{"gene":"ZFYVE16","run_date":"2026-06-11T09:02:06","timeline":{"discoveries":[{"year":2001,"finding":"ZFYVE16 (endofin/KIAA0305) localizes to early endosomes via its FYVE domain, which binds preferentially to phosphatidylinositol 3-phosphate (PI3P); a single point mutation C753S in the FYVE domain abolishes both PI3P binding and endosomal association, and wortmannin (a PI3-kinase inhibitor) disrupts endosomal localization.","method":"Indirect immunofluorescence, deletion mutagenesis, point mutagenesis (C753S), in vitro liposome binding assay, wortmannin treatment","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Strong — in vitro liposome binding assay with mutagenesis plus multiple orthogonal imaging methods in a single rigorous study","pmids":["11546807"],"is_preprint":false},{"year":2001,"finding":"ZFYVE16 co-localizes with SARA on early endosomes but does not co-immunoprecipitate with SARA in co-expressing cells, indicating they are not part of a common protein complex.","method":"Co-immunoprecipitation, co-localization by immunofluorescence","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal negative Co-IP plus co-localization imaging in a single study; the negative result is mechanistically informative","pmids":["11546807"],"is_preprint":false},{"year":2001,"finding":"ZFYVE16 does not associate with Smad2 and does not behave like SARA in affecting TGF-β signaling, as assessed in co-expressing cells.","method":"Co-immunoprecipitation, TGF-β signaling assay","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct Co-IP experiment with functional signaling readout, single study, negative result explicitly reported","pmids":["11546807"],"is_preprint":false},{"year":2001,"finding":"Overexpression of ZFYVE16 causes endosome aggregation/fusion and accumulation of endocytosed EGF in enlarged vesicular structures, implicating it in regulation of endosomal membrane traffic.","method":"Overexpression in COS7 cells, endocytosis assay with fluorescent EGF, immunofluorescence microscopy","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — overexpression phenotype in cell culture with functional endocytic readout, single study, single lab","pmids":["11546807"],"is_preprint":false},{"year":2017,"finding":"Zfyve16 knockout mice show inhibited B-lymphoid cell proliferation both in vivo and in vitro, establishing a role for ZFYVE16 in promoting B cell proliferation; concurrently, T cell proportions increased in peripheral blood, consistent with ZFYVE16 facilitating TGF-β-mediated suppression of T cells.","method":"Zfyve16 knockout mouse generation, flow cytometry, in vitro B cell proliferation assay","journal":"Frontiers of medicine","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean knockout mouse with defined hematopoietic phenotype, single lab, two cell-type readouts","pmids":["29247407"],"is_preprint":false},{"year":2017,"finding":"ZFYVE16 binds to Smad4, and this interaction affects formation of the Smad2/3-Smad4 complex in TGF-β signaling.","method":"Co-immunoprecipitation / protein interaction assay (referenced as prior finding in knockout study)","journal":"Frontiers of medicine","confidence":"Low","confidence_rationale":"Tier 3 / Weak — described as established prior finding in the knockout paper but no primary data reproduced in this abstract; single-method, single lab","pmids":["29247407"],"is_preprint":false},{"year":2026,"finding":"ZFYVE16 was identified and validated as a novel interactor of both LAMP1- and LAMP2A-positive late endosomal/lysosomal compartments in axons of human iPSC-derived cortical neurons, using proximity labelling with light-activated LOV-Turbo biotin ligase fused to LAMP1 or LAMP2A.","method":"Proximity labelling (LOV-Turbo biotin ligase), mass spectrometry interactome, validation in hiPSC-derived cortical neurons","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — proximity labelling with independent validation in human neurons, single lab, two orthogonal LAMP bait proteins","pmids":["41537223"],"is_preprint":false}],"current_model":"ZFYVE16 (endofin) is an early endosomal FYVE-domain protein that localizes to endosomes via PI3P binding through its FYVE domain, regulates endosomal membrane trafficking, binds Smad4 to modulate TGF-β/Smad signaling, promotes B-lymphoid cell proliferation in vivo, and associates with LAMP1- and LAMP2A-positive late endosomal/lysosomal compartments in neuronal axons."},"narrative":{"mechanistic_narrative":"ZFYVE16 (endofin) is a FYVE-domain endosomal protein that governs endosomal membrane trafficking and intersects with TGF-β/Smad signaling [PMID:11546807, PMID:29247407]. It is recruited to early endosomes through direct, PI3P-specific binding by its FYVE domain: a single C753S substitution abolishes both PI3P binding and endosomal association, and PI3-kinase inhibition by wortmannin displaces the protein [PMID:11546807]. Functionally, its overexpression drives endosome aggregation/fusion and accumulation of endocytosed EGF in enlarged vesicles, marking it as a regulator of endosomal membrane traffic [PMID:11546807]. Although it co-localizes with SARA on early endosomes, it neither co-immunoprecipitates with SARA nor associates with Smad2 or behaves like SARA in TGF-β signaling [PMID:11546807]; instead it binds Smad4 and modulates Smad2/3–Smad4 complex formation [PMID:29247407]. At the organismal level, Zfyve16 knockout mice show impaired B-lymphoid cell proliferation and an increased peripheral T cell proportion, linking the protein to hematopoietic regulation consistent with its TGF-β role [PMID:29247407]. ZFYVE16 also associates with LAMP1- and LAMP2A-positive late endosomal/lysosomal compartments in human neuronal axons [PMID:41537223]. Beyond these findings, the structural basis and detailed mechanism of its Smad4 interaction have not been characterized in the available corpus.","teleology":[{"year":2001,"claim":"Established how ZFYVE16 is targeted to membranes, defining it as a PI3P-dependent early endosomal protein and identifying the FYVE domain residue required for lipid binding.","evidence":"In vitro liposome binding, point mutagenesis (C753S), wortmannin treatment and immunofluorescence in cultured cells","pmids":["11546807"],"confidence":"High","gaps":["Does not define the dynamics or regulation of endosomal recruitment in vivo","No structural model of the FYVE–PI3P interaction provided"]},{"year":2001,"claim":"Distinguished ZFYVE16 from the related FYVE protein SARA, showing it does not share SARA's Smad2/TGF-β adaptor role despite co-localizing on endosomes.","evidence":"Reciprocal co-immunoprecipitation (negative), co-localization imaging, and TGF-β signaling assays in co-expressing cells","pmids":["11546807"],"confidence":"Medium","gaps":["Negative results from a single study","Did not exclude weaker or transient SARA interactions"]},{"year":2001,"claim":"Provided functional evidence that ZFYVE16 regulates endosomal membrane traffic by showing overexpression remodels endosome morphology and endocytic cargo flux.","evidence":"Overexpression in COS7 cells with fluorescent EGF endocytosis assay and immunofluorescence","pmids":["11546807"],"confidence":"Medium","gaps":["Overexpression phenotype may not reflect endogenous function","Mechanism driving endosome aggregation/fusion not resolved"]},{"year":2017,"claim":"Connected ZFYVE16 to TGF-β signaling through Smad4 binding and demonstrated a physiological role in hematopoiesis using a knockout mouse.","evidence":"Zfyve16 knockout mice with flow cytometry and B cell proliferation assays; Smad4 interaction cited as prior finding","pmids":["29247407"],"confidence":"Medium","gaps":["Smad4-binding claim lacks primary data reproduced in this study","Causal link between Smad4 interaction and the B/T cell phenotype not directly established"]},{"year":2026,"claim":"Extended ZFYVE16's compartmental association to late endosomal/lysosomal membranes in neurons, identifying it as a LAMP1/LAMP2A-proximal protein in axons.","evidence":"LOV-Turbo proximity labelling with LAMP1 and LAMP2A baits, mass spectrometry, validated in hiPSC-derived cortical neurons","pmids":["41537223"],"confidence":"Medium","gaps":["Proximity does not establish direct binding to LAMP1/LAMP2A","Functional role of ZFYVE16 at late endosomes/lysosomes in neurons unresolved"]},{"year":null,"claim":"How ZFYVE16's endosomal trafficking activity mechanistically couples to its Smad4 binding and its physiological roles in immune cells and neurons remains unknown.","evidence":"No integrating study in the available corpus","pmids":[],"confidence":"Low","gaps":["No structural or biochemical characterization of the Smad4 interaction","No reconciliation of early-endosomal versus late-endosomal/lysosomal roles","Direct binding partners at the lysosome not defined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008289","term_label":"lipid binding","supporting_discovery_ids":[0]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,3]}],"localization":[{"term_id":"GO:0005768","term_label":"endosome","supporting_discovery_ids":[0,3,6]},{"term_id":"GO:0005764","term_label":"lysosome","supporting_discovery_ids":[6]}],"pathway":[{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[0,3]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[5]}],"complexes":[],"partners":["SMAD4","SARA","LAMP1","LAMP2A"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q7Z3T8","full_name":"Zinc finger FYVE domain-containing protein 16","aliases":["Endofin","Endosome-associated FYVE domain protein"],"length_aa":1539,"mass_kda":168.9,"function":"May be involved in regulating membrane trafficking in the endosomal pathway. Overexpression induces endosome aggregation. Required to target TOM1 to endosomes","subcellular_location":"Cytoplasm; Early endosome membrane","url":"https://www.uniprot.org/uniprotkb/Q7Z3T8/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ZFYVE16","classification":"Not Classified","n_dependent_lines":11,"n_total_lines":1208,"dependency_fraction":0.009105960264900662},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/ZFYVE16","total_profiled":1310},"omim":[{"mim_id":"616889","title":"CENTROSOMAL PROTEIN, 68-KD; CEP68","url":"https://www.omim.org/entry/616889"},{"mim_id":"608880","title":"ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 16; ZFYVE16","url":"https://www.omim.org/entry/608880"},{"mim_id":"608698","title":"DISCOIDIN, CUB, AND LCCL DOMAIN-CONTAINING PROTEIN 2; DCBLD2","url":"https://www.omim.org/entry/608698"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Vesicles","reliability":"Enhanced"},{"location":"Cytosol","reliability":"Enhanced"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/ZFYVE16"},"hgnc":{"alias_symbol":["KIAA0305","PPP1R69"],"prev_symbol":[]},"alphafold":{"accession":"Q7Z3T8","domains":[{"cath_id":"3.30.40.10","chopping":"739-810","consensus_level":"medium","plddt":92.3199,"start":739,"end":810},{"cath_id":"-","chopping":"998-1220","consensus_level":"medium","plddt":88.0776,"start":998,"end":1220},{"cath_id":"3.30.1360.220","chopping":"1224-1390","consensus_level":"medium","plddt":90.1571,"start":1224,"end":1390},{"cath_id":"3.30.500.40","chopping":"1412-1537","consensus_level":"high","plddt":84.4981,"start":1412,"end":1537}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q7Z3T8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q7Z3T8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q7Z3T8-F1-predicted_aligned_error_v6.png","plddt_mean":54.59},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ZFYVE16","jax_strain_url":"https://www.jax.org/strain/search?query=ZFYVE16"},"sequence":{"accession":"Q7Z3T8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q7Z3T8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q7Z3T8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q7Z3T8"}},"corpus_meta":[{"pmid":"20933273","id":"PMC_20933273","title":"The influence of surface microroughness and hydrophilicity of titanium on the up-regulation of TGFβ/BMP signalling in osteoblasts.","date":"2010","source":"Biomaterials","url":"https://pubmed.ncbi.nlm.nih.gov/20933273","citation_count":138,"is_preprint":false},{"pmid":"25854761","id":"PMC_25854761","title":"Whole-exome SNP array identifies 15 new susceptibility loci for psoriasis.","date":"2015","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/25854761","citation_count":117,"is_preprint":false},{"pmid":"30120215","id":"PMC_30120215","title":"Perturbations of BMP/TGF-β and VEGF/VEGFR signalling pathways in non-syndromic sporadic brain arteriovenous malformations (BAVM).","date":"2018","source":"Journal of medical genetics","url":"https://pubmed.ncbi.nlm.nih.gov/30120215","citation_count":64,"is_preprint":false},{"pmid":"11546807","id":"PMC_11546807","title":"Endofin, an endosomal FYVE domain protein.","date":"2001","source":"The Journal of biological 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phosphatidylinositol 3-phosphate (PI3P); a single point mutation C753S in the FYVE domain abolishes both PI3P binding and endosomal association, and wortmannin (a PI3-kinase inhibitor) disrupts endosomal localization.\",\n      \"method\": \"Indirect immunofluorescence, deletion mutagenesis, point mutagenesis (C753S), in vitro liposome binding assay, wortmannin treatment\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro liposome binding assay with mutagenesis plus multiple orthogonal imaging methods in a single rigorous study\",\n      \"pmids\": [\"11546807\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"ZFYVE16 co-localizes with SARA on early endosomes but does not co-immunoprecipitate with SARA in co-expressing cells, indicating they are not part of a common protein complex.\",\n      \"method\": \"Co-immunoprecipitation, co-localization by immunofluorescence\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal negative Co-IP plus co-localization imaging in a single study; the negative result is mechanistically informative\",\n      \"pmids\": [\"11546807\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"ZFYVE16 does not associate with Smad2 and does not behave like SARA in affecting TGF-β signaling, as assessed in co-expressing cells.\",\n      \"method\": \"Co-immunoprecipitation, TGF-β signaling assay\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct Co-IP experiment with functional signaling readout, single study, negative result explicitly reported\",\n      \"pmids\": [\"11546807\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"Overexpression of ZFYVE16 causes endosome aggregation/fusion and accumulation of endocytosed EGF in enlarged vesicular structures, implicating it in regulation of endosomal membrane traffic.\",\n      \"method\": \"Overexpression in COS7 cells, endocytosis assay with fluorescent EGF, immunofluorescence microscopy\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — overexpression phenotype in cell culture with functional endocytic readout, single study, single lab\",\n      \"pmids\": [\"11546807\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Zfyve16 knockout mice show inhibited B-lymphoid cell proliferation both in vivo and in vitro, establishing a role for ZFYVE16 in promoting B cell proliferation; concurrently, T cell proportions increased in peripheral blood, consistent with ZFYVE16 facilitating TGF-β-mediated suppression of T cells.\",\n      \"method\": \"Zfyve16 knockout mouse generation, flow cytometry, in vitro B cell proliferation assay\",\n      \"journal\": \"Frontiers of medicine\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean knockout mouse with defined hematopoietic phenotype, single lab, two cell-type readouts\",\n      \"pmids\": [\"29247407\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"ZFYVE16 binds to Smad4, and this interaction affects formation of the Smad2/3-Smad4 complex in TGF-β signaling.\",\n      \"method\": \"Co-immunoprecipitation / protein interaction assay (referenced as prior finding in knockout study)\",\n      \"journal\": \"Frontiers of medicine\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — described as established prior finding in the knockout paper but no primary data reproduced in this abstract; single-method, single lab\",\n      \"pmids\": [\"29247407\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"ZFYVE16 was identified and validated as a novel interactor of both LAMP1- and LAMP2A-positive late endosomal/lysosomal compartments in axons of human iPSC-derived cortical neurons, using proximity labelling with light-activated LOV-Turbo biotin ligase fused to LAMP1 or LAMP2A.\",\n      \"method\": \"Proximity labelling (LOV-Turbo biotin ligase), mass spectrometry interactome, validation in hiPSC-derived cortical neurons\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — proximity labelling with independent validation in human neurons, single lab, two orthogonal LAMP bait proteins\",\n      \"pmids\": [\"41537223\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ZFYVE16 (endofin) is an early endosomal FYVE-domain protein that localizes to endosomes via PI3P binding through its FYVE domain, regulates endosomal membrane trafficking, binds Smad4 to modulate TGF-β/Smad signaling, promotes B-lymphoid cell proliferation in vivo, and associates with LAMP1- and LAMP2A-positive late endosomal/lysosomal compartments in neuronal axons.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ZFYVE16 (endofin) is a FYVE-domain endosomal protein that governs endosomal membrane trafficking and intersects with TGF-\\u03b2/Smad signaling [#0, #5]. It is recruited to early endosomes through direct, PI3P-specific binding by its FYVE domain: a single C753S substitution abolishes both PI3P binding and endosomal association, and PI3-kinase inhibition by wortmannin displaces the protein [#0]. Functionally, its overexpression drives endosome aggregation/fusion and accumulation of endocytosed EGF in enlarged vesicles, marking it as a regulator of endosomal membrane traffic [#3]. Although it co-localizes with SARA on early endosomes, it neither co-immunoprecipitates with SARA nor associates with Smad2 or behaves like SARA in TGF-\\u03b2 signaling [#1, #2]; instead it binds Smad4 and modulates Smad2/3\\u2013Smad4 complex formation [#5]. At the organismal level, Zfyve16 knockout mice show impaired B-lymphoid cell proliferation and an increased peripheral T cell proportion, linking the protein to hematopoietic regulation consistent with its TGF-\\u03b2 role [#4]. ZFYVE16 also associates with LAMP1- and LAMP2A-positive late endosomal/lysosomal compartments in human neuronal axons [#6]. Beyond these findings, the structural basis and detailed mechanism of its Smad4 interaction have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Established how ZFYVE16 is targeted to membranes, defining it as a PI3P-dependent early endosomal protein and identifying the FYVE domain residue required for lipid binding.\",\n      \"evidence\": \"In vitro liposome binding, point mutagenesis (C753S), wortmannin treatment and immunofluorescence in cultured cells\",\n      \"pmids\": [\"11546807\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not define the dynamics or regulation of endosomal recruitment in vivo\", \"No structural model of the FYVE\\u2013PI3P interaction provided\"]\n    },\n    {\n      \"year\": 2001,\n      \"claim\": \"Distinguished ZFYVE16 from the related FYVE protein SARA, showing it does not share SARA's Smad2/TGF-\\u03b2 adaptor role despite co-localizing on endosomes.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation (negative), co-localization imaging, and TGF-\\u03b2 signaling assays in co-expressing cells\",\n      \"pmids\": [\"11546807\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Negative results from a single study\", \"Did not exclude weaker or transient SARA interactions\"]\n    },\n    {\n      \"year\": 2001,\n      \"claim\": \"Provided functional evidence that ZFYVE16 regulates endosomal membrane traffic by showing overexpression remodels endosome morphology and endocytic cargo flux.\",\n      \"evidence\": \"Overexpression in COS7 cells with fluorescent EGF endocytosis assay and immunofluorescence\",\n      \"pmids\": [\"11546807\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Overexpression phenotype may not reflect endogenous function\", \"Mechanism driving endosome aggregation/fusion not resolved\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Connected ZFYVE16 to TGF-\\u03b2 signaling through Smad4 binding and demonstrated a physiological role in hematopoiesis using a knockout mouse.\",\n      \"evidence\": \"Zfyve16 knockout mice with flow cytometry and B cell proliferation assays; Smad4 interaction cited as prior finding\",\n      \"pmids\": [\"29247407\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Smad4-binding claim lacks primary data reproduced in this study\", \"Causal link between Smad4 interaction and the B/T cell phenotype not directly established\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Extended ZFYVE16's compartmental association to late endosomal/lysosomal membranes in neurons, identifying it as a LAMP1/LAMP2A-proximal protein in axons.\",\n      \"evidence\": \"LOV-Turbo proximity labelling with LAMP1 and LAMP2A baits, mass spectrometry, validated in hiPSC-derived cortical neurons\",\n      \"pmids\": [\"41537223\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Proximity does not establish direct binding to LAMP1/LAMP2A\", \"Functional role of ZFYVE16 at late endosomes/lysosomes in neurons unresolved\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How ZFYVE16's endosomal trafficking activity mechanistically couples to its Smad4 binding and its physiological roles in immune cells and neurons remains unknown.\",\n      \"evidence\": \"No integrating study in the available corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structural or biochemical characterization of the Smad4 interaction\", \"No reconciliation of early-endosomal versus late-endosomal/lysosomal roles\", \"Direct binding partners at the lysosome not defined\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008289\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005768\", \"supporting_discovery_ids\": [0, 3, 6]},\n      {\"term_id\": \"GO:0005764\", \"supporting_discovery_ids\": [6]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [5]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"SMAD4\", \"SARA\", \"LAMP1\", \"LAMP2A\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}