{"gene":"PF3D7_1476100","run_date":"2026-09-08T15:24:04","timeline":{"discoveries":[{"year":2003,"finding":"ETRAMP14.2 (PF3D7_1476100) is a member of the ETRAMP family of highly cationic membrane proteins in P. falciparum; family members including ETRAMP14.2 associate with membrane fractions and localize to the parasitophorous vacuole membrane (PVM), as demonstrated by colocalization, selective permeabilization studies, and immunoelectron microscopy. Some ETRAMPs define separate PVM domains distinct from the negatively charged EXP-1, suggesting functionally distinct microdomains.","method":"Western blot membrane fractionation, immunofluorescence with selective permeabilization, immunoelectron microscopy, Northern and Western analysis for stage-specific expression","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (fractionation, IFA, IEM) in a single lab; family-level characterization with ETRAMP14.2 as one of 13 members, so findings are inferred for this specific member","pmids":["12686607"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2006,"finding":"ETRAMP family members (including PF3D7_1476100 as part of the characterized set) form oligomeric arrays at the parasite-host cell interface, as shown by in vivo cross-linking; each ETRAMP member defines a separate array distinct from EXP-1, indicating non-random protein distribution. Three recombinant ETRAMPs oligomerized in bacterial membranes independently of other Plasmodium proteins, confirming intrinsic oligomerization capacity.","method":"In vivo cross-linking, recombinant protein oligomerization in bacterial membranes","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — two orthogonal methods (in vivo cross-linking and bacterial reconstitution) in a single lab; applies to the ETRAMP family collectively with ETRAMP14.2 as one member","pmids":["16420351"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2026,"finding":"mRNAs of the ETRAMP family (including those from the PF3D7_1476100 locus) are exported from P. falciparum-infected red blood cells, evade cytoplasmic degradation in host immune cells, and are imported into host cell nuclei where they bind the host RNA-binding proteins ACIN1 and PNN — components of the exon junction complex/splicing machinery — thereby disrupting host splicing regulation and altering immune signaling.","method":"Nuclear fractionation, RNA immunoprecipitation identifying ACIN1 and PNN as binding partners, transcriptomic splicing analysis, functional immune assays","journal":"Cell reports","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — multiple orthogonal methods (nuclear fractionation, RIP, splicing analysis) in a single lab; the finding applies to the ETRAMP mRNA family collectively and ETRAMP14.2 is one member; single study, no independent replication yet","pmids":["41689806"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"ETRAMP14.2 (PF3D7_1476100) is a highly cationic, single-transmembrane P. falciparum protein that localizes to the parasitophorous vacuole membrane where it forms oligomeric arrays defining distinct microdomains; its mRNA is exported from infected erythrocytes and imported into host immune cell nuclei, where it binds splicing-complex proteins ACIN1 and PNN to disrupt host splicing and immune signaling."},"narrative":{"mechanistic_narrative":"ETRAMP14.2 (PF3D7_1476100) is a member of the ETRAMP family of highly cationic membrane proteins in Plasmodium falciparum that localize to the parasitophorous vacuole membrane (PVM) at the parasite–host cell interface [PMID:12686607]. Family characterization, in which ETRAMP14.2 is one member, indicates that individual ETRAMPs form oligomeric arrays defining separate PVM microdomains distinct from those of EXP-1, with recombinant family members oligomerizing intrinsically in bacterial membranes independently of other parasite proteins [PMID:12686607, PMID:16420351]. mRNAs from the ETRAMP family, including transcripts from the PF3D7_1476100 locus, are exported from infected erythrocytes and imported into host immune cell nuclei, where they bind the host splicing-machinery proteins ACIN1 and PNN and disrupt host splicing and immune signaling [PMID:41689806]. Beyond membership in the family-level findings [PMID:12686607, PMID:16420351, PMID:41689806], no mechanistic property specific to ETRAMP14.2 alone has been resolved in the available corpus.","teleology":[{"year":2003,"claim":"Establishing where the ETRAMP family, including ETRAMP14.2, resides answered whether these cationic proteins act at the parasite–host boundary, placing them at the PVM in functionally distinct domains.","evidence":"membrane fractionation, immunofluorescence with selective permeabilization, and immunoelectron microscopy in P. falciparum","pmids":["12686607"],"confidence":"Medium","gaps":["Localization was characterized at the family level; the specific PVM domain occupied by ETRAMP14.2 alone is not resolved","No functional consequence of PVM localization tested for ETRAMP14.2 specifically","Topology and orientation of the single transmembrane segment not directly mapped for this member"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2006,"claim":"Whether ETRAMPs are monomeric or assemble into higher-order structures was addressed by showing they form oligomeric arrays and self-oligomerize intrinsically, defining how they organize into non-random microdomains.","evidence":"in vivo cross-linking and recombinant oligomerization in bacterial membranes","pmids":["16420351"],"confidence":"Medium","gaps":["Oligomerization shown for the family and for three recombinant ETRAMPs; direct demonstration of ETRAMP14.2 self-assembly not isolated","Stoichiometry and structure of the arrays unknown","Functional role of oligomerization for the parasite not established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2026,"claim":"The question of whether ETRAMP transcripts act beyond the parasite was addressed by showing family mRNAs, including from the PF3D7_1476100 locus, enter host immune cell nuclei and bind splicing regulators ACIN1 and PNN, revealing an mRNA-based host-manipulation route.","evidence":"nuclear fractionation, RNA immunoprecipitation identifying ACIN1/PNN, transcriptomic splicing analysis, and immune assays in P. falciparum-infected cells","pmids":["41689806"],"confidence":"Medium","gaps":["Single study without independent replication; finding applies to the ETRAMP mRNA family, so the contribution of the PF3D7_1476100 transcript specifically is not isolated","Mechanism of mRNA export and nuclear import not defined","Causal link between ACIN1/PNN binding and altered immune signaling not fully dissected"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"What ETRAMP14.2 does uniquely — as opposed to as one member of a collectively characterized family — remains unresolved, including its individual PVM function, essentiality, and whether its own transcript drives host splicing disruption.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No loss-of-function or knockout phenotype reported for ETRAMP14.2 specifically","No member-specific interaction partners at the protein level identified","Contribution of the PF3D7_1476100 transcript to host nuclear effects not separated from other family members"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["ETRAMP oligomeric arrays at the parasitophorous vacuole membrane"],"partners":["ACIN1 (HOST, MRNA-BINDING)","PNN (HOST, MRNA-BINDING)"],"other_free_text":["Highly cationic single-transmembrane protein; one of ~13 ETRAMP family members, with findings characterized largely at the family level rather than for PF3D7_1476100 individually.","Defines PVM microdomains distinct from EXP-1.","Family mRNAs are exported from infected erythrocytes and imported into host immune cell nuclei, evading cytoplasmic degradation."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"12686607","id":"PMC_12686607","title":"etramps, a new Plasmodium falciparum gene family coding for developmentally regulated and highly charged membrane proteins located at the parasite-host cell interface.","date":"2003","source":"Molecular biology of the cell","url":"https://pubmed.ncbi.nlm.nih.gov/12686607","citation_count":141,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"16420351","id":"PMC_16420351","title":"Organization of ETRAMPs and EXP-1 at the parasite-host cell interface of malaria parasites.","date":"2006","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/16420351","citation_count":64,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"12615320","id":"PMC_12615320","title":"A gene-family encoding small exported proteins is conserved across Plasmodium genus.","date":"2003","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/12615320","citation_count":32,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26149860","id":"PMC_26149860","title":"Genome-Scale Protein Microarray Comparison of Human Antibody Responses in Plasmodium vivax Relapse and Reinfection.","date":"2015","source":"The American journal of tropical medicine and hygiene","url":"https://pubmed.ncbi.nlm.nih.gov/26149860","citation_count":28,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"21819513","id":"PMC_21819513","title":"A systematic analysis of the early transcribed membrane protein family throughout the life cycle of Plasmodium yoelii.","date":"2011","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/21819513","citation_count":27,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26954579","id":"PMC_26954579","title":"Plasmodium vivax Tryptophan Rich Antigen PvTRAg36.6 Interacts with PvETRAMP and PvTRAg56.6 Interacts with PvMSP7 during Erythrocytic Stages of the Parasite.","date":"2016","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/26954579","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26011536","id":"PMC_26011536","title":"Characterization of Plasmodium vivax Early Transcribed Membrane Protein 11.2 and Exported Protein 1.","date":"2015","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/26011536","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"31856917","id":"PMC_31856917","title":"Evaluation of antibody responses to the early transcribed membrane protein family in Plasmodium vivax.","date":"2019","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/31856917","citation_count":5,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"29307698","id":"PMC_29307698","title":"Sequence and functional divergence of gametocyte-specific parasitophorous vacuole membrane proteins in Plasmodium parasites.","date":"2018","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/29307698","citation_count":5,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37461081","id":"PMC_37461081","title":"Reduced polymorphism of Plasmodium vivax early transcribed membrane protein (PvETRAMP) 11.2.","date":"2023","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/37461081","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37277106","id":"PMC_37277106","title":"Spatial Clustering and Risk Factors for Malaria Infections and Marker of Recent Exposure to Plasmodium falciparum from a Household Survey in Artibonite, Haiti.","date":"2023","source":"The American journal of tropical medicine and hygiene","url":"https://pubmed.ncbi.nlm.nih.gov/37277106","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34715088","id":"PMC_34715088","title":"Plasmodium early transcribed membrane proteins appear tailored to the host range of malaria parasites.","date":"2021","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/34715088","citation_count":1,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"41689806","id":"PMC_41689806","title":"Nuclear import of malaria RNA rewires splicing in host immune cells.","date":"2026","source":"Cell reports","url":"https://pubmed.ncbi.nlm.nih.gov/41689806","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["early transcribed membrane protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":9626,"output_tokens":1070,"usd":0.022464,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5897,"output_tokens":2162,"usd":0.041767,"stage2_stop_reason":"end_turn"},"total_usd":0.064231,"stage1_batch_id":"msgbatch_01S4WrhSkksYHeZXxqf3za3o","stage2_batch_id":"msgbatch_019VBBeuW6G52X8gZfsFDfb5","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2003,\n      \"finding\": \"ETRAMP14.2 (PF3D7_1476100) is a member of the ETRAMP family of highly cationic membrane proteins in P. falciparum; family members including ETRAMP14.2 associate with membrane fractions and localize to the parasitophorous vacuole membrane (PVM), as demonstrated by colocalization, selective permeabilization studies, and immunoelectron microscopy. Some ETRAMPs define separate PVM domains distinct from the negatively charged EXP-1, suggesting functionally distinct microdomains.\",\n      \"method\": \"Western blot membrane fractionation, immunofluorescence with selective permeabilization, immunoelectron microscopy, Northern and Western analysis for stage-specific expression\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (fractionation, IFA, IEM) in a single lab; family-level characterization with ETRAMP14.2 as one of 13 members, so findings are inferred for this specific member\",\n      \"pmids\": [\"12686607\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"ETRAMP family members (including PF3D7_1476100 as part of the characterized set) form oligomeric arrays at the parasite-host cell interface, as shown by in vivo cross-linking; each ETRAMP member defines a separate array distinct from EXP-1, indicating non-random protein distribution. Three recombinant ETRAMPs oligomerized in bacterial membranes independently of other Plasmodium proteins, confirming intrinsic oligomerization capacity.\",\n      \"method\": \"In vivo cross-linking, recombinant protein oligomerization in bacterial membranes\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — two orthogonal methods (in vivo cross-linking and bacterial reconstitution) in a single lab; applies to the ETRAMP family collectively with ETRAMP14.2 as one member\",\n      \"pmids\": [\"16420351\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"mRNAs of the ETRAMP family (including those from the PF3D7_1476100 locus) are exported from P. falciparum-infected red blood cells, evade cytoplasmic degradation in host immune cells, and are imported into host cell nuclei where they bind the host RNA-binding proteins ACIN1 and PNN — components of the exon junction complex/splicing machinery — thereby disrupting host splicing regulation and altering immune signaling.\",\n      \"method\": \"Nuclear fractionation, RNA immunoprecipitation identifying ACIN1 and PNN as binding partners, transcriptomic splicing analysis, functional immune assays\",\n      \"journal\": \"Cell reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — multiple orthogonal methods (nuclear fractionation, RIP, splicing analysis) in a single lab; the finding applies to the ETRAMP mRNA family collectively and ETRAMP14.2 is one member; single study, no independent replication yet\",\n      \"pmids\": [\"41689806\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"ETRAMP14.2 (PF3D7_1476100) is a highly cationic, single-transmembrane P. falciparum protein that localizes to the parasitophorous vacuole membrane where it forms oligomeric arrays defining distinct microdomains; its mRNA is exported from infected erythrocytes and imported into host immune cell nuclei, where it binds splicing-complex proteins ACIN1 and PNN to disrupt host splicing and immune signaling.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ETRAMP14.2 (PF3D7_1476100) is a member of the ETRAMP family of highly cationic membrane proteins in Plasmodium falciparum that localize to the parasitophorous vacuole membrane (PVM) at the parasite–host cell interface [#0]. Family characterization, in which ETRAMP14.2 is one member, indicates that individual ETRAMPs form oligomeric arrays defining separate PVM microdomains distinct from those of EXP-1, with recombinant family members oligomerizing intrinsically in bacterial membranes independently of other parasite proteins [#0, #1]. mRNAs from the ETRAMP family, including transcripts from the PF3D7_1476100 locus, are exported from infected erythrocytes and imported into host immune cell nuclei, where they bind the host splicing-machinery proteins ACIN1 and PNN and disrupt host splicing and immune signaling [#2]. Beyond membership in the family-level findings [#0, #1, #2], no mechanistic property specific to ETRAMP14.2 alone has been resolved in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2003,\n      \"claim\": \"Establishing where the ETRAMP family, including ETRAMP14.2, resides answered whether these cationic proteins act at the parasite–host boundary, placing them at the PVM in functionally distinct domains.\",\n      \"evidence\": \"membrane fractionation, immunofluorescence with selective permeabilization, and immunoelectron microscopy in P. falciparum\",\n      \"pmids\": [\"12686607\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Localization was characterized at the family level; the specific PVM domain occupied by ETRAMP14.2 alone is not resolved\",\n        \"No functional consequence of PVM localization tested for ETRAMP14.2 specifically\",\n        \"Topology and orientation of the single transmembrane segment not directly mapped for this member\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"Whether ETRAMPs are monomeric or assemble into higher-order structures was addressed by showing they form oligomeric arrays and self-oligomerize intrinsically, defining how they organize into non-random microdomains.\",\n      \"evidence\": \"in vivo cross-linking and recombinant oligomerization in bacterial membranes\",\n      \"pmids\": [\"16420351\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Oligomerization shown for the family and for three recombinant ETRAMPs; direct demonstration of ETRAMP14.2 self-assembly not isolated\",\n        \"Stoichiometry and structure of the arrays unknown\",\n        \"Functional role of oligomerization for the parasite not established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"The question of whether ETRAMP transcripts act beyond the parasite was addressed by showing family mRNAs, including from the PF3D7_1476100 locus, enter host immune cell nuclei and bind splicing regulators ACIN1 and PNN, revealing an mRNA-based host-manipulation route.\",\n      \"evidence\": \"nuclear fractionation, RNA immunoprecipitation identifying ACIN1/PNN, transcriptomic splicing analysis, and immune assays in P. falciparum-infected cells\",\n      \"pmids\": [\"41689806\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single study without independent replication; finding applies to the ETRAMP mRNA family, so the contribution of the PF3D7_1476100 transcript specifically is not isolated\",\n        \"Mechanism of mRNA export and nuclear import not defined\",\n        \"Causal link between ACIN1/PNN binding and altered immune signaling not fully dissected\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"What ETRAMP14.2 does uniquely — as opposed to as one member of a collectively characterized family — remains unresolved, including its individual PVM function, essentiality, and whether its own transcript drives host splicing disruption.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No loss-of-function or knockout phenotype reported for ETRAMP14.2 specifically\",\n        \"No member-specific interaction partners at the protein level identified\",\n        \"Contribution of the PF3D7_1476100 transcript to host nuclear effects not separated from other family members\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0042803\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0003729\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020005\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0016021\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0052572\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\n      \"ETRAMP oligomeric arrays at the parasitophorous vacuole membrane\"\n    ],\n    \"partners\": [\n      \"ACIN1 (host, mRNA-binding)\",\n      \"PNN (host, mRNA-binding)\"\n    ],\n    \"other_free_text\": [\n      \"Highly cationic single-transmembrane protein; one of ~13 ETRAMP family members, with findings characterized largely at the family level rather than for PF3D7_1476100 individually.\",\n      \"Defines PVM microdomains distinct from EXP-1.\",\n      \"Family mRNAs are exported from infected erythrocytes and imported into host immune cell nuclei, evading cytoplasmic degradation.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1476100","name":null,"product":"early transcribed membrane protein 14.2","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1246400","name":null,"product":"early transcribed membrane protein","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}