{"gene":"TADA2B","run_date":"2026-06-10T10:51:54","timeline":{"discoveries":[{"year":2021,"finding":"TADA2B, as a subunit of the chromatin-modifying SAGA complex, is a central regulator of pluripotency maintenance, survival, growth, and lineage specification in human embryonic stem cells, as determined by integrated genome-scale loss- and gain-of-function CRISPR screens.","method":"Genome-scale CRISPR knockout and gain-of-function screens in human embryonic stem cells with readouts for proliferation, differentiation into three germ layers, and apoptosis resistance","journal":"Genes & development","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genome-scale functional screening with multiple orthogonal readouts (proliferation, differentiation, survival), single lab","pmids":["34711655"],"is_preprint":false},{"year":2026,"finding":"Loss of Tada2b (a SAGA complex member) strongly inhibits hematopoiesis in vivo, causing a buildup of immature hematopoietic cells in the bone marrow; mechanistically, loss of Tada2b reduces histone H3 lysine 9 acetylation (H3K9ac) levels and alters H2B ubiquitination (H2Bub) enrichment in hematopoietic stem and progenitor cells, implicating disruption of SAGA complex acetyltransferase and deubiquitinase activities, and is associated with upregulation of interferon pathway genes, reduced mitochondrial activity, and increased megakaryocyte progenitor cell commitment.","method":"Genome-wide in vivo CRISPR knockout screen in HSPCs followed by chromatin modification analysis (H3K9ac and H2Bub levels) and transcriptomic profiling","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — in vivo CRISPR KO with specific chromatin (H3K9ac, H2Bub) and transcriptomic readouts, replicated across preprint and peer-reviewed publication from same group","pmids":["41577693"],"is_preprint":false},{"year":2025,"finding":"TADA2B (as part of the SAGA complex histone acetyltransferase module) constitutively binds XRCC1 primarily via the BRCT II domain, independent of DNA damage status or GCN5 acetyltransferase activity; depletion of TADA2B significantly impairs XRCC1 recruitment efficiency to DNA damage sites, and the SCAR26-associated XRCC1 variant disrupts TADA2B binding while maintaining LIG3 interaction.","method":"Co-immunoprecipitation/pulldown identifying TADA2B–XRCC1 interaction via distinct BRCT domain mapping; siRNA depletion of TADA2B with quantification of XRCC1 recruitment to damage foci; analysis of SCAR26-associated mutant","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct binding assay with domain mapping, depletion phenotype, and disease-variant validation; single lab, preprint not yet peer-reviewed","pmids":["bio_10.1101_2025.08.24.672030"],"is_preprint":true},{"year":2025,"finding":"TADA2B was identified as a proximity interactor of HMGB1 in resting monocytic THP-1 cells, and this interaction is significantly altered upon LPS-induced Toll-like receptor 4 activation (stress), as detected by BioID-based proximity proteomics.","method":"BioID proximity proteomics in THP-1 cells comparing resting and LPS-stressed conditions; selected interactions confirmed by proximity ligation assay","journal":"The Journal of biological chemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — proximity proteomics identification of TADA2B as HMGB1 interactor; no functional follow-up specific to TADA2B, single lab","pmids":["41161382"],"is_preprint":false}],"current_model":"TADA2B is an integral subunit of the SAGA complex histone acetyltransferase module that constitutively interacts with XRCC1 (via its BRCT II domain) to pre-organize DNA base excision/single-strand break repair machinery, while also depositing H3K9ac and regulating H2B ubiquitination in hematopoietic stem and progenitor cells to support normal hematopoiesis and pluripotency maintenance, with loss of TADA2B disrupting these chromatin modifications and activating interferon pathway gene expression."},"narrative":{"mechanistic_narrative":"TADA2B is a subunit of the chromatin-modifying SAGA complex that links histone modification to stem cell maintenance, lineage commitment, and genome stability [PMID:34711655, PMID:41577693]. Within SAGA's histone acetyltransferase module, TADA2B supports deposition of histone H3 lysine 9 acetylation (H3K9ac) and influences H2B ubiquitination (H2Bub) enrichment; in hematopoietic stem and progenitor cells, its loss reduces H3K9ac, alters H2Bub, blocks hematopoiesis with accumulation of immature bone marrow cells, lowers mitochondrial activity, skews toward megakaryocyte progenitor commitment, and activates interferon pathway gene expression [PMID:41577693]. Beyond its chromatin role, TADA2B constitutively binds the DNA single-strand break repair scaffold XRCC1 through its BRCT II domain, independent of DNA damage status and of GCN5 acetyltransferase activity, and TADA2B depletion impairs XRCC1 recruitment to damage sites; an SCAR26-associated XRCC1 variant selectively disrupts this TADA2B interaction while preserving LIG3 binding [PMID:bio_10.1101_2025.08.24.672030]. In human embryonic stem cells, TADA2B is a central regulator of pluripotency maintenance, survival, growth, and three-germ-layer lineage specification [PMID:34711655].","teleology":[{"year":2021,"claim":"Establishing whether TADA2B has a defined cellular requirement, genome-scale CRISPR screening showed it is a central regulator of pluripotency, survival, growth, and lineage specification, placing this SAGA subunit at the core of stem cell fate decisions.","evidence":"Genome-scale CRISPR knockout and gain-of-function screens in human embryonic stem cells with proliferation, differentiation, and apoptosis readouts","pmids":["34711655"],"confidence":"Medium","gaps":["Does not resolve which chromatin marks or target genes mediate the pluripotency phenotype","No mechanistic dissection of TADA2B's contribution distinct from other SAGA subunits"]},{"year":2025,"claim":"Addressing whether TADA2B has a function beyond transcription-linked chromatin, domain-mapped binding assays showed it constitutively binds the repair scaffold XRCC1 via the BRCT II domain and is needed for efficient XRCC1 recruitment to damage, defining a pre-organized link between SAGA and single-strand break repair.","evidence":"Co-IP/pulldown with BRCT domain mapping, siRNA depletion with quantification of XRCC1 damage-foci recruitment, and SCAR26 variant analysis (preprint)","pmids":["bio_10.1101_2025.08.24.672030"],"confidence":"Medium","gaps":["Preprint not yet peer-reviewed","Whether the interaction requires the intact SAGA complex or TADA2B alone is unresolved","Functional consequence of disrupted recruitment for repair efficiency and disease not directly tested"]},{"year":2025,"claim":"Probing TADA2B's broader interaction landscape, proximity proteomics placed it near HMGB1 in monocytes with the association changing upon TLR4 activation, hinting at a stress-responsive context though without functional follow-up.","evidence":"BioID proximity proteomics in resting versus LPS-stressed THP-1 cells with proximity ligation confirmation","pmids":["41161382"],"confidence":"Low","gaps":["Proximity association without functional validation specific to TADA2B","No demonstration of direct binding or biological consequence"]},{"year":2026,"claim":"Connecting TADA2B's chromatin activity to a physiological output, in vivo CRISPR knockout showed its loss reduces H3K9ac and alters H2Bub in hematopoietic stem/progenitor cells, blocking hematopoiesis and activating interferon genes, establishing it as required for normal blood cell production through SAGA acetyltransferase/deubiquitinase activities.","evidence":"Genome-wide in vivo CRISPR KO screen in HSPCs with H3K9ac/H2Bub chromatin analysis and transcriptomic profiling","pmids":["41577693"],"confidence":"High","gaps":["Direct catalytic role of TADA2B in deubiquitination versus indirect effect not separated","Mechanism linking chromatin changes to interferon gene upregulation unresolved","Relationship between hematopoietic and DNA-repair functions not addressed"]},{"year":null,"claim":"How TADA2B's SAGA-dependent chromatin role and its XRCC1-anchored DNA-repair role are mechanistically integrated, and whether they share a structural basis, remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of TADA2B within SAGA or bound to XRCC1","Whether chromatin and repair functions are coupled or independent is unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[1]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[2]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[1,2]}],"pathway":[{"term_id":"R-HSA-4839726","term_label":"Chromatin organization","supporting_discovery_ids":[1]},{"term_id":"R-HSA-73894","term_label":"DNA Repair","supporting_discovery_ids":[2]}],"complexes":["SAGA complex"],"partners":["XRCC1","HMGB1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q86TJ2","full_name":"Transcriptional adapter 2-beta","aliases":["ADA2-like protein beta","ADA2-beta"],"length_aa":420,"mass_kda":48.5,"function":"Coactivates PAX5-dependent transcription together with either SMARCA4 or GCN5L2","subcellular_location":"Nucleus","url":"https://www.uniprot.org/uniprotkb/Q86TJ2/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/TADA2B","classification":"Not Classified","n_dependent_lines":324,"n_total_lines":1208,"dependency_fraction":0.2682119205298013},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"MED19","stoichiometry":10.0},{"gene":"TAF12","stoichiometry":10.0},{"gene":"TRRAP","stoichiometry":10.0},{"gene":"ENY2","stoichiometry":0.2},{"gene":"KPNA1","stoichiometry":0.2},{"gene":"KPNA6","stoichiometry":0.2},{"gene":"MED14","stoichiometry":0.2},{"gene":"MED29","stoichiometry":0.2},{"gene":"MED31","stoichiometry":0.2},{"gene":"MED4","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/TADA2B","total_profiled":1310},"omim":[{"mim_id":"608790","title":"TRANSCRIPTIONAL ADAPTOR 2B; TADA2B","url":"https://www.omim.org/entry/608790"},{"mim_id":"602303","title":"LYSINE ACETYLTRANSFERASE 2B; KAT2B","url":"https://www.omim.org/entry/602303"},{"mim_id":"602301","title":"LYSINE ACETYLTRANSFERASE 2A; KAT2A","url":"https://www.omim.org/entry/602301"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nuclear speckles","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TADA2B"},"hgnc":{"alias_symbol":["MGC21874"],"prev_symbol":[]},"alphafold":{"accession":"Q86TJ2","domains":[{"cath_id":"1.10.10.60","chopping":"71-122","consensus_level":"medium","plddt":93.3546,"start":71,"end":122},{"cath_id":"-","chopping":"347-411","consensus_level":"high","plddt":90.1583,"start":347,"end":411},{"cath_id":"1.10.287","chopping":"150-232","consensus_level":"medium","plddt":91.3269,"start":150,"end":232}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q86TJ2","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q86TJ2-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q86TJ2-F1-predicted_aligned_error_v6.png","plddt_mean":86.69},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TADA2B","jax_strain_url":"https://www.jax.org/strain/search?query=TADA2B"},"sequence":{"accession":"Q86TJ2","fasta_url":"https://rest.uniprot.org/uniprotkb/Q86TJ2.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q86TJ2/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q86TJ2"}},"corpus_meta":[{"pmid":"24336571","id":"PMC_24336571","title":"Genome-scale CRISPR-Cas9 knockout screening in human cells.","date":"2013","source":"Science (New York, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/24336571","citation_count":4103,"is_preprint":false},{"pmid":"34711655","id":"PMC_34711655","title":"Integrated loss- and gain-of-function screens define a core network governing human embryonic stem cell behavior.","date":"2021","source":"Genes & development","url":"https://pubmed.ncbi.nlm.nih.gov/34711655","citation_count":17,"is_preprint":false},{"pmid":"38007639","id":"PMC_38007639","title":"Integrative analysis of histone acetyltransferase KAT2A in human cancer.","date":"2023","source":"Cancer biomarkers : section A of Disease markers","url":"https://pubmed.ncbi.nlm.nih.gov/38007639","citation_count":7,"is_preprint":false},{"pmid":"40475452","id":"PMC_40475452","title":"In vivo CRISPR screening identifies SAGA complex members as key regulators of hematopoiesis.","date":"2025","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/40475452","citation_count":4,"is_preprint":false},{"pmid":"39316935","id":"PMC_39316935","title":"Divergent transcriptomic profiles in depressed individuals with hyper- and hypophagia implicating inflammatory status.","date":"2024","source":"Journal of psychiatric research","url":"https://pubmed.ncbi.nlm.nih.gov/39316935","citation_count":1,"is_preprint":false},{"pmid":"41577693","id":"PMC_41577693","title":"In vivo CRISPR screening identifies SAGA complex members as key regulators of hematopoiesis.","date":"2026","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/41577693","citation_count":0,"is_preprint":false},{"pmid":"41161382","id":"PMC_41161382","title":"Mapping the intracellular HMGB1 interactome and alterations induced by Toll-like receptor 4 activation.","date":"2025","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/41161382","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.08.24.672030","title":"GCN5-TADA2B in the SAGA complex provide constitutive fine-tuning control of XRCC1 recruitment and focal retention at DNA damage sites","date":"2025-08-28","source":"bioRxiv","url":"https://doi.org/10.1101/2025.08.24.672030","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6001,"output_tokens":1250,"usd":0.018377,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7848,"output_tokens":2114,"usd":0.046045,"stage2_stop_reason":"end_turn"},"total_usd":0.064422,"stage1_batch_id":"msgbatch_017qqVz33Ga63SCDwzb35XPb","stage2_batch_id":"msgbatch_01Scr2Ei9x4HJMiRGxwrmvLK","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"TADA2B, as a subunit of the chromatin-modifying SAGA complex, is a central regulator of pluripotency maintenance, survival, growth, and lineage specification in human embryonic stem cells, as determined by integrated genome-scale loss- and gain-of-function CRISPR screens.\",\n      \"method\": \"Genome-scale CRISPR knockout and gain-of-function screens in human embryonic stem cells with readouts for proliferation, differentiation into three germ layers, and apoptosis resistance\",\n      \"journal\": \"Genes & development\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genome-scale functional screening with multiple orthogonal readouts (proliferation, differentiation, survival), single lab\",\n      \"pmids\": [\"34711655\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"Loss of Tada2b (a SAGA complex member) strongly inhibits hematopoiesis in vivo, causing a buildup of immature hematopoietic cells in the bone marrow; mechanistically, loss of Tada2b reduces histone H3 lysine 9 acetylation (H3K9ac) levels and alters H2B ubiquitination (H2Bub) enrichment in hematopoietic stem and progenitor cells, implicating disruption of SAGA complex acetyltransferase and deubiquitinase activities, and is associated with upregulation of interferon pathway genes, reduced mitochondrial activity, and increased megakaryocyte progenitor cell commitment.\",\n      \"method\": \"Genome-wide in vivo CRISPR knockout screen in HSPCs followed by chromatin modification analysis (H3K9ac and H2Bub levels) and transcriptomic profiling\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — in vivo CRISPR KO with specific chromatin (H3K9ac, H2Bub) and transcriptomic readouts, replicated across preprint and peer-reviewed publication from same group\",\n      \"pmids\": [\"41577693\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TADA2B (as part of the SAGA complex histone acetyltransferase module) constitutively binds XRCC1 primarily via the BRCT II domain, independent of DNA damage status or GCN5 acetyltransferase activity; depletion of TADA2B significantly impairs XRCC1 recruitment efficiency to DNA damage sites, and the SCAR26-associated XRCC1 variant disrupts TADA2B binding while maintaining LIG3 interaction.\",\n      \"method\": \"Co-immunoprecipitation/pulldown identifying TADA2B–XRCC1 interaction via distinct BRCT domain mapping; siRNA depletion of TADA2B with quantification of XRCC1 recruitment to damage foci; analysis of SCAR26-associated mutant\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct binding assay with domain mapping, depletion phenotype, and disease-variant validation; single lab, preprint not yet peer-reviewed\",\n      \"pmids\": [\"bio_10.1101_2025.08.24.672030\"],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TADA2B was identified as a proximity interactor of HMGB1 in resting monocytic THP-1 cells, and this interaction is significantly altered upon LPS-induced Toll-like receptor 4 activation (stress), as detected by BioID-based proximity proteomics.\",\n      \"method\": \"BioID proximity proteomics in THP-1 cells comparing resting and LPS-stressed conditions; selected interactions confirmed by proximity ligation assay\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — proximity proteomics identification of TADA2B as HMGB1 interactor; no functional follow-up specific to TADA2B, single lab\",\n      \"pmids\": [\"41161382\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TADA2B is an integral subunit of the SAGA complex histone acetyltransferase module that constitutively interacts with XRCC1 (via its BRCT II domain) to pre-organize DNA base excision/single-strand break repair machinery, while also depositing H3K9ac and regulating H2B ubiquitination in hematopoietic stem and progenitor cells to support normal hematopoiesis and pluripotency maintenance, with loss of TADA2B disrupting these chromatin modifications and activating interferon pathway gene expression.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TADA2B is a subunit of the chromatin-modifying SAGA complex that links histone modification to stem cell maintenance, lineage commitment, and genome stability [#0, #1]. Within SAGA's histone acetyltransferase module, TADA2B supports deposition of histone H3 lysine 9 acetylation (H3K9ac) and influences H2B ubiquitination (H2Bub) enrichment; in hematopoietic stem and progenitor cells, its loss reduces H3K9ac, alters H2Bub, blocks hematopoiesis with accumulation of immature bone marrow cells, lowers mitochondrial activity, skews toward megakaryocyte progenitor commitment, and activates interferon pathway gene expression [#1]. Beyond its chromatin role, TADA2B constitutively binds the DNA single-strand break repair scaffold XRCC1 through its BRCT II domain, independent of DNA damage status and of GCN5 acetyltransferase activity, and TADA2B depletion impairs XRCC1 recruitment to damage sites; an SCAR26-associated XRCC1 variant selectively disrupts this TADA2B interaction while preserving LIG3 binding [#2]. In human embryonic stem cells, TADA2B is a central regulator of pluripotency maintenance, survival, growth, and three-germ-layer lineage specification [#0].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Establishing whether TADA2B has a defined cellular requirement, genome-scale CRISPR screening showed it is a central regulator of pluripotency, survival, growth, and lineage specification, placing this SAGA subunit at the core of stem cell fate decisions.\",\n      \"evidence\": \"Genome-scale CRISPR knockout and gain-of-function screens in human embryonic stem cells with proliferation, differentiation, and apoptosis readouts\",\n      \"pmids\": [\"34711655\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Does not resolve which chromatin marks or target genes mediate the pluripotency phenotype\", \"No mechanistic dissection of TADA2B's contribution distinct from other SAGA subunits\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Addressing whether TADA2B has a function beyond transcription-linked chromatin, domain-mapped binding assays showed it constitutively binds the repair scaffold XRCC1 via the BRCT II domain and is needed for efficient XRCC1 recruitment to damage, defining a pre-organized link between SAGA and single-strand break repair.\",\n      \"evidence\": \"Co-IP/pulldown with BRCT domain mapping, siRNA depletion with quantification of XRCC1 damage-foci recruitment, and SCAR26 variant analysis (preprint)\",\n      \"pmids\": [\"bio_10.1101_2025.08.24.672030\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Preprint not yet peer-reviewed\", \"Whether the interaction requires the intact SAGA complex or TADA2B alone is unresolved\", \"Functional consequence of disrupted recruitment for repair efficiency and disease not directly tested\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Probing TADA2B's broader interaction landscape, proximity proteomics placed it near HMGB1 in monocytes with the association changing upon TLR4 activation, hinting at a stress-responsive context though without functional follow-up.\",\n      \"evidence\": \"BioID proximity proteomics in resting versus LPS-stressed THP-1 cells with proximity ligation confirmation\",\n      \"pmids\": [\"41161382\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Proximity association without functional validation specific to TADA2B\", \"No demonstration of direct binding or biological consequence\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Connecting TADA2B's chromatin activity to a physiological output, in vivo CRISPR knockout showed its loss reduces H3K9ac and alters H2Bub in hematopoietic stem/progenitor cells, blocking hematopoiesis and activating interferon genes, establishing it as required for normal blood cell production through SAGA acetyltransferase/deubiquitinase activities.\",\n      \"evidence\": \"Genome-wide in vivo CRISPR KO screen in HSPCs with H3K9ac/H2Bub chromatin analysis and transcriptomic profiling\",\n      \"pmids\": [\"41577693\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Direct catalytic role of TADA2B in deubiquitination versus indirect effect not separated\", \"Mechanism linking chromatin changes to interferon gene upregulation unresolved\", \"Relationship between hematopoietic and DNA-repair functions not addressed\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How TADA2B's SAGA-dependent chromatin role and its XRCC1-anchored DNA-repair role are mechanistically integrated, and whether they share a structural basis, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structural model of TADA2B within SAGA or bound to XRCC1\", \"Whether chromatin and repair functions are coupled or independent is unknown\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-4839726\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-73894\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\"SAGA complex\"],\n    \"partners\": [\"XRCC1\", \"HMGB1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":2,"faith_total":3,"faith_pct":66.66666666666667}}