{"gene":"ODAD2","run_date":"2026-06-10T05:19:52","timeline":{"discoveries":[{"year":2013,"finding":"Drosophila Gudu (ortholog of human ARMC4/ODAD2), an Armadillo repeat-containing protein, is required for formation of the individualization complex during spermatid maturation; RNAi knockdown using four independent lines targeting two non-overlapping regions caused defects in individualization complex formation and male infertility.","method":"RNAi loss-of-function in Drosophila (ubiquitous and testis-specific bam-Gal4 driver); phenotypic analysis of individualization complex formation and spermatogenesis","journal":"Gene","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — four independent RNAi lines with two non-overlapping target regions, both ubiquitous and tissue-specific knockdown confirming phenotype, single lab","pmids":["24055424"],"is_preprint":false},{"year":2022,"finding":"ARMC4/ODAD2 physically interacts with NF-κB (demonstrated by co-immunoprecipitation) and functions as a negative regulator of NF-κB activity; high ARMC4 expression reduced NF-κB-dependent gene expression, NF-κB transcriptional activity, cell proliferation, anchorage-independent growth, and migration in vitro, and decreased xenograft tumor growth in vivo in colorectal cancer models.","method":"Validation-based insertional mutagenesis (VBIM) screen; co-immunoprecipitation; overexpression with NF-κB reporter assays; in vitro proliferation and migration assays; in vivo xenograft tumor model","journal":"International journal of molecular sciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP plus multiple functional assays (reporter, proliferation, migration, xenograft), single lab, multiple orthogonal methods","pmids":["35269880"],"is_preprint":false},{"year":2023,"finding":"ODAD2 (ARMC4) is a component of the outer dynein arm (ODA) docking machinery in motile cilia; immunofluorescence microscopy in individuals with ODAD1, ODAD2, ODAD3, or ODAD4 defects showed that CLXN (calaxin/ODAD5) was undetectable from ciliary axonemes, placing ODAD2 as required for proper assembly/localization of ODA-docking complex-associated proteins including calaxin.","method":"Immunofluorescence microscopy of ciliary axonemes from patients with ODAD2 defects; absence of CLXN signal used as functional readout of ODA-docking complex integrity","journal":"Genetics in medicine : official journal of the American College of Medical Genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct immunofluorescence localization in human patient tissue with functional consequence for ODA assembly, single study but clear loss-of-function readout","pmids":["36727596"],"is_preprint":false},{"year":2025,"finding":"Drosophila Gudu (ortholog of ARMC4/ODAD2) is phosphorylated at Ser9 by the testis-specific kinase dTSSK2 (ortholog of human TSSK4); this phosphorylation partially contributes to individualization complex integrity and sperm motility.","method":"Phosphoproteomic analysis; identification of dTSSK2 substrate Gudu at Ser9; genetic/functional analysis of individualization complex integrity and sperm motility","journal":"Communications biology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — phosphoproteomic identification of phosphorylation site plus functional consequence for individualization complex integrity, single lab, partial contribution noted","pmids":["40335644"],"is_preprint":false}],"current_model":"ARMC4/ODAD2 is an Armadillo repeat-containing protein that functions as a subunit of the outer dynein arm docking complex in motile cilia (required for ciliary ODA assembly and localization of associated proteins including calaxin/ODAD5), is required for spermatid individualization complex formation during spermatogenesis (a role conserved from Drosophila Gudu to vertebrates, with Gudu phosphorylated at Ser9 by dTSSK2), and in colorectal cancer cells physically interacts with NF-κB and negatively regulates its transcriptional activity."},"narrative":{"mechanistic_narrative":"ODAD2 (ARMC4/Gudu) is an Armadillo repeat-containing protein that functions in the assembly of motile cilia and in spermatogenesis [PMID:24055424, PMID:36727596]. In motile cilia, ODAD2 is a component of the outer dynein arm (ODA) docking machinery; loss of ODAD2 abolishes ciliary axonemal localization of the ODA-docking-associated protein calaxin (CLXN/ODAD5), establishing ODAD2 as required for proper assembly and localization of ODA-docking complex components [PMID:36727596]. In spermatogenesis, the Drosophila ortholog Gudu is required for formation of the spermatid individualization complex, and its integrity depends in part on Gudu phosphorylation at Ser9 by the testis-specific kinase dTSSK2 (ortholog of human TSSK4), linking ODAD2 function to sperm maturation and motility [PMID:24055424, PMID:40335644]. Independently, in colorectal cancer cells ARMC4/ODAD2 physically interacts with NF-κB and acts as a negative regulator of NF-κB transcriptional activity, suppressing proliferation, anchorage-independent growth, migration, and xenograft tumor growth [PMID:35269880].","teleology":[{"year":2013,"claim":"Established the first functional role for the ODAD2 ortholog by showing Gudu is required for spermatid individualization complex formation, implicating this Armadillo-repeat protein in male fertility.","evidence":"RNAi loss-of-function in Drosophila with ubiquitous and testis-specific drivers; phenotypic analysis of individualization and spermatogenesis","pmids":["24055424"],"confidence":"Medium","gaps":["Molecular interaction partners within the individualization complex not identified","Role of the Armadillo repeats in protein-protein interactions undefined","Vertebrate spermatogenesis role not directly tested"]},{"year":2022,"claim":"Revealed an unexpected role for ARMC4/ODAD2 outside cilia, showing it physically binds NF-κB and suppresses NF-κB-driven transcription and tumor growth in colorectal cancer.","evidence":"VBIM screen, reciprocal co-immunoprecipitation, NF-κB reporter assays, proliferation/migration assays, and xenograft tumor model","pmids":["35269880"],"confidence":"Medium","gaps":["Mechanism by which ARMC4 inhibits NF-κB transcriptional output unresolved","Whether the NF-κB interaction is direct or bridged is unclear","Connection between this nuclear/signaling role and the ciliary docking role not addressed"]},{"year":2023,"claim":"Defined ODAD2 as part of the outer dynein arm docking machinery in human motile cilia by showing its loss eliminates ciliary calaxin localization.","evidence":"Immunofluorescence microscopy of ciliary axonemes from patients with ODAD2 defects, using CLXN absence as a readout of ODA-docking integrity","pmids":["36727596"],"confidence":"Medium","gaps":["Direct physical interactions among ODAD2 and other ODAD subunits not biochemically resolved","Structural basis for docking complex assembly unknown","Whether ODAD2 directly recruits calaxin or acts upstream is not distinguished"]},{"year":2025,"claim":"Connected post-translational regulation to ODAD2 ortholog function by identifying dTSSK2-mediated Ser9 phosphorylation of Gudu as a contributor to individualization complex integrity and sperm motility.","evidence":"Phosphoproteomic identification of the dTSSK2 substrate site plus genetic/functional analysis in Drosophila","pmids":["40335644"],"confidence":"Medium","gaps":["Phosphorylation contributes only partially, so additional regulatory inputs remain unidentified","Conservation of the Ser9 phospho-site regulation in human ODAD2 not demonstrated","Molecular consequence of phosphorylation on protein interactions unknown"]},{"year":null,"claim":"How ODAD2's ciliary ODA-docking role, its spermatogenesis function, and its NF-κB-regulatory activity mechanistically relate within a single protein remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of ODAD2 within the ODA docking complex","Direct binding partners mediating each function not jointly mapped","Whether the cancer-associated NF-κB role is tissue-specific or generalizes is unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[2]}],"localization":[{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[2]}],"pathway":[{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[2]}],"complexes":["outer dynein arm docking complex"],"partners":["NFKB","CLXN","TSSK4"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q5T2S8","full_name":"Outer dynein arm-docking complex subunit 2","aliases":["Armadillo repeat-containing protein 4"],"length_aa":1044,"mass_kda":115.7,"function":"Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule (PubMed:27486780). Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules (PubMed:23849778)","subcellular_location":"Cytoplasm, cytoskeleton, cilium axoneme; Cytoplasm, cytoskeleton, cilium basal body","url":"https://www.uniprot.org/uniprotkb/Q5T2S8/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ODAD2","classification":"Not Classified","n_dependent_lines":2,"n_total_lines":1208,"dependency_fraction":0.0016556291390728477},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"MIF","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/ODAD2","total_profiled":1310},"omim":[{"mim_id":"615451","title":"CILIARY DYSKINESIA, PRIMARY, 23; CILD23","url":"https://www.omim.org/entry/615451"},{"mim_id":"615408","title":"OUTER DYNEIN ARM DOCKING COMPLEX SUBUNIT 2; ODAD2","url":"https://www.omim.org/entry/615408"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"End piece","reliability":"Approved"},{"location":"Acrosome","reliability":"Additional"},{"location":"Principal piece","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"fallopian tube","ntpm":21.8},{"tissue":"testis","ntpm":38.0}],"url":"https://www.proteinatlas.org/search/ODAD2"},"hgnc":{"alias_symbol":["FLJ10817","FLJ10376","DKFZP434P1735","CILD23","gudu"],"prev_symbol":["ARMC4"]},"alphafold":{"accession":"Q5T2S8","domains":[{"cath_id":"-","chopping":"2-190","consensus_level":"high","plddt":80.2813,"start":2,"end":190},{"cath_id":"-","chopping":"197-301","consensus_level":"high","plddt":83.8154,"start":197,"end":301},{"cath_id":"1.25.10","chopping":"449-534","consensus_level":"medium","plddt":89.5715,"start":449,"end":534},{"cath_id":"1.25.10.10","chopping":"535-587_601-632_654-660","consensus_level":"medium","plddt":92.3363,"start":535,"end":660},{"cath_id":"1.25.10.10","chopping":"857-1040","consensus_level":"medium","plddt":94.9893,"start":857,"end":1040}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5T2S8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q5T2S8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q5T2S8-F1-predicted_aligned_error_v6.png","plddt_mean":80.88},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ODAD2","jax_strain_url":"https://www.jax.org/strain/search?query=ODAD2"},"sequence":{"accession":"Q5T2S8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q5T2S8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q5T2S8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5T2S8"}},"corpus_meta":[{"pmid":"24055424","id":"PMC_24055424","title":"Gudu, an Armadillo repeat-containing protein, is required for spermatogenesis in Drosophila.","date":"2013","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/24055424","citation_count":29,"is_preprint":false},{"pmid":"38203325","id":"PMC_38203325","title":"Genetic Alterations of NF-κB and Its Regulators: A Rich Platform to Advance Colorectal Cancer Diagnosis and Treatment.","date":"2023","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/38203325","citation_count":13,"is_preprint":false},{"pmid":"36727596","id":"PMC_36727596","title":"Pathogenic variants in CLXN encoding the outer dynein arm docking-associated calcium-binding protein calaxin cause primary ciliary dyskinesia.","date":"2023","source":"Genetics in medicine : official journal of the American College of Medical Genetics","url":"https://pubmed.ncbi.nlm.nih.gov/36727596","citation_count":10,"is_preprint":false},{"pmid":"35269880","id":"PMC_35269880","title":"Using VBIM Technique to Discover ARMC4/ODAD2 as a Novel Negative Regulator of NF-κB and a New Tumor Suppressor in Colorectal Cancer.","date":"2022","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/35269880","citation_count":7,"is_preprint":false},{"pmid":"12918113","id":"PMC_12918113","title":"Identification of H. pylori strain specific DNA sequences between two clinical isolates from NUD and gastric ulcer by SSH.","date":"2003","source":"World journal of gastroenterology","url":"https://pubmed.ncbi.nlm.nih.gov/12918113","citation_count":5,"is_preprint":false},{"pmid":"40335644","id":"PMC_40335644","title":"Testis-specific serine/threonine kinase dTSSK2 regulates sperm motility and male fertility in Drosophila.","date":"2025","source":"Communications biology","url":"https://pubmed.ncbi.nlm.nih.gov/40335644","citation_count":2,"is_preprint":false},{"pmid":"39004484","id":"PMC_39004484","title":"Prenatal diagnosis of a de novo 10p12.1p11.23 microdeletion encompassing the WAC gene in a fetus associated with bilateral hydronephrosis and right clubfoot on prenatal ultrasound.","date":"2024","source":"Taiwanese journal of obstetrics & gynecology","url":"https://pubmed.ncbi.nlm.nih.gov/39004484","citation_count":0,"is_preprint":false},{"pmid":"41592177","id":"PMC_41592177","title":"Navigating taxonomic confusion: three novel freshwater crabs (Brachyura: Potamonautidae: Potamonautes) nested within a species complex in the Drakensberg Mountains, South Africa.","date":"2026","source":"Invertebrate systematics","url":"https://pubmed.ncbi.nlm.nih.gov/41592177","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6458,"output_tokens":1224,"usd":0.018867,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7813,"output_tokens":2045,"usd":0.045095,"stage2_stop_reason":"end_turn"},"total_usd":0.063962,"stage1_batch_id":"msgbatch_013a8chtv3AWyTqv4z4sEF4C","stage2_batch_id":"msgbatch_01AHsuW63vinsvuTgzmQ3n62","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2013,\n      \"finding\": \"Drosophila Gudu (ortholog of human ARMC4/ODAD2), an Armadillo repeat-containing protein, is required for formation of the individualization complex during spermatid maturation; RNAi knockdown using four independent lines targeting two non-overlapping regions caused defects in individualization complex formation and male infertility.\",\n      \"method\": \"RNAi loss-of-function in Drosophila (ubiquitous and testis-specific bam-Gal4 driver); phenotypic analysis of individualization complex formation and spermatogenesis\",\n      \"journal\": \"Gene\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — four independent RNAi lines with two non-overlapping target regions, both ubiquitous and tissue-specific knockdown confirming phenotype, single lab\",\n      \"pmids\": [\"24055424\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"ARMC4/ODAD2 physically interacts with NF-κB (demonstrated by co-immunoprecipitation) and functions as a negative regulator of NF-κB activity; high ARMC4 expression reduced NF-κB-dependent gene expression, NF-κB transcriptional activity, cell proliferation, anchorage-independent growth, and migration in vitro, and decreased xenograft tumor growth in vivo in colorectal cancer models.\",\n      \"method\": \"Validation-based insertional mutagenesis (VBIM) screen; co-immunoprecipitation; overexpression with NF-κB reporter assays; in vitro proliferation and migration assays; in vivo xenograft tumor model\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP plus multiple functional assays (reporter, proliferation, migration, xenograft), single lab, multiple orthogonal methods\",\n      \"pmids\": [\"35269880\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"ODAD2 (ARMC4) is a component of the outer dynein arm (ODA) docking machinery in motile cilia; immunofluorescence microscopy in individuals with ODAD1, ODAD2, ODAD3, or ODAD4 defects showed that CLXN (calaxin/ODAD5) was undetectable from ciliary axonemes, placing ODAD2 as required for proper assembly/localization of ODA-docking complex-associated proteins including calaxin.\",\n      \"method\": \"Immunofluorescence microscopy of ciliary axonemes from patients with ODAD2 defects; absence of CLXN signal used as functional readout of ODA-docking complex integrity\",\n      \"journal\": \"Genetics in medicine : official journal of the American College of Medical Genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct immunofluorescence localization in human patient tissue with functional consequence for ODA assembly, single study but clear loss-of-function readout\",\n      \"pmids\": [\"36727596\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Drosophila Gudu (ortholog of ARMC4/ODAD2) is phosphorylated at Ser9 by the testis-specific kinase dTSSK2 (ortholog of human TSSK4); this phosphorylation partially contributes to individualization complex integrity and sperm motility.\",\n      \"method\": \"Phosphoproteomic analysis; identification of dTSSK2 substrate Gudu at Ser9; genetic/functional analysis of individualization complex integrity and sperm motility\",\n      \"journal\": \"Communications biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — phosphoproteomic identification of phosphorylation site plus functional consequence for individualization complex integrity, single lab, partial contribution noted\",\n      \"pmids\": [\"40335644\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ARMC4/ODAD2 is an Armadillo repeat-containing protein that functions as a subunit of the outer dynein arm docking complex in motile cilia (required for ciliary ODA assembly and localization of associated proteins including calaxin/ODAD5), is required for spermatid individualization complex formation during spermatogenesis (a role conserved from Drosophila Gudu to vertebrates, with Gudu phosphorylated at Ser9 by dTSSK2), and in colorectal cancer cells physically interacts with NF-κB and negatively regulates its transcriptional activity.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ODAD2 (ARMC4/Gudu) is an Armadillo repeat-containing protein that functions in the assembly of motile cilia and in spermatogenesis [#0, #2]. In motile cilia, ODAD2 is a component of the outer dynein arm (ODA) docking machinery; loss of ODAD2 abolishes ciliary axonemal localization of the ODA-docking-associated protein calaxin (CLXN/ODAD5), establishing ODAD2 as required for proper assembly and localization of ODA-docking complex components [#2]. In spermatogenesis, the Drosophila ortholog Gudu is required for formation of the spermatid individualization complex, and its integrity depends in part on Gudu phosphorylation at Ser9 by the testis-specific kinase dTSSK2 (ortholog of human TSSK4), linking ODAD2 function to sperm maturation and motility [#0, #3]. Independently, in colorectal cancer cells ARMC4/ODAD2 physically interacts with NF-\\u03baB and acts as a negative regulator of NF-\\u03baB transcriptional activity, suppressing proliferation, anchorage-independent growth, migration, and xenograft tumor growth [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Established the first functional role for the ODAD2 ortholog by showing Gudu is required for spermatid individualization complex formation, implicating this Armadillo-repeat protein in male fertility.\",\n      \"evidence\": \"RNAi loss-of-function in Drosophila with ubiquitous and testis-specific drivers; phenotypic analysis of individualization and spermatogenesis\",\n      \"pmids\": [\"24055424\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Molecular interaction partners within the individualization complex not identified\",\n        \"Role of the Armadillo repeats in protein-protein interactions undefined\",\n        \"Vertebrate spermatogenesis role not directly tested\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Revealed an unexpected role for ARMC4/ODAD2 outside cilia, showing it physically binds NF-\\u03baB and suppresses NF-\\u03baB-driven transcription and tumor growth in colorectal cancer.\",\n      \"evidence\": \"VBIM screen, reciprocal co-immunoprecipitation, NF-\\u03baB reporter assays, proliferation/migration assays, and xenograft tumor model\",\n      \"pmids\": [\"35269880\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Mechanism by which ARMC4 inhibits NF-\\u03baB transcriptional output unresolved\",\n        \"Whether the NF-\\u03baB interaction is direct or bridged is unclear\",\n        \"Connection between this nuclear/signaling role and the ciliary docking role not addressed\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Defined ODAD2 as part of the outer dynein arm docking machinery in human motile cilia by showing its loss eliminates ciliary calaxin localization.\",\n      \"evidence\": \"Immunofluorescence microscopy of ciliary axonemes from patients with ODAD2 defects, using CLXN absence as a readout of ODA-docking integrity\",\n      \"pmids\": [\"36727596\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Direct physical interactions among ODAD2 and other ODAD subunits not biochemically resolved\",\n        \"Structural basis for docking complex assembly unknown\",\n        \"Whether ODAD2 directly recruits calaxin or acts upstream is not distinguished\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Connected post-translational regulation to ODAD2 ortholog function by identifying dTSSK2-mediated Ser9 phosphorylation of Gudu as a contributor to individualization complex integrity and sperm motility.\",\n      \"evidence\": \"Phosphoproteomic identification of the dTSSK2 substrate site plus genetic/functional analysis in Drosophila\",\n      \"pmids\": [\"40335644\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Phosphorylation contributes only partially, so additional regulatory inputs remain unidentified\",\n        \"Conservation of the Ser9 phospho-site regulation in human ODAD2 not demonstrated\",\n        \"Molecular consequence of phosphorylation on protein interactions unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How ODAD2's ciliary ODA-docking role, its spermatogenesis function, and its NF-\\u03baB-regulatory activity mechanistically relate within a single protein remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"No structural model of ODAD2 within the ODA docking complex\",\n        \"Direct binding partners mediating each function not jointly mapped\",\n        \"Whether the cancer-associated NF-\\u03baB role is tissue-specific or generalizes is unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\"outer dynein arm docking complex\"],\n    \"partners\": [\"NFKB\", \"CLXN\", \"TSSK4\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}