{"gene":"PF3D7_1470900","run_date":"2026-09-08T14:19:07","timeline":{"discoveries":[{"year":2016,"finding":"The P. falciparum proteasome β2 subunit (PF3D7_1470900) has an unusually open active site compared to the human counterpart, as revealed by cryo-EM structure of the Pf20S proteasome bound to a β2-selective inhibitor at 3.6 Å resolution. Substrate profiling showed parasite-specific amino-acid preferences at the β2 active site, enabling design of inhibitors that preferentially inhibit β2.","method":"Cryo-EM single-particle analysis at 3.6 Å; substrate profiling with fluorogenic peptide libraries; in vitro enzymatic inhibition assays with β2-selective inhibitors","journal":"Nature","confidence":"High","confidence_rationale":"Tier 1 / Strong — cryo-EM structure with functional inhibitor bound, combined with substrate profiling and in vitro activity assays in a single rigorous study","pmids":["26863983"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"finding":"Cryo-EM structures of wild-type Pf20S and the resistance mutant Pf20Sβ6A117D show that the tripeptide vinyl sulfone inhibitor WLW-vs binds both the β2 subunit (PF3D7_1470900) and β5 in the β6A117D mutant background. In wild-type Pf20S, TDI-8304 also binds both β2 and β5. These structural data reveal the molecular basis for β2 active-site engagement by these inhibitors.","method":"High-resolution cryo-EM structural determination of Pf20S–inhibitor complexes; resistance selection and mutant characterization","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 / Strong — multiple high-resolution cryo-EM structures with bound inhibitors directly showing β2 subunit engagement, corroborated by resistance mutant data","pmids":["38097652"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"finding":"The cryo-EM structures of the Pf20S proteasome (including the β2-containing catalytic core, PF3D7_1470900) in complex with PfPA28 regulatory cap were solved at 3.9 Å (singly-capped) and 3.8 Å (doubly-capped), revealing that PfPA28 binds Pf20S asymmetrically, engaging subunits on only one side of the core, and undergoes rigid body motions relative to Pf20S.","method":"Single-particle cryo-EM; crystal structure of PfPA28; molecular dynamics simulations; genetic deletion of PA28","journal":"Nature microbiology","confidence":"High","confidence_rationale":"Tier 1 / Strong — cryo-EM structures of the intact complex at near-atomic resolution combined with genetic deletion functional data, all in one study","pmids":["31384003"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"Cryo-EM structures of Pf20S (containing the β2 subunit, PF3D7_1470900) in complex with β5-selective amino-amide boronate inhibitors and bortezomib revealed differences in active-site architecture between Pf20S and human constitutive 20S that explain species selectivity; these structural comparisons provide atomic-level context for the β2-containing core particle.","method":"Cryo-EM structural determination of Pf20S and Hs20Sc with inhibitors; in vitro proteasome activity assays; P. falciparum growth inhibition assays; SCID mouse in vivo model","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — high-quality cryo-EM structural data for the Pf20S core (including β2), but findings primarily characterize the β5 subunit; β2 contribution inferred from structural context in a single study","pmids":["34548400"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1470900 (Pf proteasome β2 subunit) forms part of the catalytic 20S core of the P. falciparum proteasome; cryo-EM structures reveal it harbours an unusually open active site with parasite-specific substrate preferences that can be selectively targeted by β2-preferring inhibitors, and the intact β2-containing 20S core is regulated by asymmetric binding of the PfPA28 cap complex."},"narrative":{"mechanistic_narrative":"PF3D7_1470900 encodes the β2 catalytic subunit of the Plasmodium falciparum 20S proteasome core, contributing one of the proteolytic active sites of the parasite's catalytic core particle [PMID:26863983]. Cryo-EM structure determination of the Pf20S bound to a β2-selective inhibitor, together with fluorogenic substrate profiling, established that the β2 active site is unusually open relative to its human counterpart and displays parasite-specific amino-acid preferences, providing a structural basis for selective pharmacological targeting [PMID:26863983]. Subsequent high-resolution structures of Pf20S–inhibitor complexes showed direct engagement of the β2 subunit by the tripeptide vinyl sulfone WLW-vs and by TDI-8304, which occupy both β2 and β5 active sites, with resistance-mutant (β6 A117D) backgrounds confirming the molecular basis of β2 active-site binding [PMID:38097652]. The β2-containing catalytic core assembles into the intact Pf20S particle that is regulated by asymmetric binding of the PfPA28 cap complex, which engages the core on only one side [PMID:31384003], and structural comparisons of the Pf20S core with the human constitutive 20S define the active-site features underlying species-selective inhibition [PMID:34548400]. Beyond its identity as the β2 catalytic subunit of the Pf20S core, its regulation, and its role as a selective drug target, no further mechanistic detail specific to PF3D7_1470900 has been characterized in the available corpus.","teleology":[{"year":2016,"claim":"It was unknown whether the P. falciparum proteasome β2 active site differed enough from the human enzyme to permit selective targeting; solving the Pf20S structure with a β2-selective inhibitor and profiling its substrate preferences established both a distinct active-site architecture and druggable parasite specificity.","evidence":"Cryo-EM single-particle analysis at 3.6 Å with bound β2-selective inhibitor, fluorogenic peptide substrate profiling, and in vitro inhibition assays in P. falciparum","pmids":["26863983"],"confidence":"High","gaps":["Does not resolve the cellular consequences of selective β2 inhibition in the parasite","Does not define how the β2 subunit is assembled or matured within the core"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"claim":"The regulatory context of the β2-containing catalytic core was unclear; structures of Pf20S bound to the PfPA28 cap revealed that this activator engages the core asymmetrically, defining how the intact particle is regulated.","evidence":"Single-particle cryo-EM of singly- and doubly-capped Pf20S–PfPA28 complexes (3.8–3.9 Å), crystal structure of PfPA28, molecular dynamics, and genetic deletion of PA28 in P. falciparum","pmids":["31384003"],"confidence":"High","gaps":["Does not isolate a β2-specific functional role within the capped complex","Consequences of PA28 binding for β2 catalytic activity not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"It was unclear which active-site features underlie species selectivity of proteasome inhibitors; comparative cryo-EM of Pf20S versus the human constitutive 20S with β5-selective inhibitors provided atomic context for the β2-containing core.","evidence":"Cryo-EM of Pf20S and Hs20Sc with inhibitors, in vitro proteasome activity assays, P. falciparum growth inhibition, and a SCID mouse in vivo model","pmids":["34548400"],"confidence":"Medium","gaps":["β2 contribution inferred from structural context; the study primarily characterizes β5","No direct β2-specific functional readout"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"claim":"The molecular basis for β2 engagement by dual-site inhibitors was undefined; high-resolution structures of wild-type and resistance-mutant Pf20S showed WLW-vs and TDI-8304 binding both β2 and β5, establishing how these inhibitors occupy the β2 active site.","evidence":"High-resolution cryo-EM of Pf20S–inhibitor complexes including the Pf20Sβ6A117D resistance mutant, with resistance selection and mutant characterization in P. falciparum","pmids":["38097652"],"confidence":"High","gaps":["Does not quantify the relative contribution of β2 versus β5 inhibition to parasite killing","Does not address β2-specific resistance liabilities"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The distinct cellular substrates and non-structural functional role of the β2 subunit within parasite protein homeostasis remain undefined.","evidence":"","pmids":[],"confidence":"Low","gaps":["No physiological substrates specific to the β2 active site identified","No genetic characterization of β2 subunit essentiality or assembly requirements","Contribution of β2 catalysis relative to other catalytic subunits in vivo not established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Pf20S proteasome catalytic core particle","Pf20S–PfPA28 regulatory complex"],"partners":["Β5 CATALYTIC SUBUNIT (CO-ENGAGED BY WLW-VS AND TDI-8304 INHIBITORS)","PFPA28 REGULATORY CAP COMPLEX"],"other_free_text":["β2 catalytic subunit has an unusually open active site with parasite-specific substrate preferences relative to the human proteasome [#0]","Directly engaged by β2-selective and dual β2/β5 inhibitors (WLW-vs, TDI-8304), making it a validated antimalarial drug target [#0, #1]","The β2-containing 20S core is regulated by asymmetric PfPA28 cap binding [#2]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"26863983","id":"PMC_26863983","title":"Structure- and function-based design of Plasmodium-selective proteasome inhibitors.","date":"2016","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/26863983","citation_count":196,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"24533266","id":"PMC_24533266","title":"The proteasome of malaria parasites: A multi-stage drug target for chemotherapeutic intervention?","date":"2012","source":"International journal for parasitology. Drugs and drug resistance","url":"https://pubmed.ncbi.nlm.nih.gov/24533266","citation_count":64,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"31384003","id":"PMC_31384003","title":"The structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis.","date":"2019","source":"Nature microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/31384003","citation_count":37,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34548400","id":"PMC_34548400","title":"Design of proteasome inhibitors with oral efficacy in vivo against Plasmodium falciparum and selectivity over the human proteasome.","date":"2021","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/34548400","citation_count":33,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38097652","id":"PMC_38097652","title":"Structures revealing mechanisms of resistance and collateral sensitivity of Plasmodium falciparum to proteasome inhibitors.","date":"2023","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/38097652","citation_count":21,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"39084225","id":"PMC_39084225","title":"Identification of potent and reversible piperidine carboxamides that are species-selective orally active proteasome inhibitors to treat malaria.","date":"2024","source":"Cell chemical biology","url":"https://pubmed.ncbi.nlm.nih.gov/39084225","citation_count":11,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"41148577","id":"PMC_41148577","title":"Optimization of Species-Selective Reversible Proteasome Inhibitors for the Treatment of Malaria.","date":"2025","source":"Journal of medicinal chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/41148577","citation_count":1,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6131,"output_tokens":1349,"usd":0.019314,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6240,"output_tokens":2429,"usd":0.045963,"stage2_stop_reason":"end_turn"},"total_usd":0.065277,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2016,\n      \"finding\": \"The P. falciparum proteasome β2 subunit (PF3D7_1470900) has an unusually open active site compared to the human counterpart, as revealed by cryo-EM structure of the Pf20S proteasome bound to a β2-selective inhibitor at 3.6 Å resolution. Substrate profiling showed parasite-specific amino-acid preferences at the β2 active site, enabling design of inhibitors that preferentially inhibit β2.\",\n      \"method\": \"Cryo-EM single-particle analysis at 3.6 Å; substrate profiling with fluorogenic peptide libraries; in vitro enzymatic inhibition assays with β2-selective inhibitors\",\n      \"journal\": \"Nature\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — cryo-EM structure with functional inhibitor bound, combined with substrate profiling and in vitro activity assays in a single rigorous study\",\n      \"pmids\": [\"26863983\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Cryo-EM structures of wild-type Pf20S and the resistance mutant Pf20Sβ6A117D show that the tripeptide vinyl sulfone inhibitor WLW-vs binds both the β2 subunit (PF3D7_1470900) and β5 in the β6A117D mutant background. In wild-type Pf20S, TDI-8304 also binds both β2 and β5. These structural data reveal the molecular basis for β2 active-site engagement by these inhibitors.\",\n      \"method\": \"High-resolution cryo-EM structural determination of Pf20S–inhibitor complexes; resistance selection and mutant characterization\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — multiple high-resolution cryo-EM structures with bound inhibitors directly showing β2 subunit engagement, corroborated by resistance mutant data\",\n      \"pmids\": [\"38097652\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"The cryo-EM structures of the Pf20S proteasome (including the β2-containing catalytic core, PF3D7_1470900) in complex with PfPA28 regulatory cap were solved at 3.9 Å (singly-capped) and 3.8 Å (doubly-capped), revealing that PfPA28 binds Pf20S asymmetrically, engaging subunits on only one side of the core, and undergoes rigid body motions relative to Pf20S.\",\n      \"method\": \"Single-particle cryo-EM; crystal structure of PfPA28; molecular dynamics simulations; genetic deletion of PA28\",\n      \"journal\": \"Nature microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — cryo-EM structures of the intact complex at near-atomic resolution combined with genetic deletion functional data, all in one study\",\n      \"pmids\": [\"31384003\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Cryo-EM structures of Pf20S (containing the β2 subunit, PF3D7_1470900) in complex with β5-selective amino-amide boronate inhibitors and bortezomib revealed differences in active-site architecture between Pf20S and human constitutive 20S that explain species selectivity; these structural comparisons provide atomic-level context for the β2-containing core particle.\",\n      \"method\": \"Cryo-EM structural determination of Pf20S and Hs20Sc with inhibitors; in vitro proteasome activity assays; P. falciparum growth inhibition assays; SCID mouse in vivo model\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — high-quality cryo-EM structural data for the Pf20S core (including β2), but findings primarily characterize the β5 subunit; β2 contribution inferred from structural context in a single study\",\n      \"pmids\": [\"34548400\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1470900 (Pf proteasome β2 subunit) forms part of the catalytic 20S core of the P. falciparum proteasome; cryo-EM structures reveal it harbours an unusually open active site with parasite-specific substrate preferences that can be selectively targeted by β2-preferring inhibitors, and the intact β2-containing 20S core is regulated by asymmetric binding of the PfPA28 cap complex.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1470900 encodes the β2 catalytic subunit of the Plasmodium falciparum 20S proteasome core, contributing one of the proteolytic active sites of the parasite's catalytic core particle [#0]. Cryo-EM structure determination of the Pf20S bound to a β2-selective inhibitor, together with fluorogenic substrate profiling, established that the β2 active site is unusually open relative to its human counterpart and displays parasite-specific amino-acid preferences, providing a structural basis for selective pharmacological targeting [#0]. Subsequent high-resolution structures of Pf20S–inhibitor complexes showed direct engagement of the β2 subunit by the tripeptide vinyl sulfone WLW-vs and by TDI-8304, which occupy both β2 and β5 active sites, with resistance-mutant (β6 A117D) backgrounds confirming the molecular basis of β2 active-site binding [#1]. The β2-containing catalytic core assembles into the intact Pf20S particle that is regulated by asymmetric binding of the PfPA28 cap complex, which engages the core on only one side [#2], and structural comparisons of the Pf20S core with the human constitutive 20S define the active-site features underlying species-selective inhibition [#3]. Beyond its identity as the β2 catalytic subunit of the Pf20S core, its regulation, and its role as a selective drug target, no further mechanistic detail specific to PF3D7_1470900 has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2016,\n      \"claim\": \"It was unknown whether the P. falciparum proteasome β2 active site differed enough from the human enzyme to permit selective targeting; solving the Pf20S structure with a β2-selective inhibitor and profiling its substrate preferences established both a distinct active-site architecture and druggable parasite specificity.\",\n      \"evidence\": \"Cryo-EM single-particle analysis at 3.6 Å with bound β2-selective inhibitor, fluorogenic peptide substrate profiling, and in vitro inhibition assays in P. falciparum\",\n      \"pmids\": [\"26863983\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Does not resolve the cellular consequences of selective β2 inhibition in the parasite\",\n        \"Does not define how the β2 subunit is assembled or matured within the core\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"The regulatory context of the β2-containing catalytic core was unclear; structures of Pf20S bound to the PfPA28 cap revealed that this activator engages the core asymmetrically, defining how the intact particle is regulated.\",\n      \"evidence\": \"Single-particle cryo-EM of singly- and doubly-capped Pf20S–PfPA28 complexes (3.8–3.9 Å), crystal structure of PfPA28, molecular dynamics, and genetic deletion of PA28 in P. falciparum\",\n      \"pmids\": [\"31384003\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Does not isolate a β2-specific functional role within the capped complex\",\n        \"Consequences of PA28 binding for β2 catalytic activity not defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"It was unclear which active-site features underlie species selectivity of proteasome inhibitors; comparative cryo-EM of Pf20S versus the human constitutive 20S with β5-selective inhibitors provided atomic context for the β2-containing core.\",\n      \"evidence\": \"Cryo-EM of Pf20S and Hs20Sc with inhibitors, in vitro proteasome activity assays, P. falciparum growth inhibition, and a SCID mouse in vivo model\",\n      \"pmids\": [\"34548400\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"β2 contribution inferred from structural context; the study primarily characterizes β5\",\n        \"No direct β2-specific functional readout\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"The molecular basis for β2 engagement by dual-site inhibitors was undefined; high-resolution structures of wild-type and resistance-mutant Pf20S showed WLW-vs and TDI-8304 binding both β2 and β5, establishing how these inhibitors occupy the β2 active site.\",\n      \"evidence\": \"High-resolution cryo-EM of Pf20S–inhibitor complexes including the Pf20Sβ6A117D resistance mutant, with resistance selection and mutant characterization in P. falciparum\",\n      \"pmids\": [\"38097652\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Does not quantify the relative contribution of β2 versus β5 inhibition to parasite killing\",\n        \"Does not address β2-specific resistance liabilities\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The distinct cellular substrates and non-structural functional role of the β2 subunit within parasite protein homeostasis remain undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No physiological substrates specific to the β2 active site identified\",\n        \"No genetic characterization of β2 subunit essentiality or assembly requirements\",\n        \"Contribution of β2 catalysis relative to other catalytic subunits in vivo not established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004298\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0043161\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"complexes\": [\n      \"Pf20S proteasome catalytic core particle\",\n      \"Pf20S–PfPA28 regulatory complex\"\n    ],\n    \"partners\": [\n      \"β5 catalytic subunit (co-engaged by WLW-vs and TDI-8304 inhibitors)\",\n      \"PfPA28 regulatory cap complex\"\n    ],\n    \"other_free_text\": [\n      \"β2 catalytic subunit has an unusually open active site with parasite-specific substrate preferences relative to the human proteasome [#0]\",\n      \"Directly engaged by β2-selective and dual β2/β5 inhibitors (WLW-vs, TDI-8304), making it a validated antimalarial drug target [#0, #1]\",\n      \"The β2-containing 20S core is regulated by asymmetric PfPA28 cap binding [#2]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1470900","name":null,"product":"proteasome subunit beta type-2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1334100","name":null,"product":"proteasome subunit beta type-2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1210100","name":null,"product":"proteasome subunit beta type-2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}