{"gene":"CMC1","run_date":"2026-04-28T17:28:52","timeline":{"discoveries":[{"year":2017,"finding":"CMC1 forms an early cytochrome c oxidase (CIV) assembly intermediate with COX1 and assembly factors COA3 and COX14 in the mitochondrial intermembrane space, stabilizing newly synthesized COX1 prior to incorporation of COX4 and COX5a subunits, without affecting COX1 mRNA translation rate.","method":"TALEN-mediated CMC1 knockout in HEK293T cells; co-immunoprecipitation; pulse-chase labeling of mitochondrial translation products; CIV activity assay","journal":"EMBO reports","confidence":"High","confidence_rationale":"Tier 2 — reciprocal Co-IP, clean KO with defined biochemical phenotype, and orthogonal translation assay in one study","pmids":["28082314"],"is_preprint":false},{"year":2010,"finding":"Yeast Cmc1 (ortholog of human CMC1) is a mitochondrial intermembrane space twin Cx9C protein required for cytochrome c oxidase biogenesis; it physically interacts with Cmc2, and absence of Cmc2 causes a 5-fold increase in Cmc1 accumulation, indicating cooperative but non-redundant functions.","method":"Subcellular fractionation, spectrophotometric CIV activity assay, polarographic respiration measurement, co-immunoprecipitation, genetic complementation","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 — reciprocal interaction demonstrated, clean KO phenotype, multiple orthogonal methods, replicated across yeast and C. elegans","pmids":["20220131"],"is_preprint":false},{"year":2012,"finding":"CMC1 (a twin CX9C protein) is imported into the mitochondrial intermembrane space via the Mia40/Erv1 oxidative folding pathway; CMC1 forms a stable intermediate with Mia40 and is released upon addition of Erv1, with all three proteins forming a ternary complex in mitochondria. Efficient oxidation of CMC1 requires both Mia40 and Erv1.","method":"In vitro oxidative folding assay, in organello import assay, co-immunoprecipitation, ternary complex detection","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1-2 — in vitro reconstitution combined with in organello validation and co-IP of ternary complex","pmids":["22767599"],"is_preprint":false},{"year":2024,"finding":"CMC1 acts as a positive regulator of CD8+ T cell activation and terminal differentiation/exhaustion; environmental lactate enhances CMC1 expression by inducing USP7, which stabilizes CMC1 through de-ubiquitination. Genetic loss of Cmc1 in T cells inhibits exhaustion and promotes memory-like differentiation.","method":"Cmc1 knockout mice, in vitro T cell culture, B16-OVA tumor model, mechanistic studies of USP7-mediated CMC1 de-ubiquitination","journal":"Oncoimmunology","confidence":"Medium","confidence_rationale":"Tier 2-3 — clean KO with defined cellular phenotype and identification of USP7 as a deubiquitinase writer, but mechanistic pathway placement relies on single study","pmids":["38659649"],"is_preprint":false}],"current_model":"CMC1 is a mitochondrial intermembrane space twin CX9C protein imported via the Mia40/Erv1 oxidative folding pathway that stabilizes newly synthesized COX1 within an early COX1-COA3-COX14 assembly intermediate during cytochrome c oxidase biogenesis, acts independently of COX1 metallation factors, and is also regulated by lactate-induced USP7-mediated de-ubiquitination to modulate CD8+ T cell exhaustion."},"narrative":{"teleology":[{"year":2010,"claim":"Establishing CMC1 as a mitochondrial factor required for cytochrome c oxidase biogenesis resolved its basic cellular function and revealed a functional partnership with Cmc2 in the intermembrane space.","evidence":"Yeast Cmc1 deletion with spectrophotometric CIV activity assay, respiration measurement, co-immunoprecipitation of Cmc1–Cmc2 interaction, and cross-species complementation","pmids":["20220131"],"confidence":"High","gaps":["Precise step in CIV assembly where Cmc1 acts was not defined","Whether the Cmc1–Cmc2 interaction is direct or bridged was not resolved","Mechanism by which Cmc2 loss elevates Cmc1 levels was not determined"]},{"year":2012,"claim":"Demonstrating that CMC1 is imported via the Mia40/Erv1 oxidative folding pathway and forms a ternary complex with these factors established how CMC1 reaches its functional compartment.","evidence":"In vitro oxidative folding reconstitution, in organello import assay, and co-immunoprecipitation of CMC1–Mia40–Erv1 ternary complex","pmids":["22767599"],"confidence":"High","gaps":["Whether import efficiency regulates CMC1 steady-state levels under physiological conditions was not tested","Structural basis of the twin CX9C motif recognition by Mia40 for CMC1 specifically was not resolved"]},{"year":2017,"claim":"Placing CMC1 in an early COX1–COA3–COX14 assembly intermediate and showing it stabilizes COX1 post-translationally (without affecting translation) pinpointed its precise role in complex IV biogenesis.","evidence":"TALEN-mediated CMC1 knockout in HEK293T cells with co-immunoprecipitation, pulse-chase mitochondrial translation labeling, and CIV activity assay","pmids":["28082314"],"confidence":"High","gaps":["Whether CMC1 contacts COX1 directly or solely through COA3/COX14 was not determined","Relationship between CMC1 function and COX1 metallation (copper/heme insertion) was not clarified","No structural information on the early assembly intermediate"]},{"year":2024,"claim":"Discovery that lactate-induced USP7-mediated de-ubiquitination stabilizes CMC1 and that CMC1 promotes CD8+ T cell exhaustion expanded its functional scope beyond mitochondrial assembly to immune cell fate regulation.","evidence":"Cmc1 knockout mice, in vitro T cell culture, B16-OVA tumor model, mechanistic studies of USP7-mediated de-ubiquitination","pmids":["38659649"],"confidence":"Medium","gaps":["Single study without independent replication of the T cell exhaustion phenotype","Whether the T cell effect depends on CMC1's role in complex IV activity or an independent function is unknown","USP7–CMC1 interaction site and ubiquitination sites on CMC1 were not mapped"]},{"year":null,"claim":"How CMC1 mechanistically stabilizes COX1 within the early assembly intermediate — whether through direct protein contact, chaperoning of cofactor insertion, or prevention of degradation — remains unresolved, and no high-resolution structural model of the CMC1-containing intermediate exists.","evidence":"","pmids":[],"confidence":"High","gaps":["No structural model of CMC1 or the COX1–COA3–COX14–CMC1 intermediate","No direct binding assay between CMC1 and COX1","Functional relationship between CMC1 and COX1 metallation factors is undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0044183","term_label":"protein folding chaperone","supporting_discovery_ids":[0,1]}],"localization":[{"term_id":"GO:0005739","term_label":"mitochondrion","supporting_discovery_ids":[0,1,2]}],"pathway":[{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[0,1]}],"complexes":["COX1-COA3-COX14-CMC1 early CIV assembly intermediate"],"partners":["COX1","COA3","COX14","CMC2","MIA40","ERV1","USP7"],"other_free_text":[]},"mechanistic_narrative":"CMC1 is a mitochondrial intermembrane space twin CX9C protein that functions in the early stages of cytochrome c oxidase (complex IV) assembly by stabilizing newly synthesized COX1 within an intermediate containing COA3 and COX14, prior to incorporation of COX4 and COX5a subunits, without affecting COX1 mRNA translation [PMID:28082314, PMID:20220131]. CMC1 is imported into the intermembrane space via the Mia40/Erv1 oxidative folding pathway, forming a ternary complex with Mia40 and Erv1 during its biogenesis [PMID:22767599]. In yeast, Cmc1 physically interacts with Cmc2, and their cooperative but non-redundant functions are required for normal cytochrome c oxidase activity [PMID:20220131]. Lactate-driven USP7-mediated de-ubiquitination stabilizes CMC1 in CD8+ T cells, where it promotes terminal differentiation and exhaustion [PMID:38659649]."},"prefetch_data":{"uniprot":{"accession":"Q7Z7K0","full_name":"COX assembly mitochondrial protein homolog","aliases":[],"length_aa":106,"mass_kda":12.5,"function":"Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly","subcellular_location":"Mitochondrion","url":"https://www.uniprot.org/uniprotkb/Q7Z7K0/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CMC1","classification":"Not Classified","n_dependent_lines":96,"n_total_lines":1208,"dependency_fraction":0.07947019867549669},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/CMC1","total_profiled":1310},"omim":[{"mim_id":"615166","title":"C-X9-C MOTIF-CONTAINING 1; CMC1","url":"https://www.omim.org/entry/615166"},{"mim_id":"608354","title":"CAPILLARY MALFORMATION-ARTERIOVENOUS MALFORMATION 1; CMAVM1","url":"https://www.omim.org/entry/608354"},{"mim_id":"607850","title":"OSTEOARTHRITIS SUSCEPTIBILITY 3; OS3","url":"https://www.omim.org/entry/607850"},{"mim_id":"602089","title":"HEMANGIOMA, CAPILLARY INFANTILE","url":"https://www.omim.org/entry/602089"},{"mim_id":"600998","title":"GUANINE NUCLEOTIDE-BINDING PROTEIN, Q POLYPEPTIDE; GNAQ","url":"https://www.omim.org/entry/600998"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/CMC1"},"hgnc":{"alias_symbol":["MGC61571"],"prev_symbol":["C3orf68"]},"alphafold":{"accession":"Q7Z7K0","domains":[{"cath_id":"-","chopping":"24-90","consensus_level":"high","plddt":93.5391,"start":24,"end":90}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q7Z7K0","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q7Z7K0-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q7Z7K0-F1-predicted_aligned_error_v6.png","plddt_mean":87.0},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CMC1","jax_strain_url":"https://www.jax.org/strain/search?query=CMC1"},"sequence":{"accession":"Q7Z7K0","fasta_url":"https://rest.uniprot.org/uniprotkb/Q7Z7K0.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q7Z7K0/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q7Z7K0"}},"corpus_meta":[{"pmid":"28082314","id":"PMC_28082314","title":"A CMC1-knockout reveals translation-independent control of human mitochondrial complex IV biogenesis.","date":"2017","source":"EMBO reports","url":"https://pubmed.ncbi.nlm.nih.gov/28082314","citation_count":64,"is_preprint":false},{"pmid":"18704277","id":"PMC_18704277","title":"Catalytic and thermodynamic characterization of endoglucanase (CMCase) from Aspergillus oryzae cmc-1.","date":"2008","source":"Applied biochemistry and biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/18704277","citation_count":47,"is_preprint":false},{"pmid":"19010064","id":"PMC_19010064","title":"High hand joint mobility is associated with radiological CMC1 osteoarthritis: the AGES-Reykjavik study.","date":"2008","source":"Osteoarthritis and cartilage","url":"https://pubmed.ncbi.nlm.nih.gov/19010064","citation_count":41,"is_preprint":false},{"pmid":"20220131","id":"PMC_20220131","title":"The conserved mitochondrial twin Cx9C protein Cmc2 Is a Cmc1 homologue essential for cytochrome c oxidase biogenesis.","date":"2010","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/20220131","citation_count":34,"is_preprint":false},{"pmid":"22767599","id":"PMC_22767599","title":"Role of twin Cys-Xaa9-Cys motif cysteines in mitochondrial import of the cytochrome C oxidase biogenesis factor Cmc1.","date":"2012","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/22767599","citation_count":24,"is_preprint":false},{"pmid":"38659649","id":"PMC_38659649","title":"The potential role of CMC1 as an immunometabolic checkpoint in T cell immunity.","date":"2024","source":"Oncoimmunology","url":"https://pubmed.ncbi.nlm.nih.gov/38659649","citation_count":10,"is_preprint":false},{"pmid":"18661108","id":"PMC_18661108","title":"Improvement of Aspergillus oryzae for hyperproduction of endoglucanase: expression cloning of cmc-1 gene of Aspergillus aculeatus.","date":"2008","source":"Biotechnology letters","url":"https://pubmed.ncbi.nlm.nih.gov/18661108","citation_count":9,"is_preprint":false},{"pmid":"39513308","id":"PMC_39513308","title":"The Risk Genes S1PR5, CMC1, and ASAH1 as Potential Targets for the Diagnosis, Immunotherapy, and Treatment of Colon Adenocarcinoma by Single-Cell and Bulk RNA Sequencing Analysis.","date":"2024","source":"Current medicinal chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/39513308","citation_count":7,"is_preprint":false},{"pmid":"32060600","id":"PMC_32060600","title":"Directed modification of a ruminal cellulase gene (CMC-1) from a metagenomic library isolated from Yunnan gayal (Bos frontalis).","date":"2020","source":"Archives of microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/32060600","citation_count":6,"is_preprint":false},{"pmid":"9933935","id":"PMC_9933935","title":"Cloning and complete nucleotide sequence of Acinetobacter radioresistens CMC-1 AglyA gene encoding serine hydroxymethyltransferase.","date":"1999","source":"FEMS microbiology letters","url":"https://pubmed.ncbi.nlm.nih.gov/9933935","citation_count":3,"is_preprint":false},{"pmid":"41688906","id":"PMC_41688906","title":"Transcriptomics and proteomics insights into carotenoid differentiation in tissue cultured Rehmannia glutinosa root cambial meristematic cells: REG-CMC1 and non-somaclonal REG-CMC2.","date":"2026","source":"BMC plant biology","url":"https://pubmed.ncbi.nlm.nih.gov/41688906","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.10.16.682832","title":"Decoding the human PBMC isonome: Isoform-level resolution with single-cell long-read transcriptomics","date":"2025-10-17","source":"bioRxiv","url":"https://doi.org/10.1101/2025.10.16.682832","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.09.26.615232","title":"Subchondral bone marrow adipose tissue lipolysis regulates bone formation in hand osteoarthritis","date":"2024-09-29","source":"bioRxiv","url":"https://doi.org/10.1101/2024.09.26.615232","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7909,"output_tokens":1107,"usd":0.020166},"stage2":{"model":"claude-opus-4-6","input_tokens":4305,"output_tokens":1581,"usd":0.091575},"total_usd":0.111741,"stage1_batch_id":"msgbatch_011kfMfE81o6CTcyhVUqumuW","stage2_batch_id":"msgbatch_01DTputS6WNkH745x1nVSoBo","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"CMC1 forms an early cytochrome c oxidase (CIV) assembly intermediate with COX1 and assembly factors COA3 and COX14 in the mitochondrial intermembrane space, stabilizing newly synthesized COX1 prior to incorporation of COX4 and COX5a subunits, without affecting COX1 mRNA translation rate.\",\n      \"method\": \"TALEN-mediated CMC1 knockout in HEK293T cells; co-immunoprecipitation; pulse-chase labeling of mitochondrial translation products; CIV activity assay\",\n      \"journal\": \"EMBO reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal Co-IP, clean KO with defined biochemical phenotype, and orthogonal translation assay in one study\",\n      \"pmids\": [\"28082314\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Yeast Cmc1 (ortholog of human CMC1) is a mitochondrial intermembrane space twin Cx9C protein required for cytochrome c oxidase biogenesis; it physically interacts with Cmc2, and absence of Cmc2 causes a 5-fold increase in Cmc1 accumulation, indicating cooperative but non-redundant functions.\",\n      \"method\": \"Subcellular fractionation, spectrophotometric CIV activity assay, polarographic respiration measurement, co-immunoprecipitation, genetic complementation\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal interaction demonstrated, clean KO phenotype, multiple orthogonal methods, replicated across yeast and C. elegans\",\n      \"pmids\": [\"20220131\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"CMC1 (a twin CX9C protein) is imported into the mitochondrial intermembrane space via the Mia40/Erv1 oxidative folding pathway; CMC1 forms a stable intermediate with Mia40 and is released upon addition of Erv1, with all three proteins forming a ternary complex in mitochondria. Efficient oxidation of CMC1 requires both Mia40 and Erv1.\",\n      \"method\": \"In vitro oxidative folding assay, in organello import assay, co-immunoprecipitation, ternary complex detection\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1-2 — in vitro reconstitution combined with in organello validation and co-IP of ternary complex\",\n      \"pmids\": [\"22767599\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"CMC1 acts as a positive regulator of CD8+ T cell activation and terminal differentiation/exhaustion; environmental lactate enhances CMC1 expression by inducing USP7, which stabilizes CMC1 through de-ubiquitination. Genetic loss of Cmc1 in T cells inhibits exhaustion and promotes memory-like differentiation.\",\n      \"method\": \"Cmc1 knockout mice, in vitro T cell culture, B16-OVA tumor model, mechanistic studies of USP7-mediated CMC1 de-ubiquitination\",\n      \"journal\": \"Oncoimmunology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2-3 — clean KO with defined cellular phenotype and identification of USP7 as a deubiquitinase writer, but mechanistic pathway placement relies on single study\",\n      \"pmids\": [\"38659649\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CMC1 is a mitochondrial intermembrane space twin CX9C protein imported via the Mia40/Erv1 oxidative folding pathway that stabilizes newly synthesized COX1 within an early COX1-COA3-COX14 assembly intermediate during cytochrome c oxidase biogenesis, acts independently of COX1 metallation factors, and is also regulated by lactate-induced USP7-mediated de-ubiquitination to modulate CD8+ T cell exhaustion.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"CMC1 is a mitochondrial intermembrane space twin CX9C protein that functions in the early stages of cytochrome c oxidase (complex IV) assembly by stabilizing newly synthesized COX1 within an intermediate containing COA3 and COX14, prior to incorporation of COX4 and COX5a subunits, without affecting COX1 mRNA translation [PMID:28082314, PMID:20220131]. CMC1 is imported into the intermembrane space via the Mia40/Erv1 oxidative folding pathway, forming a ternary complex with Mia40 and Erv1 during its biogenesis [PMID:22767599]. In yeast, Cmc1 physically interacts with Cmc2, and their cooperative but non-redundant functions are required for normal cytochrome c oxidase activity [PMID:20220131]. Lactate-driven USP7-mediated de-ubiquitination stabilizes CMC1 in CD8+ T cells, where it promotes terminal differentiation and exhaustion [PMID:38659649].\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"Establishing CMC1 as a mitochondrial factor required for cytochrome c oxidase biogenesis resolved its basic cellular function and revealed a functional partnership with Cmc2 in the intermembrane space.\",\n      \"evidence\": \"Yeast Cmc1 deletion with spectrophotometric CIV activity assay, respiration measurement, co-immunoprecipitation of Cmc1–Cmc2 interaction, and cross-species complementation\",\n      \"pmids\": [\"20220131\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Precise step in CIV assembly where Cmc1 acts was not defined\",\n        \"Whether the Cmc1–Cmc2 interaction is direct or bridged was not resolved\",\n        \"Mechanism by which Cmc2 loss elevates Cmc1 levels was not determined\"\n      ]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Demonstrating that CMC1 is imported via the Mia40/Erv1 oxidative folding pathway and forms a ternary complex with these factors established how CMC1 reaches its functional compartment.\",\n      \"evidence\": \"In vitro oxidative folding reconstitution, in organello import assay, and co-immunoprecipitation of CMC1–Mia40–Erv1 ternary complex\",\n      \"pmids\": [\"22767599\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether import efficiency regulates CMC1 steady-state levels under physiological conditions was not tested\",\n        \"Structural basis of the twin CX9C motif recognition by Mia40 for CMC1 specifically was not resolved\"\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Placing CMC1 in an early COX1–COA3–COX14 assembly intermediate and showing it stabilizes COX1 post-translationally (without affecting translation) pinpointed its precise role in complex IV biogenesis.\",\n      \"evidence\": \"TALEN-mediated CMC1 knockout in HEK293T cells with co-immunoprecipitation, pulse-chase mitochondrial translation labeling, and CIV activity assay\",\n      \"pmids\": [\"28082314\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether CMC1 contacts COX1 directly or solely through COA3/COX14 was not determined\",\n        \"Relationship between CMC1 function and COX1 metallation (copper/heme insertion) was not clarified\",\n        \"No structural information on the early assembly intermediate\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Discovery that lactate-induced USP7-mediated de-ubiquitination stabilizes CMC1 and that CMC1 promotes CD8+ T cell exhaustion expanded its functional scope beyond mitochondrial assembly to immune cell fate regulation.\",\n      \"evidence\": \"Cmc1 knockout mice, in vitro T cell culture, B16-OVA tumor model, mechanistic studies of USP7-mediated de-ubiquitination\",\n      \"pmids\": [\"38659649\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single study without independent replication of the T cell exhaustion phenotype\",\n        \"Whether the T cell effect depends on CMC1's role in complex IV activity or an independent function is unknown\",\n        \"USP7–CMC1 interaction site and ubiquitination sites on CMC1 were not mapped\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How CMC1 mechanistically stabilizes COX1 within the early assembly intermediate — whether through direct protein contact, chaperoning of cofactor insertion, or prevention of degradation — remains unresolved, and no high-resolution structural model of the CMC1-containing intermediate exists.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No structural model of CMC1 or the COX1–COA3–COX14–CMC1 intermediate\",\n        \"No direct binding assay between CMC1 and COX1\",\n        \"Functional relationship between CMC1 and COX1 metallation factors is undefined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0044183\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\n      \"COX1-COA3-COX14-CMC1 early CIV assembly intermediate\"\n    ],\n    \"partners\": [\n      \"COX1\",\n      \"COA3\",\n      \"COX14\",\n      \"CMC2\",\n      \"MIA40\",\n      \"ERV1\",\n      \"USP7\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}