{"gene":"TAF6L","run_date":"2026-06-10T10:51:54","timeline":{"discoveries":[{"year":2019,"finding":"TAF5L and TAF6L, components/co-activators of GNAT-HAT complexes, are required for self-renewal of mouse ESCs; they transcriptionally activate c-Myc and Oct4 and their regulatory networks, predominantly through H3K9ac deposition and c-MYC recruitment.","method":"CRISPR-Cas9 loss-of-function genetic screen followed by detailed molecular studies (ChIP, gene expression analysis) in mouse ESCs","journal":"Molecular cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — CRISPR screen plus orthogonal molecular studies (H3K9ac ChIP, transcriptional assays) in single lab","pmids":["31005419"],"is_preprint":false},{"year":2026,"finding":"TAF6L (along with TADA1 and TAF5L) is a non-enzymatic SAGA CORE module subunit necessary for stability of the catalytic subunit KAT2A; loss of TAF6L disrupts SAGA complex integrity, causing non-chromatin-bound KAT2A to be degraded by the proteasome via the E3 ligase UBR5, with consequent reduction in H3K9 acetylation.","method":"Fluorescence-based KAT2A stability reporter, CRISPR perturbation of SAGA CORE subunits, proteomic profiling, focused CRISPR screen of ubiquitin-proteasome system genes","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (reporter assay, proteomics, CRISPR screen) in a single rigorous study establishing mechanism","pmids":["42009663"],"is_preprint":false},{"year":2026,"finding":"Cryo-EM structure of endogenous human SAGA reveals that the TAF6L HEAT repeat domain provides a docking surface for the splicing-factor module (SPL); major structural differences between TAF6L and its canonical paralog TAF6 enable SPL accommodation within SAGA, and SPL engages SAGA through a substantially smaller interface than in U2snRNP.","method":"High-resolution cryo-EM structure of affinity-ligand purified endogenous human SAGA complex (no genomic engineering)","journal":"Science advances","confidence":"High","confidence_rationale":"Tier 1 / Strong — high-resolution structural determination of endogenous complex with domain-level functional assignment","pmids":["41849588"],"is_preprint":false},{"year":2025,"finding":"TAF6L is identified as a regulator of cell recovery from cisplatin-induced cytotoxicity in primary human gastric organoids, placing it in the DNA damage response/recovery pathway in this context.","method":"Large-scale CRISPR-based genetic screens (knockout, CRISPRi, CRISPRa) combined with single-cell transcriptomics in primary human 3D gastric organoids","journal":"Nature communications","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — CRISPR screen with single-cell transcriptomics but mechanistic detail limited to phenotypic recovery; single study","pmids":["40813572"],"is_preprint":false},{"year":2025,"finding":"Cryo-EM structure of endogenous human SAGA (preprint) corroborates that the TAF6L HEAT repeat domain docks the SPL splicing-factor module; structural differences from canonical TAF6 are required for SPL accommodation, and the weaker SPL-SAGA interface (vs. U2snRNP) suggests SAGA may relay SPL to the splicing machinery.","method":"High-resolution cryo-EM of affinity-ligand purified endogenous human SAGA","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 1 / Moderate — high-resolution structure but preprint and overlapping with published peer-reviewed version (PMID:41849588)","pmids":["bio_10.1101_2025.07.31.667873"],"is_preprint":true}],"current_model":"TAF6L is a SAGA-specific paralog of TAF6 that forms part of the non-enzymatic SAGA CORE module; its HEAT repeat domain provides a structural docking surface for the metazoan-specific splicing-factor module (SPL), it is required for the stability and chromatin association of the catalytic subunit KAT2A (whose loss leads to proteasomal degradation via UBR5), and it drives H3K9 acetylation and transcriptional activation of the MYC/OCT4 regulatory network to maintain embryonic stem cell self-renewal."},"narrative":{"mechanistic_narrative":"TAF6L is a non-enzymatic subunit of the SAGA transcriptional co-activator complex that links chromatin acetylation to the activation of pluripotency gene networks [PMID:31005419, PMID:42009663]. As part of the SAGA CORE module, TAF6L is required for the structural integrity of the complex and for the stability of the catalytic histone acetyltransferase subunit KAT2A; loss of TAF6L disrupts SAGA assembly and shunts non-chromatin-bound KAT2A to proteasomal degradation via the E3 ligase UBR5, reducing H3K9 acetylation [PMID:42009663]. Through this acetyltransferase-supporting role, TAF6L drives H3K9ac deposition and the transcriptional activation of the c-Myc and Oct4 regulatory networks that maintain embryonic stem cell self-renewal [PMID:31005419]. Structurally, the TAF6L HEAT repeat domain diverges from its canonical paralog TAF6 to provide a docking surface for the metazoan splicing-factor module (SPL) within SAGA, engaging SPL through a comparatively small interface [PMID:41849588]. TAF6L also functions in recovery from cisplatin-induced cytotoxicity in gastric organoids, placing it within a DNA damage response/recovery context [PMID:40813572].","teleology":[{"year":2019,"claim":"Established that TAF6L is functionally required for stem cell self-renewal and acts by driving acetylation-coupled transcription of the core pluripotency network, defining its biological role beyond being a structural complex subunit.","evidence":"CRISPR-Cas9 loss-of-function screen with ChIP and transcriptional analysis in mouse ESCs","pmids":["31005419"],"confidence":"Medium","gaps":["Does not resolve whether the transcriptional effect is direct via SAGA at target promoters or indirect through c-MYC","Mechanism linking TAF6L to H3K9ac deposition not structurally defined","Restricted to mouse ESC context"]},{"year":2026,"claim":"Defined the molecular basis by which TAF6L sustains SAGA enzymatic output, showing it stabilizes the catalytic subunit KAT2A and that its loss triggers UBR5-mediated proteasomal turnover of unincorporated KAT2A.","evidence":"KAT2A stability reporter, CRISPR perturbation of SAGA CORE subunits, proteomics, and a focused ubiquitin-proteasome CRISPR screen","pmids":["42009663"],"confidence":"High","gaps":["Does not establish whether UBR5 directly ubiquitinates KAT2A or acts through an intermediary","Quantitative contribution of TAF6L loss to global vs. locus-specific H3K9ac not delineated"]},{"year":2026,"claim":"Resolved how TAF6L structurally distinguishes SAGA from canonical TFIID-associated assemblies, showing its HEAT repeat domain creates a docking surface for the splicing-factor module absent in the paralog TAF6.","evidence":"High-resolution cryo-EM of affinity-purified endogenous human SAGA (peer-reviewed; corroborated by an earlier preprint, idx 4)","pmids":["41849588"],"confidence":"High","gaps":["Functional consequence of SPL docking for splicing output not demonstrated","The weaker SPL-SAGA interface implies a hand-off model that is not experimentally tested"]},{"year":2025,"claim":"Extended TAF6L function into a stress-response context by identifying it as a regulator of recovery from cisplatin cytotoxicity in human gastric tissue.","evidence":"CRISPR knockout/CRISPRi/CRISPRa screens with single-cell transcriptomics in primary human 3D gastric organoids","pmids":["40813572"],"confidence":"Medium","gaps":["Mechanistic detail limited to phenotypic recovery; no molecular link to SAGA activity demonstrated in this context","Single study in one tissue model"]},{"year":null,"claim":"How TAF6L-dependent SPL docking is coupled to active splicing, and whether its DNA damage recovery role operates through SAGA-mediated transcription, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No functional demonstration that SPL recruitment via TAF6L alters splicing outcomes","No mechanistic connection between TAF6L's transcriptional/acetylation role and cisplatin recovery","Direct enzymology of UBR5-KAT2A relationship unestablished"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[1,2]},{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[0,1]}],"pathway":[{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[0,1]},{"term_id":"R-HSA-4839726","term_label":"Chromatin organization","supporting_discovery_ids":[0,1]}],"complexes":["SAGA","SAGA CORE module"],"partners":["KAT2A","TAF5L","TADA1","UBR5"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9Y6J9","full_name":"TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","aliases":["PCAF-associated factor 65-alpha","PAF65-alpha"],"length_aa":622,"mass_kda":67.8,"function":"Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex (Probable). With TAF5L, acts as an epigenetic regulator essential for somatic reprogramming. Regulates target genes through H3K9ac deposition and MYC recruitment which trigger MYC regulatory network to orchestrate gene expression programs to control embryonic stem cell state. Functions with MYC to activate target gene expression through RNA polymerase II pause release (By similarity)","subcellular_location":"Nucleus","url":"https://www.uniprot.org/uniprotkb/Q9Y6J9/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/TAF6L","classification":"Not Classified","n_dependent_lines":469,"n_total_lines":1208,"dependency_fraction":0.3882450331125828},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"TAF12","stoichiometry":10.0},{"gene":"TRRAP","stoichiometry":10.0},{"gene":"ENY2","stoichiometry":0.2},{"gene":"SF3B3","stoichiometry":0.2},{"gene":"SF3B5","stoichiometry":0.2},{"gene":"USP22","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/TAF6L","total_profiled":1310},"omim":[{"mim_id":"602946","title":"TAF6-LIKE RNA POLYMERASE II; TAF6L","url":"https://www.omim.org/entry/602946"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TAF6L"},"hgnc":{"alias_symbol":["PAF65A"],"prev_symbol":[]},"alphafold":{"accession":"Q9Y6J9","domains":[{"cath_id":"1.10.20.10","chopping":"15-105","consensus_level":"high","plddt":90.627,"start":15,"end":105},{"cath_id":"1.25.40.770","chopping":"156-298","consensus_level":"high","plddt":93.0478,"start":156,"end":298},{"cath_id":"1.10.287","chopping":"319-378_437-457","consensus_level":"medium","plddt":89.4748,"start":319,"end":457}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9Y6J9","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9Y6J9-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9Y6J9-F1-predicted_aligned_error_v6.png","plddt_mean":67.88},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TAF6L","jax_strain_url":"https://www.jax.org/strain/search?query=TAF6L"},"sequence":{"accession":"Q9Y6J9","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9Y6J9.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9Y6J9/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9Y6J9"}},"corpus_meta":[{"pmid":"31005419","id":"PMC_31005419","title":"TAF5L and TAF6L Maintain Self-Renewal of Embryonic Stem Cells via the MYC Regulatory Network.","date":"2019","source":"Molecular cell","url":"https://pubmed.ncbi.nlm.nih.gov/31005419","citation_count":37,"is_preprint":false},{"pmid":"17351670","id":"PMC_17351670","title":"A common cis-element in promoters of protein synthesis and cell cycle genes.","date":"2007","source":"Acta biochimica Polonica","url":"https://pubmed.ncbi.nlm.nih.gov/17351670","citation_count":17,"is_preprint":false},{"pmid":"40813572","id":"PMC_40813572","title":"Large-scale CRISPR screening in primary human 3D gastric organoids enables comprehensive dissection of gene-drug interactions.","date":"2025","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/40813572","citation_count":13,"is_preprint":false},{"pmid":"35044082","id":"PMC_35044082","title":"Identification of a glioma functional network from gene fitness data using machine learning.","date":"2022","source":"Journal of cellular and molecular medicine","url":"https://pubmed.ncbi.nlm.nih.gov/35044082","citation_count":7,"is_preprint":false},{"pmid":"42009663","id":"PMC_42009663","title":"Disruption of the SAGA CORE triggers collateral degradation of KAT2A.","date":"2026","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/42009663","citation_count":1,"is_preprint":false},{"pmid":"41849588","id":"PMC_41849588","title":"Insights into the structure and evolution of the human SAGA complex by affinity-ligand purification.","date":"2026","source":"Science advances","url":"https://pubmed.ncbi.nlm.nih.gov/41849588","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.07.31.667873","title":"Novel insights into the structure and evolution of the human SAGA complex by affinity-ligand purification","date":"2025-08-02","source":"bioRxiv","url":"https://doi.org/10.1101/2025.07.31.667873","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5211,"output_tokens":1304,"usd":0.017597,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7946,"output_tokens":2037,"usd":0.045327,"stage2_stop_reason":"end_turn"},"total_usd":0.062924,"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\": 2019,\n      \"finding\": \"TAF5L and TAF6L, components/co-activators of GNAT-HAT complexes, are required for self-renewal of mouse ESCs; they transcriptionally activate c-Myc and Oct4 and their regulatory networks, predominantly through H3K9ac deposition and c-MYC recruitment.\",\n      \"method\": \"CRISPR-Cas9 loss-of-function genetic screen followed by detailed molecular studies (ChIP, gene expression analysis) in mouse ESCs\",\n      \"journal\": \"Molecular cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — CRISPR screen plus orthogonal molecular studies (H3K9ac ChIP, transcriptional assays) in single lab\",\n      \"pmids\": [\"31005419\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"TAF6L (along with TADA1 and TAF5L) is a non-enzymatic SAGA CORE module subunit necessary for stability of the catalytic subunit KAT2A; loss of TAF6L disrupts SAGA complex integrity, causing non-chromatin-bound KAT2A to be degraded by the proteasome via the E3 ligase UBR5, with consequent reduction in H3K9 acetylation.\",\n      \"method\": \"Fluorescence-based KAT2A stability reporter, CRISPR perturbation of SAGA CORE subunits, proteomic profiling, focused CRISPR screen of ubiquitin-proteasome system genes\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (reporter assay, proteomics, CRISPR screen) in a single rigorous study establishing mechanism\",\n      \"pmids\": [\"42009663\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"Cryo-EM structure of endogenous human SAGA reveals that the TAF6L HEAT repeat domain provides a docking surface for the splicing-factor module (SPL); major structural differences between TAF6L and its canonical paralog TAF6 enable SPL accommodation within SAGA, and SPL engages SAGA through a substantially smaller interface than in U2snRNP.\",\n      \"method\": \"High-resolution cryo-EM structure of affinity-ligand purified endogenous human SAGA complex (no genomic engineering)\",\n      \"journal\": \"Science advances\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — high-resolution structural determination of endogenous complex with domain-level functional assignment\",\n      \"pmids\": [\"41849588\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TAF6L is identified as a regulator of cell recovery from cisplatin-induced cytotoxicity in primary human gastric organoids, placing it in the DNA damage response/recovery pathway in this context.\",\n      \"method\": \"Large-scale CRISPR-based genetic screens (knockout, CRISPRi, CRISPRa) combined with single-cell transcriptomics in primary human 3D gastric organoids\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — CRISPR screen with single-cell transcriptomics but mechanistic detail limited to phenotypic recovery; single study\",\n      \"pmids\": [\"40813572\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Cryo-EM structure of endogenous human SAGA (preprint) corroborates that the TAF6L HEAT repeat domain docks the SPL splicing-factor module; structural differences from canonical TAF6 are required for SPL accommodation, and the weaker SPL-SAGA interface (vs. U2snRNP) suggests SAGA may relay SPL to the splicing machinery.\",\n      \"method\": \"High-resolution cryo-EM of affinity-ligand purified endogenous human SAGA\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — high-resolution structure but preprint and overlapping with published peer-reviewed version (PMID:41849588)\",\n      \"pmids\": [\"bio_10.1101_2025.07.31.667873\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"TAF6L is a SAGA-specific paralog of TAF6 that forms part of the non-enzymatic SAGA CORE module; its HEAT repeat domain provides a structural docking surface for the metazoan-specific splicing-factor module (SPL), it is required for the stability and chromatin association of the catalytic subunit KAT2A (whose loss leads to proteasomal degradation via UBR5), and it drives H3K9 acetylation and transcriptional activation of the MYC/OCT4 regulatory network to maintain embryonic stem cell self-renewal.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TAF6L is a non-enzymatic subunit of the SAGA transcriptional co-activator complex that links chromatin acetylation to the activation of pluripotency gene networks [#0, #1]. As part of the SAGA CORE module, TAF6L is required for the structural integrity of the complex and for the stability of the catalytic histone acetyltransferase subunit KAT2A; loss of TAF6L disrupts SAGA assembly and shunts non-chromatin-bound KAT2A to proteasomal degradation via the E3 ligase UBR5, reducing H3K9 acetylation [#1]. Through this acetyltransferase-supporting role, TAF6L drives H3K9ac deposition and the transcriptional activation of the c-Myc and Oct4 regulatory networks that maintain embryonic stem cell self-renewal [#0]. Structurally, the TAF6L HEAT repeat domain diverges from its canonical paralog TAF6 to provide a docking surface for the metazoan splicing-factor module (SPL) within SAGA, engaging SPL through a comparatively small interface [#2]. TAF6L also functions in recovery from cisplatin-induced cytotoxicity in gastric organoids, placing it within a DNA damage response/recovery context [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2019,\n      \"claim\": \"Established that TAF6L is functionally required for stem cell self-renewal and acts by driving acetylation-coupled transcription of the core pluripotency network, defining its biological role beyond being a structural complex subunit.\",\n      \"evidence\": \"CRISPR-Cas9 loss-of-function screen with ChIP and transcriptional analysis in mouse ESCs\",\n      \"pmids\": [\"31005419\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Does not resolve whether the transcriptional effect is direct via SAGA at target promoters or indirect through c-MYC\",\n        \"Mechanism linking TAF6L to H3K9ac deposition not structurally defined\",\n        \"Restricted to mouse ESC context\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Defined the molecular basis by which TAF6L sustains SAGA enzymatic output, showing it stabilizes the catalytic subunit KAT2A and that its loss triggers UBR5-mediated proteasomal turnover of unincorporated KAT2A.\",\n      \"evidence\": \"KAT2A stability reporter, CRISPR perturbation of SAGA CORE subunits, proteomics, and a focused ubiquitin-proteasome CRISPR screen\",\n      \"pmids\": [\"42009663\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Does not establish whether UBR5 directly ubiquitinates KAT2A or acts through an intermediary\",\n        \"Quantitative contribution of TAF6L loss to global vs. locus-specific H3K9ac not delineated\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Resolved how TAF6L structurally distinguishes SAGA from canonical TFIID-associated assemblies, showing its HEAT repeat domain creates a docking surface for the splicing-factor module absent in the paralog TAF6.\",\n      \"evidence\": \"High-resolution cryo-EM of affinity-purified endogenous human SAGA (peer-reviewed; corroborated by an earlier preprint, idx 4)\",\n      \"pmids\": [\"41849588\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Functional consequence of SPL docking for splicing output not demonstrated\",\n        \"The weaker SPL-SAGA interface implies a hand-off model that is not experimentally tested\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Extended TAF6L function into a stress-response context by identifying it as a regulator of recovery from cisplatin cytotoxicity in human gastric tissue.\",\n      \"evidence\": \"CRISPR knockout/CRISPRi/CRISPRa screens with single-cell transcriptomics in primary human 3D gastric organoids\",\n      \"pmids\": [\"40813572\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanistic detail limited to phenotypic recovery; no molecular link to SAGA activity demonstrated in this context\",\n        \"Single study in one tissue model\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How TAF6L-dependent SPL docking is coupled to active splicing, and whether its DNA damage recovery role operates through SAGA-mediated transcription, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No functional demonstration that SPL recruitment via TAF6L alters splicing outcomes\",\n        \"No mechanistic connection between TAF6L's transcriptional/acetylation role and cisplatin recovery\",\n        \"Direct enzymology of UBR5-KAT2A relationship unestablished\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [1, 2]},\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"R-HSA-4839726\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\"SAGA\", \"SAGA CORE module\"],\n    \"partners\": [\"KAT2A\", \"TAF5L\", \"TADA1\", \"UBR5\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}