{"gene":"ANKRD53","run_date":"2026-06-09T22:02:43","timeline":{"discoveries":[{"year":2016,"finding":"ANKRD53 was identified as a novel DDA3-interacting protein through proteomic analysis, and is recruited to the mitotic spindle by DDA3.","method":"Proteomic analysis (co-immunoprecipitation/mass spectrometry), subcellular localization experiments","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — proteomic identification with localization data, single lab, multiple supporting observations","pmids":["26820536"],"is_preprint":false},{"year":2016,"finding":"ANKRD53 is phosphorylated by mitotic kinases during mitosis, as indicated by expression profile analysis during mitotic progression.","method":"Expression profiling and phosphorylation analysis during mitosis","journal":"Biochemical and biophysical research communications","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single method, no mutagenesis or kinase identification","pmids":["26820536"],"is_preprint":false},{"year":2016,"finding":"Depletion of ANKRD53 in HeLa cells delayed mitotic progression, increased unaligned chromosomes, decreased spindle MT polymerization, activated the spindle assembly checkpoint (SAC), and increased bi-nuclei and polylobed nuclei, establishing a role in spindle dynamics and cytokinesis.","method":"siRNA knockdown in HeLa cells with mitotic phenotype readouts (chromosome alignment, spindle dynamics, SAC activation, nuclear morphology)","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean KD with multiple defined cellular phenotypes, single lab","pmids":["26820536"],"is_preprint":false},{"year":2016,"finding":"Although ANKRD53 is recruited to the mitotic spindle by DDA3, it counteracts DDA3 activity for spindle MT polymerization, placing ANKRD53 as a functional antagonist of DDA3 in this pathway.","method":"Genetic epistasis/functional comparison in DDA3 and ANKRD53 knockdown cells with spindle dynamics readouts","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — epistasis with defined phenotypic readout, single lab","pmids":["26820536"],"is_preprint":false},{"year":2026,"finding":"ANKRD53 overexpression enhanced forskolin-stimulated lipolysis and mitochondrial respiration in human primary adipocytes, while silencing impaired these processes; adipose-targeted overexpression in mice increased lipolysis in vivo.","method":"Overexpression and knockdown in human primary adipocytes (lipolysis assay: free fatty acid/glycerol release; mitochondrial respiration: oxygen consumption rate); AAV-mediated overexpression in mouse iWAT","journal":"Molecular metabolism","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — loss-of-function and gain-of-function with multiple orthogonal functional readouts in vitro and in vivo, single lab","pmids":["41654016"],"is_preprint":false},{"year":2026,"finding":"ANKRD53 interacts with ACSL1 (identified by immunoprecipitation-mass spectrometry) and promotes ACSL1 mitochondrial localization, thereby channeling lipolysis-derived free fatty acids into β-oxidation; silencing ACSL1 abrogated ANKRD53's metabolic effects.","method":"Immunoprecipitation-mass spectrometry for interactor identification; subcellular fractionation/localization of ACSL1; ACSL1 knockdown epistasis experiment","journal":"Molecular metabolism","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal IP-MS plus epistasis with defined functional rescue, single lab","pmids":["41654016"],"is_preprint":false}],"current_model":"ANKRD53 is a scaffold protein with at least two distinct mechanistic roles: during mitosis, it is recruited to the mitotic spindle by DDA3 (and is phosphorylated by mitotic kinases), where it counteracts DDA3 to regulate spindle MT polymerization, chromosome alignment, SAC activation, and cytokinesis; in adipocytes, it acts as an ankyrin repeat scaffold that interacts with ACSL1 and promotes its mitochondrial localization, thereby coupling lipolysis-derived fatty acid release to β-oxidation and mitochondrial respiration."},"narrative":{"mechanistic_narrative":"ANKRD53 is an ankyrin repeat scaffold protein with distinct roles in mitotic spindle regulation and adipocyte lipid metabolism [PMID:26820536, PMID:41654016]. In mitosis, it was identified as a DDA3-interacting protein that is recruited to the mitotic spindle by DDA3 [PMID:26820536], where it functionally antagonizes DDA3 to control spindle microtubule polymerization [PMID:26820536]; its depletion delays mitotic progression, produces unaligned chromosomes, reduces spindle MT polymerization, activates the spindle assembly checkpoint, and causes bi-nucleate and polylobed nuclei, indicating a requirement for proper chromosome alignment and cytokinesis [PMID:26820536]. In adipocytes, ANKRD53 binds ACSL1 and promotes its mitochondrial localization, thereby channeling lipolysis-derived free fatty acids into β-oxidation; loss of ACSL1 abolishes ANKRD53's metabolic effects [PMID:41654016], and ANKRD53 levels bidirectionally regulate forskolin-stimulated lipolysis and mitochondrial respiration in human primary adipocytes and in mouse adipose tissue [PMID:41654016]. Beyond these two contexts, no further mechanistic detail has been characterized in the available corpus.","teleology":[{"year":2016,"claim":"Established ANKRD53 as a spindle-associated factor by identifying it as a DDA3 interactor recruited to the mitotic spindle, defining a starting point for its mitotic function.","evidence":"Co-IP/mass spectrometry and subcellular localization in cultured cells","pmids":["26820536"],"confidence":"Medium","gaps":["Interaction domain and the structural basis of DDA3-mediated recruitment not mapped","Whether the DDA3 interaction is direct not established"]},{"year":2016,"claim":"Indicated ANKRD53 is a mitotic phosphoprotein, hinting at regulation by cell-cycle kinases.","evidence":"Expression and phosphorylation profiling across mitotic progression","pmids":["26820536"],"confidence":"Low","gaps":["No responsible kinase identified","No phosphosite mapping or mutagenesis","Functional consequence of phosphorylation unknown"]},{"year":2016,"claim":"Defined the functional requirement of ANKRD53 in mitosis, showing it is needed for chromosome alignment, spindle MT polymerization, SAC silencing, and faithful cytokinesis.","evidence":"siRNA knockdown in HeLa cells with multiple mitotic phenotype readouts","pmids":["26820536"],"confidence":"Medium","gaps":["Mechanism by which ANKRD53 promotes MT polymerization unknown","Single-lab, single-cell-line evidence","No rescue with wild-type vs mutant constructs reported"]},{"year":2016,"claim":"Resolved the apparent paradox of co-localization by showing ANKRD53 antagonizes DDA3 in spindle MT polymerization, placing the two proteins in opposition within one pathway.","evidence":"Genetic epistasis/functional comparison of DDA3 and ANKRD53 knockdowns with spindle readouts","pmids":["26820536"],"confidence":"Medium","gaps":["Molecular basis of antagonism not defined","Whether antagonism involves competition for a shared effector unknown"]},{"year":2026,"claim":"Revealed an unrelated metabolic function, demonstrating ANKRD53 bidirectionally controls lipolysis and mitochondrial respiration in adipocytes in vitro and in vivo.","evidence":"Overexpression/knockdown in human primary adipocytes (FFA/glycerol release, OCR) and AAV overexpression in mouse iWAT","pmids":["41654016"],"confidence":"Medium","gaps":["Single-lab evidence","Connection, if any, between mitotic and metabolic roles unestablished"]},{"year":2026,"claim":"Provided the mechanism for the metabolic effect, showing ANKRD53 binds ACSL1 and drives its mitochondrial localization to couple FFA release to β-oxidation.","evidence":"IP-MS interactor identification, ACSL1 subcellular localization, and ACSL1 knockdown epistasis","pmids":["41654016"],"confidence":"Medium","gaps":["Whether ANKRD53-ACSL1 binding is direct not shown","ANKRD53 domain mediating ACSL1 binding/mitochondrial targeting not mapped"]},{"year":null,"claim":"Whether the mitotic spindle role and the adipocyte metabolic role reflect a unifying scaffold mechanism, and how ANKRD53 is regulated across these contexts, remains unresolved.","evidence":"No discovery in the corpus links the two functions","pmids":[],"confidence":"Low","gaps":["No structural model of ANKRD53","No shared interactor connecting spindle and metabolic functions","Tissue-specific expression and regulation not characterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,5]},{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[0,3]}],"localization":[],"pathway":[{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[2,3]},{"term_id":"R-HSA-1430728","term_label":"Metabolism","supporting_discovery_ids":[4,5]}],"complexes":[],"partners":["DDA3","ACSL1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8N9V6","full_name":"Ankyrin repeat domain-containing protein 53","aliases":[],"length_aa":530,"mass_kda":59.6,"function":"Required for normal progression through mitosis. Involved in chromosome alignment and cytokinesis via regulation of microtubules polymerization","subcellular_location":"Cytoplasm, cytoskeleton, spindle; Cytoplasm, cytoskeleton, spindle pole","url":"https://www.uniprot.org/uniprotkb/Q8N9V6/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ANKRD53","classification":"Not Classified","n_dependent_lines":6,"n_total_lines":1208,"dependency_fraction":0.004966887417218543},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/ANKRD53","total_profiled":1310},"omim":[{"mim_id":"617009","title":"ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 53; ANKRD53","url":"https://www.omim.org/entry/617009"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"testis","ntpm":25.3}],"url":"https://www.proteinatlas.org/search/ANKRD53"},"hgnc":{"alias_symbol":["FLJ12056","FLJ36160"],"prev_symbol":[]},"alphafold":{"accession":"Q8N9V6","domains":[{"cath_id":"1.25.40.20","chopping":"103-273","consensus_level":"medium","plddt":85.0422,"start":103,"end":273}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N9V6","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N9V6-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N9V6-F1-predicted_aligned_error_v6.png","plddt_mean":61.94},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ANKRD53","jax_strain_url":"https://www.jax.org/strain/search?query=ANKRD53"},"sequence":{"accession":"Q8N9V6","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8N9V6.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8N9V6/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N9V6"}},"corpus_meta":[{"pmid":"26820536","id":"PMC_26820536","title":"ANKRD53 interacts with DDA3 and regulates chromosome integrity during mitosis.","date":"2016","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/26820536","citation_count":13,"is_preprint":false},{"pmid":"38801557","id":"PMC_38801557","title":"Integrative analysis indicates the potential values of ANKRD53 in stomach adenocarcinoma.","date":"2024","source":"Discover oncology","url":"https://pubmed.ncbi.nlm.nih.gov/38801557","citation_count":3,"is_preprint":false},{"pmid":"35064135","id":"PMC_35064135","title":"Identification of differentially methylated genes in first-trimester placentas with trisomy 16.","date":"2022","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/35064135","citation_count":2,"is_preprint":false},{"pmid":"41654016","id":"PMC_41654016","title":"ANKRD53 is downregulated in human obesity and coordinates lipolysis with mitochondrial oxidative metabolism in adipocytes.","date":"2026","source":"Molecular metabolism","url":"https://pubmed.ncbi.nlm.nih.gov/41654016","citation_count":0,"is_preprint":false},{"pmid":"41300918","id":"PMC_41300918","title":"Decoding Multi-Omics Signatures in Lower-Grade Glioma Using Protein-Protein Interaction-Informed Graph Attention Networks and Ensemble Learning.","date":"2025","source":"Diagnostics (Basel, Switzerland)","url":"https://pubmed.ncbi.nlm.nih.gov/41300918","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4678,"output_tokens":1307,"usd":0.01682,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8049,"output_tokens":2195,"usd":0.04756,"stage2_stop_reason":"end_turn"},"total_usd":0.06438,"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\": 2016,\n      \"finding\": \"ANKRD53 was identified as a novel DDA3-interacting protein through proteomic analysis, and is recruited to the mitotic spindle by DDA3.\",\n      \"method\": \"Proteomic analysis (co-immunoprecipitation/mass spectrometry), subcellular localization experiments\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — proteomic identification with localization data, single lab, multiple supporting observations\",\n      \"pmids\": [\"26820536\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"ANKRD53 is phosphorylated by mitotic kinases during mitosis, as indicated by expression profile analysis during mitotic progression.\",\n      \"method\": \"Expression profiling and phosphorylation analysis during mitosis\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single method, no mutagenesis or kinase identification\",\n      \"pmids\": [\"26820536\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Depletion of ANKRD53 in HeLa cells delayed mitotic progression, increased unaligned chromosomes, decreased spindle MT polymerization, activated the spindle assembly checkpoint (SAC), and increased bi-nuclei and polylobed nuclei, establishing a role in spindle dynamics and cytokinesis.\",\n      \"method\": \"siRNA knockdown in HeLa cells with mitotic phenotype readouts (chromosome alignment, spindle dynamics, SAC activation, nuclear morphology)\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean KD with multiple defined cellular phenotypes, single lab\",\n      \"pmids\": [\"26820536\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Although ANKRD53 is recruited to the mitotic spindle by DDA3, it counteracts DDA3 activity for spindle MT polymerization, placing ANKRD53 as a functional antagonist of DDA3 in this pathway.\",\n      \"method\": \"Genetic epistasis/functional comparison in DDA3 and ANKRD53 knockdown cells with spindle dynamics readouts\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — epistasis with defined phenotypic readout, single lab\",\n      \"pmids\": [\"26820536\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"ANKRD53 overexpression enhanced forskolin-stimulated lipolysis and mitochondrial respiration in human primary adipocytes, while silencing impaired these processes; adipose-targeted overexpression in mice increased lipolysis in vivo.\",\n      \"method\": \"Overexpression and knockdown in human primary adipocytes (lipolysis assay: free fatty acid/glycerol release; mitochondrial respiration: oxygen consumption rate); AAV-mediated overexpression in mouse iWAT\",\n      \"journal\": \"Molecular metabolism\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function and gain-of-function with multiple orthogonal functional readouts in vitro and in vivo, single lab\",\n      \"pmids\": [\"41654016\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"ANKRD53 interacts with ACSL1 (identified by immunoprecipitation-mass spectrometry) and promotes ACSL1 mitochondrial localization, thereby channeling lipolysis-derived free fatty acids into β-oxidation; silencing ACSL1 abrogated ANKRD53's metabolic effects.\",\n      \"method\": \"Immunoprecipitation-mass spectrometry for interactor identification; subcellular fractionation/localization of ACSL1; ACSL1 knockdown epistasis experiment\",\n      \"journal\": \"Molecular metabolism\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal IP-MS plus epistasis with defined functional rescue, single lab\",\n      \"pmids\": [\"41654016\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ANKRD53 is a scaffold protein with at least two distinct mechanistic roles: during mitosis, it is recruited to the mitotic spindle by DDA3 (and is phosphorylated by mitotic kinases), where it counteracts DDA3 to regulate spindle MT polymerization, chromosome alignment, SAC activation, and cytokinesis; in adipocytes, it acts as an ankyrin repeat scaffold that interacts with ACSL1 and promotes its mitochondrial localization, thereby coupling lipolysis-derived fatty acid release to β-oxidation and mitochondrial respiration.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ANKRD53 is an ankyrin repeat scaffold protein with distinct roles in mitotic spindle regulation and adipocyte lipid metabolism [#0, #5]. In mitosis, it was identified as a DDA3-interacting protein that is recruited to the mitotic spindle by DDA3 [#0], where it functionally antagonizes DDA3 to control spindle microtubule polymerization [#3]; its depletion delays mitotic progression, produces unaligned chromosomes, reduces spindle MT polymerization, activates the spindle assembly checkpoint, and causes bi-nucleate and polylobed nuclei, indicating a requirement for proper chromosome alignment and cytokinesis [#2]. In adipocytes, ANKRD53 binds ACSL1 and promotes its mitochondrial localization, thereby channeling lipolysis-derived free fatty acids into β-oxidation; loss of ACSL1 abolishes ANKRD53's metabolic effects [#5], and ANKRD53 levels bidirectionally regulate forskolin-stimulated lipolysis and mitochondrial respiration in human primary adipocytes and in mouse adipose tissue [#4]. Beyond these two contexts, no further mechanistic detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2016,\n      \"claim\": \"Established ANKRD53 as a spindle-associated factor by identifying it as a DDA3 interactor recruited to the mitotic spindle, defining a starting point for its mitotic function.\",\n      \"evidence\": \"Co-IP/mass spectrometry and subcellular localization in cultured cells\",\n      \"pmids\": [\"26820536\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Interaction domain and the structural basis of DDA3-mediated recruitment not mapped\", \"Whether the DDA3 interaction is direct not established\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Indicated ANKRD53 is a mitotic phosphoprotein, hinting at regulation by cell-cycle kinases.\",\n      \"evidence\": \"Expression and phosphorylation profiling across mitotic progression\",\n      \"pmids\": [\"26820536\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No responsible kinase identified\", \"No phosphosite mapping or mutagenesis\", \"Functional consequence of phosphorylation unknown\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Defined the functional requirement of ANKRD53 in mitosis, showing it is needed for chromosome alignment, spindle MT polymerization, SAC silencing, and faithful cytokinesis.\",\n      \"evidence\": \"siRNA knockdown in HeLa cells with multiple mitotic phenotype readouts\",\n      \"pmids\": [\"26820536\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism by which ANKRD53 promotes MT polymerization unknown\", \"Single-lab, single-cell-line evidence\", \"No rescue with wild-type vs mutant constructs reported\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Resolved the apparent paradox of co-localization by showing ANKRD53 antagonizes DDA3 in spindle MT polymerization, placing the two proteins in opposition within one pathway.\",\n      \"evidence\": \"Genetic epistasis/functional comparison of DDA3 and ANKRD53 knockdowns with spindle readouts\",\n      \"pmids\": [\"26820536\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular basis of antagonism not defined\", \"Whether antagonism involves competition for a shared effector unknown\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Revealed an unrelated metabolic function, demonstrating ANKRD53 bidirectionally controls lipolysis and mitochondrial respiration in adipocytes in vitro and in vivo.\",\n      \"evidence\": \"Overexpression/knockdown in human primary adipocytes (FFA/glycerol release, OCR) and AAV overexpression in mouse iWAT\",\n      \"pmids\": [\"41654016\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single-lab evidence\", \"Connection, if any, between mitotic and metabolic roles unestablished\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Provided the mechanism for the metabolic effect, showing ANKRD53 binds ACSL1 and drives its mitochondrial localization to couple FFA release to β-oxidation.\",\n      \"evidence\": \"IP-MS interactor identification, ACSL1 subcellular localization, and ACSL1 knockdown epistasis\",\n      \"pmids\": [\"41654016\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether ANKRD53-ACSL1 binding is direct not shown\", \"ANKRD53 domain mediating ACSL1 binding/mitochondrial targeting not mapped\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether the mitotic spindle role and the adipocyte metabolic role reflect a unifying scaffold mechanism, and how ANKRD53 is regulated across these contexts, remains unresolved.\",\n      \"evidence\": \"No discovery in the corpus links the two functions\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structural model of ANKRD53\", \"No shared interactor connecting spindle and metabolic functions\", \"Tissue-specific expression and regulation not characterized\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 5]},\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005819\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [2, 3]},\n      {\"term_id\": \"R-HSA-1430728\", \"supporting_discovery_ids\": [4, 5]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"DDA3\", \"ACSL1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":3,"faith_total":3,"faith_pct":100.0}}