{"gene":"PF3D7_0512300","run_date":"2026-09-07T10:55:52","timeline":{"discoveries":[{"year":2006,"finding":"PfMAT1 (PF3D7_0512300) was identified as an effector protein that stimulates Pfmrk kinase activity in a cyclin-dependent manner; addition of PfMAT1 stimulated RNA polymerase II CTD phosphorylation but had no effect on the inability of Pfmrk to phosphorylate PfPK5, suggesting Pfmrk functions as a CTD kinase rather than a CAK in this context.","method":"In vitro kinase assay with recombinant proteins; substrate phosphorylation assays (RNA Pol II CTD, PfPK5)","journal":"Molecular and biochemical parasitology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — in vitro kinase reconstitution with multiple substrates tested, active-site mutagenesis performed, replicated in follow-up study (PMID:20332005)","pmids":["16737745"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"Co-immunoprecipitation demonstrated physical interaction between PfMAT1 (PF3D7_0512300) and Pfmrk, and mapped the C-terminal domain of PfMAT1 as the Pfmrk activator domain.","method":"Co-immunoprecipitation; domain-mapping experiments","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP with domain mapping, single lab, confirmed prior interaction data","pmids":["20332005"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"Immunofluorescence using GFP- and RFP-tagged versions of Pfmrk and PfMAT1 (PF3D7_0512300), respectively, demonstrated co-localization of the two proteins to the parasite nucleus.","method":"Immunofluorescence microscopy with GFP/RFP-tagged proteins","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct fluorescence localization experiment, single lab, two orthogonal tags used","pmids":["20332005"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"PfMAT1 (PF3D7_0512300) confers substrate specificity to the Pfmrk kinase complex; in the presence of PfMAT1, Pfmrk phosphorylates DNA replication proteins PfRFC-5 and PfMCM6 (identified as Pfmrk interactors via bacterial two-hybrid screen).","method":"Bacterial two-hybrid screen of P. falciparum cDNA library; in vitro kinase phosphorylation assays","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 1 / Moderate — in vitro phosphorylation assay demonstrating substrate specificity conferred by PfMAT1, single lab","pmids":["20332005"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"Co-immunoprecipitation of PfCyc1 from P. falciparum parasites identified PfMAT1 (PF3D7_0512300) and PfMRK as specific interaction partners, establishing a conserved PfCyc1/PfMAT1/PfMRK trimeric complex in the parasite.","method":"Co-immunoprecipitation from parasite lysate followed by mass spectrometry/western blot","journal":"mBio","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP from native parasite extract, single lab, confirmed trimeric complex membership","pmids":["28611247"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PfMAT1 (PF3D7_0512300) is a nuclear-localized effector protein that forms a trimeric complex with Pfmrk (a CDK7 homolog) and PfCyc1 (a cyclin H homolog); its C-terminal domain directly activates Pfmrk kinase activity in a cyclin-dependent manner, stimulates RNA Pol II CTD phosphorylation, and confers substrate specificity toward DNA replication proteins PfRFC-5 and PfMCM6, suggesting roles in both transcriptional regulation and DNA replication in P. falciparum."},"narrative":{"mechanistic_narrative":"MAT1 (PF3D7_0512300) is a nuclear effector subunit of a trimeric CDK-activating kinase-like complex in Plasmodium falciparum, assembling with the CDK7 homolog Pfmrk and the cyclin H homolog PfCyc1 [PMID:16737745, PMID:28611247]. Its C-terminal domain physically engages Pfmrk and functions as the kinase-activator domain, stimulating Pfmrk activity in a cyclin-dependent manner [PMID:16737745, PMID:20332005]. Functionally, MAT1 both promotes RNA polymerase II CTD phosphorylation and redirects Pfmrk substrate specificity, enabling phosphorylation of the DNA replication proteins PfRFC-5 and PfMCM6, thereby linking the complex to transcriptional regulation and DNA replication [PMID:16737745, PMID:20332005]. Notably, MAT1-activated Pfmrk phosphorylates the CTD but not PfPK5, indicating the complex acts as a CTD kinase rather than a canonical CAK in this context [PMID:16737745]. MAT1 and Pfmrk co-localize to the parasite nucleus [PMID:20332005]. Beyond its role within this complex, no genetic loss-of-function phenotype or structural characterization of MAT1 itself has been reported in the available corpus.","teleology":[{"year":2006,"claim":"Establishing whether Pfmrk required an accessory activator resolved how this Plasmodium CDK7 homolog is switched on; MAT1 was shown to be the effector that stimulates Pfmrk kinase activity toward the RNA Pol II CTD.","evidence":"In vitro kinase assays with recombinant proteins testing RNA Pol II CTD and PfPK5 as substrates","pmids":["16737745"],"confidence":"High","gaps":["Did not map the region of MAT1 responsible for activation","Physiological substrates in the parasite not defined","No structural basis for activation"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"Defining the physical basis of activation and the subcellular context showed that MAT1 directly binds Pfmrk through its C-terminal domain and that the two proteins co-localize in the nucleus, consistent with an in vivo assembly.","evidence":"Reciprocal co-immunoprecipitation with domain mapping and immunofluorescence of GFP/RFP-tagged proteins","pmids":["20332005"],"confidence":"Medium","gaps":["Single-lab interaction data without structural detail","Timing of complex assembly across the cell cycle unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"Determining whether MAT1 does more than activate kinase output revealed that it confers substrate specificity, directing Pfmrk to phosphorylate the DNA replication factors PfRFC-5 and PfMCM6.","evidence":"Bacterial two-hybrid screen of a P. falciparum cDNA library and in vitro phosphorylation assays","pmids":["20332005"],"confidence":"Medium","gaps":["In vitro phosphorylation not validated as an in vivo regulatory event","Functional consequence for replication timing not tested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"Confirming the native complex composition, pulldown of the cyclin subunit demonstrated that MAT1, Pfmrk, and PfCyc1 form a trimeric complex in the parasite rather than only in reconstituted systems.","evidence":"Co-immunoprecipitation of PfCyc1 from parasite lysate with mass spectrometry/western detection","pmids":["28611247"],"confidence":"Medium","gaps":["Stoichiometry and structure of the trimeric complex not resolved","Regulation of complex formation across the life cycle unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The essentiality and in vivo function of MAT1 itself — through genetic disruption and separation of its transcriptional versus replication-linked roles — remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No loss-of-function/knockout phenotype for MAT1 reported","No structure of MAT1 or the trimeric complex","In vivo relevance of PfRFC-5/PfMCM6 phosphorylation not established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["PfCyc1/PfMAT1/PfMRK (Pfmrk) trimeric CDK-activating kinase-like complex"],"partners":["PFMRK (CDK7 HOMOLOG)","PFCYC1 (CYCLIN H HOMOLOG)","PFRFC-5 (SUBSTRATE)","PFMCM6 (SUBSTRATE)"],"other_free_text":["C-terminal domain of MAT1 serves as the Pfmrk-activator domain [#1]","MAT1-activated Pfmrk phosphorylates RNA Pol II CTD but not PfPK5, indicating CTD-kinase rather than CAK activity in this context [#0]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"16737745","id":"PMC_16737745","title":"Identification of an effector protein and gain-of-function mutants that activate Pfmrk, a malarial cyclin-dependent protein kinase.","date":"2006","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/16737745","citation_count":29,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["MAT1","CDK","PfMAT1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28611247","id":"PMC_28611247","title":"The Malaria Parasite Cyclin H Homolog PfCyc1 Is Required for Efficient Cytokinesis in Blood-Stage Plasmodium falciparum.","date":"2017","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/28611247","citation_count":28,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["MAT1","PfMAT1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"20332005","id":"PMC_20332005","title":"The malarial CDK Pfmrk and its effector PfMAT1 phosphorylate DNA replication proteins and co-localize in the nucleus.","date":"2010","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/20332005","citation_count":25,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CDK","PfMAT1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26780367","id":"PMC_26780367","title":"Regulation of DNA replication proteins in parasitic protozoans: possible role of CDK-like kinases.","date":"2016","source":"Current genetics","url":"https://pubmed.ncbi.nlm.nih.gov/26780367","citation_count":9,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CDK"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19519480","id":"PMC_19519480","title":"Evolutionary divergence of Plasmodium falciparum: sequences, protein-protein interactions, pathways and processes.","date":"2009","source":"Infectious disorders drug targets","url":"https://pubmed.ncbi.nlm.nih.gov/19519480","citation_count":8,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CDK"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23484876","id":"PMC_23484876","title":"In silico three-dimensional pharmacophores for aiding the discovery of the Pfmrk (Plasmodium cyclin-dependent protein kinases) specific inhibitors for the therapeutic treatment of malaria.","date":"2007","source":"Expert opinion on drug discovery","url":"https://pubmed.ncbi.nlm.nih.gov/23484876","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CDK"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"14604516","id":"PMC_14604516","title":"Can mosquitoes be bitten? A new hope for anti-malarial drug design.","date":"2003","source":"Structure (London, England : 1993)","url":"https://pubmed.ncbi.nlm.nih.gov/14604516","citation_count":2,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CDK"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23998890","id":"PMC_23998890","title":"In silico characterization and molecular dynamics simulation of Pfcyc-1, a cyclin homolog of Plasmodium falciparum.","date":"2013","source":"Journal of biomolecular structure & dynamics","url":"https://pubmed.ncbi.nlm.nih.gov/23998890","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CDK"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6311,"output_tokens":1380,"usd":0.019817,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6308,"output_tokens":2239,"usd":0.043757,"stage2_stop_reason":"end_turn"},"total_usd":0.063574,"stage1_batch_id":"msgbatch_01DbiymDmubkPpYvdbAu5a7V","stage2_batch_id":"msgbatch_012TbrWvMRH129T7PQ4SmvrJ","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2006,\n      \"finding\": \"PfMAT1 (PF3D7_0512300) was identified as an effector protein that stimulates Pfmrk kinase activity in a cyclin-dependent manner; addition of PfMAT1 stimulated RNA polymerase II CTD phosphorylation but had no effect on the inability of Pfmrk to phosphorylate PfPK5, suggesting Pfmrk functions as a CTD kinase rather than a CAK in this context.\",\n      \"method\": \"In vitro kinase assay with recombinant proteins; substrate phosphorylation assays (RNA Pol II CTD, PfPK5)\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in vitro kinase reconstitution with multiple substrates tested, active-site mutagenesis performed, replicated in follow-up study (PMID:20332005)\",\n      \"pmids\": [\"16737745\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Co-immunoprecipitation demonstrated physical interaction between PfMAT1 (PF3D7_0512300) and Pfmrk, and mapped the C-terminal domain of PfMAT1 as the Pfmrk activator domain.\",\n      \"method\": \"Co-immunoprecipitation; domain-mapping experiments\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP with domain mapping, single lab, confirmed prior interaction data\",\n      \"pmids\": [\"20332005\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Immunofluorescence using GFP- and RFP-tagged versions of Pfmrk and PfMAT1 (PF3D7_0512300), respectively, demonstrated co-localization of the two proteins to the parasite nucleus.\",\n      \"method\": \"Immunofluorescence microscopy with GFP/RFP-tagged proteins\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct fluorescence localization experiment, single lab, two orthogonal tags used\",\n      \"pmids\": [\"20332005\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"PfMAT1 (PF3D7_0512300) confers substrate specificity to the Pfmrk kinase complex; in the presence of PfMAT1, Pfmrk phosphorylates DNA replication proteins PfRFC-5 and PfMCM6 (identified as Pfmrk interactors via bacterial two-hybrid screen).\",\n      \"method\": \"Bacterial two-hybrid screen of P. falciparum cDNA library; in vitro kinase phosphorylation assays\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in vitro phosphorylation assay demonstrating substrate specificity conferred by PfMAT1, single lab\",\n      \"pmids\": [\"20332005\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Co-immunoprecipitation of PfCyc1 from P. falciparum parasites identified PfMAT1 (PF3D7_0512300) and PfMRK as specific interaction partners, establishing a conserved PfCyc1/PfMAT1/PfMRK trimeric complex in the parasite.\",\n      \"method\": \"Co-immunoprecipitation from parasite lysate followed by mass spectrometry/western blot\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP from native parasite extract, single lab, confirmed trimeric complex membership\",\n      \"pmids\": [\"28611247\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PfMAT1 (PF3D7_0512300) is a nuclear-localized effector protein that forms a trimeric complex with Pfmrk (a CDK7 homolog) and PfCyc1 (a cyclin H homolog); its C-terminal domain directly activates Pfmrk kinase activity in a cyclin-dependent manner, stimulates RNA Pol II CTD phosphorylation, and confers substrate specificity toward DNA replication proteins PfRFC-5 and PfMCM6, suggesting roles in both transcriptional regulation and DNA replication in P. falciparum.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MAT1 (PF3D7_0512300) is a nuclear effector subunit of a trimeric CDK-activating kinase-like complex in Plasmodium falciparum, assembling with the CDK7 homolog Pfmrk and the cyclin H homolog PfCyc1 [#0, #4]. Its C-terminal domain physically engages Pfmrk and functions as the kinase-activator domain, stimulating Pfmrk activity in a cyclin-dependent manner [#0, #1]. Functionally, MAT1 both promotes RNA polymerase II CTD phosphorylation and redirects Pfmrk substrate specificity, enabling phosphorylation of the DNA replication proteins PfRFC-5 and PfMCM6, thereby linking the complex to transcriptional regulation and DNA replication [#0, #3]. Notably, MAT1-activated Pfmrk phosphorylates the CTD but not PfPK5, indicating the complex acts as a CTD kinase rather than a canonical CAK in this context [#0]. MAT1 and Pfmrk co-localize to the parasite nucleus [#2]. Beyond its role within this complex, no genetic loss-of-function phenotype or structural characterization of MAT1 itself has been reported in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"Establishing whether Pfmrk required an accessory activator resolved how this Plasmodium CDK7 homolog is switched on; MAT1 was shown to be the effector that stimulates Pfmrk kinase activity toward the RNA Pol II CTD.\",\n      \"evidence\": \"In vitro kinase assays with recombinant proteins testing RNA Pol II CTD and PfPK5 as substrates\",\n      \"pmids\": [\"16737745\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Did not map the region of MAT1 responsible for activation\",\n        \"Physiological substrates in the parasite not defined\",\n        \"No structural basis for activation\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Defining the physical basis of activation and the subcellular context showed that MAT1 directly binds Pfmrk through its C-terminal domain and that the two proteins co-localize in the nucleus, consistent with an in vivo assembly.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation with domain mapping and immunofluorescence of GFP/RFP-tagged proteins\",\n      \"pmids\": [\"20332005\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single-lab interaction data without structural detail\",\n        \"Timing of complex assembly across the cell cycle unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Determining whether MAT1 does more than activate kinase output revealed that it confers substrate specificity, directing Pfmrk to phosphorylate the DNA replication factors PfRFC-5 and PfMCM6.\",\n      \"evidence\": \"Bacterial two-hybrid screen of a P. falciparum cDNA library and in vitro phosphorylation assays\",\n      \"pmids\": [\"20332005\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"In vitro phosphorylation not validated as an in vivo regulatory event\",\n        \"Functional consequence for replication timing not tested\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Confirming the native complex composition, pulldown of the cyclin subunit demonstrated that MAT1, Pfmrk, and PfCyc1 form a trimeric complex in the parasite rather than only in reconstituted systems.\",\n      \"evidence\": \"Co-immunoprecipitation of PfCyc1 from parasite lysate with mass spectrometry/western detection\",\n      \"pmids\": [\"28611247\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Stoichiometry and structure of the trimeric complex not resolved\",\n        \"Regulation of complex formation across the life cycle unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The essentiality and in vivo function of MAT1 itself — through genetic disruption and separation of its transcriptional versus replication-linked roles — remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No loss-of-function/knockout phenotype for MAT1 reported\",\n        \"No structure of MAT1 or the trimeric complex\",\n        \"In vivo relevance of PfRFC-5/PfMCM6 phosphorylation not established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0061575\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0019887\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006366\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0006260\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [\n      \"PfCyc1/PfMAT1/PfMRK (Pfmrk) trimeric CDK-activating kinase-like complex\"\n    ],\n    \"partners\": [\n      \"Pfmrk (CDK7 homolog)\",\n      \"PfCyc1 (cyclin H homolog)\",\n      \"PfRFC-5 (substrate)\",\n      \"PfMCM6 (substrate)\"\n    ],\n    \"other_free_text\": [\n      \"C-terminal domain of MAT1 serves as the Pfmrk-activator domain [#1]\",\n      \"MAT1-activated Pfmrk phosphorylates RNA Pol II CTD but not PfPK5, indicating CTD-kinase rather than CAK activity in this context [#0]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0512300","name":null,"product":"CDK-activating kinase assembly factor MAT1","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1111900","name":null,"product":"CDK-activating kinase assembly factor MAT1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1020900","name":null,"product":"CDK-activating kinase assembly factor MAT1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"MAT1","evaluation":null}