{"gene":"DCAF10","run_date":"2026-06-09T22:57:19","timeline":{"discoveries":[{"year":2026,"finding":"DCAF10 functions as the substrate receptor (N-recognin) of the CUL4A-DDB1-DCAF10 E3 ubiquitin ligase complex, specifically recognizing N-terminally acetylated Src-family kinases (SFKs) via an N-terminal acetylated glycine residue, and the reconstituted CUL4A-DDB1-DCAF10 complex ubiquitinates N-terminally acetylated SFKs in vitro. DCAF10 thus monitors replacement of N-terminal myristoylation by acetylation and targets mis-acetylated SFKs for degradation.","method":"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, siRNA-mediated knockdown, CRISPR/Cas9-mediated knockout of endogenous Lyn, inducible Lyn-GFP variants, and in vitro ubiquitination reconstitution assay","journal":"Nature Communications","confidence":"High","confidence_rationale":"Tier 1 / Strong — in vitro reconstitution of ubiquitination by the CUL4A-DDB1-DCAF10 complex, combined with multiple orthogonal methods (peptide pull-down, MS, CRISPR KO, siRNA KD, structural prediction) in a single rigorous study","pmids":["41484149"],"is_preprint":false},{"year":2023,"finding":"Adenovirus E1A binds DCAF10 to assemble a CUL4-based ubiquitin ligase complex that polyubiquitinates RUVBL1 and RUVBL2, inducing their proteasomal degradation; this suppresses accumulation of active IRF3 and expression of antiviral interferon-stimulated genes.","method":"Proteasomal degradation assays, viral infection experiments, functional readout of IRF3 activity and ISG expression upon E1A-DCAF10-CUL4 complex assembly","journal":"Journal of Virology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct functional complex assembly and degradation demonstrated, but mechanistic details are abstracted and full methodological depth is not specified in the abstract","pmids":["37962355"],"is_preprint":false},{"year":2021,"finding":"OTUD1 stabilizes DCAF10 (via deubiquitination) and recruits the CUL4A-DDB1-DCAF10 complex to promote ubiquitin-mediated proteasomal degradation of MCL1, thereby activating caspase-dependent apoptotic signaling.","method":"Co-immunoprecipitation, deubiquitination assays, protein stability/degradation assays, functional apoptosis readouts","journal":"Advanced Science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP and functional apoptosis readout in single lab; DCAF10 role within the complex is established but the abstract does not detail mutagenesis or in vitro reconstitution specific to DCAF10","pmids":["33898171"],"is_preprint":false},{"year":2025,"finding":"The CUL4/DDB1/DCAF10 E3 ligase complex mediates proteasome-dependent degradation of ALOX15B after ABHD17C-driven depalmitoylation causes ALOX15B membrane-to-cytoplasm translocation in KRAS-mutant pancreatic cancer cells.","method":"Co-immunoprecipitation (interaction of ALOX15B with CUL4/DDB1/DCAF10), proteasome inhibitor rescue experiments, depalmitoylation assays, in vivo tumor and organoid functional assays","journal":"Advanced Science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP demonstrating substrate interaction with the complex and proteasomal degradation rescue, in a single lab study with multiple supporting functional assays","pmids":["40569151"],"is_preprint":false}],"current_model":"DCAF10 is a substrate receptor (WD40-repeat N-recognin) of the CUL4A-DDB1 E3 ubiquitin ligase complex that targets diverse substrates for ubiquitin-mediated proteasomal degradation: it recognizes N-terminally acetylated Src-family kinases (via an Ac/N-degron pathway monitoring myristoylation-to-acetylation switching), is hijacked by adenovirus E1A to degrade RUVBL1/2 and suppress innate immunity, is stabilized by OTUD1 to degrade MCL1 and promote apoptosis, and mediates degradation of cytoplasmic ALOX15B to support ferroptosis evasion in KRAS-mutant pancreatic cancer."},"narrative":{"mechanistic_narrative":"DCAF10 is a WD40-repeat substrate receptor (N-recognin) of the CUL4A-DDB1 cullin-RING E3 ubiquitin ligase that selects diverse cytoplasmic proteins for ubiquitin-mediated proteasomal degradation [PMID:41484149]. Its defining biochemical activity is recognition of N-terminally acetylated Src-family kinases through an N-terminal acetyl-glycine degron, allowing DCAF10 to monitor the switch from N-terminal myristoylation to acetylation and to direct mis-acetylated kinases to the reconstituted CUL4A-DDB1-DCAF10 complex for ubiquitination [PMID:41484149]. Through this same ligase architecture, DCAF10 drives degradation of additional substrates with distinct physiological consequences: it is stabilized by the deubiquitinase OTUD1 to degrade MCL1 and activate caspase-dependent apoptosis [PMID:33898171], and it degrades cytoplasm-translocated ALOX15B following ABHD17C-driven depalmitoylation in KRAS-mutant pancreatic cancer [PMID:40569151]. The complex is also subverted by adenovirus E1A, which binds DCAF10 to assemble a CUL4 ligase that destroys RUVBL1/2, blocks IRF3 activation, and suppresses antiviral interferon-stimulated gene expression [PMID:37962355].","teleology":[{"year":2021,"claim":"Established that DCAF10 acts as a functional substrate receptor within the CUL4A-DDB1 ligase and that its own stability is controlled by deubiquitination, linking it to apoptotic control via MCL1 turnover.","evidence":"Co-immunoprecipitation, deubiquitination and degradation assays with apoptosis readouts showing OTUD1 stabilizes DCAF10 to degrade MCL1","pmids":["33898171"],"confidence":"Medium","gaps":["No in vitro reconstitution or DCAF10 mutagenesis defining the MCL1 recognition interface","Degron determinant on MCL1 not identified"]},{"year":2023,"claim":"Revealed that DCAF10 can be hijacked by a viral effector to redirect CUL4 ligase activity against host innate-immune machinery, defining a pathogen-exploited substrate-recruitment route.","evidence":"Adenovirus E1A binding and CUL4 complex assembly with RUVBL1/2 degradation and IRF3/ISG functional readouts","pmids":["37962355"],"confidence":"Medium","gaps":["Structural basis of E1A-DCAF10 interaction not resolved","Whether RUVBL1/2 are endogenous DCAF10 substrates absent E1A is unclear"]},{"year":2025,"claim":"Extended the DCAF10 substrate range to a lipid-modified enzyme, showing that loss of a membrane-anchoring acyl modification creates a cytoplasmic pool recognized by the ligase, tying DCAF10 to ferroptosis evasion.","evidence":"Co-IP of ALOX15B with CUL4/DDB1/DCAF10, depalmitoylation and proteasome-rescue assays, organoid and in vivo tumor models","pmids":["40569151"],"confidence":"Medium","gaps":["Direct degron on ALOX15B not mapped","No reconstituted ubiquitination of ALOX15B by the complex"]},{"year":2026,"claim":"Defined the molecular logic of DCAF10 substrate selection by identifying it as an N-recognin reading an N-terminal acetyl-glycine degron, establishing a quality-control role over lipidation-versus-acetylation status of Src-family kinases.","evidence":"Peptide pull-downs, mass spectrometry, AlphaFold 3 predictions, CRISPR/siRNA perturbation, and in vitro reconstituted ubiquitination of N-acetylated SFKs","pmids":["41484149"],"confidence":"High","gaps":["Experimental high-resolution structure of the DCAF10-degron complex not determined","Full breadth of endogenous N-acetyl-degron substrates beyond SFKs unknown"]},{"year":null,"claim":"It remains unresolved whether DCAF10's diverse substrates (SFKs, MCL1, ALOX15B, RUVBL1/2) share a unifying recognition principle or whether distinct degron classes are read by the same WD40 receptor.","evidence":"","pmids":[],"confidence":"Low","gaps":["No comparison of degron features across the reported substrates","Regulatory inputs governing substrate choice in different cell contexts not defined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[0,1,2,3]},{"term_id":"GO:0016874","term_label":"ligase activity","supporting_discovery_ids":[0]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0,3]}],"pathway":[{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[0,1,2,3]},{"term_id":"R-HSA-5357801","term_label":"Programmed Cell Death","supporting_discovery_ids":[2,3]},{"term_id":"R-HSA-168256","term_label":"Immune System","supporting_discovery_ids":[1]}],"complexes":["CUL4A-DDB1-DCAF10 E3 ubiquitin ligase"],"partners":["CUL4A","DDB1","OTUD1","RUVBL1","RUVBL2","MCL1","ALOX15B"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q5QP82","full_name":"DDB1- and CUL4-associated factor 10","aliases":["WD repeat-containing protein 32"],"length_aa":559,"mass_kda":60.6,"function":"May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex","subcellular_location":"","url":"https://www.uniprot.org/uniprotkb/Q5QP82/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/DCAF10","classification":"Not Classified","n_dependent_lines":19,"n_total_lines":1208,"dependency_fraction":0.015728476821192054},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"DDB1","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/DCAF10","total_profiled":1310},"omim":[{"mim_id":"620295","title":"DDB1- AND CUL4-ASSOCIATED FACTOR 10; DCAF10","url":"https://www.omim.org/entry/620295"},{"mim_id":"612022","title":"OTU DOMAIN-CONTAINING PROTEIN 1; OTUD1","url":"https://www.omim.org/entry/612022"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoli fibrillar center","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/DCAF10"},"hgnc":{"alias_symbol":["MGC10765","FLJ23201"],"prev_symbol":["WDR32"]},"alphafold":{"accession":"Q5QP82","domains":[],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5QP82","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q5QP82-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q5QP82-F1-predicted_aligned_error_v6.png","plddt_mean":69.56},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=DCAF10","jax_strain_url":"https://www.jax.org/strain/search?query=DCAF10"},"sequence":{"accession":"Q5QP82","fasta_url":"https://rest.uniprot.org/uniprotkb/Q5QP82.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q5QP82/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5QP82"}},"corpus_meta":[{"pmid":"33898171","id":"PMC_33898171","title":"OTUD1 Activates Caspase-Independent and Caspase-Dependent Apoptosis by Promoting AIF Nuclear Translocation and MCL1 Degradation.","date":"2021","source":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","url":"https://pubmed.ncbi.nlm.nih.gov/33898171","citation_count":67,"is_preprint":false},{"pmid":"28336923","id":"PMC_28336923","title":"Integrative analysis of multi-omics data reveals distinct impacts of DDB1-CUL4 associated factors in human lung adenocarcinomas.","date":"2017","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/28336923","citation_count":16,"is_preprint":false},{"pmid":"40569151","id":"PMC_40569151","title":"KRAS/ABHD17C/ALOX15B Axis Promotes Pancreatic Cancer Progression via Ferroptosis Evasion.","date":"2025","source":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","url":"https://pubmed.ncbi.nlm.nih.gov/40569151","citation_count":7,"is_preprint":false},{"pmid":"35968900","id":"PMC_35968900","title":"Integrated microarray for identifying the hub mRNAs and constructed miRNA-mRNA network in coronary in-stent restenosis.","date":"2022","source":"Physiological genomics","url":"https://pubmed.ncbi.nlm.nih.gov/35968900","citation_count":3,"is_preprint":false},{"pmid":"37962355","id":"PMC_37962355","title":"Adenovirus E1A binding to DCAF10 targets proteasomal degradation of RUVBL1/2 AAA+ ATPases required for quaternary assembly of multiprotein machines, innate immunity, and responses to metabolic stress.","date":"2023","source":"Journal of virology","url":"https://pubmed.ncbi.nlm.nih.gov/37962355","citation_count":2,"is_preprint":false},{"pmid":"41484149","id":"PMC_41484149","title":"CUL4A-DDB1-DCAF10 is an N-recognin for N-terminally acetylated Src kinases.","date":"2026","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/41484149","citation_count":1,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5205,"output_tokens":1328,"usd":0.017767,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7930,"output_tokens":2203,"usd":0.047363,"stage2_stop_reason":"end_turn"},"total_usd":0.06513,"stage1_batch_id":"msgbatch_01ACAxJQabDsht39JXeWG22d","stage2_batch_id":"msgbatch_01QEU22A9U5sbPTgsMzTmvSf","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2026,\n      \"finding\": \"DCAF10 functions as the substrate receptor (N-recognin) of the CUL4A-DDB1-DCAF10 E3 ubiquitin ligase complex, specifically recognizing N-terminally acetylated Src-family kinases (SFKs) via an N-terminal acetylated glycine residue, and the reconstituted CUL4A-DDB1-DCAF10 complex ubiquitinates N-terminally acetylated SFKs in vitro. DCAF10 thus monitors replacement of N-terminal myristoylation by acetylation and targets mis-acetylated SFKs for degradation.\",\n      \"method\": \"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, siRNA-mediated knockdown, CRISPR/Cas9-mediated knockout of endogenous Lyn, inducible Lyn-GFP variants, and in vitro ubiquitination reconstitution assay\",\n      \"journal\": \"Nature Communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro reconstitution of ubiquitination by the CUL4A-DDB1-DCAF10 complex, combined with multiple orthogonal methods (peptide pull-down, MS, CRISPR KO, siRNA KD, structural prediction) in a single rigorous study\",\n      \"pmids\": [\"41484149\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Adenovirus E1A binds DCAF10 to assemble a CUL4-based ubiquitin ligase complex that polyubiquitinates RUVBL1 and RUVBL2, inducing their proteasomal degradation; this suppresses accumulation of active IRF3 and expression of antiviral interferon-stimulated genes.\",\n      \"method\": \"Proteasomal degradation assays, viral infection experiments, functional readout of IRF3 activity and ISG expression upon E1A-DCAF10-CUL4 complex assembly\",\n      \"journal\": \"Journal of Virology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct functional complex assembly and degradation demonstrated, but mechanistic details are abstracted and full methodological depth is not specified in the abstract\",\n      \"pmids\": [\"37962355\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"OTUD1 stabilizes DCAF10 (via deubiquitination) and recruits the CUL4A-DDB1-DCAF10 complex to promote ubiquitin-mediated proteasomal degradation of MCL1, thereby activating caspase-dependent apoptotic signaling.\",\n      \"method\": \"Co-immunoprecipitation, deubiquitination assays, protein stability/degradation assays, functional apoptosis readouts\",\n      \"journal\": \"Advanced Science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and functional apoptosis readout in single lab; DCAF10 role within the complex is established but the abstract does not detail mutagenesis or in vitro reconstitution specific to DCAF10\",\n      \"pmids\": [\"33898171\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"The CUL4/DDB1/DCAF10 E3 ligase complex mediates proteasome-dependent degradation of ALOX15B after ABHD17C-driven depalmitoylation causes ALOX15B membrane-to-cytoplasm translocation in KRAS-mutant pancreatic cancer cells.\",\n      \"method\": \"Co-immunoprecipitation (interaction of ALOX15B with CUL4/DDB1/DCAF10), proteasome inhibitor rescue experiments, depalmitoylation assays, in vivo tumor and organoid functional assays\",\n      \"journal\": \"Advanced Science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP demonstrating substrate interaction with the complex and proteasomal degradation rescue, in a single lab study with multiple supporting functional assays\",\n      \"pmids\": [\"40569151\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"DCAF10 is a substrate receptor (WD40-repeat N-recognin) of the CUL4A-DDB1 E3 ubiquitin ligase complex that targets diverse substrates for ubiquitin-mediated proteasomal degradation: it recognizes N-terminally acetylated Src-family kinases (via an Ac/N-degron pathway monitoring myristoylation-to-acetylation switching), is hijacked by adenovirus E1A to degrade RUVBL1/2 and suppress innate immunity, is stabilized by OTUD1 to degrade MCL1 and promote apoptosis, and mediates degradation of cytoplasmic ALOX15B to support ferroptosis evasion in KRAS-mutant pancreatic cancer.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"DCAF10 is a WD40-repeat substrate receptor (N-recognin) of the CUL4A-DDB1 cullin-RING E3 ubiquitin ligase that selects diverse cytoplasmic proteins for ubiquitin-mediated proteasomal degradation [#0]. Its defining biochemical activity is recognition of N-terminally acetylated Src-family kinases through an N-terminal acetyl-glycine degron, allowing DCAF10 to monitor the switch from N-terminal myristoylation to acetylation and to direct mis-acetylated kinases to the reconstituted CUL4A-DDB1-DCAF10 complex for ubiquitination [#0]. Through this same ligase architecture, DCAF10 drives degradation of additional substrates with distinct physiological consequences: it is stabilized by the deubiquitinase OTUD1 to degrade MCL1 and activate caspase-dependent apoptosis [#2], and it degrades cytoplasm-translocated ALOX15B following ABHD17C-driven depalmitoylation in KRAS-mutant pancreatic cancer [#3]. The complex is also subverted by adenovirus E1A, which binds DCAF10 to assemble a CUL4 ligase that destroys RUVBL1/2, blocks IRF3 activation, and suppresses antiviral interferon-stimulated gene expression [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Established that DCAF10 acts as a functional substrate receptor within the CUL4A-DDB1 ligase and that its own stability is controlled by deubiquitination, linking it to apoptotic control via MCL1 turnover.\",\n      \"evidence\": \"Co-immunoprecipitation, deubiquitination and degradation assays with apoptosis readouts showing OTUD1 stabilizes DCAF10 to degrade MCL1\",\n      \"pmids\": [\"33898171\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No in vitro reconstitution or DCAF10 mutagenesis defining the MCL1 recognition interface\",\n        \"Degron determinant on MCL1 not identified\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Revealed that DCAF10 can be hijacked by a viral effector to redirect CUL4 ligase activity against host innate-immune machinery, defining a pathogen-exploited substrate-recruitment route.\",\n      \"evidence\": \"Adenovirus E1A binding and CUL4 complex assembly with RUVBL1/2 degradation and IRF3/ISG functional readouts\",\n      \"pmids\": [\"37962355\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Structural basis of E1A-DCAF10 interaction not resolved\",\n        \"Whether RUVBL1/2 are endogenous DCAF10 substrates absent E1A is unclear\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Extended the DCAF10 substrate range to a lipid-modified enzyme, showing that loss of a membrane-anchoring acyl modification creates a cytoplasmic pool recognized by the ligase, tying DCAF10 to ferroptosis evasion.\",\n      \"evidence\": \"Co-IP of ALOX15B with CUL4/DDB1/DCAF10, depalmitoylation and proteasome-rescue assays, organoid and in vivo tumor models\",\n      \"pmids\": [\"40569151\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct degron on ALOX15B not mapped\",\n        \"No reconstituted ubiquitination of ALOX15B by the complex\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Defined the molecular logic of DCAF10 substrate selection by identifying it as an N-recognin reading an N-terminal acetyl-glycine degron, establishing a quality-control role over lipidation-versus-acetylation status of Src-family kinases.\",\n      \"evidence\": \"Peptide pull-downs, mass spectrometry, AlphaFold 3 predictions, CRISPR/siRNA perturbation, and in vitro reconstituted ubiquitination of N-acetylated SFKs\",\n      \"pmids\": [\"41484149\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Experimental high-resolution structure of the DCAF10-degron complex not determined\",\n        \"Full breadth of endogenous N-acetyl-degron substrates beyond SFKs unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unresolved whether DCAF10's diverse substrates (SFKs, MCL1, ALOX15B, RUVBL1/2) share a unifying recognition principle or whether distinct degron classes are read by the same WD40 receptor.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No comparison of degron features across the reported substrates\",\n        \"Regulatory inputs governing substrate choice in different cell contexts not defined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [0, 1, 2, 3]},\n      {\"term_id\": \"GO:0016874\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [0, 1, 2, 3]},\n      {\"term_id\": \"R-HSA-5357801\", \"supporting_discovery_ids\": [2, 3]},\n      {\"term_id\": \"R-HSA-168256\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\n      \"CUL4A-DDB1-DCAF10 E3 ubiquitin ligase\"\n    ],\n    \"partners\": [\n      \"CUL4A\",\n      \"DDB1\",\n      \"OTUD1\",\n      \"RUVBL1\",\n      \"RUVBL2\",\n      \"MCL1\",\n      \"ALOX15B\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}