{"gene":"ANAPC16","run_date":"2026-06-09T22:02:43","timeline":{"discoveries":[{"year":2014,"finding":"Crystal structures of APC3Δloop alone and in complex with the C-terminal domain of APC16 revealed that one APC16 molecule binds asymmetrically to the symmetric APC3 homodimer, establishing the structural basis for APC3-APC16 interaction and showing how APC16 recruits APC7 to APC3 within the APC/C Arc Lamp subcomplex.","method":"X-ray crystallography, biochemical mapping, mutagenesis","journal":"Journal of molecular biology","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structures of the complex combined with biochemical validation and mutagenesis in a single rigorous study","pmids":["25490258"],"is_preprint":false},{"year":2014,"finding":"APC16 is located in the Arc Lamp subcomplex of the APC/C together with CDC26, APC13, and TPR proteins (APC7, APC3, APC6, APC8), where it mediates assembly by bridging APC3 and APC7.","method":"Structural analysis (crystallography) and biochemical fractionation","journal":"Journal of molecular biology","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystallographic and biochemical evidence from a single rigorous study with multiple orthogonal methods","pmids":["25490258"],"is_preprint":false},{"year":2010,"finding":"APC16 is a bona fide subunit of the human APC/C, present in APC/C complexes throughout the cell cycle; depletion of APC16 reduces APC/C ubiquitin ligase activity toward mitotic substrates and phenocopies depletion of other APC/C subunits.","method":"Tandem-affinity purification, co-immunoprecipitation, siRNA knockdown with APC/C activity assays","journal":"Journal of cell science","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal purification plus functional APC/C activity assays plus knockdown phenotype, replicated in C. elegans and zebrafish orthologs","pmids":["20392738"],"is_preprint":false},{"year":2010,"finding":"APC16 is conserved in metazoans but not fungi; C. elegans K10D2.4 and zebrafish zgc:110659 are functional equivalents of human APC16, establishing its role as a metazoan-specific APC/C subunit.","method":"Sequence homology analysis combined with functional complementation/depletion experiments in C. elegans and zebrafish","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional equivalence demonstrated by depletion phenotype in model organisms, single lab","pmids":["20392738"],"is_preprint":false},{"year":2011,"finding":"C. elegans emb-1 encodes the APC16 homolog K10D2.4; emb-1 loss-of-function arrests one-cell embryos in metaphase of meiosis I, and the phenotype is enhanced in double mutants with other APC/C subunits and suppressed by known APC/C suppressors, placing APC16/EMB-1 within the APC/C pathway for meiotic progression.","method":"Genetic epistasis (double mutant analysis), temperature-sensitive mutants, genetic suppressor/enhancer screens","journal":"Genetics","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic epistasis with multiple APC/C subunit combinations and suppressors establishes pathway position robustly","pmids":["21775471"],"is_preprint":false},{"year":2011,"finding":"In addition to its meiotic role, C. elegans APC16 (EMB-1) is required for mitotic proliferation of the germline, indicating a mitotic function consistent with its role as an APC/C subunit.","method":"Loss-of-function genetic analysis in C. elegans","journal":"Genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean loss-of-function with defined cellular phenotype, single lab","pmids":["21775471"],"is_preprint":false}],"current_model":"ANAPC16 (APC16) is a conserved metazoan-specific subunit of the APC/C E3 ubiquitin ligase that resides in the Arc Lamp subcomplex, where its C-terminal domain binds asymmetrically to the APC3 homodimer to recruit APC7, thereby contributing to APC/C assembly and activity toward mitotic and meiotic substrates."},"narrative":{"mechanistic_narrative":"ANAPC16 (APC16) is a metazoan-specific subunit of the APC/C E3 ubiquitin ligase that contributes to the ubiquitination of cell-cycle substrates required for mitotic and meiotic progression [PMID:20392738, PMID:21775471]. It is a bona fide component of the human APC/C present throughout the cell cycle, and its depletion reduces APC/C ubiquitin ligase activity toward mitotic substrates, phenocopying loss of other APC/C subunits [PMID:20392738]. Structurally, APC16 resides in the Arc Lamp subcomplex together with CDC26, APC13, and the TPR proteins APC7, APC3, APC6, and APC8, where a single APC16 molecule binds asymmetrically to the symmetric APC3 homodimer and bridges APC3 to APC7, recruiting APC7 into the assembly [PMID:25490258]. APC16 is conserved across metazoans but absent in fungi, with functional equivalents identified in C. elegans (emb-1/K10D2.4) and zebrafish [PMID:20392738]; in C. elegans, loss of emb-1 arrests one-cell embryos in metaphase of meiosis I and is genetically suppressed and enhanced by known APC/C regulators, and it is additionally required for mitotic germline proliferation, placing APC16 firmly within the APC/C pathway for both meiotic and mitotic cell division [PMID:21775471].","teleology":[{"year":2010,"claim":"Established that APC16 is a genuine, constitutive subunit of the human APC/C rather than a transient interactor, and that it is functionally required for APC/C ligase activity.","evidence":"Tandem-affinity purification, reciprocal co-IP, and siRNA knockdown coupled to APC/C activity assays in human cells","pmids":["20392738"],"confidence":"High","gaps":["Did not resolve where APC16 sits structurally within the complex","Mechanism by which depletion lowers ligase activity not defined"]},{"year":2010,"claim":"Defined APC16 as a metazoan-specific APC/C subunit by showing functional equivalence of C. elegans and zebrafish orthologs, distinguishing it from fungal APC/C architecture.","evidence":"Sequence homology analysis with depletion/complementation in C. elegans and zebrafish (single lab)","pmids":["20392738"],"confidence":"Medium","gaps":["Functional equivalence based on depletion phenotype only","No biochemical demonstration that orthologs occupy the same APC/C position"]},{"year":2011,"claim":"Placed APC16/EMB-1 within the APC/C pathway controlling meiotic progression, answering whether its loss specifically disrupts cell-division control.","evidence":"Genetic epistasis with temperature-sensitive mutants, double-mutant analysis, and suppressor/enhancer screens in C. elegans","pmids":["21775471"],"confidence":"High","gaps":["Does not identify the molecular step in meiosis I that APC16 enables","Substrate(s) whose ubiquitination requires APC16 not defined"]},{"year":2011,"claim":"Extended APC16's role beyond meiosis by showing a requirement in mitotic germline proliferation, consistent with a general APC/C function.","evidence":"Loss-of-function genetic analysis in C. elegans germline (single lab)","pmids":["21775471"],"confidence":"Medium","gaps":["Mitotic phenotype characterized at cellular but not molecular level","Relationship between meiotic and mitotic requirements not dissected"]},{"year":2014,"claim":"Provided the structural basis for APC16 function, showing how it physically assembles part of the APC/C by bridging APC3 to APC7.","evidence":"X-ray crystallography of APC3Δloop alone and bound to the APC16 C-terminal domain, with biochemical mapping and mutagenesis","pmids":["25490258"],"confidence":"High","gaps":["Structural work used isolated APC3-APC16 module, not the holo-APC/C","Functional consequence of disrupting the asymmetric APC3-APC16 interface not tested in cells"]},{"year":null,"claim":"How APC16-mediated APC7 recruitment quantitatively shapes APC/C substrate selectivity and activity in vivo remains unresolved.","evidence":"","pmids":[],"confidence":"High","gaps":["No defined set of substrates dependent specifically on the APC16-APC7 module","Regulation of APC16 across cell-cycle phases not characterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1]}],"localization":[],"pathway":[{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[2,4,5]},{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[2]}],"complexes":["APC/C","Arc Lamp subcomplex"],"partners":["APC3","APC7"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q96DE5","full_name":"Anaphase-promoting complex subunit 16","aliases":["Cyclosome subunit 16"],"length_aa":110,"mass_kda":11.7,"function":"Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:20360068). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:20360068). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132)","subcellular_location":"Cytoplasm; Nucleus; Chromosome, centromere, kinetochore","url":"https://www.uniprot.org/uniprotkb/Q96DE5/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ANAPC16","classification":"Not Classified","n_dependent_lines":4,"n_total_lines":1208,"dependency_fraction":0.0033112582781456954},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000166295","cell_line_id":"CID000222","localizations":[{"compartment":"cytoplasmic","grade":3},{"compartment":"nucleoplasm","grade":3},{"compartment":"cytoskeleton","grade":1}],"interactors":[{"gene":"NEK2","stoichiometry":10.0},{"gene":"CDC27","stoichiometry":10.0},{"gene":"ANAPC5","stoichiometry":10.0},{"gene":"ANAPC13","stoichiometry":10.0},{"gene":"ANAPC1","stoichiometry":10.0},{"gene":"ANAPC10","stoichiometry":10.0},{"gene":"ANAPC4","stoichiometry":10.0},{"gene":"ANAPC7","stoichiometry":10.0},{"gene":"CDC23","stoichiometry":10.0},{"gene":"CDC26","stoichiometry":10.0}],"url":"https://opencell.sf.czbiohub.org/target/CID000222","total_profiled":1310},"omim":[{"mim_id":"613427","title":"ANAPHASE-PROMOTING COMPLEX, SUBUNIT 16; ANAPC16","url":"https://www.omim.org/entry/613427"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Cytosol","reliability":"Supported"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/ANAPC16"},"hgnc":{"alias_symbol":["bA570G20.3","FLJ33728","APC16","CENP-27"],"prev_symbol":["C10orf104"]},"alphafold":{"accession":"Q96DE5","domains":[{"cath_id":"1.20.5","chopping":"48-94","consensus_level":"medium","plddt":93.7343,"start":48,"end":94}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q96DE5","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q96DE5-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q96DE5-F1-predicted_aligned_error_v6.png","plddt_mean":71.31},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ANAPC16","jax_strain_url":"https://www.jax.org/strain/search?query=ANAPC16"},"sequence":{"accession":"Q96DE5","fasta_url":"https://rest.uniprot.org/uniprotkb/Q96DE5.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q96DE5/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q96DE5"}},"corpus_meta":[{"pmid":"25490258","id":"PMC_25490258","title":"Structure of an APC3-APC16 complex: insights into assembly of the anaphase-promoting complex/cyclosome.","date":"2014","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/25490258","citation_count":31,"is_preprint":false},{"pmid":"20392738","id":"PMC_20392738","title":"APC16 is a conserved subunit of the anaphase-promoting complex/cyclosome.","date":"2010","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/20392738","citation_count":26,"is_preprint":false},{"pmid":"21775471","id":"PMC_21775471","title":"emb-1 encodes the APC16 subunit of the Caenorhabditis elegans anaphase-promoting complex.","date":"2011","source":"Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/21775471","citation_count":13,"is_preprint":false},{"pmid":"32286337","id":"PMC_32286337","title":"Alkyl-carbon chain length of two distinct compounds and derivatives are key determinants of their anti-Acanthamoeba activities.","date":"2020","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/32286337","citation_count":13,"is_preprint":false},{"pmid":"33479685","id":"PMC_33479685","title":"Drug combinations as effective anti-leishmanials against drug resistant Leishmania mexicana.","date":"2020","source":"RSC medicinal chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/33479685","citation_count":9,"is_preprint":false},{"pmid":"39774722","id":"PMC_39774722","title":"A genome-wide scan of non-coding RNAs and enhancers for refractive error and myopia.","date":"2025","source":"Human genetics","url":"https://pubmed.ncbi.nlm.nih.gov/39774722","citation_count":3,"is_preprint":false},{"pmid":"35924985","id":"PMC_35924985","title":"Correlations of expression of nuclear and mitochondrial genes in triploid fish.","date":"2022","source":"G3 (Bethesda, Md.)","url":"https://pubmed.ncbi.nlm.nih.gov/35924985","citation_count":1,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5680,"output_tokens":1329,"usd":0.018488,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7946,"output_tokens":1929,"usd":0.043978,"stage2_stop_reason":"end_turn"},"total_usd":0.062466,"stage1_batch_id":"msgbatch_0179Z2pxRYBsXi2xADneafRw","stage2_batch_id":"msgbatch_01LaY9ZaVdgjWArcZo9eqQE5","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"Crystal structures of APC3Δloop alone and in complex with the C-terminal domain of APC16 revealed that one APC16 molecule binds asymmetrically to the symmetric APC3 homodimer, establishing the structural basis for APC3-APC16 interaction and showing how APC16 recruits APC7 to APC3 within the APC/C Arc Lamp subcomplex.\",\n      \"method\": \"X-ray crystallography, biochemical mapping, mutagenesis\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structures of the complex combined with biochemical validation and mutagenesis in a single rigorous study\",\n      \"pmids\": [\"25490258\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"APC16 is located in the Arc Lamp subcomplex of the APC/C together with CDC26, APC13, and TPR proteins (APC7, APC3, APC6, APC8), where it mediates assembly by bridging APC3 and APC7.\",\n      \"method\": \"Structural analysis (crystallography) and biochemical fractionation\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystallographic and biochemical evidence from a single rigorous study with multiple orthogonal methods\",\n      \"pmids\": [\"25490258\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"APC16 is a bona fide subunit of the human APC/C, present in APC/C complexes throughout the cell cycle; depletion of APC16 reduces APC/C ubiquitin ligase activity toward mitotic substrates and phenocopies depletion of other APC/C subunits.\",\n      \"method\": \"Tandem-affinity purification, co-immunoprecipitation, siRNA knockdown with APC/C activity assays\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal purification plus functional APC/C activity assays plus knockdown phenotype, replicated in C. elegans and zebrafish orthologs\",\n      \"pmids\": [\"20392738\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"APC16 is conserved in metazoans but not fungi; C. elegans K10D2.4 and zebrafish zgc:110659 are functional equivalents of human APC16, establishing its role as a metazoan-specific APC/C subunit.\",\n      \"method\": \"Sequence homology analysis combined with functional complementation/depletion experiments in C. elegans and zebrafish\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional equivalence demonstrated by depletion phenotype in model organisms, single lab\",\n      \"pmids\": [\"20392738\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"C. elegans emb-1 encodes the APC16 homolog K10D2.4; emb-1 loss-of-function arrests one-cell embryos in metaphase of meiosis I, and the phenotype is enhanced in double mutants with other APC/C subunits and suppressed by known APC/C suppressors, placing APC16/EMB-1 within the APC/C pathway for meiotic progression.\",\n      \"method\": \"Genetic epistasis (double mutant analysis), temperature-sensitive mutants, genetic suppressor/enhancer screens\",\n      \"journal\": \"Genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic epistasis with multiple APC/C subunit combinations and suppressors establishes pathway position robustly\",\n      \"pmids\": [\"21775471\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"In addition to its meiotic role, C. elegans APC16 (EMB-1) is required for mitotic proliferation of the germline, indicating a mitotic function consistent with its role as an APC/C subunit.\",\n      \"method\": \"Loss-of-function genetic analysis in C. elegans\",\n      \"journal\": \"Genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean loss-of-function with defined cellular phenotype, single lab\",\n      \"pmids\": [\"21775471\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ANAPC16 (APC16) is a conserved metazoan-specific subunit of the APC/C E3 ubiquitin ligase that resides in the Arc Lamp subcomplex, where its C-terminal domain binds asymmetrically to the APC3 homodimer to recruit APC7, thereby contributing to APC/C assembly and activity toward mitotic and meiotic substrates.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ANAPC16 (APC16) is a metazoan-specific subunit of the APC/C E3 ubiquitin ligase that contributes to the ubiquitination of cell-cycle substrates required for mitotic and meiotic progression [#2, #4]. It is a bona fide component of the human APC/C present throughout the cell cycle, and its depletion reduces APC/C ubiquitin ligase activity toward mitotic substrates, phenocopying loss of other APC/C subunits [#2]. Structurally, APC16 resides in the Arc Lamp subcomplex together with CDC26, APC13, and the TPR proteins APC7, APC3, APC6, and APC8, where a single APC16 molecule binds asymmetrically to the symmetric APC3 homodimer and bridges APC3 to APC7, recruiting APC7 into the assembly [#0, #1]. APC16 is conserved across metazoans but absent in fungi, with functional equivalents identified in C. elegans (emb-1/K10D2.4) and zebrafish [#3]; in C. elegans, loss of emb-1 arrests one-cell embryos in metaphase of meiosis I and is genetically suppressed and enhanced by known APC/C regulators, and it is additionally required for mitotic germline proliferation, placing APC16 firmly within the APC/C pathway for both meiotic and mitotic cell division [#4, #5].\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"Established that APC16 is a genuine, constitutive subunit of the human APC/C rather than a transient interactor, and that it is functionally required for APC/C ligase activity.\",\n      \"evidence\": \"Tandem-affinity purification, reciprocal co-IP, and siRNA knockdown coupled to APC/C activity assays in human cells\",\n      \"pmids\": [\"20392738\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not resolve where APC16 sits structurally within the complex\", \"Mechanism by which depletion lowers ligase activity not defined\"]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Defined APC16 as a metazoan-specific APC/C subunit by showing functional equivalence of C. elegans and zebrafish orthologs, distinguishing it from fungal APC/C architecture.\",\n      \"evidence\": \"Sequence homology analysis with depletion/complementation in C. elegans and zebrafish (single lab)\",\n      \"pmids\": [\"20392738\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional equivalence based on depletion phenotype only\", \"No biochemical demonstration that orthologs occupy the same APC/C position\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Placed APC16/EMB-1 within the APC/C pathway controlling meiotic progression, answering whether its loss specifically disrupts cell-division control.\",\n      \"evidence\": \"Genetic epistasis with temperature-sensitive mutants, double-mutant analysis, and suppressor/enhancer screens in C. elegans\",\n      \"pmids\": [\"21775471\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not identify the molecular step in meiosis I that APC16 enables\", \"Substrate(s) whose ubiquitination requires APC16 not defined\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Extended APC16's role beyond meiosis by showing a requirement in mitotic germline proliferation, consistent with a general APC/C function.\",\n      \"evidence\": \"Loss-of-function genetic analysis in C. elegans germline (single lab)\",\n      \"pmids\": [\"21775471\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mitotic phenotype characterized at cellular but not molecular level\", \"Relationship between meiotic and mitotic requirements not dissected\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Provided the structural basis for APC16 function, showing how it physically assembles part of the APC/C by bridging APC3 to APC7.\",\n      \"evidence\": \"X-ray crystallography of APC3\\u0394loop alone and bound to the APC16 C-terminal domain, with biochemical mapping and mutagenesis\",\n      \"pmids\": [\"25490258\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural work used isolated APC3-APC16 module, not the holo-APC/C\", \"Functional consequence of disrupting the asymmetric APC3-APC16 interface not tested in cells\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How APC16-mediated APC7 recruitment quantitatively shapes APC/C substrate selectivity and activity in vivo remains unresolved.\",\n      \"evidence\": null,\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No defined set of substrates dependent specifically on the APC16-APC7 module\", \"Regulation of APC16 across cell-cycle phases not characterized\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [2, 4, 5]},\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\"APC/C\", \"Arc Lamp subcomplex\"],\n    \"partners\": [\"APC3\", \"APC7\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}