{"gene":"PF3D7_1205800","run_date":"2026-09-08T16:26:55","timeline":{"discoveries":[{"year":2006,"finding":"PF3D7_1205800 (HMGB3) was identified by computational analysis as a large (~2,284 amino acid) P. falciparum HMG box protein containing two HMG box domains and additional putative functional motifs including one Myb domain, distinguishing it structurally from the smaller single-box HMGB1 and HMGB2 paralogs.","method":"Computational sequence analysis / bioinformatics domain prediction","journal":"Eukaryotic cell","confidence":"Low","confidence_rationale":"Tier 4 / Weak — computational prediction only, no direct experimental characterization of HMGB3 protein function performed in this study","pmids":["16607015"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"finding":"HMGB3 (PF3D7_1205800) was co-enriched with the transcription factor AP2-I in DNA pulldown experiments using probes containing de novo regulatory motif 028, alongside bromodomain proteins and an SWIB/MDM2 domain-containing protein, suggesting HMGB3 associates with AP2-I at target gene promoters as part of a chromatin regulatory complex.","method":"DNA affinity pulldown / mass spectrometry (oligo-based protein enrichment with motif-containing probes)","journal":"Cell host & microbe","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single pulldown experiment, single lab, HMGB3 identified as co-enriched factor but no direct functional follow-up on HMGB3 itself","pmids":["29649445"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"finding":"HMGB3 (PF3D7_1205800) was identified as a co-purifying protein in PfEAF2 reciprocal pulldowns, placing it in the context of the PfSWR1 chromatin remodeling complex in P. falciparum.","method":"Reciprocal affinity pulldown / mass spectrometry (PfEAF2 as bait)","journal":"mSphere","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single co-purification experiment identifying HMGB3 as a minor associated factor; no direct functional characterization of HMGB3 itself was performed","pmids":["38564734"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"finding":"HMGB3 (PF3D7_1205800) was identified as an interacting partner of PfHSP70-2 in a yeast two-hybrid screen.","method":"Yeast two-hybrid interaction screen","journal":"Heliyon","confidence":"Low","confidence_rationale":"Tier 3 / Weak — yeast two-hybrid identification only, single method, no functional follow-up on the interaction","pmids":["32529065"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"HMGB3 (PF3D7_1205800) was detected in the proteome of sporozoites across multiple tested Plasmodium species, and is noted as the only HMGB family member that possesses a Myb-binding domain, suggesting a potential role as a transcription factor in the sporozoite stage.","method":"Proteomic detection (mass spectrometry of sporozoite proteomes)","journal":"Frontiers in cellular and infection microbiology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — proteomics detection across species without functional experiment on HMGB3 itself; Myb-domain annotation is computational","pmids":["33585284"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1205800 (HMGB3) is a large, multi-domain P. falciparum nuclear protein bearing two HMG box domains and a Myb-binding domain; it has been co-purified with the chromatin remodeling factor PfEAF2 (PfSWR1 complex context), co-enriched with the AP2-I transcription factor at regulatory DNA motifs, identified as a PfHSP70-2 interactor by yeast two-hybrid, and detected in sporozoite proteomes, but no direct loss-of-function experiment or in vitro biochemical characterization of HMGB3 itself has been reported."},"narrative":{"mechanistic_narrative":"PF3D7_1205800 (HMGB3) is a large (~2,284 amino acid) predicted P. falciparum HMG box protein distinguished from the smaller single-box HMGB1 and HMGB2 paralogs by two HMG box domains and an additional putative Myb domain [PMID:16607015, PMID:33585284]. The available evidence positions HMGB3 in the context of nuclear chromatin regulation rather than assigning it a direct biochemical function: it co-enriches with the transcription factor AP2-I on regulatory motif 028-containing promoter DNA alongside bromodomain and SWIB/MDM2 proteins [PMID:29649445], and it co-purifies with PfEAF2 in the context of the PfSWR1 chromatin remodeling complex [PMID:38564734]. HMGB3 was also recovered as a PfHSP70-2 interactor in a yeast two-hybrid screen [PMID:32529065] and detected in sporozoite proteomes across Plasmodium species [PMID:33585284]. No direct loss-of-function experiment or in vitro biochemical characterization of HMGB3 itself has been reported in the available corpus; all functional inference rests on computational domain prediction and association with named partners and complexes.","teleology":[{"year":2006,"claim":"Establishing that the P. falciparum HMGB family includes a distinct large member answered whether all Plasmodium HMGB proteins are functionally equivalent, revealing HMGB3 as structurally unique.","evidence":"Computational sequence/domain analysis of the P. falciparum HMGB family","pmids":["16607015"],"confidence":"Low","gaps":["Domain content is predicted only, with no experimental validation of DNA binding or Myb-domain function","No evidence for the biological process HMGB3 participates in"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"claim":"Identifying HMGB3 among proteins captured on a specific regulatory motif addressed where in the genome it might act, linking it to promoter-associated chromatin regulation with AP2-I.","evidence":"DNA affinity pulldown with motif-028 probes and mass spectrometry","pmids":["29649445"],"confidence":"Low","gaps":["Single pulldown without functional follow-up on HMGB3 itself","Does not establish direct DNA binding by HMGB3 versus indirect recruitment","No demonstration that HMGB3 loss affects AP2-I target expression"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"claim":"A yeast two-hybrid screen added HMGB3 to the interactome of PfHSP70-2, raising the question of whether HMGB3 is a chaperone client or partner.","evidence":"Yeast two-hybrid interaction screen","pmids":["32529065"],"confidence":"Low","gaps":["Single-method interaction with no reciprocal or in vivo validation","Functional consequence of the HSP70-2 interaction unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"Detecting HMGB3 in sporozoite proteomes across species addressed its stage expression and, combined with its unique Myb-binding domain, motivated a candidate transcription-factor role in the sporozoite.","evidence":"Mass spectrometry of sporozoite proteomes across Plasmodium species","pmids":["33585284"],"confidence":"Low","gaps":["Proteomic presence does not establish transcriptional activity","Myb-domain role is inferred from computational annotation, not tested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"claim":"Reciprocal PfEAF2 pulldowns placed HMGB3 within the PfSWR1 chromatin remodeling complex context, refining its inferred association from promoter DNA to a defined remodeling machinery.","evidence":"Reciprocal affinity pulldown/mass spectrometry with PfEAF2 as bait","pmids":["38564734"],"confidence":"Low","gaps":["HMGB3 recovered as a minor associated factor without direct functional role in the complex","No stoichiometry or direct binding data","No loss-of-function test of HMGB3 within PfSWR1"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether HMGB3 has any intrinsic DNA-binding, chromatin-remodeling, or transcriptional activity, and whether it is essential at any parasite stage, remains undetermined absent any direct loss-of-function or in vitro biochemical experiment.","evidence":"No direct functional characterization of HMGB3 in the available corpus","pmids":[],"confidence":"Low","gaps":["No knockout, knockdown, or complementation of HMGB3","No in vitro reconstitution of HMG-box DNA binding or Myb-domain function","No demonstration that any co-purification reflects a direct interaction"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["PfSWR1 chromatin remodeling complex (co-purified with PfEAF2) [#2]"],"partners":["AP2-I (CO-ENRICHED ON MOTIF-028 REGULATORY DNA) [#1]","PFHSP70-2 (YEAST TWO-HYBRID INTERACTOR) [#3]","PFEAF2 (RECIPROCAL PULLDOWN) [#2]"],"other_free_text":["Large (~2,284 aa) HMGB family member with two HMG box domains and a putative Myb domain, unique among P. falciparum HMGB proteins [#0, #4]","Detected in sporozoite proteomes across multiple Plasmodium species [#4]","No direct loss-of-function or in vitro biochemical characterization of HMGB3 itself has been reported; all inference rests on computational prediction and association with named partners/complexes"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"16607015","id":"PMC_16607015","title":"High-mobility-group box nuclear factors of Plasmodium falciparum.","date":"2006","source":"Eukaryotic cell","url":"https://pubmed.ncbi.nlm.nih.gov/16607015","citation_count":42,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40223817","id":"","title":"Aptamers as innovative tools for malaria diagnosis and treatment: advances and future perspectives.","date":"2025","source":"Biology methods & protocols","url":"https://pubmed.ncbi.nlm.nih.gov/40223817","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36506024","id":"","title":"PfHMGB2 has a role in malaria parasite mosquito infection.","date":"2022","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/36506024","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"39341498","id":"","title":"Plasmodium berghei HMGB1 controls the host immune responses and splenic clearance by regulating the expression of pir genes.","date":"2024","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/39341498","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"40626563","id":"","title":"The ribosomal RNA transcription landscapes of Plasmodium falciparum and related apicomplexan parasites.","date":"2025","source":"Nucleic acids research","url":"https://pubmed.ncbi.nlm.nih.gov/40626563","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38564734","id":"","title":"MYST regulates DNA repair and forms a NuA4-like complex in the malaria parasite Plasmodium falciparum.","date":"2024","source":"mSphere","url":"https://pubmed.ncbi.nlm.nih.gov/38564734","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33585284","id":"","title":"Preparing for Transmission: Gene Regulation in Plasmodium Sporozoites.","date":"2021","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/33585284","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32529065","id":"","title":"Identification of Plasmodium falciparum HSP70-2 as a resident of the Plasmodium export compartment.","date":"2020","source":"Heliyon","url":"https://pubmed.ncbi.nlm.nih.gov/32529065","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"31220867","id":"","title":"What functional genomics has taught us about transcriptional regulation in malaria parasites.","date":"2019","source":"Briefings in functional genomics","url":"https://pubmed.ncbi.nlm.nih.gov/31220867","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"22131806","id":"","title":"Emerging functions of transcription factors in malaria parasite.","date":"2011","source":"Journal of biomedicine & biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/22131806","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"29649445","id":"","title":"Chromatin Accessibility-Based Characterization of the Gene Regulatory Network Underlying Plasmodium falciparum Blood-Stage Development.","date":"2018","source":"Cell host & microbe","url":"https://pubmed.ncbi.nlm.nih.gov/29649445","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["HMGB3"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":13880,"output_tokens":1350,"usd":0.030945,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6220,"output_tokens":2437,"usd":0.046012,"stage2_stop_reason":"end_turn"},"total_usd":0.076957,"stage1_batch_id":"msgbatch_01NE1MTa8x1hW7Lo4tAaNzY1","stage2_batch_id":"msgbatch_0141vaQdeFvbo2q39AinvXM9","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2006,\n      \"finding\": \"PF3D7_1205800 (HMGB3) was identified by computational analysis as a large (~2,284 amino acid) P. falciparum HMG box protein containing two HMG box domains and additional putative functional motifs including one Myb domain, distinguishing it structurally from the smaller single-box HMGB1 and HMGB2 paralogs.\",\n      \"method\": \"Computational sequence analysis / bioinformatics domain prediction\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — computational prediction only, no direct experimental characterization of HMGB3 protein function performed in this study\",\n      \"pmids\": [\"16607015\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"HMGB3 (PF3D7_1205800) was co-enriched with the transcription factor AP2-I in DNA pulldown experiments using probes containing de novo regulatory motif 028, alongside bromodomain proteins and an SWIB/MDM2 domain-containing protein, suggesting HMGB3 associates with AP2-I at target gene promoters as part of a chromatin regulatory complex.\",\n      \"method\": \"DNA affinity pulldown / mass spectrometry (oligo-based protein enrichment with motif-containing probes)\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single pulldown experiment, single lab, HMGB3 identified as co-enriched factor but no direct functional follow-up on HMGB3 itself\",\n      \"pmids\": [\"29649445\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"HMGB3 (PF3D7_1205800) was identified as a co-purifying protein in PfEAF2 reciprocal pulldowns, placing it in the context of the PfSWR1 chromatin remodeling complex in P. falciparum.\",\n      \"method\": \"Reciprocal affinity pulldown / mass spectrometry (PfEAF2 as bait)\",\n      \"journal\": \"mSphere\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single co-purification experiment identifying HMGB3 as a minor associated factor; no direct functional characterization of HMGB3 itself was performed\",\n      \"pmids\": [\"38564734\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"HMGB3 (PF3D7_1205800) was identified as an interacting partner of PfHSP70-2 in a yeast two-hybrid screen.\",\n      \"method\": \"Yeast two-hybrid interaction screen\",\n      \"journal\": \"Heliyon\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — yeast two-hybrid identification only, single method, no functional follow-up on the interaction\",\n      \"pmids\": [\"32529065\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"HMGB3 (PF3D7_1205800) was detected in the proteome of sporozoites across multiple tested Plasmodium species, and is noted as the only HMGB family member that possesses a Myb-binding domain, suggesting a potential role as a transcription factor in the sporozoite stage.\",\n      \"method\": \"Proteomic detection (mass spectrometry of sporozoite proteomes)\",\n      \"journal\": \"Frontiers in cellular and infection microbiology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — proteomics detection across species without functional experiment on HMGB3 itself; Myb-domain annotation is computational\",\n      \"pmids\": [\"33585284\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1205800 (HMGB3) is a large, multi-domain P. falciparum nuclear protein bearing two HMG box domains and a Myb-binding domain; it has been co-purified with the chromatin remodeling factor PfEAF2 (PfSWR1 complex context), co-enriched with the AP2-I transcription factor at regulatory DNA motifs, identified as a PfHSP70-2 interactor by yeast two-hybrid, and detected in sporozoite proteomes, but no direct loss-of-function experiment or in vitro biochemical characterization of HMGB3 itself has been reported.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1205800 (HMGB3) is a large (~2,284 amino acid) predicted P. falciparum HMG box protein distinguished from the smaller single-box HMGB1 and HMGB2 paralogs by two HMG box domains and an additional putative Myb domain [#0, #4]. The available evidence positions HMGB3 in the context of nuclear chromatin regulation rather than assigning it a direct biochemical function: it co-enriches with the transcription factor AP2-I on regulatory motif 028-containing promoter DNA alongside bromodomain and SWIB/MDM2 proteins [#1], and it co-purifies with PfEAF2 in the context of the PfSWR1 chromatin remodeling complex [#2]. HMGB3 was also recovered as a PfHSP70-2 interactor in a yeast two-hybrid screen [#3] and detected in sporozoite proteomes across Plasmodium species [#4]. No direct loss-of-function experiment or in vitro biochemical characterization of HMGB3 itself has been reported in the available corpus; all functional inference rests on computational domain prediction and association with named partners and complexes.\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"Establishing that the P. falciparum HMGB family includes a distinct large member answered whether all Plasmodium HMGB proteins are functionally equivalent, revealing HMGB3 as structurally unique.\",\n      \"evidence\": \"Computational sequence/domain analysis of the P. falciparum HMGB family\",\n      \"pmids\": [\"16607015\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Domain content is predicted only, with no experimental validation of DNA binding or Myb-domain function\", \"No evidence for the biological process HMGB3 participates in\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Identifying HMGB3 among proteins captured on a specific regulatory motif addressed where in the genome it might act, linking it to promoter-associated chromatin regulation with AP2-I.\",\n      \"evidence\": \"DNA affinity pulldown with motif-028 probes and mass spectrometry\",\n      \"pmids\": [\"29649445\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single pulldown without functional follow-up on HMGB3 itself\", \"Does not establish direct DNA binding by HMGB3 versus indirect recruitment\", \"No demonstration that HMGB3 loss affects AP2-I target expression\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"A yeast two-hybrid screen added HMGB3 to the interactome of PfHSP70-2, raising the question of whether HMGB3 is a chaperone client or partner.\",\n      \"evidence\": \"Yeast two-hybrid interaction screen\",\n      \"pmids\": [\"32529065\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single-method interaction with no reciprocal or in vivo validation\", \"Functional consequence of the HSP70-2 interaction unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Detecting HMGB3 in sporozoite proteomes across species addressed its stage expression and, combined with its unique Myb-binding domain, motivated a candidate transcription-factor role in the sporozoite.\",\n      \"evidence\": \"Mass spectrometry of sporozoite proteomes across Plasmodium species\",\n      \"pmids\": [\"33585284\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Proteomic presence does not establish transcriptional activity\", \"Myb-domain role is inferred from computational annotation, not tested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Reciprocal PfEAF2 pulldowns placed HMGB3 within the PfSWR1 chromatin remodeling complex context, refining its inferred association from promoter DNA to a defined remodeling machinery.\",\n      \"evidence\": \"Reciprocal affinity pulldown/mass spectrometry with PfEAF2 as bait\",\n      \"pmids\": [\"38564734\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"HMGB3 recovered as a minor associated factor without direct functional role in the complex\", \"No stoichiometry or direct binding data\", \"No loss-of-function test of HMGB3 within PfSWR1\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether HMGB3 has any intrinsic DNA-binding, chromatin-remodeling, or transcriptional activity, and whether it is essential at any parasite stage, remains undetermined absent any direct loss-of-function or in vitro biochemical experiment.\",\n      \"evidence\": \"No direct functional characterization of HMGB3 in the available corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No knockout, knockdown, or complementation of HMGB3\", \"No in vitro reconstitution of HMG-box DNA binding or Myb-domain function\", \"No demonstration that any co-purification reflects a direct interaction\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003677\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006338\", \"supporting_discovery_ids\": [2]},\n      {\"term_id\": \"GO:0006355\", \"supporting_discovery_ids\": [1, 4]}\n    ],\n    \"complexes\": [\n      \"PfSWR1 chromatin remodeling complex (co-purified with PfEAF2) [#2]\"\n    ],\n    \"partners\": [\n      \"AP2-I (co-enriched on motif-028 regulatory DNA) [#1]\",\n      \"PfHSP70-2 (yeast two-hybrid interactor) [#3]\",\n      \"PfEAF2 (reciprocal pulldown) [#2]\"\n    ],\n    \"other_free_text\": [\n      \"Large (~2,284 aa) HMGB family member with two HMG box domains and a putative Myb domain, unique among P. falciparum HMGB proteins [#0, #4]\",\n      \"Detected in sporozoite proteomes across multiple Plasmodium species [#4]\",\n      \"No direct loss-of-function or in vitro biochemical characterization of HMGB3 itself has been reported; all inference rests on computational prediction and association with named partners/complexes\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1205800","name":null,"product":"high mobility group protein B3, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0604500","name":null,"product":"high mobility group protein B3, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1305500","name":null,"product":"high mobility group protein B3, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"HMGB3","evaluation":null}