{"gene":"ENDOD1","run_date":"2026-06-09T23:54:43","timeline":{"discoveries":[{"year":2023,"finding":"ENDOD1 (renamed NUMEN) is a transmembrane nuclease that generates short 5' overhangs through its endonuclease and 3'→5' exonuclease activities, facilitating non-homologous end joining (NHEJ)-dependent repair of double-stranded DNA breaks at the nuclear periphery, including heterochromatic lamina-associated domain breaks and deprotected telomeres. It functions as a downstream effector of DNA-dependent protein kinase catalytic subunit (DNA-PKcs).","method":"Genome-wide synthetic viability CRISPR-Cas9 screen, in vitro nuclease activity assays, nuclear periphery localization experiments, genetic epistasis with DNA-PKcs, BRCA1-deficient breast cancer cell models","journal":"Nature cell biology","confidence":"High","confidence_rationale":"Tier 1-2 / Strong — multiple orthogonal methods including CRISPR screen, in vitro enzymatic assays, mutagenesis-implied mechanistic dissection, and genetic epistasis in a single rigorous study","pmids":["37322289"],"is_preprint":false},{"year":2022,"finding":"ENDOD1 functions in DNA repair: it is enriched in the nucleus following H2O2-induced oxidative stress, and ENDOD1-knockout cells show increased PARP chromatin-association. Loss of ENDOD1 is synthetic lethal with homologous recombination defects, causing accumulation of DNA double-strand breaks. Additionally, ENDOD1 depletion in TP53-mutated tumor cells results in rapid single-stranded DNA accumulation and cell death, revealing a synthetic lethality between ENDOD1 and p53.","method":"ENDOD1 knockout cell lines, cellular fractionation/chromatin association assays (PARP), H2O2 treatment with nuclear localization imaging, siRNA knockdown, xenograft tumor models with siRNA knockdown","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (KO cells, fractionation, nuclear localization, xenograft models) in a single rigorous study with clear functional readouts","pmids":["35606358"],"is_preprint":false},{"year":2020,"finding":"ENDOD1 co-assembles with RNF26, TMEM43, TMEM33, and TMED1 at the ER membrane to form a complex capable of modulating innate immune signalling through the cGAS-STING pathway.","method":"Comparative proteomic workflow (protein-protein interaction mapping by MS), Co-immunoprecipitation of ER-localized E3 ubiquitin ligase RNF26 and its interactors, functional innate immune signalling assays","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — proteomic interaction mapping plus functional innate immune signalling assay, single lab study","pmids":["32614325"],"is_preprint":false},{"year":2016,"finding":"Recombinant ENDOD1 protein from Japanese flounder (Paralichthys olivaceus, Jf_ENDOD1) produced in E. coli displays DNase (endonuclease) activity in vitro, consistent with its classification as a member of the DNA/RNA non-specific nucleases family. DNase activity in kidney and spleen extracts was elevated after bacterial challenge, correlating with ENDOD1 upregulation.","method":"Recombinant protein expression in E. coli, in vitro DNase activity assay, tissue DNase activity measurement after bacterial injection","journal":"Fish & shellfish immunology","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — direct in vitro enzymatic reconstitution, but performed in fish ortholog (single lab, not replicated in mammalian system)","pmids":["26784919"],"is_preprint":false},{"year":2017,"finding":"In prostate cancer cells, overexpression of ENDOD1 suppresses cell proliferation, induces G0/G1 cell cycle arrest, and inhibits cell migration and invasion; conversely, siRNA-mediated silencing of ENDOD1 promotes cell proliferation, migration, and invasion. No apoptotic effects were observed upon ENDOD1 manipulation.","method":"Overexpression and siRNA knockdown in PCa cell lines, MTT proliferation assay, flow cytometry cell cycle analysis, Transwell migration and invasion assays","journal":"BMC cancer","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — bidirectional manipulation (OE and KD) with multiple functional readouts in cell lines, single lab","pmids":["28532481"],"is_preprint":false}],"current_model":"ENDOD1 (also called NUMEN) is a transmembrane nuclease with intrinsic endonuclease and 3'→5' exonuclease activities that localizes to the nuclear periphery upon DNA damage; it generates 5' overhangs to facilitate DNA-PKcs-dependent NHEJ repair of double-strand breaks at lamina-associated domains and deprotected telomeres, is synthetic lethal with both homologous recombination deficiency and TP53 mutation, and additionally participates in innate immune modulation via the cGAS-STING pathway as part of an ER-membrane complex with RNF26, TMEM43, TMEM33, and TMED1."},"narrative":{"mechanistic_narrative":"ENDOD1 (also called NUMEN) is a transmembrane nuclease of the DNA/RNA non-specific nuclease family that acts in the repair of DNA double-strand breaks at the nuclear periphery [PMID:37322289]. It carries intrinsic endonuclease and 3'→5' exonuclease activities that generate short 5' overhangs, operating as a downstream effector of DNA-PKcs to drive non-homologous end joining at heterochromatic lamina-associated domain breaks and deprotected telomeres [PMID:37322289]. ENDOD1 is enriched in the nucleus following oxidative stress, and its loss is synthetic lethal both with homologous recombination deficiency, producing accumulation of double-strand breaks, and with TP53 mutation, producing rapid single-stranded DNA accumulation and cell death [PMID:35606358]. Beyond its repair role, ENDOD1 co-assembles with the ER-membrane E3 ligase RNF26 together with TMEM43, TMEM33, and TMED1 to modulate innate immune signalling through the cGAS-STING pathway [PMID:32614325], and its expression restrains proliferation, migration, and invasion in cancer cells [PMID:28532481]. Recombinant nuclease activity confirmed in a fish ortholog, where it is induced upon bacterial challenge, supports the conserved catalytic identity of the protein [PMID:26784919].","teleology":[{"year":2016,"claim":"Established that ENDOD1 is a bona fide nuclease, answering whether the protein possesses intrinsic catalytic activity and linking it to immune-responsive contexts.","evidence":"Recombinant Japanese flounder ENDOD1 expressed in E. coli with in vitro DNase assays and tissue DNase measurement after bacterial injection","pmids":["26784919"],"confidence":"Medium","gaps":["Demonstrated in a fish ortholog, not in a mammalian system","Does not define substrate specificity (endo vs exo) or directionality","No link to a specific cellular pathway"]},{"year":2017,"claim":"Showed that ENDOD1 acts as a growth-suppressive factor in cancer, raising the question of how a nuclease constrains proliferation and motility.","evidence":"Bidirectional overexpression and siRNA knockdown in prostate cancer cell lines with proliferation, cell-cycle, and migration/invasion assays","pmids":["28532481"],"confidence":"Medium","gaps":["Molecular mechanism linking nuclease activity to G0/G1 arrest not defined","No connection to DNA repair pathway established at this stage","Single lineage (prostate) tested"]},{"year":2020,"claim":"Identified an ER-membrane complex containing ENDOD1, revealing a role distinct from nuclear DNA processing in innate immune regulation.","evidence":"Proteomic interaction mapping and Co-IP of RNF26 with TMEM43, TMEM33, TMED1, plus cGAS-STING innate immune signalling assays","pmids":["32614325"],"confidence":"Medium","gaps":["Direct vs indirect membership of ENDOD1 in the complex not resolved","Whether nuclease activity is required for immune modulation unknown","Single-lab interaction dataset"]},{"year":2022,"claim":"Defined ENDOD1 as a DNA-repair factor whose loss creates synthetic lethal vulnerabilities, establishing therapeutic relevance in HR-deficient and TP53-mutant tumors.","evidence":"Knockout cell lines, chromatin-association fractionation (PARP), H2O2-induced nuclear localization imaging, siRNA, and xenograft models","pmids":["35606358"],"confidence":"High","gaps":["Catalytic mechanism underlying the repair role not biochemically dissected here","Pathway step at which ENDOD1 acts left unspecified","Relationship between nuclear enrichment signal and damage type unclear"]},{"year":2023,"claim":"Resolved the molecular mechanism: ENDOD1/NUMEN generates short 5' overhangs via endo- and exonuclease activities to enable DNA-PKcs-dependent NHEJ at the nuclear periphery.","evidence":"Genome-wide synthetic viability CRISPR screen, in vitro nuclease assays, nuclear periphery localization, genetic epistasis with DNA-PKcs in BRCA1-deficient cells","pmids":["37322289"],"confidence":"High","gaps":["Structural basis of overhang generation not determined","How its transmembrane topology is reconciled with nuclear-periphery DNA access is unresolved","Mechanistic relationship between the repair and cGAS-STING roles not connected"]},{"year":null,"claim":"How ENDOD1's nuclease-driven DNA repair function mechanistically intersects with its ER-membrane cGAS-STING role and its growth-suppressive activity remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No unifying model linking nuclear repair and ER-membrane immune signalling","No structural model of the catalytic mechanism","Recruitment to and topology at the nuclear periphery undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140097","term_label":"catalytic activity, acting on DNA","supporting_discovery_ids":[0,3]},{"term_id":"GO:0016787","term_label":"hydrolase activity","supporting_discovery_ids":[0,3]}],"localization":[{"term_id":"GO:0005635","term_label":"nuclear envelope","supporting_discovery_ids":[0]},{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[1]},{"term_id":"GO:0005783","term_label":"endoplasmic reticulum","supporting_discovery_ids":[2]}],"pathway":[{"term_id":"R-HSA-73894","term_label":"DNA Repair","supporting_discovery_ids":[0,1]}],"complexes":["RNF26-TMEM43-TMEM33-TMED1 ER-membrane complex"],"partners":["RNF26","TMEM43","TMEM33","TMED1","PRKDC"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O94919","full_name":"Endonuclease domain-containing 1 protein","aliases":[],"length_aa":500,"mass_kda":55.0,"function":"May act as a DNase and a RNase. Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26","subcellular_location":"Secreted","url":"https://www.uniprot.org/uniprotkb/O94919/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ENDOD1","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":"RTN4","stoichiometry":10.0},{"gene":"COPB2","stoichiometry":0.2},{"gene":"VAPA","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/ENDOD1","total_profiled":1310},"omim":[{"mim_id":"619568","title":"ENDONUCLEASE DOMAIN-CONTAINING PROTEIN 1; ENDOD1","url":"https://www.omim.org/entry/619568"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nuclear membrane","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/ENDOD1"},"hgnc":{"alias_symbol":["KIAA0830"],"prev_symbol":[]},"alphafold":{"accession":"O94919","domains":[{"cath_id":"3.40.570.10","chopping":"23-275","consensus_level":"high","plddt":86.5166,"start":23,"end":275}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O94919","model_url":"https://alphafold.ebi.ac.uk/files/AF-O94919-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O94919-F1-predicted_aligned_error_v6.png","plddt_mean":80.88},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ENDOD1","jax_strain_url":"https://www.jax.org/strain/search?query=ENDOD1"},"sequence":{"accession":"O94919","fasta_url":"https://rest.uniprot.org/uniprotkb/O94919.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O94919/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O94919"}},"corpus_meta":[{"pmid":"11921445","id":"PMC_11921445","title":"Towards complete analysis of the platelet proteome.","date":"2002","source":"Proteomics","url":"https://pubmed.ncbi.nlm.nih.gov/11921445","citation_count":144,"is_preprint":false},{"pmid":"32614325","id":"PMC_32614325","title":"Interaction mapping of endoplasmic reticulum ubiquitin ligases identifies modulators of innate immune signalling.","date":"2020","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/32614325","citation_count":71,"is_preprint":false},{"pmid":"21332311","id":"PMC_21332311","title":"Genome-wide expression profiling of human lymphoblastoid cell lines identifies CHL1 as a putative SSRI antidepressant response biomarker.","date":"2011","source":"Pharmacogenomics","url":"https://pubmed.ncbi.nlm.nih.gov/21332311","citation_count":50,"is_preprint":false},{"pmid":"21829708","id":"PMC_21829708","title":"Modulation of androgen receptor signaling in hormonal therapy-resistant prostate cancer cell lines.","date":"2011","source":"PloS 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It functions as a downstream effector of DNA-dependent protein kinase catalytic subunit (DNA-PKcs).\",\n      \"method\": \"Genome-wide synthetic viability CRISPR-Cas9 screen, in vitro nuclease activity assays, nuclear periphery localization experiments, genetic epistasis with DNA-PKcs, BRCA1-deficient breast cancer cell models\",\n      \"journal\": \"Nature cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 / Strong — multiple orthogonal methods including CRISPR screen, in vitro enzymatic assays, mutagenesis-implied mechanistic dissection, and genetic epistasis in a single rigorous study\",\n      \"pmids\": [\"37322289\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"ENDOD1 functions in DNA repair: it is enriched in the nucleus following H2O2-induced oxidative stress, and ENDOD1-knockout cells show increased PARP chromatin-association. Loss of ENDOD1 is synthetic lethal with homologous recombination defects, causing accumulation of DNA double-strand breaks. Additionally, ENDOD1 depletion in TP53-mutated tumor cells results in rapid single-stranded DNA accumulation and cell death, revealing a synthetic lethality between ENDOD1 and p53.\",\n      \"method\": \"ENDOD1 knockout cell lines, cellular fractionation/chromatin association assays (PARP), H2O2 treatment with nuclear localization imaging, siRNA knockdown, xenograft tumor models with siRNA knockdown\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (KO cells, fractionation, nuclear localization, xenograft models) in a single rigorous study with clear functional readouts\",\n      \"pmids\": [\"35606358\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"ENDOD1 co-assembles with RNF26, TMEM43, TMEM33, and TMED1 at the ER membrane to form a complex capable of modulating innate immune signalling through the cGAS-STING pathway.\",\n      \"method\": \"Comparative proteomic workflow (protein-protein interaction mapping by MS), Co-immunoprecipitation of ER-localized E3 ubiquitin ligase RNF26 and its interactors, functional innate immune signalling assays\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — proteomic interaction mapping plus functional innate immune signalling assay, single lab study\",\n      \"pmids\": [\"32614325\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Recombinant ENDOD1 protein from Japanese flounder (Paralichthys olivaceus, Jf_ENDOD1) produced in E. coli displays DNase (endonuclease) activity in vitro, consistent with its classification as a member of the DNA/RNA non-specific nucleases family. DNase activity in kidney and spleen extracts was elevated after bacterial challenge, correlating with ENDOD1 upregulation.\",\n      \"method\": \"Recombinant protein expression in E. coli, in vitro DNase activity assay, tissue DNase activity measurement after bacterial injection\",\n      \"journal\": \"Fish & shellfish immunology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — direct in vitro enzymatic reconstitution, but performed in fish ortholog (single lab, not replicated in mammalian system)\",\n      \"pmids\": [\"26784919\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"In prostate cancer cells, overexpression of ENDOD1 suppresses cell proliferation, induces G0/G1 cell cycle arrest, and inhibits cell migration and invasion; conversely, siRNA-mediated silencing of ENDOD1 promotes cell proliferation, migration, and invasion. No apoptotic effects were observed upon ENDOD1 manipulation.\",\n      \"method\": \"Overexpression and siRNA knockdown in PCa cell lines, MTT proliferation assay, flow cytometry cell cycle analysis, Transwell migration and invasion assays\",\n      \"journal\": \"BMC cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — bidirectional manipulation (OE and KD) with multiple functional readouts in cell lines, single lab\",\n      \"pmids\": [\"28532481\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ENDOD1 (also called NUMEN) is a transmembrane nuclease with intrinsic endonuclease and 3'→5' exonuclease activities that localizes to the nuclear periphery upon DNA damage; it generates 5' overhangs to facilitate DNA-PKcs-dependent NHEJ repair of double-strand breaks at lamina-associated domains and deprotected telomeres, is synthetic lethal with both homologous recombination deficiency and TP53 mutation, and additionally participates in innate immune modulation via the cGAS-STING pathway as part of an ER-membrane complex with RNF26, TMEM43, TMEM33, and TMED1.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ENDOD1 (also called NUMEN) is a transmembrane nuclease of the DNA/RNA non-specific nuclease family that acts in the repair of DNA double-strand breaks at the nuclear periphery [#0]. It carries intrinsic endonuclease and 3'\\u21925' exonuclease activities that generate short 5' overhangs, operating as a downstream effector of DNA-PKcs to drive non-homologous end joining at heterochromatic lamina-associated domain breaks and deprotected telomeres [#0]. ENDOD1 is enriched in the nucleus following oxidative stress, and its loss is synthetic lethal both with homologous recombination deficiency, producing accumulation of double-strand breaks, and with TP53 mutation, producing rapid single-stranded DNA accumulation and cell death [#1]. Beyond its repair role, ENDOD1 co-assembles with the ER-membrane E3 ligase RNF26 together with TMEM43, TMEM33, and TMED1 to modulate innate immune signalling through the cGAS-STING pathway [#2], and its expression restrains proliferation, migration, and invasion in cancer cells [#4]. Recombinant nuclease activity confirmed in a fish ortholog, where it is induced upon bacterial challenge, supports the conserved catalytic identity of the protein [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2016,\n      \"claim\": \"Established that ENDOD1 is a bona fide nuclease, answering whether the protein possesses intrinsic catalytic activity and linking it to immune-responsive contexts.\",\n      \"evidence\": \"Recombinant Japanese flounder ENDOD1 expressed in E. coli with in vitro DNase assays and tissue DNase measurement after bacterial injection\",\n      \"pmids\": [\"26784919\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Demonstrated in a fish ortholog, not in a mammalian system\",\n        \"Does not define substrate specificity (endo vs exo) or directionality\",\n        \"No link to a specific cellular pathway\"\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Showed that ENDOD1 acts as a growth-suppressive factor in cancer, raising the question of how a nuclease constrains proliferation and motility.\",\n      \"evidence\": \"Bidirectional overexpression and siRNA knockdown in prostate cancer cell lines with proliferation, cell-cycle, and migration/invasion assays\",\n      \"pmids\": [\"28532481\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Molecular mechanism linking nuclease activity to G0/G1 arrest not defined\",\n        \"No connection to DNA repair pathway established at this stage\",\n        \"Single lineage (prostate) tested\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Identified an ER-membrane complex containing ENDOD1, revealing a role distinct from nuclear DNA processing in innate immune regulation.\",\n      \"evidence\": \"Proteomic interaction mapping and Co-IP of RNF26 with TMEM43, TMEM33, TMED1, plus cGAS-STING innate immune signalling assays\",\n      \"pmids\": [\"32614325\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct vs indirect membership of ENDOD1 in the complex not resolved\",\n        \"Whether nuclease activity is required for immune modulation unknown\",\n        \"Single-lab interaction dataset\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Defined ENDOD1 as a DNA-repair factor whose loss creates synthetic lethal vulnerabilities, establishing therapeutic relevance in HR-deficient and TP53-mutant tumors.\",\n      \"evidence\": \"Knockout cell lines, chromatin-association fractionation (PARP), H2O2-induced nuclear localization imaging, siRNA, and xenograft models\",\n      \"pmids\": [\"35606358\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Catalytic mechanism underlying the repair role not biochemically dissected here\",\n        \"Pathway step at which ENDOD1 acts left unspecified\",\n        \"Relationship between nuclear enrichment signal and damage type unclear\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Resolved the molecular mechanism: ENDOD1/NUMEN generates short 5' overhangs via endo- and exonuclease activities to enable DNA-PKcs-dependent NHEJ at the nuclear periphery.\",\n      \"evidence\": \"Genome-wide synthetic viability CRISPR screen, in vitro nuclease assays, nuclear periphery localization, genetic epistasis with DNA-PKcs in BRCA1-deficient cells\",\n      \"pmids\": [\"37322289\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of overhang generation not determined\",\n        \"How its transmembrane topology is reconciled with nuclear-periphery DNA access is unresolved\",\n        \"Mechanistic relationship between the repair and cGAS-STING roles not connected\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How ENDOD1's nuclease-driven DNA repair function mechanistically intersects with its ER-membrane cGAS-STING role and its growth-suppressive activity remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No unifying model linking nuclear repair and ER-membrane immune signalling\",\n        \"No structural model of the catalytic mechanism\",\n        \"Recruitment to and topology at the nuclear periphery undefined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140097\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0016787\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005635\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005783\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-73894\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\n      \"RNF26-TMEM43-TMEM33-TMED1 ER-membrane complex\"\n    ],\n    \"partners\": [\n      \"RNF26\",\n      \"TMEM43\",\n      \"TMEM33\",\n      \"TMED1\",\n      \"PRKDC\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":5,"faith_pct":80.0}}