{"gene":"CNTROB","run_date":"2026-06-09T22:57:18","timeline":{"discoveries":[{"year":2009,"finding":"Centrobin (CNTROB) localizes to the manchette, centrosome, and the marginal ring of the spermatid acroplaxome during spermiogenesis, where it interacts with keratin 5-containing intermediate filaments. A truncated centrobin (caused by an endogenous retroviral insertion in intron 10 of Cntrob in hd mutant rats) results in a defective acroplaxome marginal ring and separation of the centrosome from its nuclear attachment site, leading to disruption of the head-tail coupling apparatus, spermatid decapitation, and male infertility.","method":"Genetic (rat hd mutant with retroviral insertion in Cntrob), immunofluorescence localization, co-localization with keratin 5 intermediate filaments, ultrastructural analysis of mutant spermatids","journal":"Biology of reproduction","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic loss-of-function with defined cellular phenotype and direct localization experiments in a single lab study; interaction with keratin 5 shown by co-localization but not biochemically reconstituted","pmids":["19710508"],"is_preprint":false},{"year":2018,"finding":"Centrobin (CNTROB) is required for primary ciliogenesis: CNTROB knockout in hTERT-RPE1 cells increased the frequency of monocentriolar and acentriolar cells and abrogated primary ciliation upon serum starvation. Ultrastructural analysis showed defective axonemal extension after mother centriole docking. Centrobin primarily localizes to daughter centrioles but also associates with mother centrioles upon serum starvation. A C-terminal portion of centrobin that interacts with CP110 and tubulin is required for ciliogenesis. Centrobin depletion in zebrafish embryos caused microcephaly, body curvature, and laterality defects consistent with ciliary dysfunction.","method":"Genome editing (CNTROB knockout in hTERT-RPE1), novel monoclonal antibody localization, ultrastructural analysis (electron microscopy), co-immunoprecipitation/interaction with CP110 and tubulin, centrobin depletion in zebrafish embryos with morphological and laterality phenotyping","journal":"The Journal of cell biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — genome-edited knockout with defined cellular phenotype, ultrastructural analysis, protein interaction studies (CP110 and tubulin), and in vivo validation in zebrafish; multiple orthogonal methods in a single rigorous study","pmids":["29440264"],"is_preprint":false}],"current_model":"Centrobin (CNTROB) is a centrosomal protein that localizes primarily to daughter centrioles (and to mother centrioles upon serum starvation) and functions as a positive regulator of primary ciliogenesis by enabling axonemal extension after mother centriole docking, interacting with CP110 and tubulin via its C-terminal domain; it also plays an essential role in spermatogenesis by localizing to the acroplaxome marginal ring and interacting with keratin 5-containing intermediate filaments to maintain the head-tail coupling apparatus and prevent spermatid decapitation."},"narrative":{"mechanistic_narrative":"Centrobin (CNTROB) is a centriolar protein that links centriole biology to ciliogenesis and to the structural integrity of the spermatid head-tail junction [PMID:29440264, PMID:19710508]. In cycling cells it localizes primarily to daughter centrioles and additionally associates with mother centrioles upon serum starvation, where it is required for primary ciliogenesis: its loss increases monocentriolar and acentriolar cells and blocks axonemal extension after mother centriole docking, a function that depends on a C-terminal region interacting with CP110 and tubulin [PMID:29440264]. Consistent with a conserved ciliary role, centrobin depletion in zebrafish produces microcephaly, body curvature, and laterality defects characteristic of ciliary dysfunction [PMID:29440264]. During spermiogenesis centrobin localizes to the manchette, centrosome, and the acroplaxome marginal ring, where it associates with keratin 5-containing intermediate filaments to maintain the head-tail coupling apparatus; a truncating Cntrob mutation in hd mutant rats disrupts the marginal ring, detaches the centrosome from its nuclear attachment site, and causes spermatid decapitation and male infertility [PMID:19710508].","teleology":[{"year":2009,"claim":"Established the first in vivo function of centrobin, showing it anchors the spermatid centrosome to the nucleus and maintains the head-tail coupling apparatus rather than acting solely as a generic centriolar marker.","evidence":"Genetic rat hd mutant (retroviral insertion in Cntrob intron 10), immunofluorescence co-localization with keratin 5 intermediate filaments, and ultrastructural analysis of mutant spermatids","pmids":["19710508"],"confidence":"Medium","gaps":["Keratin 5 interaction shown by co-localization, not biochemically reconstituted","Domain of centrobin mediating intermediate filament association not mapped","Single-lab study in one model system"]},{"year":2018,"claim":"Defined centrobin as a positive regulator of primary ciliogenesis, resolving how it acts at the centriole by mapping a C-terminal CP110/tubulin-interacting region required for axonemal extension after mother centriole docking.","evidence":"CNTROB knockout in hTERT-RPE1 cells, monoclonal antibody localization, electron microscopy, co-immunoprecipitation with CP110 and tubulin, and centrobin depletion in zebrafish embryos","pmids":["29440264"],"confidence":"High","gaps":["Mechanism by which the CP110/tubulin interaction promotes axonemal extension not resolved at molecular detail","Basis of daughter- versus mother-centriole localization switch upon serum starvation unclear","Relationship between the ciliary and spermatogenic functions not directly tested"]},{"year":null,"claim":"How centrobin's centriolar/ciliary role and its spermatid head-tail anchoring role are mechanistically unified, and whether the same interaction surfaces underlie both, remains open.","evidence":"","pmids":[],"confidence":"High","gaps":["No structural model of centrobin or its interaction interfaces","Regulation of centrobin localization across cell types not characterized","No defined enzymatic activity or post-translational regulation reported"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[1]}],"localization":[{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[0,1]},{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[1]},{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[1]},{"term_id":"R-HSA-1474165","term_label":"Reproduction","supporting_discovery_ids":[0]}],"complexes":[],"partners":["CP110","TUBB","KRT5"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8N137","full_name":"Centrobin","aliases":["Centrosomal BRCA2-interacting protein","LYST-interacting protein 8"],"length_aa":903,"mass_kda":101.3,"function":"Required for centriole duplication. Inhibition of centriole duplication leading to defects in cytokinesis","subcellular_location":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole","url":"https://www.uniprot.org/uniprotkb/Q8N137/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CNTROB","classification":"Not Classified","n_dependent_lines":18,"n_total_lines":1208,"dependency_fraction":0.014900662251655629},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/CNTROB","total_profiled":1310},"omim":[{"mim_id":"613529","title":"CENTROSOMAL PROTEIN, 152-KD; CEP152","url":"https://www.omim.org/entry/613529"},{"mim_id":"611425","title":"CENTROBIN, CENTRIOLE DUPLICATION AND SPINDLE ASSEMBLY PROTEIN; CNTROB","url":"https://www.omim.org/entry/611425"},{"mim_id":"609279","title":"CENTROMERIC PROTEIN J; CENPJ","url":"https://www.omim.org/entry/609279"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Centrosome","reliability":"Supported"},{"location":"Basal body","reliability":"Supported"},{"location":"Flagellar centriole","reliability":"Supported"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/CNTROB"},"hgnc":{"alias_symbol":["LIP8","PP1221"],"prev_symbol":[]},"alphafold":{"accession":"Q8N137","domains":[],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N137","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N137-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N137-F1-predicted_aligned_error_v6.png","plddt_mean":66.0},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CNTROB","jax_strain_url":"https://www.jax.org/strain/search?query=CNTROB"},"sequence":{"accession":"Q8N137","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8N137.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8N137/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N137"}},"corpus_meta":[{"pmid":"11131027","id":"PMC_11131027","title":"Secreted lipases of Candida albicans: cloning, characterisation and expression analysis of a new gene family with at least ten members.","date":"2000","source":"Archives of microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/11131027","citation_count":156,"is_preprint":false},{"pmid":"17646357","id":"PMC_17646357","title":"Lipase 8 affects the pathogenesis of Candida albicans.","date":"2007","source":"Infection and immunity","url":"https://pubmed.ncbi.nlm.nih.gov/17646357","citation_count":68,"is_preprint":false},{"pmid":"15707847","id":"PMC_15707847","title":"Identification and characterisation of LIP7 and LIP8 genes encoding two extracellular triacylglycerol lipases in the yeast Yarrowia lipolytica.","date":"2005","source":"Fungal genetics and biology : FG & B","url":"https://pubmed.ncbi.nlm.nih.gov/15707847","citation_count":67,"is_preprint":false},{"pmid":"19710508","id":"PMC_19710508","title":"Rat hd mutation reveals an essential role of centrobin in spermatid head shaping and assembly of the head-tail coupling apparatus.","date":"2009","source":"Biology of reproduction","url":"https://pubmed.ncbi.nlm.nih.gov/19710508","citation_count":62,"is_preprint":false},{"pmid":"32786123","id":"PMC_32786123","title":"Identification of a lipase gene with a role in tomato fruit short-chain fatty acid-derived flavor volatiles by genome-wide association.","date":"2020","source":"The Plant journal : for cell and molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/32786123","citation_count":47,"is_preprint":false},{"pmid":"33332529","id":"PMC_33332529","title":"Metabolic engineering of Saccharomyces cerevisiae for production of β-carotene from hydrophobic substrates.","date":"2021","source":"FEMS yeast research","url":"https://pubmed.ncbi.nlm.nih.gov/33332529","citation_count":33,"is_preprint":false},{"pmid":"22639089","id":"PMC_22639089","title":"Extracellular expression and characterization of thermostable lipases, LIP8, LIP14 and LIP18, from Yarrowia lipolytica.","date":"2012","source":"Biotechnology letters","url":"https://pubmed.ncbi.nlm.nih.gov/22639089","citation_count":28,"is_preprint":false},{"pmid":"36344539","id":"PMC_36344539","title":"The diagnostic yield, candidate genes, and pitfalls for a genetic study of intellectual disability in 118 middle eastern families.","date":"2022","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/36344539","citation_count":28,"is_preprint":false},{"pmid":"25514405","id":"PMC_25514405","title":"Modulation of induced cytotoxicity of doxorubicin by using apoferritin and liposomal cages.","date":"2014","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/25514405","citation_count":25,"is_preprint":false},{"pmid":"29440264","id":"PMC_29440264","title":"Centrobin controls primary ciliogenesis in vertebrates.","date":"2018","source":"The Journal of cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/29440264","citation_count":24,"is_preprint":false},{"pmid":"20676630","id":"PMC_20676630","title":"Surface display of active lipases Lip7 and Lip8 from Yarrowia lipolytica on Saccharomyces cerevisiae.","date":"2010","source":"Applied microbiology and biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/20676630","citation_count":18,"is_preprint":false},{"pmid":"19887576","id":"PMC_19887576","title":"A novel active endogenous retrovirus family contributes to genome variability in rat inbred strains.","date":"2009","source":"Genome research","url":"https://pubmed.ncbi.nlm.nih.gov/19887576","citation_count":15,"is_preprint":false},{"pmid":"15383719","id":"PMC_15383719","title":"Cloning, expression, and characterization of a lipolytic enzyme gene (lip8) from Pseudomonas aeruginosa LST-03.","date":"2004","source":"Journal of molecular microbiology and biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/15383719","citation_count":14,"is_preprint":false},{"pmid":"25449652","id":"PMC_25449652","title":"Biochemical characterization of Yarrowia lipolytica LIP8, a secreted lipase with a cleavable C-terminal region.","date":"2014","source":"Biochimica et biophysica acta","url":"https://pubmed.ncbi.nlm.nih.gov/25449652","citation_count":4,"is_preprint":false},{"pmid":"37020999","id":"PMC_37020999","title":"Using multi-tissue transcriptome-wide association study to identify candidate susceptibility genes for respiratory infectious diseases.","date":"2023","source":"Frontiers in genetics","url":"https://pubmed.ncbi.nlm.nih.gov/37020999","citation_count":3,"is_preprint":false},{"pmid":"27918162","id":"PMC_27918162","title":"[Mutations in genes affecting fertility of men - current routine laboratory genetic diagnostics and searching for more DNA segments and genes influencing spermatogenesis].","date":"2016","source":"Ceska gynekologie","url":"https://pubmed.ncbi.nlm.nih.gov/27918162","citation_count":2,"is_preprint":false},{"pmid":"27380164","id":"PMC_27380164","title":"Expression, purification, crystallization, and diffraction analysis of a selenomethionyl lipase Lip8 from Yarrowia lipolytica.","date":"2018","source":"Preparative biochemistry & biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/27380164","citation_count":1,"is_preprint":false},{"pmid":"40711600","id":"PMC_40711600","title":"A missense mutation in TCFL5 is associated with male infertility due to oligoasthenoteratozoospermia.","date":"2025","source":"Molecular genetics and genomics : MGG","url":"https://pubmed.ncbi.nlm.nih.gov/40711600","citation_count":1,"is_preprint":false},{"pmid":"41522695","id":"PMC_41522695","title":"Genetic architecture of the tomato fruit lipidome.","date":"2025","source":"PNAS nexus","url":"https://pubmed.ncbi.nlm.nih.gov/41522695","citation_count":0,"is_preprint":false},{"pmid":"21634119","id":"PMC_21634119","title":"[Methylation profiling of the cell cycle regulating genes in placenta of human embryos with chromosomal mosaicism].","date":"2011","source":"Molekuliarnaia biologiia","url":"https://pubmed.ncbi.nlm.nih.gov/21634119","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.07.08.602461","title":"Genetic architecture of the tomato fruit lipidome; new insights link lipid and volatile compounds","date":"2024-07-08","source":"bioRxiv","url":"https://doi.org/10.1101/2024.07.08.602461","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":12211,"output_tokens":1305,"usd":0.028104,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7321,"output_tokens":1536,"usd":0.037503,"stage2_stop_reason":"end_turn"},"total_usd":0.065607,"stage1_batch_id":"msgbatch_01ACAxJQabDsht39JXeWG22d","stage2_batch_id":"msgbatch_01QEU22A9U5sbPTgsMzTmvSf","note":"batch pricing = 50% of standard"},"stage1_raw":"I need to carefully classify each paper before extracting discoveries.\n\n**Classification:**\n- Papers [1], [2], [3], [5], [6], [7], [11], [13], [14], [17], [19], [21]: These describe LIP8 genes in fungi (Candida albicans, Yarrowia lipolytica, Pseudomonas aeruginosa, Saccharomyces cerevisiae) or plants (tomato Sl-LIP8). These are SYMBOL COLLISIONS — the LIP8 alias for CNTROB refers to the human gene (also known as PP1221/CNTROB), not microbial/plant lipases. The corpus is predominantly about CNTROB as a centrosomal protein; these lipase papers are unrelated.\n\n- Paper [4]: Describes rat Cntrob (centrobin) — ORTHOLOG. Include.\n- Paper [10]: Describes human CNTROB (centrobin) — canonical. Include.\n- Paper [12]: Describes an ERV insertion disrupting Cntrob splicing in rats — relevant context for [4]. Include.\n- Paper [8]: Lists CNTROB as a candidate gene for intellectual disability — association study, no mechanism. Exclude.\n- Paper [15]: TWAS association study listing CNTROB — no mechanism. Exclude.\n- Paper [16]: Screening study listing CNTROB — no mechanism. Exclude.\n- Paper [18]: Lists CNTROB as a transcriptional target of TCFL5 — no direct mechanism for CNTROB protein. Exclude.\n- Paper [20]: Methylation profiling listing CNTROB — no mechanism. Exclude.\n- Paper [9]: About liposomal doxorubicin formulation \"lip-8-dox\" — unrelated. Exclude.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2009,\n      \"finding\": \"Centrobin (CNTROB) localizes to the manchette, centrosome, and the marginal ring of the spermatid acroplaxome during spermiogenesis, where it interacts with keratin 5-containing intermediate filaments. A truncated centrobin (caused by an endogenous retroviral insertion in intron 10 of Cntrob in hd mutant rats) results in a defective acroplaxome marginal ring and separation of the centrosome from its nuclear attachment site, leading to disruption of the head-tail coupling apparatus, spermatid decapitation, and male infertility.\",\n      \"method\": \"Genetic (rat hd mutant with retroviral insertion in Cntrob), immunofluorescence localization, co-localization with keratin 5 intermediate filaments, ultrastructural analysis of mutant spermatids\",\n      \"journal\": \"Biology of reproduction\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic loss-of-function with defined cellular phenotype and direct localization experiments in a single lab study; interaction with keratin 5 shown by co-localization but not biochemically reconstituted\",\n      \"pmids\": [\"19710508\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Centrobin (CNTROB) is required for primary ciliogenesis: CNTROB knockout in hTERT-RPE1 cells increased the frequency of monocentriolar and acentriolar cells and abrogated primary ciliation upon serum starvation. Ultrastructural analysis showed defective axonemal extension after mother centriole docking. Centrobin primarily localizes to daughter centrioles but also associates with mother centrioles upon serum starvation. A C-terminal portion of centrobin that interacts with CP110 and tubulin is required for ciliogenesis. Centrobin depletion in zebrafish embryos caused microcephaly, body curvature, and laterality defects consistent with ciliary dysfunction.\",\n      \"method\": \"Genome editing (CNTROB knockout in hTERT-RPE1), novel monoclonal antibody localization, ultrastructural analysis (electron microscopy), co-immunoprecipitation/interaction with CP110 and tubulin, centrobin depletion in zebrafish embryos with morphological and laterality phenotyping\",\n      \"journal\": \"The Journal of cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genome-edited knockout with defined cellular phenotype, ultrastructural analysis, protein interaction studies (CP110 and tubulin), and in vivo validation in zebrafish; multiple orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"29440264\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"Centrobin (CNTROB) is a centrosomal protein that localizes primarily to daughter centrioles (and to mother centrioles upon serum starvation) and functions as a positive regulator of primary ciliogenesis by enabling axonemal extension after mother centriole docking, interacting with CP110 and tubulin via its C-terminal domain; it also plays an essential role in spermatogenesis by localizing to the acroplaxome marginal ring and interacting with keratin 5-containing intermediate filaments to maintain the head-tail coupling apparatus and prevent spermatid decapitation.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"Centrobin (CNTROB) is a centriolar protein that links centriole biology to ciliogenesis and to the structural integrity of the spermatid head-tail junction [#1, #0]. In cycling cells it localizes primarily to daughter centrioles and additionally associates with mother centrioles upon serum starvation, where it is required for primary ciliogenesis: its loss increases monocentriolar and acentriolar cells and blocks axonemal extension after mother centriole docking, a function that depends on a C-terminal region interacting with CP110 and tubulin [#1]. Consistent with a conserved ciliary role, centrobin depletion in zebrafish produces microcephaly, body curvature, and laterality defects characteristic of ciliary dysfunction [#1]. During spermiogenesis centrobin localizes to the manchette, centrosome, and the acroplaxome marginal ring, where it associates with keratin 5-containing intermediate filaments to maintain the head-tail coupling apparatus; a truncating Cntrob mutation in hd mutant rats disrupts the marginal ring, detaches the centrosome from its nuclear attachment site, and causes spermatid decapitation and male infertility [#0].\",\n  \"teleology\": [\n    {\n      \"year\": 2009,\n      \"claim\": \"Established the first in vivo function of centrobin, showing it anchors the spermatid centrosome to the nucleus and maintains the head-tail coupling apparatus rather than acting solely as a generic centriolar marker.\",\n      \"evidence\": \"Genetic rat hd mutant (retroviral insertion in Cntrob intron 10), immunofluorescence co-localization with keratin 5 intermediate filaments, and ultrastructural analysis of mutant spermatids\",\n      \"pmids\": [\"19710508\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Keratin 5 interaction shown by co-localization, not biochemically reconstituted\",\n        \"Domain of centrobin mediating intermediate filament association not mapped\",\n        \"Single-lab study in one model system\"\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Defined centrobin as a positive regulator of primary ciliogenesis, resolving how it acts at the centriole by mapping a C-terminal CP110/tubulin-interacting region required for axonemal extension after mother centriole docking.\",\n      \"evidence\": \"CNTROB knockout in hTERT-RPE1 cells, monoclonal antibody localization, electron microscopy, co-immunoprecipitation with CP110 and tubulin, and centrobin depletion in zebrafish embryos\",\n      \"pmids\": [\"29440264\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Mechanism by which the CP110/tubulin interaction promotes axonemal extension not resolved at molecular detail\",\n        \"Basis of daughter- versus mother-centriole localization switch upon serum starvation unclear\",\n        \"Relationship between the ciliary and spermatogenic functions not directly tested\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How centrobin's centriolar/ciliary role and its spermatid head-tail anchoring role are mechanistically unified, and whether the same interaction surfaces underlie both, remains open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No structural model of centrobin or its interaction interfaces\",\n        \"Regulation of centrobin localization across cell types not characterized\",\n        \"No defined enzymatic activity or post-translational regulation reported\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-1474165\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"CP110\", \"TUBB\", \"KRT5\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}