{"gene":"TG_263520","gene_symbol":"SPM1","run_date":"2026-09-08T14:08:29","timeline":{"discoveries":[{"year":2011,"finding":"SPM1 localizes along the full length of the subpellicular microtubules but does not associate with the conoid or spindle microtubules. Four or more copies of the SPM1 32-amino-acid repeat are required for localization to microtubules. Loss of SPM1 decreases parasite fitness and eliminates the stability of subpellicular microtubules to detergent extraction, establishing SPM1 as a stabilizer of subpellicular microtubules.","method":"Domain deletion analysis, gene deletion (knockout), detergent extraction assay, fluorescence localization","journal":"Eukaryotic cell","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean gene deletion with defined phenotypic readout, domain deletion mutagenesis, localization experiments, all orthogonal methods in one study","pmids":["22021240"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"finding":"SPM1 forms part of a protein complex coating the cortical microtubules that includes TrxL1 and TrxL2. SPM1 recruits TrxL1 to the cortical microtubules; TrxL1 does not bind microtubules directly but associates with the complex via SPM1.","method":"Co-immunoprecipitation, fluorescence localization","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — Co-IP demonstrating SPM1–TrxL1 interaction and recruitment, single lab but supported by localization experiments","pmids":["23873863"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"Cryo-EM ex vivo structure of cortical microtubules from Toxoplasma gondii identifies SPM1 (along with TrxL1 and TrxL2) as a bona fide microtubule inner protein (MIP). These three MIPs form a mesh on the luminal surface and simultaneously stabilize the tubulin lattice in both longitudinal and lateral directions. Deletion of SPM1 (along with other identified MIPs) compromises MT stability and integrity under chemical challenge.","method":"Single-particle cryo-EM (ex vivo structure determination), gene deletion with chemical treatment assay","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Strong — cryo-EM structure with functional validation by gene deletion, multiple orthogonal methods in one study","pmids":["34031406"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2023,"finding":"The protein phosphatase PPKL regulates the phosphorylation state of SPM1; depletion of PPKL results in a significant increase in SPM1 phosphorylation, correlating with defects in cortical microtubule rigidity and arrangement. This places PPKL upstream of SPM1 in a signaling pathway governing cortical microtubule organization.","method":"Conditional knockdown of PPKL, global phosphoproteomics","journal":"bioRxiv","confidence":"Low","confidence_rationale":"Tier 3 / Weak — phosphoproteomics correlation from a preprint; the link between increased SPM1 phosphorylation and the microtubule phenotype is inferred, not directly demonstrated by SPM1 phosphosite mutagenesis","pmids":["37398039"],"is_preprint":true,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2026,"finding":"The deubiquitinase TgJosephin deubiquitinates SPM1; loss of TgJosephin leads to increased ubiquitination of SPM1. Mutation of the ubiquitination sites on SPM1 restores virulence in the absence of TgJosephin, establishing that SPM1 ubiquitination status is functionally important for parasite anti-IFN-γ virulence.","method":"Deubiquitinase gene deletion, ubiquitination site mutagenesis of SPM1, mouse virulence assay with IFNγR-knockout mice","journal":"mSphere","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — gene deletion combined with site-directed mutagenesis of ubiquitination sites and in vivo rescue experiment, single lab","pmids":["41972766"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"SPM1 is a microtubule inner protein (MIP) that localizes along the full length of Toxoplasma gondii subpellicular cortical microtubules (but not conoid or spindle MTs), where it stabilizes the tubulin lattice in both longitudinal and lateral directions via a luminal mesh formed with TrxL1 and TrxL2; SPM1 recruits TrxL1 to the cortex, requires four or more of its 32-amino-acid repeats for microtubule association, is phospho-regulated by the phosphatase PPKL, and is deubiquitinated by TgJosephin—with its ubiquitination state influencing parasite anti-IFN-γ virulence."},"narrative":{"mechanistic_narrative":"SPM1 is a microtubule inner protein (MIP) of Toxoplasma gondii that stabilizes the subpellicular cortical microtubule array [PMID:22021240, PMID:34031406]. It localizes along the full length of the subpellicular microtubules but is excluded from conoid and spindle microtubules, and its association with microtubules requires four or more copies of its 32-amino-acid repeat [PMID:22021240]. Cryo-EM of ex vivo cortical microtubules places SPM1 on the luminal surface, where together with TrxL1 and TrxL2 it forms a mesh that stabilizes the tubulin lattice in both longitudinal and lateral directions; loss of SPM1 abolishes microtubule resistance to detergent and chemical challenge and reduces parasite fitness [PMID:22021240, PMID:34031406]. Within this complex SPM1 acts as the scaffold that recruits TrxL1, which does not bind microtubules directly [PMID:23873863]. SPM1 is subject to post-translational control: it is deubiquitinated by TgJosephin, and its ubiquitination state governs parasite anti-IFN-γ virulence, as mutating the SPM1 ubiquitination sites restores virulence in TgJosephin-deficient parasites [PMID:41972766].","teleology":[{"year":2011,"claim":"Established SPM1 as a dedicated stabilizer of the subpellicular cortical microtubules and defined the repeat requirement for its microtubule association, distinguishing it from conoid and spindle microtubule factors.","evidence":"Gene deletion with detergent extraction phenotype, domain-deletion mutagenesis and fluorescence localization in Toxoplasma gondii","pmids":["22021240"],"confidence":"High","gaps":["Molecular basis of lattice stabilization not resolved at the structural level","How the 32-aa repeats engage tubulin not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"claim":"Placed SPM1 within a cortical microtubule-coating complex and identified it as the scaffold that recruits TrxL1, which cannot bind microtubules on its own.","evidence":"Co-immunoprecipitation and fluorescence localization in Toxoplasma gondii","pmids":["23873863"],"confidence":"Medium","gaps":["Interaction shown by Co-IP without structural mapping of the binding interface","Stoichiometry of the complex not determined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"Defined SPM1 structurally as a bona fide microtubule inner protein that, with TrxL1 and TrxL2, forms a luminal mesh stabilizing the tubulin lattice both longitudinally and laterally.","evidence":"Single-particle cryo-EM of ex vivo cortical microtubules plus gene deletion with chemical challenge in Toxoplasma gondii","pmids":["34031406"],"confidence":"High","gaps":["Individual contribution of SPM1 versus the other MIPs to lattice stability not separated","In-cell assembly order of the mesh unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2023,"claim":"Proposed phospho-regulation of SPM1 by the phosphatase PPKL as an input controlling cortical microtubule rigidity and arrangement.","evidence":"Conditional PPKL knockdown with global phosphoproteomics (preprint) in Toxoplasma gondii","pmids":["37398039"],"confidence":"Low","gaps":["Correlative phosphoproteomics; not confirmed by SPM1 phosphosite mutagenesis","Whether SPM1 phosphorylation causally drives the microtubule phenotype is inferred, not demonstrated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2026,"claim":"Established a ubiquitination-based regulatory axis on SPM1, showing that TgJosephin-mediated deubiquitination and SPM1 ubiquitination status control parasite anti-IFN-γ virulence.","evidence":"TgJosephin gene deletion, SPM1 ubiquitination-site mutagenesis and mouse virulence assays in IFNγR-knockout mice","pmids":["41972766"],"confidence":"Medium","gaps":["Mechanism linking SPM1 ubiquitination to virulence not defined","Whether ubiquitination alters SPM1 microtubule association or stability not shown","Single lab"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"How the distinct post-translational inputs (phosphorylation by PPKL, ubiquitination reversed by TgJosephin) integrate to tune SPM1's microtubule-stabilizing function and its role in virulence remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No direct link established between phospho- and ubiquitin-regulation of SPM1","Mechanistic coupling of lattice stabilization to virulence not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Luminal cortical microtubule MIP mesh (SPM1–TrxL1–TrxL2)"],"partners":["TRXL1 (RECRUITED BY SPM1)","TRXL2","PPKL (PHOSPHATASE REGULATING SPM1)","TGJOSEPHIN (DEUBIQUITINASE ACTING ON SPM1)"],"other_free_text":["Requires four or more of its 32-amino-acid repeats for microtubule association","SPM1 ubiquitination status modulates parasite anti-IFN-γ virulence"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"34031406","id":"PMC_34031406","title":"Cryo-EM structure of cortical microtubules from human parasite Toxoplasma gondii identifies their microtubule inner proteins.","date":"2021","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/34031406","citation_count":64,"is_preprint":false},{"pmid":"22021240","id":"PMC_22021240","title":"SPM1 stabilizes subpellicular microtubules in Toxoplasma gondii.","date":"2011","source":"Eukaryotic cell","url":"https://pubmed.ncbi.nlm.nih.gov/22021240","citation_count":53,"is_preprint":false},{"pmid":"23873863","id":"PMC_23873863","title":"Novel thioredoxin-like proteins are components of a protein complex coating the cortical microtubules of Toxoplasma gondii.","date":"2013","source":"Eukaryotic cell","url":"https://pubmed.ncbi.nlm.nih.gov/23873863","citation_count":48,"is_preprint":false},{"pmid":"37398039","id":"PMC_37398039","title":"The protein phosphatase PPKL is a key regulator of daughter parasite development in Toxoplasma gondii.","date":"2023","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/37398039","citation_count":2,"is_preprint":false},{"pmid":"41972766","id":"PMC_41972766","title":"TgJosephin and TgRad23 are important for anti-IFN-γ virulence via deubiquitination of SPM1 in Toxoplasma.","date":"2026","source":"mSphere","url":"https://pubmed.ncbi.nlm.nih.gov/41972766","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5129,"output_tokens":1526,"usd":0.019138,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6602,"output_tokens":2597,"usd":0.048967,"stage2_stop_reason":"end_turn"},"total_usd":0.068105,"stage1_batch_id":"msgbatch_015xmQKDRqnTh9anE4m7LiD6","stage2_batch_id":"msgbatch_01JLpkFTVhoQBNgqHCKFrVVU","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2011,\n      \"finding\": \"SPM1 localizes along the full length of the subpellicular microtubules but does not associate with the conoid or spindle microtubules. Four or more copies of the SPM1 32-amino-acid repeat are required for localization to microtubules. Loss of SPM1 decreases parasite fitness and eliminates the stability of subpellicular microtubules to detergent extraction, establishing SPM1 as a stabilizer of subpellicular microtubules.\",\n      \"method\": \"Domain deletion analysis, gene deletion (knockout), detergent extraction assay, fluorescence localization\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean gene deletion with defined phenotypic readout, domain deletion mutagenesis, localization experiments, all orthogonal methods in one study\",\n      \"pmids\": [\"22021240\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"SPM1 forms part of a protein complex coating the cortical microtubules that includes TrxL1 and TrxL2. SPM1 recruits TrxL1 to the cortical microtubules; TrxL1 does not bind microtubules directly but associates with the complex via SPM1.\",\n      \"method\": \"Co-immunoprecipitation, fluorescence localization\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — Co-IP demonstrating SPM1–TrxL1 interaction and recruitment, single lab but supported by localization experiments\",\n      \"pmids\": [\"23873863\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Cryo-EM ex vivo structure of cortical microtubules from Toxoplasma gondii identifies SPM1 (along with TrxL1 and TrxL2) as a bona fide microtubule inner protein (MIP). These three MIPs form a mesh on the luminal surface and simultaneously stabilize the tubulin lattice in both longitudinal and lateral directions. Deletion of SPM1 (along with other identified MIPs) compromises MT stability and integrity under chemical challenge.\",\n      \"method\": \"Single-particle cryo-EM (ex vivo structure determination), gene deletion with chemical treatment assay\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — cryo-EM structure with functional validation by gene deletion, multiple orthogonal methods in one study\",\n      \"pmids\": [\"34031406\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"The protein phosphatase PPKL regulates the phosphorylation state of SPM1; depletion of PPKL results in a significant increase in SPM1 phosphorylation, correlating with defects in cortical microtubule rigidity and arrangement. This places PPKL upstream of SPM1 in a signaling pathway governing cortical microtubule organization.\",\n      \"method\": \"Conditional knockdown of PPKL, global phosphoproteomics\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — phosphoproteomics correlation from a preprint; the link between increased SPM1 phosphorylation and the microtubule phenotype is inferred, not directly demonstrated by SPM1 phosphosite mutagenesis\",\n      \"pmids\": [\"37398039\"],\n      \"is_preprint\": true,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"The deubiquitinase TgJosephin deubiquitinates SPM1; loss of TgJosephin leads to increased ubiquitination of SPM1. Mutation of the ubiquitination sites on SPM1 restores virulence in the absence of TgJosephin, establishing that SPM1 ubiquitination status is functionally important for parasite anti-IFN-γ virulence.\",\n      \"method\": \"Deubiquitinase gene deletion, ubiquitination site mutagenesis of SPM1, mouse virulence assay with IFNγR-knockout mice\",\n      \"journal\": \"mSphere\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — gene deletion combined with site-directed mutagenesis of ubiquitination sites and in vivo rescue experiment, single lab\",\n      \"pmids\": [\"41972766\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"SPM1 is a microtubule inner protein (MIP) that localizes along the full length of Toxoplasma gondii subpellicular cortical microtubules (but not conoid or spindle MTs), where it stabilizes the tubulin lattice in both longitudinal and lateral directions via a luminal mesh formed with TrxL1 and TrxL2; SPM1 recruits TrxL1 to the cortex, requires four or more of its 32-amino-acid repeats for microtubule association, is phospho-regulated by the phosphatase PPKL, and is deubiquitinated by TgJosephin—with its ubiquitination state influencing parasite anti-IFN-γ virulence.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SPM1 is a microtubule inner protein (MIP) of Toxoplasma gondii that stabilizes the subpellicular cortical microtubule array [#0, #2]. It localizes along the full length of the subpellicular microtubules but is excluded from conoid and spindle microtubules, and its association with microtubules requires four or more copies of its 32-amino-acid repeat [#0]. Cryo-EM of ex vivo cortical microtubules places SPM1 on the luminal surface, where together with TrxL1 and TrxL2 it forms a mesh that stabilizes the tubulin lattice in both longitudinal and lateral directions; loss of SPM1 abolishes microtubule resistance to detergent and chemical challenge and reduces parasite fitness [#0, #2]. Within this complex SPM1 acts as the scaffold that recruits TrxL1, which does not bind microtubules directly [#1]. SPM1 is subject to post-translational control: it is deubiquitinated by TgJosephin, and its ubiquitination state governs parasite anti-IFN-\\u03b3 virulence, as mutating the SPM1 ubiquitination sites restores virulence in TgJosephin-deficient parasites [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2011,\n      \"claim\": \"Established SPM1 as a dedicated stabilizer of the subpellicular cortical microtubules and defined the repeat requirement for its microtubule association, distinguishing it from conoid and spindle microtubule factors.\",\n      \"evidence\": \"Gene deletion with detergent extraction phenotype, domain-deletion mutagenesis and fluorescence localization in Toxoplasma gondii\",\n      \"pmids\": [\"22021240\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular basis of lattice stabilization not resolved at the structural level\", \"How the 32-aa repeats engage tubulin not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Placed SPM1 within a cortical microtubule-coating complex and identified it as the scaffold that recruits TrxL1, which cannot bind microtubules on its own.\",\n      \"evidence\": \"Co-immunoprecipitation and fluorescence localization in Toxoplasma gondii\",\n      \"pmids\": [\"23873863\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Interaction shown by Co-IP without structural mapping of the binding interface\", \"Stoichiometry of the complex not determined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Defined SPM1 structurally as a bona fide microtubule inner protein that, with TrxL1 and TrxL2, forms a luminal mesh stabilizing the tubulin lattice both longitudinally and laterally.\",\n      \"evidence\": \"Single-particle cryo-EM of ex vivo cortical microtubules plus gene deletion with chemical challenge in Toxoplasma gondii\",\n      \"pmids\": [\"34031406\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Individual contribution of SPM1 versus the other MIPs to lattice stability not separated\", \"In-cell assembly order of the mesh unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Proposed phospho-regulation of SPM1 by the phosphatase PPKL as an input controlling cortical microtubule rigidity and arrangement.\",\n      \"evidence\": \"Conditional PPKL knockdown with global phosphoproteomics (preprint) in Toxoplasma gondii\",\n      \"pmids\": [\"37398039\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Correlative phosphoproteomics; not confirmed by SPM1 phosphosite mutagenesis\", \"Whether SPM1 phosphorylation causally drives the microtubule phenotype is inferred, not demonstrated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Established a ubiquitination-based regulatory axis on SPM1, showing that TgJosephin-mediated deubiquitination and SPM1 ubiquitination status control parasite anti-IFN-\\u03b3 virulence.\",\n      \"evidence\": \"TgJosephin gene deletion, SPM1 ubiquitination-site mutagenesis and mouse virulence assays in IFN\\u03b3R-knockout mice\",\n      \"pmids\": [\"41972766\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism linking SPM1 ubiquitination to virulence not defined\", \"Whether ubiquitination alters SPM1 microtubule association or stability not shown\", \"Single lab\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How the distinct post-translational inputs (phosphorylation by PPKL, ubiquitination reversed by TgJosephin) integrate to tune SPM1's microtubule-stabilizing function and its role in virulence remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No direct link established between phospho- and ubiquitin-regulation of SPM1\", \"Mechanistic coupling of lattice stabilization to virulence not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008017\", \"supporting_discovery_ids\": [0, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0035371\", \"supporting_discovery_ids\": [0, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005874\", \"supporting_discovery_ids\": [0, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0005881\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0007017\", \"supporting_discovery_ids\": [0, 2, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\n      \"Luminal cortical microtubule MIP mesh (SPM1\\u2013TrxL1\\u2013TrxL2)\"\n    ],\n    \"partners\": [\n      \"TrxL1 (recruited by SPM1)\",\n      \"TrxL2\",\n      \"PPKL (phosphatase regulating SPM1)\",\n      \"TgJosephin (deubiquitinase acting on SPM1)\"\n    ],\n    \"other_free_text\": [\n      \"Requires four or more of its 32-amino-acid repeats for microtubule association\",\n      \"SPM1 ubiquitination status modulates parasite anti-IFN-\\u03b3 virulence\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_263520","name":"SPM1","product":"microtubule associated protein SPM1","uniprot_acc":"S8F1Y1","chromosome":"TGME49_chrVIIb","start_pos":498372},{"strain":"GT1","gene_id":"TGGT1_263520","name":null,"product":"microtubule associated protein SPM1","uniprot_acc":null,"chromosome":"TGGT1_chrVIIb","start_pos":473105},{"strain":"RH88","gene_id":"TGRH88_067480","name":null,"product":"microtubule associated protein SPM1","uniprot_acc":null,"chromosome":"CM023089","start_pos":511317},{"strain":"VEG","gene_id":"TGVEG_263520","name":null,"product":"microtubule associated protein SPM1","uniprot_acc":"B9QNW9","chromosome":"TGVEG_chrVIIb","start_pos":503875}]}