{"gene":"SOBP","run_date":"2026-06-10T07:46:37","timeline":{"discoveries":[{"year":2008,"finding":"Jxc1/Sobp encodes a nuclear zinc finger protein with two FCS-type zinc finger domains and nuclear localization signals; wild-type protein is targeted to the nucleus, while mutant isoforms are mislocalized to the cytoplasm, establishing that nuclear localization is required for its function in cochlear growth and organ of Corti patterning.","method":"Transient expression of wild-type and mutant isoforms in cells with subcellular localization readout; genetic analysis of the jc mouse mutant","journal":"The Journal of neuroscience","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiment with functional consequence (nuclear vs. cytoplasmic mislocalization), combined with in vivo loss-of-function phenotype, single lab","pmids":["18579736"],"is_preprint":false},{"year":2010,"finding":"In jc/jc (Sobp null) mouse brains compared to +/jc controls, proteomic analysis detected differential expression of 24 proteins including dynamin and pacsin1, two interacting proteins, suggesting Sobp participates in a pathway involving these proteins during brain development.","method":"Comparative proteomics (mass spectrometry) of +/jc vs. jc/jc mouse brains","journal":"American journal of human genetics","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single proteomic screen, no direct binding or functional validation of Sobp-dynamin/pacsin1 interaction","pmids":["21035105"],"is_preprint":false},{"year":2021,"finding":"Sobp binds to Six1 and colocalizes with it in the cell nucleus, and Sobp interferes with (represses) the transcriptional activation of Six1+Eya1 target genes.","method":"Co-immunoprecipitation, immunofluorescence colocalization, luciferase transcriptional reporter assays in Xenopus embryos and cell culture; gain- and loss-of-function experiments in Xenopus","journal":"Development (Cambridge, England)","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP demonstrating direct binding, colocalization confirming nuclear complex, luciferase assay establishing transcriptional repression; multiple orthogonal methods, independently replicated in Xenopus developmental model","pmids":["34414417"],"is_preprint":false},{"year":2024,"finding":"SOBP is a bona fide SIX1 co-factor that represses SIX1+EYA transcriptional activity in mouse; SOBP can directly translocate EYA to the nucleus. SOBP co-expression with SIX1 is conserved in the mandibular arch and its derivatives during craniofacial development.","method":"Co-immunoprecipitation (SIX1-SOBP binding), luciferase transcriptional reporter assays, nuclear translocation assays in mouse cells","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP and functional luciferase assays in mouse system, direct nuclear translocation assay, single lab, preprint not yet peer-reviewed","pmids":["bio_10.1101_2024.09.28.615612"],"is_preprint":true}],"current_model":"SOBP (Jxc1) is a nuclear zinc finger protein that acts as a transcriptional co-factor by directly binding the transcription factor SIX1 in the nucleus, repressing SIX1+EYA1-driven transcriptional activation, and facilitating nuclear translocation of EYA; loss-of-function in mice disrupts cochlear growth and organ of Corti patterning, while mutations in humans cause intellectual disability, linking its nuclear transcriptional regulatory role to sensory organ and brain development."},"narrative":{"mechanistic_narrative":"SOBP (Jxc1) is a nuclear zinc finger protein that functions as a transcriptional co-factor regulating SIX1-driven gene expression during sensory organ and craniofacial development [PMID:18579736, PMID:34414417]. It contains two FCS-type zinc finger domains and nuclear localization signals that target it to the nucleus; this nuclear localization is required for its role in cochlear growth and organ of Corti patterning, since mutant isoforms are mislocalized to the cytoplasm and fail to function [PMID:18579736]. In the nucleus, SOBP directly binds SIX1 and colocalizes with it, repressing transcriptional activation of SIX1+EYA1 target genes [PMID:34414417]. SOBP also directly translocates EYA to the nucleus, and its co-expression with SIX1 is conserved in the developing mandibular arch [PMID:bio_10.1101_2024.09.28.615612]. Beyond this SIX1/EYA regulatory axis and its developmental phenotypes, no further biochemical mechanism has been characterized in the available corpus.","teleology":[{"year":2008,"claim":"Established that Jxc1/Sobp is a nuclear zinc finger protein whose nuclear localization is functionally required, answering where the protein acts and why mutant alleles fail.","evidence":"Subcellular localization of wild-type versus mutant isoforms in transfected cells, combined with genetic analysis of the jc mouse mutant","pmids":["18579736"],"confidence":"Medium","gaps":["No molecular partner or DNA target identified at this stage","Mechanism linking nuclear localization to cochlear patterning unresolved","FCS zinc finger domain function not biochemically defined"]},{"year":2010,"claim":"A proteomic screen of Sobp-null brains began to place Sobp within a broader protein network, hinting at developmental pathways affected by its loss.","evidence":"Comparative mass spectrometry of +/jc versus jc/jc mouse brains, detecting differential expression of dynamin and pacsin1 among 24 proteins","pmids":["21035105"],"confidence":"Low","gaps":["Single proteomic screen with no direct binding or functional validation of Sobp–dynamin/pacsin1 interaction","Differential abundance could be indirect or downstream","No mechanistic link to the later-defined SIX1/EYA role"]},{"year":2021,"claim":"Identified SIX1 as a direct nuclear binding partner and defined SOBP as a repressor of SIX1+EYA1 transcriptional output, supplying the molecular mechanism behind its developmental function.","evidence":"Reciprocal Co-IP, immunofluorescence colocalization, and luciferase reporter assays with gain- and loss-of-function in Xenopus embryos and cell culture","pmids":["34414417"],"confidence":"High","gaps":["Direct DNA-binding versus co-factor-only repression not distinguished","Specific target genes repressed in vivo not enumerated","Structural basis of SIX1–SOBP interaction unknown"]},{"year":2024,"claim":"Extended the SIX1 co-factor model to mouse and craniofacial development, adding the finding that SOBP can directly drive EYA nuclear translocation.","evidence":"Co-IP, luciferase reporter assays, and nuclear translocation assays in mouse cells (preprint)","pmids":["bio_10.1101_2024.09.28.615612"],"confidence":"Medium","gaps":["Preprint not yet peer-reviewed; single lab","Mechanism of EYA translocation not defined at the domain level","In vivo consequence of repression for craniofacial outcomes not established"]},{"year":null,"claim":"How SOBP molecularly couples SIX1 binding to transcriptional repression and EYA shuttling, and whether it contacts DNA directly, remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the SOBP–SIX1–EYA assembly","Direct DNA-binding activity of the FCS zinc fingers untested","Full set of regulated target genes unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[2,3]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[2,3]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,2]}],"pathway":[{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[2,3]}],"complexes":[],"partners":["SIX1","EYA1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"A7XYQ1","full_name":"Sine oculis-binding protein homolog","aliases":["Jackson circler protein 1"],"length_aa":873,"mass_kda":92.7,"function":"Implicated in development of the cochlea","subcellular_location":"","url":"https://www.uniprot.org/uniprotkb/A7XYQ1/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/SOBP","classification":"Not Classified","n_dependent_lines":1,"n_total_lines":1208,"dependency_fraction":0.0008278145695364238},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"MIF","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/SOBP","total_profiled":1310},"omim":[{"mim_id":"613671","title":"IMPAIRED INTELLECTUAL DEVELOPMENT, ANTERIOR MAXILLARY PROTRUSION, AND STRABISMUS; MRAMS","url":"https://www.omim.org/entry/613671"},{"mim_id":"613667","title":"SINE OCULIS-BINDING PROTEIN HOMOLOG; SOBP","url":"https://www.omim.org/entry/613667"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"},{"location":"Vesicles","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in many","driving_tissues":[],"url":"https://www.proteinatlas.org/search/SOBP"},"hgnc":{"alias_symbol":["FLJ10159"],"prev_symbol":[]},"alphafold":{"accession":"A7XYQ1","domains":[{"cath_id":"-","chopping":"146-193","consensus_level":"medium","plddt":89.6708,"start":146,"end":193},{"cath_id":"2.30.170","chopping":"221-268","consensus_level":"medium","plddt":79.7531,"start":221,"end":268}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/A7XYQ1","model_url":"https://alphafold.ebi.ac.uk/files/AF-A7XYQ1-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-A7XYQ1-F1-predicted_aligned_error_v6.png","plddt_mean":51.41},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SOBP","jax_strain_url":"https://www.jax.org/strain/search?query=SOBP"},"sequence":{"accession":"A7XYQ1","fasta_url":"https://rest.uniprot.org/uniprotkb/A7XYQ1.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/A7XYQ1/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/A7XYQ1"}},"corpus_meta":[{"pmid":"18579736","id":"PMC_18579736","title":"Jxc1/Sobp, encoding a nuclear zinc finger protein, is critical for cochlear growth, cell fate, and patterning of the organ of corti.","date":"2008","source":"The Journal of neuroscience : the official journal of the Society for Neuroscience","url":"https://pubmed.ncbi.nlm.nih.gov/18579736","citation_count":30,"is_preprint":false},{"pmid":"21035105","id":"PMC_21035105","title":"SOBP is mutated in syndromic and nonsyndromic intellectual disability and is highly expressed in the brain limbic system.","date":"2010","source":"American journal of human genetics","url":"https://pubmed.ncbi.nlm.nih.gov/21035105","citation_count":23,"is_preprint":false},{"pmid":"34414417","id":"PMC_34414417","title":"Sobp modulates the transcriptional activation of Six1 target genes and is required during craniofacial development.","date":"2021","source":"Development (Cambridge, England)","url":"https://pubmed.ncbi.nlm.nih.gov/34414417","citation_count":18,"is_preprint":false},{"pmid":"28599495","id":"PMC_28599495","title":"Investigation of the relative biological effectiveness and uniform isobiological killing effects of irradiation with a clinical carbon SOBP beam on DNA repair deficient CHO cells.","date":"2017","source":"Oncology letters","url":"https://pubmed.ncbi.nlm.nih.gov/28599495","citation_count":6,"is_preprint":false},{"pmid":"27875573","id":"PMC_27875573","title":"A Nucleoside Anticancer Drug, 1-(3-C-Ethynyl-β-D-Ribo-Pentofuranosyl)Cytosine, Induces Depth-Dependent Enhancement of Tumor Cell Death in Spread-Out Bragg Peak (SOBP) of Proton Beam.","date":"2016","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/27875573","citation_count":6,"is_preprint":false},{"pmid":"22802190","id":"PMC_22802190","title":"Chicken sine oculis binding protein homolog (sobp), a novel gene that may regulate feather development.","date":"2012","source":"Poultry science","url":"https://pubmed.ncbi.nlm.nih.gov/22802190","citation_count":4,"is_preprint":false},{"pmid":"31686349","id":"PMC_31686349","title":"Recurrent intragenic exon rearrangements of SOBP and AUTS2 in non-Hodgkin B-cell lymphoma.","date":"2019","source":"International journal of hematology","url":"https://pubmed.ncbi.nlm.nih.gov/31686349","citation_count":4,"is_preprint":false},{"pmid":"38219488","id":"PMC_38219488","title":"The contribution of high-LET track to DNA damage formation and cell death for Monoenergy and SOBP carbon ion irradiation.","date":"2024","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/38219488","citation_count":3,"is_preprint":false},{"pmid":"37673077","id":"PMC_37673077","title":"Monte Carlo simulations of cell survival in proton SOBP.","date":"2023","source":"Physics in medicine and biology","url":"https://pubmed.ncbi.nlm.nih.gov/37673077","citation_count":2,"is_preprint":false},{"pmid":"38377599","id":"PMC_38377599","title":"Calculation of biological effectiveness of SOBP proton beams: a TOPAS Monte Carlo study.","date":"2024","source":"Biomedical physics & engineering express","url":"https://pubmed.ncbi.nlm.nih.gov/38377599","citation_count":1,"is_preprint":false},{"pmid":"36675684","id":"PMC_36675684","title":"Monte Carlo-Based Radiobiological Investigation of the Most Optimal Ion Beam Forming SOBP for Particle Therapy.","date":"2022","source":"Journal of personalized medicine","url":"https://pubmed.ncbi.nlm.nih.gov/36675684","citation_count":0,"is_preprint":false},{"pmid":"40769191","id":"PMC_40769191","title":"Calculation of DNA damage at different depths of proton SOBP based on a new method and its applications.","date":"2025","source":"Physics in medicine and biology","url":"https://pubmed.ncbi.nlm.nih.gov/40769191","citation_count":0,"is_preprint":false},{"pmid":"42243886","id":"PMC_42243886","title":"Tissue-level RBE determination and normal lung responses along the proton SOBP.","date":"2026","source":"Radiation oncology (London, England)","url":"https://pubmed.ncbi.nlm.nih.gov/42243886","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.09.28.615612","title":"Direct and Indirect Regulation of SIX1+EYA Transcriptional Activity by PA2G4, MCRS1, and SOBP","date":"2024-09-30","source":"bioRxiv","url":"https://doi.org/10.1101/2024.09.28.615612","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.09.04.611307","title":"Discordance in acute gastrointestinal toxicity between synchrotron-based proton and linac-based electron ultra-high dose rate irradiation","date":"2024-09-08","source":"bioRxiv","url":"https://doi.org/10.1101/2024.09.04.611307","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.08.10.607473","title":"3D printed microtissue cassettes enabling high throughput proton radiobiological assays","date":"2024-08-11","source":"bioRxiv","url":"https://doi.org/10.1101/2024.08.10.607473","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.07.12.603197","title":"FLASH Bragg-peak irradiation with a therapeutic carbon ion beam: first in vivo results","date":"2024-07-16","source":"bioRxiv","url":"https://doi.org/10.1101/2024.07.12.603197","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":11251,"output_tokens":1068,"usd":0.024886,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7614,"output_tokens":1823,"usd":0.041822,"stage2_stop_reason":"end_turn"},"total_usd":0.066708,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2008,\n      \"finding\": \"Jxc1/Sobp encodes a nuclear zinc finger protein with two FCS-type zinc finger domains and nuclear localization signals; wild-type protein is targeted to the nucleus, while mutant isoforms are mislocalized to the cytoplasm, establishing that nuclear localization is required for its function in cochlear growth and organ of Corti patterning.\",\n      \"method\": \"Transient expression of wild-type and mutant isoforms in cells with subcellular localization readout; genetic analysis of the jc mouse mutant\",\n      \"journal\": \"The Journal of neuroscience\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiment with functional consequence (nuclear vs. cytoplasmic mislocalization), combined with in vivo loss-of-function phenotype, single lab\",\n      \"pmids\": [\"18579736\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"In jc/jc (Sobp null) mouse brains compared to +/jc controls, proteomic analysis detected differential expression of 24 proteins including dynamin and pacsin1, two interacting proteins, suggesting Sobp participates in a pathway involving these proteins during brain development.\",\n      \"method\": \"Comparative proteomics (mass spectrometry) of +/jc vs. jc/jc mouse brains\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single proteomic screen, no direct binding or functional validation of Sobp-dynamin/pacsin1 interaction\",\n      \"pmids\": [\"21035105\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Sobp binds to Six1 and colocalizes with it in the cell nucleus, and Sobp interferes with (represses) the transcriptional activation of Six1+Eya1 target genes.\",\n      \"method\": \"Co-immunoprecipitation, immunofluorescence colocalization, luciferase transcriptional reporter assays in Xenopus embryos and cell culture; gain- and loss-of-function experiments in Xenopus\",\n      \"journal\": \"Development (Cambridge, England)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP demonstrating direct binding, colocalization confirming nuclear complex, luciferase assay establishing transcriptional repression; multiple orthogonal methods, independently replicated in Xenopus developmental model\",\n      \"pmids\": [\"34414417\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"SOBP is a bona fide SIX1 co-factor that represses SIX1+EYA transcriptional activity in mouse; SOBP can directly translocate EYA to the nucleus. SOBP co-expression with SIX1 is conserved in the mandibular arch and its derivatives during craniofacial development.\",\n      \"method\": \"Co-immunoprecipitation (SIX1-SOBP binding), luciferase transcriptional reporter assays, nuclear translocation assays in mouse cells\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP and functional luciferase assays in mouse system, direct nuclear translocation assay, single lab, preprint not yet peer-reviewed\",\n      \"pmids\": [\"bio_10.1101_2024.09.28.615612\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"SOBP (Jxc1) is a nuclear zinc finger protein that acts as a transcriptional co-factor by directly binding the transcription factor SIX1 in the nucleus, repressing SIX1+EYA1-driven transcriptional activation, and facilitating nuclear translocation of EYA; loss-of-function in mice disrupts cochlear growth and organ of Corti patterning, while mutations in humans cause intellectual disability, linking its nuclear transcriptional regulatory role to sensory organ and brain development.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SOBP (Jxc1) is a nuclear zinc finger protein that functions as a transcriptional co-factor regulating SIX1-driven gene expression during sensory organ and craniofacial development [#0, #2]. It contains two FCS-type zinc finger domains and nuclear localization signals that target it to the nucleus; this nuclear localization is required for its role in cochlear growth and organ of Corti patterning, since mutant isoforms are mislocalized to the cytoplasm and fail to function [#0]. In the nucleus, SOBP directly binds SIX1 and colocalizes with it, repressing transcriptional activation of SIX1+EYA1 target genes [#2]. SOBP also directly translocates EYA to the nucleus, and its co-expression with SIX1 is conserved in the developing mandibular arch [#3]. Beyond this SIX1/EYA regulatory axis and its developmental phenotypes, no further biochemical mechanism has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2008,\n      \"claim\": \"Established that Jxc1/Sobp is a nuclear zinc finger protein whose nuclear localization is functionally required, answering where the protein acts and why mutant alleles fail.\",\n      \"evidence\": \"Subcellular localization of wild-type versus mutant isoforms in transfected cells, combined with genetic analysis of the jc mouse mutant\",\n      \"pmids\": [\"18579736\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No molecular partner or DNA target identified at this stage\",\n        \"Mechanism linking nuclear localization to cochlear patterning unresolved\",\n        \"FCS zinc finger domain function not biochemically defined\"\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"A proteomic screen of Sobp-null brains began to place Sobp within a broader protein network, hinting at developmental pathways affected by its loss.\",\n      \"evidence\": \"Comparative mass spectrometry of +/jc versus jc/jc mouse brains, detecting differential expression of dynamin and pacsin1 among 24 proteins\",\n      \"pmids\": [\"21035105\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Single proteomic screen with no direct binding or functional validation of Sobp\\u2013dynamin/pacsin1 interaction\",\n        \"Differential abundance could be indirect or downstream\",\n        \"No mechanistic link to the later-defined SIX1/EYA role\"\n      ]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Identified SIX1 as a direct nuclear binding partner and defined SOBP as a repressor of SIX1+EYA1 transcriptional output, supplying the molecular mechanism behind its developmental function.\",\n      \"evidence\": \"Reciprocal Co-IP, immunofluorescence colocalization, and luciferase reporter assays with gain- and loss-of-function in Xenopus embryos and cell culture\",\n      \"pmids\": [\"34414417\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct DNA-binding versus co-factor-only repression not distinguished\",\n        \"Specific target genes repressed in vivo not enumerated\",\n        \"Structural basis of SIX1\\u2013SOBP interaction unknown\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Extended the SIX1 co-factor model to mouse and craniofacial development, adding the finding that SOBP can directly drive EYA nuclear translocation.\",\n      \"evidence\": \"Co-IP, luciferase reporter assays, and nuclear translocation assays in mouse cells (preprint)\",\n      \"pmids\": [\"bio_10.1101_2024.09.28.615612\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Preprint not yet peer-reviewed; single lab\",\n        \"Mechanism of EYA translocation not defined at the domain level\",\n        \"In vivo consequence of repression for craniofacial outcomes not established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How SOBP molecularly couples SIX1 binding to transcriptional repression and EYA shuttling, and whether it contacts DNA directly, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of the SOBP\\u2013SIX1\\u2013EYA assembly\",\n        \"Direct DNA-binding activity of the FCS zinc fingers untested\",\n        \"Full set of regulated target genes unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [2, 3]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"SIX1\", \"EYA1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":3,"faith_total":3,"faith_pct":100.0}}