{"gene":"TG_316540","gene_symbol":"ISP3","run_date":"2026-09-11T11:01:00","timeline":{"discoveries":[{"year":2010,"finding":"ISP3 localizes to the central plus basal region of the Toxoplasma gondii IMC, and this targeting is dependent upon N-terminal residues predicted for coordinated myristoylation and palmitoylation. Disruption of ISP1 causes dramatic relocalization of ISP3 (and ISP2) to the apical cap, demonstrating that ISP1 acts as a gatekeeper that hierarchically controls ISP3 sub-compartment targeting.","method":"Fluorescence microscopy of tagged ISP3 in wild-type and ISP1-knockout parasites; N-terminal myristoylation/palmitoylation site mutagenesis","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal genetic epistasis (ISP1 KO causing ISP3 mislocalization) combined with mutagenesis of targeting residues, replicated across multiple ISP family members in one rigorous study","pmids":["20844581"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"Crystal structures of TgISP3 (and TgISP1) at 2.32 Å (and 2.10 Å) resolution reveal that both proteins adopt a pleckstrin homology (PH) fold. Biochemical assays showed no detectable phospholipid-binding activity despite the PH fold; instead, mapping of conserved surface residues and crystal packing analysis suggests the phospholipid-binding site has been repurposed to coordinate protein–protein interactions, likely recruiting partner proteins to the IMC.","method":"X-ray crystallography; phospholipid-binding biochemical assays; conserved surface residue mapping; crystal packing analysis","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure solved with functional validation by biochemical assay and surface analysis in a single rigorous study; no independent replication but multiple orthogonal methods","pmids":["24675080"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"finding":"Depletion of the palmitoyl acyltransferase TgDHHC2 causes ISP3 (along with ISP1) to lose membrane association, identifying TgDHHC2 as the likely palmitoylating enzyme (writer) responsible for ISP3 membrane anchoring. TgDHHC14 depletion does not affect ISP1/3 localization, indicating sequential and distinct PAT requirements for different IMC sub-compartments.","method":"Conditional knockdown of TgDHHC2 and TgDHHC14 followed by fluorescence microscopy to assess ISP3 membrane association","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — clean conditional KO with defined localization phenotype in a single lab; ISP3 identified as likely substrate but direct palmitoylation of ISP3 by TgDHHC2 not biochemically reconstituted","pmids":["32329212"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"ISP3 is a Toxoplasma gondii IMC sub-compartment protein that localizes to the central plus basal region of the IMC via coordinated N-terminal myristoylation and palmitoylation (written by TgDHHC2); its sub-compartment targeting is hierarchically controlled by ISP1 (loss of ISP1 relocalizes ISP3 to the apical cap); structurally, ISP3 adopts a pleckstrin homology fold that lacks phospholipid-binding activity but instead appears to mediate protein–protein interactions, likely recruiting partner proteins to the IMC to support daughter cell formation; ISP3 itself is dispensable for tachyzoite lytic cycle growth."},"narrative":{"mechanistic_narrative":"ISP3 is a Toxoplasma gondii inner membrane complex (IMC) sub-compartment protein that localizes to the central and basal region of the IMC [PMID:20844581]. Its membrane targeting depends on N-terminal residues predicted for coordinated myristoylation and palmitoylation, and this sub-compartment addressing is hierarchically controlled by ISP1: loss of ISP1 relocalizes ISP3 to the apical cap, establishing ISP1 as a gatekeeper of ISP3 targeting [PMID:20844581]. Depletion of the palmitoyl acyltransferase TgDHHC2 causes ISP3 (along with ISP1) to lose membrane association, identifying TgDHHC2 as the likely enzyme responsible for palmitoylating ISP3, while TgDHHC14 depletion does not affect ISP3 localization [PMID:32329212]. Structurally, ISP3 adopts a pleckstrin homology (PH) fold that lacks detectable phospholipid-binding activity; conserved surface residue mapping indicates the canonical lipid-binding site has been repurposed to mediate protein–protein interactions, consistent with a role in recruiting partner proteins to the IMC [PMID:24675080]. The specific partner proteins recruited by ISP3 have not been identified in the available corpus.","teleology":[{"year":2010,"claim":"Established where ISP3 resides in the parasite and how its sub-compartment identity is set, revealing a hierarchical targeting logic among IMC proteins.","evidence":"Fluorescence microscopy of tagged ISP3 in wild-type and ISP1-knockout parasites plus N-terminal acylation site mutagenesis in T. gondii","pmids":["20844581"],"confidence":"High","gaps":["Direct enzymatic demonstration of myristoylation/palmitoylation not shown","Mechanism by which ISP1 excludes ISP3 from the apical cap not defined","Functional consequence of correct central/basal targeting not established"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"Resolved the ISP3 fold and its molecular activity, showing a PH fold that has lost lipid binding and is instead configured for protein–protein interaction.","evidence":"X-ray crystallography at 2.32 Å, phospholipid-binding assays, and conserved surface/crystal-packing analysis of TgISP3","pmids":["24675080"],"confidence":"High","gaps":["No specific interacting partner identified or co-crystallized","Repurposed interaction surface inferred from surface mapping, not from a bound complex"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["ISP1 (HIERARCHICAL GATEKEEPER OF ISP3 SUB-COMPARTMENT TARGETING) [#0]","TGDHHC2 (PALMITOYL ACYLTRANSFERASE REQUIRED FOR ISP3 MEMBRANE ANCHORING) [#2]"],"other_free_text":["Membrane targeting requires N-terminal residues predicted for coordinated myristoylation and palmitoylation [#0].","Adopts a pleckstrin homology fold lacking phospholipid-binding activity, with the lipid-binding site apparently repurposed for protein–protein interaction [#1].","Dispensable for the tachyzoite lytic cycle [#3].","TgDHHC14 depletion does not affect ISP3 localization, indicating distinct PAT requirements among IMC sub-compartments [#2]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"20844581","id":"PMC_20844581","title":"A novel family of Toxoplasma IMC proteins displays a hierarchical organization and functions in coordinating parasite division.","date":"2010","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/20844581","citation_count":192,"is_preprint":false},{"pmid":"27548677","id":"PMC_27548677","title":"Virus-Like Nanoparticle Vaccine Confers Protection against Toxoplasma gondii.","date":"2016","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/27548677","citation_count":33,"is_preprint":false},{"pmid":"21829561","id":"PMC_21829561","title":"Subcellular antigen location influences T-cell activation during acute infection with Toxoplasma gondii.","date":"2011","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/21829561","citation_count":33,"is_preprint":false},{"pmid":"25088010","id":"PMC_25088010","title":"Identification and characterization of Toxoplasma SIP, a conserved apicomplexan cytoskeleton protein involved in maintaining the shape, motility and virulence of the parasite.","date":"2014","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/25088010","citation_count":28,"is_preprint":false},{"pmid":"27586039","id":"PMC_27586039","title":"Cross-protection induced by Toxoplasma gondii virus-like particle vaccine upon intraperitoneal route challenge.","date":"2016","source":"Acta tropica","url":"https://pubmed.ncbi.nlm.nih.gov/27586039","citation_count":15,"is_preprint":false},{"pmid":"34634933","id":"PMC_34634933","title":"A Novel Toxoplasma Inner Membrane Complex Suture-Associated Protein Regulates Suture Protein Targeting and Colocalizes with Membrane Trafficking Machinery.","date":"2021","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/34634933","citation_count":12,"is_preprint":false},{"pmid":"24675080","id":"PMC_24675080","title":"The inner membrane complex sub-compartment proteins critical for replication of the apicomplexan parasite Toxoplasma gondii adopt a pleckstrin homology fold.","date":"2014","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/24675080","citation_count":12,"is_preprint":false},{"pmid":"40801525","id":"PMC_40801525","title":"Co-dependent formation of the Toxoplasma gondii subpellicular microtubules and inner membrane skeleton.","date":"2025","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/40801525","citation_count":11,"is_preprint":false},{"pmid":"19820829","id":"PMC_19820829","title":"Toxoplasma gondii: further studies on the subpellicular network.","date":"2009","source":"Memorias do Instituto Oswaldo Cruz","url":"https://pubmed.ncbi.nlm.nih.gov/19820829","citation_count":11,"is_preprint":false},{"pmid":"38270431","id":"PMC_38270431","title":"Apical annuli are specialised sites of post-invasion secretion of dense granules in Toxoplasma.","date":"2024","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/38270431","citation_count":10,"is_preprint":false},{"pmid":"32329212","id":"PMC_32329212","title":"Two palmitoyl acyltransferases involved sequentially in the biogenesis of the inner membrane complex of Toxoplasma gondii.","date":"2020","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/32329212","citation_count":7,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":23438,"output_tokens":1621,"usd":0.047315,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6791,"output_tokens":2479,"usd":0.047965,"stage2_stop_reason":"end_turn"},"total_usd":0.003572,"stage1_batch_id":"msgbatch_01WgHz6kceqm573AGLyz57at","stage2_batch_id":"msgbatch_01LK4wDYj5zYquahv7gi9893","note":"batch pricing = 50% of standard","skipped":true,"corrective_rerun":"2026-09-10 wrong-gene rerun (round-4 rules)","corrective_reason":"summary amended","hand_review_edit_usd":0.003817,"hand_review_patch":"2026-09-11 AK hand-review verdicts (handoff/tools_2026-09-11/patch)","hand_review_verdict":"edit"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2010,\n      \"finding\": \"ISP3 localizes to the central plus basal region of the Toxoplasma gondii IMC, and this targeting is dependent upon N-terminal residues predicted for coordinated myristoylation and palmitoylation. Disruption of ISP1 causes dramatic relocalization of ISP3 (and ISP2) to the apical cap, demonstrating that ISP1 acts as a gatekeeper that hierarchically controls ISP3 sub-compartment targeting.\",\n      \"method\": \"Fluorescence microscopy of tagged ISP3 in wild-type and ISP1-knockout parasites; N-terminal myristoylation/palmitoylation site mutagenesis\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal genetic epistasis (ISP1 KO causing ISP3 mislocalization) combined with mutagenesis of targeting residues, replicated across multiple ISP family members in one rigorous study\",\n      \"pmids\": [\"20844581\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Crystal structures of TgISP3 (and TgISP1) at 2.32 Å (and 2.10 Å) resolution reveal that both proteins adopt a pleckstrin homology (PH) fold. Biochemical assays showed no detectable phospholipid-binding activity despite the PH fold; instead, mapping of conserved surface residues and crystal packing analysis suggests the phospholipid-binding site has been repurposed to coordinate protein–protein interactions, likely recruiting partner proteins to the IMC.\",\n      \"method\": \"X-ray crystallography; phospholipid-binding biochemical assays; conserved surface residue mapping; crystal packing analysis\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure solved with functional validation by biochemical assay and surface analysis in a single rigorous study; no independent replication but multiple orthogonal methods\",\n      \"pmids\": [\"24675080\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Depletion of the palmitoyl acyltransferase TgDHHC2 causes ISP3 (along with ISP1) to lose membrane association, identifying TgDHHC2 as the likely palmitoylating enzyme (writer) responsible for ISP3 membrane anchoring. TgDHHC14 depletion does not affect ISP1/3 localization, indicating sequential and distinct PAT requirements for different IMC sub-compartments.\",\n      \"method\": \"Conditional knockdown of TgDHHC2 and TgDHHC14 followed by fluorescence microscopy to assess ISP3 membrane association\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean conditional KO with defined localization phenotype in a single lab; ISP3 identified as likely substrate but direct palmitoylation of ISP3 by TgDHHC2 not biochemically reconstituted\",\n      \"pmids\": [\"32329212\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"ISP3 (like ISP1) is dispensable for the tachyzoite lytic cycle, as disruption of ISP3 does not produce gross replication or growth defects, in contrast to ISP2 deletion which causes replication defects.\",\n      \"method\": \"Gene disruption (knockout) with plaque/growth assay\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean genetic knockout with defined phenotypic readout (growth/lytic cycle) in a single study; negative result (dispensability) explicitly demonstrated\",\n      \"pmids\": [\"22659420\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"Preliminary X-ray diffraction data were collected for TgISP1 crystals (as a prerequisite to solving the ISP fold later confirmed to include ISP3); an N-terminally truncated form of TgISP1 was purified from E. coli and crystallized, yielding diffraction to 2.05–2.10 Å. (Note: this is a crystallographic methods paper for ISP1, providing the foundation for the subsequent ISP3 structure in PMID 24675080.)\",\n      \"method\": \"Recombinant protein purification from E. coli; crystallization; X-ray diffraction\",\n      \"journal\": \"Acta crystallographica. Section F, Structural biology and crystallization communications\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 1 / Weak — crystallographic methods paper for ISP1 only; ISP3 structure not yet solved in this work; included only as precursor to PMID 24675080\",\n      \"pmids\": [\"22750877\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"ISP3 is a Toxoplasma gondii IMC sub-compartment protein that localizes to the central plus basal region of the IMC via coordinated N-terminal myristoylation and palmitoylation (written by TgDHHC2); its sub-compartment targeting is hierarchically controlled by ISP1 (loss of ISP1 relocalizes ISP3 to the apical cap); structurally, ISP3 adopts a pleckstrin homology fold that lacks phospholipid-binding activity but instead appears to mediate protein–protein interactions, likely recruiting partner proteins to the IMC to support daughter cell formation; ISP3 itself is dispensable for tachyzoite lytic cycle growth.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"ISP3 is a Toxoplasma gondii inner membrane complex (IMC) sub-compartment protein that localizes to the central and basal region of the IMC [#0]. Its membrane targeting depends on N-terminal residues predicted for coordinated myristoylation and palmitoylation, and this sub-compartment addressing is hierarchically controlled by ISP1: loss of ISP1 relocalizes ISP3 to the apical cap, establishing ISP1 as a gatekeeper of ISP3 targeting [#0]. Membrane anchoring is provided by the palmitoyl acyltransferase TgDHHC2, whose depletion abolishes ISP3 membrane association, whereas TgDHHC14 is dispensable for this step [#2]. Structurally, ISP3 adopts a pleckstrin homology (PH) fold that lacks detectable phospholipid-binding activity; conserved surface residue mapping indicates the canonical lipid-binding site has been repurposed to mediate protein–protein interactions, consistent with a role in recruiting partner proteins to the IMC [#1]. ISP3 is dispensable for the tachyzoite lytic cycle, as its disruption produces no gross replication or growth defect [#3]. The specific partner proteins recruited by ISP3 have not been identified in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"Established where ISP3 resides in the parasite and how its sub-compartment identity is set, revealing a hierarchical targeting logic among IMC proteins.\",\n      \"evidence\": \"Fluorescence microscopy of tagged ISP3 in wild-type and ISP1-knockout parasites plus N-terminal acylation site mutagenesis in T. gondii\",\n      \"pmids\": [\"20844581\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct enzymatic demonstration of myristoylation/palmitoylation not shown\",\n        \"Mechanism by which ISP1 excludes ISP3 from the apical cap not defined\",\n        \"Functional consequence of correct central/basal targeting not established\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Determined whether ISP3 is required for parasite proliferation, showing it is dispensable for the tachyzoite lytic cycle unlike its paralog ISP2.\",\n      \"evidence\": \"Gene knockout with plaque/growth assay in T. gondii\",\n      \"pmids\": [\"22659420\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Possible redundancy with other ISP proteins not tested\",\n        \"Phenotypes outside the tachyzoite lytic cycle (e.g. other life stages) not examined\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Provided the crystallographic foundation for the ISP fold by purifying and crystallizing TgISP1, enabling the later ISP3 structure.\",\n      \"evidence\": \"Recombinant purification from E. coli, crystallization and X-ray diffraction of truncated TgISP1 (methods paper for ISP1)\",\n      \"pmids\": [\"22750877\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"ISP3 structure not solved in this work; only ISP1 crystals characterized\",\n        \"No functional or biochemical data reported\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Resolved the ISP3 fold and its molecular activity, showing a PH fold that has lost lipid binding and is instead configured for protein–protein interaction.\",\n      \"evidence\": \"X-ray crystallography at 2.32 Å, phospholipid-binding assays, and conserved surface/crystal-packing analysis of TgISP3\",\n      \"pmids\": [\"24675080\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No specific interacting partner identified or co-crystallized\",\n        \"Repurposed interaction surface inferred from surface mapping, not from a bound complex\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Identified the enzyme responsible for ISP3 membrane anchoring, distinguishing sequential palmitoyl acyltransferase requirements across IMC sub-compartments.\",\n      \"evidence\": \"Conditional knockdown of TgDHHC2 and TgDHHC14 with fluorescence microscopy assessing ISP3 membrane association in T. gondii\",\n      \"pmids\": [\"32329212\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct palmitoylation of ISP3 by TgDHHC2 not biochemically reconstituted\",\n        \"Whether the effect is direct or via loss of an intermediate factor not resolved\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The partner proteins recruited by the repurposed PH surface of ISP3 and the specific process they serve remain unidentified.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No ISP3 interacting partner has been isolated or co-structured\",\n        \"Downstream functional role of ISP3-mediated recruitment at the IMC undefined\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0070258\", \"supporting_discovery_ids\": [0, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [\n      \"ISP1 (hierarchical gatekeeper of ISP3 sub-compartment targeting) [#0]\",\n      \"TgDHHC2 (palmitoyl acyltransferase required for ISP3 membrane anchoring) [#2]\"\n    ],\n    \"other_free_text\": [\n      \"Membrane targeting requires N-terminal residues predicted for coordinated myristoylation and palmitoylation [#0].\",\n      \"Adopts a pleckstrin homology fold lacking phospholipid-binding activity, with the lipid-binding site apparently repurposed for protein–protein interaction [#1].\",\n      \"Dispensable for the tachyzoite lytic cycle [#3].\",\n      \"TgDHHC14 depletion does not affect ISP3 localization, indicating distinct PAT requirements among IMC sub-compartments [#2].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_316540","name":"ISP3","product":"IMC sub-compartment protein ISP3","uniprot_acc":"A0A125YUT6","chromosome":"TGME49_chrXI","start_pos":5390304},{"strain":"GT1","gene_id":"TGGT1_316540","name":null,"product":"IMC sub-compartment protein ISP3","uniprot_acc":null,"chromosome":"TGGT1_chrXI","start_pos":5335579},{"strain":"RH88","gene_id":"TGRH88_055250","name":null,"product":"IMC sub-compartment protein ISP3","uniprot_acc":null,"chromosome":"CM023092","start_pos":5456761},{"strain":"VEG","gene_id":"TGVEG_316540","name":null,"product":"IMC sub-compartment protein ISP3","uniprot_acc":"B9PJE6","chromosome":"TGVEG_chrXI","start_pos":5413041}]}