to kinetochore fits the established APC function or location. Reason: PMID17227893 APC depletion in human cells perturbs kinetochore tension and checkpoint recruitment, supporting regulation of spindle-microtubule attachment. Supporting Evidence: |
| GO:0051988 regulation of attachment of spindle microtubules to kinetochore | NAS PMID:11283619 A role for the Adenomatous Polyposis Coli protein in chromos... | ACCEPT | Summary: Regulation of attachment of spindle microtubules to kinetochore fits the established APC function or location. Reason: PMID11283619 places APC at kinetochore-associated microtubule ends and links APC truncation to chromosome-segregation abnormalities. Preserve the existing attachment-regulation assertion. Supporting Evidence: |
| GO:0060632 regulation of microtubule-based movement | IEP PMID:28057765 Insulin signaling regulates a functional interaction between... | ACCEPT | Summary: Regulation of microtubule-based movement fits the established APC function or location. Reason: Human APC fragments associate with dynein and APC influences microtubule-dependent transport. Retain regulation of movement while keeping the mixed-species reconstitution explicit and excluding motor activity for APC. Supporting Evidence: |
| GO:0065003 protein-containing complex assembly | IDA PMID:16188939 The adenomatous polyposis coli protein (APC) exists in two d... | ACCEPT | Summary: Protein-containing complex assembly fits the established APC function or location. Reason: APC organizes substrate-containing complexes; the cited beta-catenin-targeting versus microtubule-binding pools support this protein-complex assembly role. Supporting Evidence: |
| GO:0070830 bicellular tight junction assembly | NAS PMID:18502210 The armadillo repeat domain of the APC tumor suppressor prot... | KEEP AS NON CORE | Summary: Bicellular tight junction assembly is supported but secondary to APCβs principal activities. Reason: Retain tight-junction assembly as a contextual epithelial function supported by APC-associated striatin/junctional organization, rather than defining a separate core molecular activity. Supporting Evidence: |
| GO:0070840 dynein complex binding | IPI PMID:28057765 Insulin signaling regulates a functional interaction between... | ACCEPT | Summary: Dynein complex binding fits the established APC function or location. Reason: The actual source establishes human APC C-terminal-fragment association with purified bovine dynein and in COS-7 experiments, with endogenous mouse-brain corroboration. Retain dynein-complex binding without claiming a purified full-length all-human interaction. Supporting Evidence: |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: Negative regulation of canonical Wnt signaling is an established APC function, grounded in beta-catenin recruitment, phosphorylation and degradation. Preserve the source-specific curator assertion and evidence; a source abstract foregrounding another effect is not grounds for removal. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000288612 UNRESOLVED The original ancestral-node identifier is preserved. Full PAINT tree/MSA placement was not reconstructed; the target literature supplies independent context. Donor count and target self-inclusion are not failure evidence. Supporting Evidence: |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IC PMID:9601641 Downregulation of beta-catenin by human Axin and its associa... | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: Negative regulation of canonical Wnt signaling is an established APC function, grounded in beta-catenin recruitment, phosphorylation and degradation. Preserve the source-specific curator assertion and evidence; a source abstract foregrounding another effect is not grounds for removal. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: Negative regulation of canonical Wnt signaling is an established APC function, grounded in beta-catenin recruitment, phosphorylation and degradation. Preserve the source-specific curator assertion and evidence; a source abstract foregrounding another effect is not grounds for removal. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00027950 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. Supporting Evidence: |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IGI PMID:12952940 Wnt-5a inhibits the canonical Wnt pathway by promoting GSK-3... | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: Negative regulation of canonical Wnt signaling is an established APC function, grounded in beta-catenin recruitment, phosphorylation and degradation. Preserve the source-specific curator assertion and evidence; a source abstract foregrounding another effect is not grounds for removal. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IGI PMID:12952940 Wnt-5a inhibits the canonical Wnt pathway by promoting GSK-3... | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: Negative regulation of canonical Wnt signaling is an established APC function, grounded in beta-catenin recruitment, phosphorylation and degradation. Preserve the source-specific curator assertion and evidence; a source abstract foregrounding another effect is not grounds for removal. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IGI PMID:21471006 Deconstructing the Γcatenin destruction complex: mechanistic... | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: Negative regulation of canonical Wnt signaling is an established APC function, grounded in beta-catenin recruitment, phosphorylation and degradation. Preserve the source-specific curator assertion and evidence; a source abstract foregrounding another effect is not grounds for removal. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IMP PMID:10656683 The APC-hDLG complex negatively regulates cell cycle progres... | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: The PMID10656683 annotation is retained as the curatorβs APC negative-Wnt assertion, with independent beta-catenin/destruction-complex experiments corroborating the well-established function. Its accessible abstract primarily reports DLG-dependent cell-cycle suppression, so that abstract is not presented as a Wnt assay. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IMP PMID:30374053 TMEM9 promotes intestinal tumorigenesis through vacuolar-ATP... | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: Negative regulation of canonical Wnt signaling is an established APC function, grounded in beta-catenin recruitment, phosphorylation and degradation. Preserve the source-specific curator assertion and evidence; a source abstract foregrounding another effect is not grounds for removal. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | NAS PMID:16344550 Differential use of functional domains by coiled-coil coacti... | ACCEPT | Summary: Negative regulation of canonical Wnt signaling pathway fits the established APC function or location. Reason: The PMID16344550 annotation is retained with independent destruction-complex evidence for APCβs established negative-Wnt role. The accessible CoCoA coactivation abstract does not independently expose its precise APC intervention; it is not relabeled as a newly inspected APC mechanism. |
| GO:0120025 plasma membrane bounded cell projection | IEA GO_REF:0000117 | ACCEPT | Summary: Plasma membrane bounded cell projection fits the established APC function or location. Reason: APC at cell projections is consistent with its leading-edge and protrusion-associated cytoskeletal function; retain the broad electronic location inference. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00028036 UNRESOLVED Historical electronic mapping or donor experiment was not independently reconstructed. Current target evidence is assessed separately; no failed propagation is inferred from incomplete tracing. |
| GO:0120162 positive regulation of cold-induced thermogenesis | ISS PMID:26948948 Extensive metabolic disorders are present in APC(min) tumori... | UNDECIDED | Summary: The mouse cold-tolerance phenotype does not yet resolve APCβs specific regulatory contribution. Reason: The complete accessible abstract reports cold intolerance, reduced brown-adipose glucose uptake and altered adipocyte morphology in Apc-min mice. The normal cache is abstract-only, and the full experimental controls were not recovered. These observations do not yet distinguish an APC regulatory contribution from secondary systemic effects; they also do not prove that tumor burden is the sole explanation. GO:0120162 describes positive regulation, so APC need not generate heat directly to participate. The mouse donor experiment and its transfer to human APC require source-local adjudication before either retention as an established function or an over-annotation judgment. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q61315 UNRESOLVED The actual mouse-source abstract was read, but full experimental controls and the historical ISS derivation were not reconstructed. Cold intolerance alone does not resolve an APC regulatory role versus indirect disease effects; no failed transfer is asserted. Supporting Evidence: |
| GO:1902807 negative regulation of cell cycle G1/S phase transition | IDA PMID:8521819 The tumour suppressor gene product APC blocks cell cycle pro... | KEEP AS NON CORE | Summary: Negative regulation of cell cycle G1/S phase transition is supported but secondary to APCβs principal activities. Reason: APC negatively regulates cell-cycle progression through signaling and cyclin/CDK control. Retain this downstream process separately from its core molecular binding/scaffolding activities. Supporting Evidence: |
| GO:1904781 positive regulation of protein localization to centrosome | IMP PMID:28057765 Insulin signaling regulates a functional interaction between... | KEEP AS NON CORE | Summary: Positive regulation of protein localization to centrosome is supported but secondary to APCβs principal activities. Reason: The source describes APC-dependent dynein redistribution toward centrosomes in an insulin-regulated setting. Retain the contextual localization process without asserting that APC itself is a resident centrosomal component. Supporting Evidence: |
| GO:1990909 Wnt signalosome | NAS PMID:24115276 The regulation and deregulation of Wnt signaling by PARK gen... | UNDECIDED | Summary: Source-local evidence remains unresolved for Wnt signalosome. Reason: The inspected review discussion of the Wnt signalosome focuses on LRRK2/DVL/LRP6 and does not resolve an APC-specific receptor-associated location. Additional direct APC evidence is needed; no absence or wrong-protein claim is made. |
| GO:2000134 negative regulation of G1/S transition of mitotic cell cycle | IMP PMID:10656683 The APC-hDLG complex negatively regulates cell cycle progres... | KEEP AS NON CORE | Summary: Negative regulation of G1/S transition of mitotic cell cycle is supported but secondary to APCβs principal activities. Reason: APC negatively regulates cell-cycle progression through signaling and cyclin/CDK control. Retain this downstream process separately from its core molecular binding/scaffolding activities. Supporting Evidence: |
| GO:0003779 actin binding | IDA PMID:20566685 Adenomatous polyposis coli protein nucleates actin assembly ... | NEW | Summary: APC directly binds actin. Reason: Purified APC basic/C-terminal fragments directly recruit actin monomers; human basic-domain binding and human full-length separation-of-function rescue corroborate the APC activity. Reagent species and cellular hosts are distinguished in the reference reviews. Supporting Evidence: PMID:20566685 APC-B dimerization and recruitment of multiple actin monomers PMID:22654058 APC plays the central role in assembling the nucleation seed PMID:17293347 purified carboxyl-terminal basic domain of human APC protein (APC-basic) bound directly to and bundled actin filaments PMID:28663347 Silencing APC led to a significant reduction in F-actin density (fluorescence intensity per area) in cells, and these defects were rescued by expression of FL-APC (WT) but not FL-APC (m4) |
| GO:0045010 actin nucleation | IDA PMID:20566685 Adenomatous polyposis coli protein nucleates actin assembly ... | NEW | Summary: APC directly nucleates actin filaments. Reason: APC itself recruits actin monomers and builds the nucleation seed in purified and single-molecule experiments; its formin partner performs subsequent elongation. Human full-length APC rescue with a nucleation-defective mutant separates this work from mere necessity and from microtubule binding. Parent, same-role comparator, existing-term redundancy and GO-CAM checks support this single process level; no additional actin-process descendant is proposed. Supporting Evidence: PMID:20566685 APC-B dimerization and recruitment of multiple actin monomers PMID:22654058 APC plays the central role in assembling the nucleation seed PMID:17293347 purified carboxyl-terminal basic domain of human APC protein (APC-basic) bound directly to and bundled actin filaments PMID:28663347 Silencing APC led to a significant reduction in F-actin density (fluorescence intensity per area) in cells, and these defects were rescued by expression of FL-APC (WT) but not FL-APC (m4) |
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Download this section (compressed HTML)Q: Which unresolved interaction records establish a source-specific APC domain or regulatory mechanism, and which reflect indirect coassembly? Independent positive experiments do not establish the exact assay in an unread screen.
Q: How are APC beta-catenin destruction, microtubule organization, actin nucleation and Asef activation coordinated between cellular pools and endogenous isoforms?
Q: Which APC constructs and cellular conditions reconcile the intact-destruction-complex model with proposed component-disassembly models?
Q: What direct target-specific evidence places APC at centrosomes or in receptor-associated Wnt signalosomes, beyond movement of its partners or broad pathway membership?
Q: Would the purified human APC basic-domain filament binding and bundling reported in PMID:17293347 justify refining broad actin binding to actin filament binding (GO:0051015)? Keep monomer recruitment for nucleation distinct from filament binding, and avoid adding a redundant parent/child NEW pair without resolving their separate evidence scopes.
Experiment: Compare matched full-length human APC and separation-of-function mutants in endogenous rescue, measuring beta-catenin turnover, actin nucleation, microtubule organization and Asef activation separately, with isoform and expression controls.
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