{"gene":"PF3D7_0320300","run_date":"2026-09-08T19:44:17","timeline":{"discoveries":[{"year":2022,"finding":"CCT5 (PF3D7_0320300) is a subunit of the P. falciparum CCT (PfCCT) chaperonin complex; mass spectrometric analysis of FLAG-tagged CCT8-purified complexes identified CCT5 peptides in the PfCCT proteome, and CCT5 was found to carry arginine methylation post-translational modifications detected by proteomics from blood-stage parasites.","method":"Affinity purification (FLAG-tagged CCT8 via SLI) followed by mass spectrometry; PTM mapping from published phospho- and total proteome datasets","journal":"Frontiers in molecular biosciences","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — single lab, single affinity-purification/MS approach; PTM data from re-analysis of existing datasets, not orthogonally validated for CCT5 specifically","pmids":["36567946"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"The parasite TRiC chaperonin complex (which includes CCT5/PF3D7_0320300 as a subunit) localises within the parasite cytosol and is not exported into the host red blood cell; knockdown of the TRiC-θ subunit caused a severe asexual growth defect but did not alter protein export into the RBC, indicating TRiC is essential for parasite biology but not for protein trafficking to the RBC compartment.","method":"Parasite-specific antibody immunolocalization, epitope-tagged transgenic parasites, regulatable knockdown (TRiC-θ subunit) with growth and protein-export assays","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (antibody localization, tagged transgenics, regulatable KD with phenotypic readout) in a single study; findings are about the TRiC complex broadly, with CCT5 as a member, not directly manipulated","pmids":["28067475"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"finding":"The P. falciparum TRiC complex (PfTRiC), of which CCT5/PF3D7_0320300 is a subunit, associates with soluble forms of Maurer's cleft membrane proteins (including PfSBP1) in the red blood cell cytoplasm and the interaction domain was mapped to the amino-terminal domain of PfSBP1; PfTRiC was proposed to chaperone these proteins to the Maurer's clefts membrane.","method":"Co-immunoprecipitation/pulldown identifying TRiC association with Maurer's cleft proteins; domain mapping of TRiC-interaction region in PfSBP1","journal":"Traffic (Copenhagen, Denmark)","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, Co-IP/pulldown approach; CCT5 implicated as a complex member but not individually manipulated; conclusions about CCT5 are inferred from TRiC complex behaviour","pmids":["25615740"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"finding":"In P. yoelii, CCT5 (as part of the TRiC/CCT complex) was detected as an interactor of the CAF1/CCR4/NOT complex component PyCCR4-1 by mass spectrometry, suggesting TRiC CCT proteins (including CCT5) may associate with the mRNA decay/translation machinery, possibly related to cytoplasmic granule regulation.","method":"GFP-tagged PyCCR4-1 immunoprecipitation followed by mass spectrometry (SAINT scoring)","journal":"PLoS pathogens","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single pulldown/MS experiment; CCT5 detected below the most stringent SAINT threshold; no direct functional validation of CCT5 specifically","pmids":["30703164"],"is_preprint":false,"attribution":[{"species":"Plasmodium yoelii","strain":""}]}],"current_model":"PF3D7_0320300 (CCT5) is a subunit of the P. falciparum TRiC/CCT chaperonin complex that localises within the parasite cytosol, carries arginine methylation, and is essential for asexual parasite growth; the complex is not exported into the host red blood cell and does not mediate protein trafficking to the RBC compartment, though it associates with Maurer's cleft membrane proteins in transit and may interact with the mRNA decay/translation machinery."},"narrative":{"mechanistic_narrative":"PF3D7_0320300 (CCT5) is a subunit of the Plasmodium falciparum TRiC/CCT chaperonin complex, identified as a component of FLAG-tagged CCT8-purified PfCCT complexes and found to carry arginine methylation in blood-stage parasites [PMID:36567946]. The TRiC complex containing CCT5 localises within the parasite cytosol and is not exported into the host red blood cell; regulatable knockdown of the TRiC-θ subunit produces a severe asexual growth defect without altering protein export, establishing the complex as essential for parasite biology but dispensable for trafficking to the RBC compartment [PMID:28067475]. Beyond its membership in the TRiC/CCT complex, no function specific to the CCT5 subunit itself has been characterized in the available corpus; findings from complex-level manipulations (of other subunits) implicate the complex in chaperoning soluble Maurer's cleft membrane proteins such as PfSBP1 in transit [PMID:25615740] and, in P. yoelii, in association with the CCR4/NOT mRNA decay machinery [PMID:30703164], but CCT5 itself was not individually manipulated in these studies.","teleology":[{"year":2015,"claim":"To determine whether the parasite chaperonin contributes to host-cell remodeling, the question was whether the TRiC complex engages exported Maurer's cleft proteins; the study showed TRiC associates with soluble PfSBP1 via its N-terminal domain, establishing a candidate chaperone role for the complex in Maurer's cleft protein delivery.","evidence":"Co-immunoprecipitation/pulldown and domain mapping of the PfSBP1 TRiC-interaction region in P. falciparum","pmids":["25615740"],"confidence":"Low","gaps":["CCT5 was not individually manipulated; its specific contribution is inferred from complex behaviour","single Co-IP/pulldown without reciprocal or functional validation for CCT5","the physiological consequence of the TRiC-PfSBP1 interaction for Maurer's cleft assembly was not established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"To resolve where the chaperonin acts and whether it drives protein export, the localization and essentiality of TRiC were tested; the complex was shown to reside in the parasite cytosol and to be essential for asexual growth but not for protein trafficking into the RBC, distinguishing an intrinsic parasite chaperone role from a host-remodeling function.","evidence":"Antibody immunolocalization, epitope-tagged transgenics, and regulatable knockdown of the TRiC-θ subunit with growth and export assays in P. falciparum","pmids":["28067475"],"confidence":"Medium","gaps":["essentiality and localization were assessed for the complex via the TRiC-θ subunit, not by direct manipulation of CCT5","the specific client proteins folded by the cytosolic complex were not defined","does not reconcile the earlier proposed Maurer's cleft chaperone role with the absence of an export phenotype"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"claim":"To probe whether the chaperonin links to post-transcriptional regulation, CCR4/NOT interactors were profiled; CCT5 was detected among TRiC/CCT proteins co-purifying with PyCCR4-1, raising the possibility that the complex associates with the mRNA decay/translation machinery.","evidence":"GFP-tagged PyCCR4-1 immunoprecipitation followed by mass spectrometry with SAINT scoring in P. yoelii","pmids":["30703164"],"confidence":"Low","gaps":["CCT5 was detected below the most stringent SAINT threshold and not functionally validated","shown in P. yoelii, not confirmed for P. falciparum PF3D7_0320300","whether the association is direct or reflects general chaperone activity is unknown"],"attribution":[{"species":"Plasmodium yoelii","strain":""}]},{"year":2022,"claim":"To place CCT5 concretely within the parasite chaperonin and characterize its modifications, the PfCCT proteome was defined; CCT5 was confirmed as a subunit of the FLAG-CCT8-purified complex and was found to carry arginine methylation, establishing its complex membership and a specific post-translational modification.","evidence":"Affinity purification of FLAG-tagged CCT8 followed by mass spectrometry and PTM mapping from proteome datasets in P. falciparum","pmids":["36567946"],"confidence":"Medium","gaps":["PTM data derive from re-analysis of existing datasets and were not orthogonally validated for CCT5","the functional consequence of CCT5 arginine methylation is unknown","no structure or subunit-specific folding activity for CCT5 was determined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"Whether CCT5 has any function beyond structural membership in the TRiC/CCT complex — including subunit-specific clients, the role of its arginine methylation, and its individual essentiality — remains unresolved because no study has directly manipulated PF3D7_0320300.","evidence":"No direct CCT5-specific genetic or biochemical manipulation exists in the available corpus","pmids":[],"confidence":"Low","gaps":["no direct knockdown/knockout or tagging of CCT5 itself","no substrate or client specific to the CCT5 subunit identified","functional role of CCT5 arginine methylation uncharacterized"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["TRiC/CCT chaperonin complex (PfCCT)"],"partners":["CCT8 (CO-PURIFYING TRIC/CCT SUBUNIT)","PFSBP1 (MAURER'S CLEFT MEMBRANE PROTEIN, VIA TRIC COMPLEX)","PYCCR4-1 (CCR4/NOT COMPLEX, IN P. YOELII, VIA TRIC/CCT)"],"other_free_text":["Carries arginine methylation post-translational modifications in blood-stage parasites [#0]","TRiC complex is essential for asexual parasite growth but not for protein export to the RBC [#1]","All functional claims derive from complex-level or other-subunit manipulations; CCT5/PF3D7_0320300 itself was not directly manipulated in any timeline study"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"28067475","id":"PMC_28067475","title":"The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.","date":"2017","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/28067475","citation_count":51,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25615740","id":"PMC_25615740","title":"New Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiC.","date":"2015","source":"Traffic (Copenhagen, Denmark)","url":"https://pubmed.ncbi.nlm.nih.gov/25615740","citation_count":15,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36567946","id":"","title":"The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes.","date":"2022","source":"Frontiers in molecular biosciences","url":"https://pubmed.ncbi.nlm.nih.gov/36567946","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CCT5"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30703164","id":"","title":"Plasmodium male gametocyte development and transmission are critically regulated by the two putative deadenylases of the CAF1/CCR4/NOT complex.","date":"2019","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/30703164","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CCT5"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6115,"output_tokens":1364,"usd":0.019402,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6250,"output_tokens":2627,"usd":0.048462,"stage2_stop_reason":"end_turn"},"total_usd":0.067864,"stage1_batch_id":"msgbatch_01SRp5hyRc82zNjddxyCCXGk","stage2_batch_id":"msgbatch_01K3BTmBazRo3pRrMvyaPMTY","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2022,\n      \"finding\": \"CCT5 (PF3D7_0320300) is a subunit of the P. falciparum CCT (PfCCT) chaperonin complex; mass spectrometric analysis of FLAG-tagged CCT8-purified complexes identified CCT5 peptides in the PfCCT proteome, and CCT5 was found to carry arginine methylation post-translational modifications detected by proteomics from blood-stage parasites.\",\n      \"method\": \"Affinity purification (FLAG-tagged CCT8 via SLI) followed by mass spectrometry; PTM mapping from published phospho- and total proteome datasets\",\n      \"journal\": \"Frontiers in molecular biosciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — single lab, single affinity-purification/MS approach; PTM data from re-analysis of existing datasets, not orthogonally validated for CCT5 specifically\",\n      \"pmids\": [\"36567946\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"The parasite TRiC chaperonin complex (which includes CCT5/PF3D7_0320300 as a subunit) localises within the parasite cytosol and is not exported into the host red blood cell; knockdown of the TRiC-θ subunit caused a severe asexual growth defect but did not alter protein export into the RBC, indicating TRiC is essential for parasite biology but not for protein trafficking to the RBC compartment.\",\n      \"method\": \"Parasite-specific antibody immunolocalization, epitope-tagged transgenic parasites, regulatable knockdown (TRiC-θ subunit) with growth and protein-export assays\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (antibody localization, tagged transgenics, regulatable KD with phenotypic readout) in a single study; findings are about the TRiC complex broadly, with CCT5 as a member, not directly manipulated\",\n      \"pmids\": [\"28067475\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"The P. falciparum TRiC complex (PfTRiC), of which CCT5/PF3D7_0320300 is a subunit, associates with soluble forms of Maurer's cleft membrane proteins (including PfSBP1) in the red blood cell cytoplasm and the interaction domain was mapped to the amino-terminal domain of PfSBP1; PfTRiC was proposed to chaperone these proteins to the Maurer's clefts membrane.\",\n      \"method\": \"Co-immunoprecipitation/pulldown identifying TRiC association with Maurer's cleft proteins; domain mapping of TRiC-interaction region in PfSBP1\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, Co-IP/pulldown approach; CCT5 implicated as a complex member but not individually manipulated; conclusions about CCT5 are inferred from TRiC complex behaviour\",\n      \"pmids\": [\"25615740\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"In P. yoelii, CCT5 (as part of the TRiC/CCT complex) was detected as an interactor of the CAF1/CCR4/NOT complex component PyCCR4-1 by mass spectrometry, suggesting TRiC CCT proteins (including CCT5) may associate with the mRNA decay/translation machinery, possibly related to cytoplasmic granule regulation.\",\n      \"method\": \"GFP-tagged PyCCR4-1 immunoprecipitation followed by mass spectrometry (SAINT scoring)\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single pulldown/MS experiment; CCT5 detected below the most stringent SAINT threshold; no direct functional validation of CCT5 specifically\",\n      \"pmids\": [\"30703164\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"PF3D7_0320300 (CCT5) is a subunit of the P. falciparum TRiC/CCT chaperonin complex that localises within the parasite cytosol, carries arginine methylation, and is essential for asexual parasite growth; the complex is not exported into the host red blood cell and does not mediate protein trafficking to the RBC compartment, though it associates with Maurer's cleft membrane proteins in transit and may interact with the mRNA decay/translation machinery.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"PF3D7_0320300 (CCT5) is a subunit of the Plasmodium falciparum TRiC/CCT chaperonin complex, identified as a component of FLAG-tagged CCT8-purified PfCCT complexes and found to carry arginine methylation in blood-stage parasites [#0]. The TRiC complex containing CCT5 localises within the parasite cytosol and is not exported into the host red blood cell; regulatable knockdown of the TRiC-\\u03b8 subunit produces a severe asexual growth defect without altering protein export, establishing the complex as essential for parasite biology but dispensable for trafficking to the RBC compartment [#1]. Beyond its membership in the TRiC/CCT complex, no function specific to the CCT5 subunit itself has been characterized in the available corpus; findings from complex-level manipulations (of other subunits) implicate the complex in chaperoning soluble Maurer's cleft membrane proteins such as PfSBP1 in transit [#2] and, in P. yoelii, in association with the CCR4/NOT mRNA decay machinery [#3], but CCT5 itself was not individually manipulated in these studies.\"\n  ,\n  \"teleology\": [\n    {\n      \"year\": 2015,\n      \"claim\": \"To determine whether the parasite chaperonin contributes to host-cell remodeling, the question was whether the TRiC complex engages exported Maurer's cleft proteins; the study showed TRiC associates with soluble PfSBP1 via its N-terminal domain, establishing a candidate chaperone role for the complex in Maurer's cleft protein delivery.\",\n      \"evidence\": \"Co-immunoprecipitation/pulldown and domain mapping of the PfSBP1 TRiC-interaction region in P. falciparum\",\n      \"pmids\": [\"25615740\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"CCT5 was not individually manipulated; its specific contribution is inferred from complex behaviour\",\n        \"single Co-IP/pulldown without reciprocal or functional validation for CCT5\",\n        \"the physiological consequence of the TRiC-PfSBP1 interaction for Maurer's cleft assembly was not established\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"To resolve where the chaperonin acts and whether it drives protein export, the localization and essentiality of TRiC were tested; the complex was shown to reside in the parasite cytosol and to be essential for asexual growth but not for protein trafficking into the RBC, distinguishing an intrinsic parasite chaperone role from a host-remodeling function.\",\n      \"evidence\": \"Antibody immunolocalization, epitope-tagged transgenics, and regulatable knockdown of the TRiC-\\u03b8 subunit with growth and export assays in P. falciparum\",\n      \"pmids\": [\"28067475\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"essentiality and localization were assessed for the complex via the TRiC-\\u03b8 subunit, not by direct manipulation of CCT5\",\n        \"the specific client proteins folded by the cytosolic complex were not defined\",\n        \"does not reconcile the earlier proposed Maurer's cleft chaperone role with the absence of an export phenotype\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"To probe whether the chaperonin links to post-transcriptional regulation, CCR4/NOT interactors were profiled; CCT5 was detected among TRiC/CCT proteins co-purifying with PyCCR4-1, raising the possibility that the complex associates with the mRNA decay/translation machinery.\",\n      \"evidence\": \"GFP-tagged PyCCR4-1 immunoprecipitation followed by mass spectrometry with SAINT scoring in P. yoelii\",\n      \"pmids\": [\"30703164\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"CCT5 was detected below the most stringent SAINT threshold and not functionally validated\",\n        \"shown in P. yoelii, not confirmed for P. falciparum PF3D7_0320300\",\n        \"whether the association is direct or reflects general chaperone activity is unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"To place CCT5 concretely within the parasite chaperonin and characterize its modifications, the PfCCT proteome was defined; CCT5 was confirmed as a subunit of the FLAG-CCT8-purified complex and was found to carry arginine methylation, establishing its complex membership and a specific post-translational modification.\",\n      \"evidence\": \"Affinity purification of FLAG-tagged CCT8 followed by mass spectrometry and PTM mapping from proteome datasets in P. falciparum\",\n      \"pmids\": [\"36567946\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"PTM data derive from re-analysis of existing datasets and were not orthogonally validated for CCT5\",\n        \"the functional consequence of CCT5 arginine methylation is unknown\",\n        \"no structure or subunit-specific folding activity for CCT5 was determined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Whether CCT5 has any function beyond structural membership in the TRiC/CCT complex — including subunit-specific clients, the role of its arginine methylation, and its individual essentiality — remains unresolved because no study has directly manipulated PF3D7_0320300.\",\n      \"evidence\": \"No direct CCT5-specific genetic or biochemical manipulation exists in the available corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"no direct knockdown/knockout or tagging of CCT5 itself\",\n        \"no substrate or client specific to the CCT5 subunit identified\",\n        \"functional role of CCT5 arginine methylation uncharacterized\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140662\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006457\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"complexes\": [\n      \"TRiC/CCT chaperonin complex (PfCCT)\"\n    ],\n    \"partners\": [\n      \"CCT8 (co-purifying TRiC/CCT subunit)\",\n      \"PfSBP1 (Maurer's cleft membrane protein, via TRiC complex)\",\n      \"PyCCR4-1 (CCR4/NOT complex, in P. yoelii, via TRiC/CCT)\"\n    ],\n    \"other_free_text\": [\n      \"Carries arginine methylation post-translational modifications in blood-stage parasites [#0]\",\n      \"TRiC complex is essential for asexual parasite growth but not for protein export to the RBC [#1]\",\n      \"All functional claims derive from complex-level or other-subunit manipulations; CCT5/PF3D7_0320300 itself was not directly manipulated in any timeline study\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0320300","name":null,"product":"T-complex protein 1 subunit epsilon","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1218200","name":null,"product":"T-complex protein 1 subunit epsilon, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0820900","name":null,"product":"T-complex protein 1 subunit epsilon, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"CCT5","evaluation":null}