{"gene":"PF3D7_1333200","run_date":"2026-09-08T14:19:06","timeline":{"discoveries":[{"year":2009,"finding":"PfsUba1 (the apicoplast-targeted ubiquitin-activating enzyme, encoded by PF3D7_1333200 ortholog) localizes to the apicoplast of P. falciparum, as demonstrated by fluorescence imaging of the full-length protein and N-terminal GFP fusions.","method":"Transfection with GFP fusions and fluorescence imaging of full-length PfsUba1","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct fluorescence localization of full-length protein in live parasites, single lab, single method","pmids":["19502583"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2012,"finding":"PfUBA1 (E1 ubiquitin-activating enzyme) mediates in vitro ubiquitylation activity and localizes to the cytosol of P. falciparum, as part of the parasite ERAD system.","method":"In vitro ubiquitylation assay and immunofluorescence microscopy","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vitro enzymatic reconstitution plus localization, single lab, two orthogonal methods","pmids":["22912882"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"finding":"The apicoplast-localized ubiquitin-activating enzyme (E1; PF3D7_1333200 ortholog, termed PfsUba1) is biochemically active in vitro and is required for import of nuclear-encoded plastid proteins and parasite survival, as demonstrated by conditional gene ablation and complementation in P. falciparum and T. gondii.","method":"In vitro ubiquitylation reconstitution, conditional gene ablation, complementation analysis, and apicoplast protein import assay","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — in vitro reconstitution of enzymatic activity plus conditional genetic ablation with specific organellar import phenotype, multiple orthogonal methods in one study","pmids":["23785288"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"finding":"Inhibition of the ubiquitin-activating enzyme E1 (PF3D7_1333200) reduces the level of damaged, polyubiquitinated proteins and alleviates the ER stress response, dramatically antagonizing dihydroartemisinin (DHA) activity in P. falciparum, placing E1 upstream of polyubiquitin accumulation in the DHA killing mechanism.","method":"Pharmacological inhibition of E1 combined with DHA treatment; measurement of polyubiquitinated protein levels and ER stress markers","journal":"Nature communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — chemical-genetic epistasis with functional readouts, single lab, but pathway placement is clear","pmids":["30228310"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"finding":"PfUBA1 (E1 ubiquitin-activating enzyme; PF3D7_1333200) is essential for schizont maturation to merozoites in P. falciparum blood-stage development; conditional deletion of uba1 blocks nuclear division and formation of intracellular merozoite structures at the schizont stage. Recombinant PfUBA1 is potently inhibited by MLN7243 (TAK-243) in vitro, and a structural homology model identifies the enzyme-inhibitor interaction interface.","method":"Rapamycin-inducible conditional gene deletion, in vitro inhibition of recombinant PfUBA1, structural homology modeling, ubiquitylation site proteomics","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — conditional genetic knockout with defined developmental phenotype, in vitro enzymatic inhibition of recombinant protein, structural modeling, multiple orthogonal methods in one study","pmids":["32569299"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1333200 encodes the P. falciparum ubiquitin-activating enzyme (E1/UBA1/PfsUba1), which has two functional pools: an apicoplast-localized form (PfsUba1) that is biochemically active and essential for import of nuclear-encoded apicoplast proteins, and a cytosolic form (PfUBA1) that drives the ERAD ubiquitylation cascade; the enzyme is additionally required for the final differentiation of schizonts to merozoites during blood-stage development, and its inhibition collapses the polyubiquitinated protein pool that underlies artemisinin-mediated parasite killing."},"narrative":{"mechanistic_narrative":"PF3D7_1333200 encodes the P. falciparum ubiquitin-activating enzyme (E1; variously termed PfsUba1/PfUBA1), the apex enzyme that charges ubiquitin and initiates ubiquitylation cascades essential for parasite viability [PMID:23785288, PMID:32569299]. The enzyme is biochemically active in vitro and partitions between two functional pools: an apicoplast-associated form required for import of nuclear-encoded plastid proteins, whose conditional ablation blocks organellar protein import and kills the parasite [PMID:19502583, PMID:23785288], and a cytosolic form that supplies activated ubiquitin to the parasite ERAD system [PMID:22912882]. During blood-stage development the enzyme is essential for the final differentiation of schizonts to merozoites, with conditional deletion arresting nuclear division and intracellular merozoite formation [PMID:32569299]. Recombinant enzyme is potently inhibited by MLN7243 (TAK-243), and E1 activity sits upstream of the polyubiquitinated protein pool whose accumulation drives dihydroartemisinin-mediated killing, such that E1 inhibition antagonizes artemisinin activity [PMID:30228310, PMID:32569299]. Beyond these roles, the substrate repertoire and the mechanism governing dual apicoplast/cytosolic partitioning have not been characterized in the available corpus.","teleology":[{"year":2009,"claim":"Establishing where the parasite E1 enzyme acts was the first step; imaging placed PfsUba1 at the apicoplast, raising the possibility of an organelle-associated ubiquitylation system distinct from the canonical cytosolic pathway.","evidence":"GFP-fusion transfection and fluorescence imaging of full-length PfsUba1 in P. falciparum","pmids":["19502583"],"confidence":"Medium","gaps":["Localization from a single method and lab","No enzymatic activity demonstrated at this stage","Cytosolic pool not yet distinguished"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2012,"claim":"Whether the enzyme is catalytically functional and where it operates in the ubiquitin-proteasome pathway was addressed by showing in vitro ubiquitylation activity and cytosolic localization within the ERAD system.","evidence":"In vitro ubiquitylation assay and immunofluorescence microscopy in P. falciparum","pmids":["22912882"],"confidence":"Medium","gaps":["Relationship between cytosolic and apicoplast pools unresolved","Specific ERAD substrates not identified","No genetic essentiality data"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"claim":"The functional consequence of the apicoplast pool was resolved by conditional ablation and complementation, establishing that the biochemically active enzyme is required for import of nuclear-encoded plastid proteins and for parasite survival.","evidence":"In vitro reconstitution, conditional gene ablation, complementation, and apicoplast protein import assay in P. falciparum and T. gondii","pmids":["23785288"],"confidence":"High","gaps":["Molecular mechanism coupling ubiquitin activation to plastid import unclear","Substrate proteins of the import-linked ubiquitylation not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"claim":"The enzyme's placement in the artemisinin killing pathway was defined by chemical-genetic epistasis, showing E1 inhibition depletes polyubiquitinated proteins and antagonizes dihydroartemisinin, positioning E1 upstream of the polyubiquitin accumulation that mediates drug lethality.","evidence":"Pharmacological E1 inhibition combined with DHA treatment; polyubiquitin and ER stress marker readouts in P. falciparum","pmids":["30228310"],"confidence":"Medium","gaps":["Inhibitor specificity for E1 not fully excluded","Identity of the artemisinin-damaged substrates unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"claim":"The blood-stage developmental requirement and druggability were established by conditional deletion causing a schizont-to-merozoite differentiation block and by potent in vitro inhibition of recombinant enzyme by MLN7243.","evidence":"Rapamycin-inducible conditional deletion, in vitro inhibition of recombinant PfUBA1, structural homology modeling, and ubiquitylation-site proteomics in P. falciparum","pmids":["32569299"],"confidence":"High","gaps":["Structure is a homology model, not experimental","Downstream E2/E3 partners driving merozoite formation not defined","Direct substrates at the schizont transition not mapped"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"How a single E1 enzyme is partitioned between the apicoplast and cytosol, and what substrate/E2-E3 networks it feeds in each compartment, remains open.","evidence":"","pmids":[],"confidence":"Medium","gaps":["Targeting/partitioning mechanism between compartments unknown","No comprehensive substrate map","Downstream ubiquitin conjugation partners uncharacterized in the corpus"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["Required for schizont-to-merozoite differentiation during blood-stage development [#4]","Acts upstream of polyubiquitin accumulation in dihydroartemisinin-mediated killing; inhibition antagonizes DHA [#3]","Recombinant enzyme potently inhibited by MLN7243 (TAK-243) [#4]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"30228310","id":"PMC_30228310","title":"Artemisinin kills malaria parasites by damaging proteins and inhibiting the proteasome.","date":"2018","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/30228310","citation_count":224,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ubiquitin activating enzyme","ubiquitin-activating enzyme"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19502583","id":"PMC_19502583","title":"An unusual ERAD-like complex is targeted to the apicoplast of Plasmodium falciparum.","date":"2009","source":"Eukaryotic cell","url":"https://pubmed.ncbi.nlm.nih.gov/19502583","citation_count":109,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23785288","id":"PMC_23785288","title":"An apicoplast localized ubiquitylation system is required for the import of nuclear-encoded plastid proteins.","date":"2013","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/23785288","citation_count":55,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"22912882","id":"PMC_22912882","title":"Characterization of the ubiquitylating components of the human malaria parasite's protein degradation pathway.","date":"2012","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/22912882","citation_count":43,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["UBA1","ubiquitin activating enzyme","ubiquitin-activating enzyme"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32569299","id":"PMC_32569299","title":"Ubiquitin activation is essential for schizont maturation in Plasmodium falciparum blood-stage development.","date":"2020","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/32569299","citation_count":36,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["UBA1","ubiquitin activating enzyme","ubiquitin-activating enzyme","PfUBA1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28577368","id":"PMC_28577368","title":"Inhibitors of ubiquitin E3 ligase as potential new antimalarial drug leads.","date":"2017","source":"BMC pharmacology & toxicology","url":"https://pubmed.ncbi.nlm.nih.gov/28577368","citation_count":23,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ubiquitin activating enzyme","ubiquitin-activating enzyme"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6054,"output_tokens":1462,"usd":0.020046,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6385,"output_tokens":2527,"usd":0.04755,"stage2_stop_reason":"end_turn"},"total_usd":0.067596,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2009,\n      \"finding\": \"PfsUba1 (the apicoplast-targeted ubiquitin-activating enzyme, encoded by PF3D7_1333200 ortholog) localizes to the apicoplast of P. falciparum, as demonstrated by fluorescence imaging of the full-length protein and N-terminal GFP fusions.\",\n      \"method\": \"Transfection with GFP fusions and fluorescence imaging of full-length PfsUba1\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct fluorescence localization of full-length protein in live parasites, single lab, single method\",\n      \"pmids\": [\"19502583\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"PfUBA1 (E1 ubiquitin-activating enzyme) mediates in vitro ubiquitylation activity and localizes to the cytosol of P. falciparum, as part of the parasite ERAD system.\",\n      \"method\": \"In vitro ubiquitylation assay and immunofluorescence microscopy\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vitro enzymatic reconstitution plus localization, single lab, two orthogonal methods\",\n      \"pmids\": [\"22912882\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"The apicoplast-localized ubiquitin-activating enzyme (E1; PF3D7_1333200 ortholog, termed PfsUba1) is biochemically active in vitro and is required for import of nuclear-encoded plastid proteins and parasite survival, as demonstrated by conditional gene ablation and complementation in P. falciparum and T. gondii.\",\n      \"method\": \"In vitro ubiquitylation reconstitution, conditional gene ablation, complementation analysis, and apicoplast protein import assay\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — in vitro reconstitution of enzymatic activity plus conditional genetic ablation with specific organellar import phenotype, multiple orthogonal methods in one study\",\n      \"pmids\": [\"23785288\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Inhibition of the ubiquitin-activating enzyme E1 (PF3D7_1333200) reduces the level of damaged, polyubiquitinated proteins and alleviates the ER stress response, dramatically antagonizing dihydroartemisinin (DHA) activity in P. falciparum, placing E1 upstream of polyubiquitin accumulation in the DHA killing mechanism.\",\n      \"method\": \"Pharmacological inhibition of E1 combined with DHA treatment; measurement of polyubiquitinated protein levels and ER stress markers\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — chemical-genetic epistasis with functional readouts, single lab, but pathway placement is clear\",\n      \"pmids\": [\"30228310\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"PfUBA1 (E1 ubiquitin-activating enzyme; PF3D7_1333200) is essential for schizont maturation to merozoites in P. falciparum blood-stage development; conditional deletion of uba1 blocks nuclear division and formation of intracellular merozoite structures at the schizont stage. Recombinant PfUBA1 is potently inhibited by MLN7243 (TAK-243) in vitro, and a structural homology model identifies the enzyme-inhibitor interaction interface.\",\n      \"method\": \"Rapamycin-inducible conditional gene deletion, in vitro inhibition of recombinant PfUBA1, structural homology modeling, ubiquitylation site proteomics\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — conditional genetic knockout with defined developmental phenotype, in vitro enzymatic inhibition of recombinant protein, structural modeling, multiple orthogonal methods in one study\",\n      \"pmids\": [\"32569299\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1333200 encodes the P. falciparum ubiquitin-activating enzyme (E1/UBA1/PfsUba1), which has two functional pools: an apicoplast-localized form (PfsUba1) that is biochemically active and essential for import of nuclear-encoded apicoplast proteins, and a cytosolic form (PfUBA1) that drives the ERAD ubiquitylation cascade; the enzyme is additionally required for the final differentiation of schizonts to merozoites during blood-stage development, and its inhibition collapses the polyubiquitinated protein pool that underlies artemisinin-mediated parasite killing.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"PF3D7_1333200 encodes the P. falciparum ubiquitin-activating enzyme (E1; variously termed PfsUba1/PfUBA1), the apex enzyme that charges ubiquitin and initiates ubiquitylation cascades essential for parasite viability [#2, #4]. The enzyme is biochemically active in vitro and partitions between two functional pools: an apicoplast-associated form required for import of nuclear-encoded plastid proteins, whose conditional ablation blocks organellar protein import and kills the parasite [#0, #2], and a cytosolic form that supplies activated ubiquitin to the parasite ERAD system [#1]. During blood-stage development the enzyme is essential for the final differentiation of schizonts to merozoites, with conditional deletion arresting nuclear division and intracellular merozoite formation [#4]. Recombinant enzyme is potently inhibited by MLN7243 (TAK-243), and E1 activity sits upstream of the polyubiquitinated protein pool whose accumulation drives dihydroartemisinin-mediated killing, such that E1 inhibition antagonizes artemisinin activity [#3, #4]. Beyond these roles, the substrate repertoire and the mechanism governing dual apicoplast/cytosolic partitioning have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2009,\n      \"claim\": \"Establishing where the parasite E1 enzyme acts was the first step; imaging placed PfsUba1 at the apicoplast, raising the possibility of an organelle-associated ubiquitylation system distinct from the canonical cytosolic pathway.\",\n      \"evidence\": \"GFP-fusion transfection and fluorescence imaging of full-length PfsUba1 in P. falciparum\",\n      \"pmids\": [\"19502583\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Localization from a single method and lab\", \"No enzymatic activity demonstrated at this stage\", \"Cytosolic pool not yet distinguished\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Whether the enzyme is catalytically functional and where it operates in the ubiquitin-proteasome pathway was addressed by showing in vitro ubiquitylation activity and cytosolic localization within the ERAD system.\",\n      \"evidence\": \"In vitro ubiquitylation assay and immunofluorescence microscopy in P. falciparum\",\n      \"pmids\": [\"22912882\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Relationship between cytosolic and apicoplast pools unresolved\", \"Specific ERAD substrates not identified\", \"No genetic essentiality data\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"The functional consequence of the apicoplast pool was resolved by conditional ablation and complementation, establishing that the biochemically active enzyme is required for import of nuclear-encoded plastid proteins and for parasite survival.\",\n      \"evidence\": \"In vitro reconstitution, conditional gene ablation, complementation, and apicoplast protein import assay in P. falciparum and T. gondii\",\n      \"pmids\": [\"23785288\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular mechanism coupling ubiquitin activation to plastid import unclear\", \"Substrate proteins of the import-linked ubiquitylation not defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"The enzyme's placement in the artemisinin killing pathway was defined by chemical-genetic epistasis, showing E1 inhibition depletes polyubiquitinated proteins and antagonizes dihydroartemisinin, positioning E1 upstream of the polyubiquitin accumulation that mediates drug lethality.\",\n      \"evidence\": \"Pharmacological E1 inhibition combined with DHA treatment; polyubiquitin and ER stress marker readouts in P. falciparum\",\n      \"pmids\": [\"30228310\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Inhibitor specificity for E1 not fully excluded\", \"Identity of the artemisinin-damaged substrates unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"The blood-stage developmental requirement and druggability were established by conditional deletion causing a schizont-to-merozoite differentiation block and by potent in vitro inhibition of recombinant enzyme by MLN7243.\",\n      \"evidence\": \"Rapamycin-inducible conditional deletion, in vitro inhibition of recombinant PfUBA1, structural homology modeling, and ubiquitylation-site proteomics in P. falciparum\",\n      \"pmids\": [\"32569299\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structure is a homology model, not experimental\", \"Downstream E2/E3 partners driving merozoite formation not defined\", \"Direct substrates at the schizont transition not mapped\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How a single E1 enzyme is partitioned between the apicoplast and cytosol, and what substrate/E2-E3 networks it feeds in each compartment, remains open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Targeting/partitioning mechanism between compartments unknown\", \"No comprehensive substrate map\", \"Downstream ubiquitin conjugation partners uncharacterized in the corpus\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004839\", \"supporting_discovery_ids\": [1, 2, 4]},\n      {\"term_id\": \"GO:0016881\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020011\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0016567\", \"supporting_discovery_ids\": [1, 3, 4]},\n      {\"term_id\": \"GO:0030433\", \"supporting_discovery_ids\": [1, 3]},\n      {\"term_id\": \"GO:0045037\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"Required for schizont-to-merozoite differentiation during blood-stage development [#4]\",\n      \"Acts upstream of polyubiquitin accumulation in dihydroartemisinin-mediated killing; inhibition antagonizes DHA [#3]\",\n      \"Recombinant enzyme potently inhibited by MLN7243 (TAK-243) [#4]\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1333200","name":null,"product":"ubiquitin-activating enzyme","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1347900","name":null,"product":"ubiquitin activating enzyme, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1267400","name":null,"product":"ubiquitin activating enzyme, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"UBA1","evaluation":null}