{"gene":"TG_310930","gene_symbol":"FBXO1","run_date":"2026-09-08T15:15:13","timeline":{"discoveries":[{"year":2019,"finding":"TgFBXO1 interacts with Toxoplasma SKP1, confirming it as a bona fide F-box protein and substrate receptor for the SKP1-Cullin F-box E3 ubiquitin ligase complex.","method":"Interactome screen and direct binding confirmation (Co-IP/pulldown with SKP1)","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal interaction confirmed by interactome screen and direct binding assay in a single lab study","pmids":["31348812"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"finding":"In interphase parasites, TgFBXO1 localizes to the Inner Membrane Complex (IMC), an organelle underlying the plasma membrane.","method":"Fluorescence microscopy / live imaging / subcellular localization","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization by imaging, single lab, consistent with functional role","pmids":["31348812"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"finding":"Early during replication, TgFBXO1 localizes to the developing daughter cell scaffold (the site where daughter cell IMC and microtubules form), with timing dependent on centrosome duplication occurring before kinetochore separation.","method":"Fluorescence microscopy, cell cycle stage-specific localization analysis","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization imaging with cell-cycle markers, single lab","pmids":["31348812"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"finding":"TgFBXO1 localization to the daughter cell scaffold requires N-myristoylation of TgFBXO1.","method":"Mutagenesis of N-myristoylation site combined with fluorescence localization","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 1-2 / Moderate — mutagenesis with functional localization readout, single lab","pmids":["31348812"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"finding":"TgFBXO1 localization to the daughter cell scaffold is dependent on the small GTPase TgRab11b, placing TgFBXO1 downstream of TgRab11b in the pathway governing daughter cell scaffold assembly.","method":"Genetic epistasis / loss-of-function of TgRab11b with localization readout","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — epistasis experiment with localization phenotype, single lab","pmids":["31348812"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"finding":"TgFBXO1 is required for parasite growth, functioning specifically as a daughter cell scaffold effector during replication, as demonstrated by loss-of-function experiments showing defective scaffold function.","method":"Loss-of-function (knockdown/knockout) with parasite growth and scaffold phenotype readout","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — loss-of-function with defined cellular phenotype, single lab","pmids":["31348812"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"FBXO1 abundance is NOT affected by loss of PHYa (the O2-sensing SKP1 hydroxylase), indicating that FBXO1 stability is independent of oxygen-dependent SKP1 glycosylation, in contrast to FBXO13 and FBXO14.","method":"PHYa deletion mutant analysis with quantitative interactome and protein abundance measurements","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — negative finding for FBXO1 specifically, established by comparison in PHYaΔ interactome screen, single lab","pmids":["39307307"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgFBXO1 is a bona fide F-box protein that binds SKP1 to form part of an SCF E3 ubiquitin ligase complex; it localizes to the Inner Membrane Complex in interphase and translocates to the daughter cell scaffold during replication in an N-myristoylation- and TgRab11b-dependent manner, where it is required for daughter cell scaffold function and thus parasite growth, while its stability is not regulated by oxygen-dependent SKP1 glycosylation."},"narrative":{"mechanistic_narrative":"TgFBXO1 is a bona fide F-box protein of Toxoplasma gondii that binds SKP1 to serve as a substrate receptor within an SCF (SKP1-Cullin-F-box) E3 ubiquitin ligase complex, and it functions as an effector of daughter cell scaffold assembly during parasite replication [PMID:31348812]. In interphase parasites it localizes to the Inner Membrane Complex, and early in replication it translocates to the developing daughter cell scaffold in a cell-cycle-coupled manner tied to centrosome duplication [PMID:31348812]. This scaffold recruitment requires N-myristoylation of TgFBXO1 and depends on the small GTPase TgRab11b, placing TgFBXO1 downstream of TgRab11b in the pathway governing daughter cell scaffold formation [PMID:31348812]. Loss of TgFBXO1 impairs scaffold function and blocks parasite growth [PMID:31348812]. Unlike the F-box proteins FBXO13 and FBXO14, TgFBXO1 abundance is independent of oxygen-dependent SKP1 glycosylation controlled by the O2-sensing hydroxylase PHYa [PMID:39307307]. The ubiquitylation substrates of the TgFBXO1-containing SCF complex have not been identified in the available corpus.","teleology":[{"year":2019,"claim":"Whether TgFBXO1 acts as a canonical SCF substrate receptor was unknown; demonstrating direct SKP1 binding established it as a bona fide F-box protein and component of an E3 ubiquitin ligase complex.","evidence":"Interactome screen with reciprocal Co-IP/pulldown confirming SKP1 binding in T. gondii","pmids":["31348812"],"confidence":"Medium","gaps":["No ubiquitylation substrate of the TgFBXO1-SCF complex identified","Cullin and full complex composition not defined for this receptor"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"claim":"The cellular role of TgFBXO1 was unknown; cell-cycle-resolved imaging established that it moves from the interphase IMC to the developing daughter cell scaffold in coordination with centrosome duplication.","evidence":"Fluorescence/live imaging and cell-cycle-stage-specific localization with centrosome and kinetochore markers","pmids":["31348812"],"confidence":"Medium","gaps":["Molecular trigger coupling relocalization to centrosome duplication not defined","Does not establish whether ubiquitin ligase activity is required at the scaffold"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"claim":"How TgFBXO1 is targeted to the daughter scaffold was unknown; mutagenesis and epistasis showed recruitment requires N-myristoylation and the small GTPase TgRab11b, defining an ordered targeting pathway.","evidence":"N-myristoylation-site mutagenesis and TgRab11b loss-of-function, each with localization readout","pmids":["31348812"],"confidence":"Medium","gaps":["Mechanism linking TgRab11b to TgFBXO1 delivery not defined","Whether myristoylation and TgRab11b act in the same or parallel steps not resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2019,"claim":"Whether TgFBXO1 is functionally important was unknown; loss-of-function showed it is required for daughter cell scaffold function and parasite growth, establishing it as a scaffold effector.","evidence":"Knockdown/knockout with parasite growth assay and scaffold phenotype analysis","pmids":["31348812"],"confidence":"Medium","gaps":["Molecular basis of the scaffold defect not defined","Substrate(s) whose regulation underlies the phenotype unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"Whether TgFBXO1 stability is under oxygen-dependent control via SKP1 glycosylation was unknown; PHYa deletion analysis showed FBXO1 abundance is unaffected, distinguishing it from oxygen-regulated F-box proteins FBXO13 and FBXO14.","evidence":"PHYa deletion mutant with quantitative interactome and protein abundance measurements","pmids":["39307307"],"confidence":"Medium","gaps":["What does regulate TgFBXO1 abundance/turnover is unknown","Negative finding from a single interactome comparison"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The ubiquitylation substrates of the TgFBXO1-SCF complex and the biochemical basis of its role in daughter cell scaffold assembly remain unidentified.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No substrate identified for the TgFBXO1 substrate receptor","Link between E3 ligase activity and scaffold function not established"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["SCF (SKP1-Cullin-F-box) E3 ubiquitin ligase complex [#0]"],"partners":["SKP1 [#0]","TGRAB11B (UPSTREAM, TARGETING DEPENDENCY) [#4]"],"other_free_text":["Recruitment to daughter cell scaffold requires N-myristoylation of TgFBXO1 [#3]","Required for daughter cell scaffold function and parasite growth [#5]","Abundance independent of PHYa-mediated oxygen-dependent SKP1 glycosylation, unlike FBXO13 and FBXO14 [#6]"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"31348812","id":"PMC_31348812","title":"Toxoplasma F-box protein 1 is required for daughter cell scaffold function during parasite replication.","date":"2019","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/31348812","citation_count":36,"is_preprint":false},{"pmid":"39307307","id":"PMC_39307307","title":"Oxygen-dependent regulation of F-box proteins in Toxoplasma gondii is mediated by Skp1 glycosylation.","date":"2024","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/39307307","citation_count":12,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3631,"output_tokens":1529,"usd":0.016914,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6672,"output_tokens":2665,"usd":0.049993,"stage2_stop_reason":"end_turn"},"total_usd":0.066907,"stage1_batch_id":"msgbatch_01S6GjoYQm8LTPUsdhASdqag","stage2_batch_id":"msgbatch_01VX63RTMdBJqsG6gQMqoCjz","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2019,\n      \"finding\": \"TgFBXO1 interacts with Toxoplasma SKP1, confirming it as a bona fide F-box protein and substrate receptor for the SKP1-Cullin F-box E3 ubiquitin ligase complex.\",\n      \"method\": \"Interactome screen and direct binding confirmation (Co-IP/pulldown with SKP1)\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal interaction confirmed by interactome screen and direct binding assay in a single lab study\",\n      \"pmids\": [\"31348812\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"In interphase parasites, TgFBXO1 localizes to the Inner Membrane Complex (IMC), an organelle underlying the plasma membrane.\",\n      \"method\": \"Fluorescence microscopy / live imaging / subcellular localization\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization by imaging, single lab, consistent with functional role\",\n      \"pmids\": [\"31348812\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Early during replication, TgFBXO1 localizes to the developing daughter cell scaffold (the site where daughter cell IMC and microtubules form), with timing dependent on centrosome duplication occurring before kinetochore separation.\",\n      \"method\": \"Fluorescence microscopy, cell cycle stage-specific localization analysis\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization imaging with cell-cycle markers, single lab\",\n      \"pmids\": [\"31348812\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TgFBXO1 localization to the daughter cell scaffold requires N-myristoylation of TgFBXO1.\",\n      \"method\": \"Mutagenesis of N-myristoylation site combined with fluorescence localization\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — mutagenesis with functional localization readout, single lab\",\n      \"pmids\": [\"31348812\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TgFBXO1 localization to the daughter cell scaffold is dependent on the small GTPase TgRab11b, placing TgFBXO1 downstream of TgRab11b in the pathway governing daughter cell scaffold assembly.\",\n      \"method\": \"Genetic epistasis / loss-of-function of TgRab11b with localization readout\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — epistasis experiment with localization phenotype, single lab\",\n      \"pmids\": [\"31348812\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"TgFBXO1 is required for parasite growth, functioning specifically as a daughter cell scaffold effector during replication, as demonstrated by loss-of-function experiments showing defective scaffold function.\",\n      \"method\": \"Loss-of-function (knockdown/knockout) with parasite growth and scaffold phenotype readout\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function with defined cellular phenotype, single lab\",\n      \"pmids\": [\"31348812\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"FBXO1 abundance is NOT affected by loss of PHYa (the O2-sensing SKP1 hydroxylase), indicating that FBXO1 stability is independent of oxygen-dependent SKP1 glycosylation, in contrast to FBXO13 and FBXO14.\",\n      \"method\": \"PHYa deletion mutant analysis with quantitative interactome and protein abundance measurements\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — negative finding for FBXO1 specifically, established by comparison in PHYaΔ interactome screen, single lab\",\n      \"pmids\": [\"39307307\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgFBXO1 is a bona fide F-box protein that binds SKP1 to form part of an SCF E3 ubiquitin ligase complex; it localizes to the Inner Membrane Complex in interphase and translocates to the daughter cell scaffold during replication in an N-myristoylation- and TgRab11b-dependent manner, where it is required for daughter cell scaffold function and thus parasite growth, while its stability is not regulated by oxygen-dependent SKP1 glycosylation.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"TgFBXO1 is a bona fide F-box protein of Toxoplasma gondii that binds SKP1 to serve as a substrate receptor within an SCF (SKP1-Cullin-F-box) E3 ubiquitin ligase complex, and it functions as an effector of daughter cell scaffold assembly during parasite replication [#0, #5]. In interphase parasites it localizes to the Inner Membrane Complex, and early in replication it translocates to the developing daughter cell scaffold in a cell-cycle-coupled manner tied to centrosome duplication [#1, #2]. This scaffold recruitment requires N-myristoylation of TgFBXO1 and depends on the small GTPase TgRab11b, placing TgFBXO1 downstream of TgRab11b in the pathway governing daughter cell scaffold formation [#3, #4]. Loss of TgFBXO1 impairs scaffold function and blocks parasite growth [#5]. Unlike the F-box proteins FBXO13 and FBXO14, TgFBXO1 abundance is independent of oxygen-dependent SKP1 glycosylation controlled by the O2-sensing hydroxylase PHYa [#6]. The ubiquitylation substrates of the TgFBXO1-containing SCF complex have not been identified in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2019,\n      \"claim\": \"Whether TgFBXO1 acts as a canonical SCF substrate receptor was unknown; demonstrating direct SKP1 binding established it as a bona fide F-box protein and component of an E3 ubiquitin ligase complex.\",\n      \"evidence\": \"Interactome screen with reciprocal Co-IP/pulldown confirming SKP1 binding in T. gondii\",\n      \"pmids\": [\"31348812\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No ubiquitylation substrate of the TgFBXO1-SCF complex identified\", \"Cullin and full complex composition not defined for this receptor\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"The cellular role of TgFBXO1 was unknown; cell-cycle-resolved imaging established that it moves from the interphase IMC to the developing daughter cell scaffold in coordination with centrosome duplication.\",\n      \"evidence\": \"Fluorescence/live imaging and cell-cycle-stage-specific localization with centrosome and kinetochore markers\",\n      \"pmids\": [\"31348812\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular trigger coupling relocalization to centrosome duplication not defined\", \"Does not establish whether ubiquitin ligase activity is required at the scaffold\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"How TgFBXO1 is targeted to the daughter scaffold was unknown; mutagenesis and epistasis showed recruitment requires N-myristoylation and the small GTPase TgRab11b, defining an ordered targeting pathway.\",\n      \"evidence\": \"N-myristoylation-site mutagenesis and TgRab11b loss-of-function, each with localization readout\",\n      \"pmids\": [\"31348812\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism linking TgRab11b to TgFBXO1 delivery not defined\", \"Whether myristoylation and TgRab11b act in the same or parallel steps not resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Whether TgFBXO1 is functionally important was unknown; loss-of-function showed it is required for daughter cell scaffold function and parasite growth, establishing it as a scaffold effector.\",\n      \"evidence\": \"Knockdown/knockout with parasite growth assay and scaffold phenotype analysis\",\n      \"pmids\": [\"31348812\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular basis of the scaffold defect not defined\", \"Substrate(s) whose regulation underlies the phenotype unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Whether TgFBXO1 stability is under oxygen-dependent control via SKP1 glycosylation was unknown; PHYa deletion analysis showed FBXO1 abundance is unaffected, distinguishing it from oxygen-regulated F-box proteins FBXO13 and FBXO14.\",\n      \"evidence\": \"PHYa deletion mutant with quantitative interactome and protein abundance measurements\",\n      \"pmids\": [\"39307307\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"What does regulate TgFBXO1 abundance/turnover is unknown\", \"Negative finding from a single interactome comparison\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The ubiquitylation substrates of the TgFBXO1-SCF complex and the biochemical basis of its role in daughter cell scaffold assembly remain unidentified.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No substrate identified for the TgFBXO1 substrate receptor\", \"Link between E3 ligase activity and scaffold function not established\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0019005\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0061630\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0070258\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0016567\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0051301\", \"supporting_discovery_ids\": [2, 5], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\n      \"SCF (SKP1-Cullin-F-box) E3 ubiquitin ligase complex [#0]\"\n    ],\n    \"partners\": [\n      \"SKP1 [#0]\",\n      \"TgRab11b (upstream, targeting dependency) [#4]\"\n    ],\n    \"other_free_text\": [\n      \"Recruitment to daughter cell scaffold requires N-myristoylation of TgFBXO1 [#3]\",\n      \"Required for daughter cell scaffold function and parasite growth [#5]\",\n      \"Abundance independent of PHYa-mediated oxygen-dependent SKP1 glycosylation, unlike FBXO13 and FBXO14 [#6]\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_310930","name":"FBXO1","product":"F-box protein FBXO1","uniprot_acc":"A0A125YLS3","chromosome":"TGME49_chrXI","start_pos":1673065},{"strain":"GT1","gene_id":"TGGT1_310930","name":null,"product":"hypothetical protein","uniprot_acc":null,"chromosome":"TGGT1_chrXI","start_pos":1636895},{"strain":"RH88","gene_id":"TGRH88_050450","name":null,"product":"unspecified product","uniprot_acc":null,"chromosome":"CM023092","start_pos":1722530},{"strain":"VEG","gene_id":"TGVEG_310930","name":null,"product":"hypothetical protein","uniprot_acc":"B6KAF9","chromosome":"TGVEG_chrXI","start_pos":1685521}]}