{"gene":"ZCCHC10","run_date":"2026-06-11T09:02:06","timeline":{"discoveries":[{"year":2019,"finding":"ZCCHC10 physically binds p53 and disrupts the p53-MDM2 interaction, thereby blocking MDM2-mediated ubiquitination and degradation of p53 and stabilizing the p53 protein. This activity requires wild-type p53, as ZCCHC10 had no effect on p53-null or p53-mutant lung cancer cells.","method":"Co-immunoprecipitation, overexpression/knockdown in lung cancer cell lines, p53 inhibitor (pifithrin-α) and activator (Nutlin3) rescue experiments, in vivo tumor xenograft assays","journal":"Cell death & disease","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal co-IP demonstrating protein-protein interaction, epistasis via pharmacological rescue (pifithrin-α and Nutlin3), orthogonal in vitro and in vivo validation in a single study","pmids":["31138778"],"is_preprint":false},{"year":2019,"finding":"ZCCHC10 interacts with the homeodomain transcription factor PITX1 (identified by FLAG pull-down assay), and the ZCCHC10–PITX1 complex cooperatively suppresses transcription of the hTERT gene promoter in melanoma cells. Deletion of the homeodomain region of PITX1 that mediates interaction with ZCCHC10 abolished hTERT transcriptional repression.","method":"FLAG pull-down assay, co-expression rescue, luciferase/transcriptional reporter assays, homeodomain deletion mutagenesis of PITX1","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal pull-down and mutagenesis in a single lab, two orthogonal methods (pull-down + transcription assay with deletion mutant)","pmids":["31404068"],"is_preprint":false},{"year":2021,"finding":"miR-410-3p directly targets the ZCCHC10 3′UTR (validated by dual-luciferase reporter assay), reducing ZCCHC10 protein levels. Loss of ZCCHC10 activates the NF-κB signaling pathway, promoting epithelial-mesenchymal transition (EMT), cell migration, and invasion in colorectal cancer cells. NF-κB inhibitor BAY 11-7082 rescued the pro-invasive phenotype caused by ZCCHC10 knockdown, and ZCCHC10 overexpression reversed miR-410-3p-driven effects.","method":"Dual-luciferase reporter assay, siRNA knockdown, miRNA mimic overexpression, NF-κB inhibitor rescue, wound-healing and Transwell invasion assays, western blot","journal":"Cytokine","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — dual-luciferase validation of direct miRNA targeting, pharmacological epistasis, and rescue by ZCCHC10 overexpression in single lab","pmids":["33517196"],"is_preprint":false},{"year":2023,"finding":"The lncRNA SNHG1 epigenetically silences ZCCHC10 by binding simultaneously to the ZCCHC10 promoter CpG island and to DNA methyltransferases DNMT1 and DNMT3B, thereby recruiting them to the promoter and inducing hypermethylation. Overexpression of SNHG1 with deletion of its ZCCHC10-promoter binding motif failed to induce methylation, confirming sequence-specificity. Suppression of SNHG1 decreased ZCCHC10 promoter methylation and restored ZCCHC10 expression, which in turn increased p53 levels, suppressed AML cell proliferation, and sensitized cells to venetoclax.","method":"ChIP/promoter methylation assays, SNHG1 deletion mutant overexpression, RNA immunoprecipitation (SNHG1–DNMT1/DNMT3B interaction), ZCCHC10 overexpression in AML cell lines, xenograft mouse model","journal":"International journal of oncology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (promoter methylation, RNA-IP, deletion mutagenesis, in vivo xenograft) in a single lab","pmids":["37052262"],"is_preprint":false}],"current_model":"ZCCHC10 is a tumor suppressor that stabilizes p53 by directly binding p53 and competitively disrupting the p53–MDM2 interaction to block ubiquitin-mediated degradation; it also forms a complex with the transcription factor PITX1 to repress hTERT transcription, is targeted for silencing by miR-410-3p (leading to NF-κB-dependent EMT) and by SNHG1-recruited DNMT1/DNMT3B-mediated promoter hypermethylation, collectively placing ZCCHC10 at the intersection of p53 stabilization, telomerase regulation, and NF-κB-driven invasion."},"narrative":{"mechanistic_narrative":"ZCCHC10 is a tumor suppressor that converges on p53 stabilization and telomerase repression to restrain cancer cell proliferation and invasion [PMID:31138778, PMID:31404068]. It directly binds p53 and competitively disrupts the p53–MDM2 interaction, blocking MDM2-mediated ubiquitination and degradation and thereby stabilizing p53 protein; this activity is strictly dependent on wild-type p53, as ZCCHC10 has no effect in p53-null or p53-mutant lung cancer cells [PMID:31138778]. Independently, ZCCHC10 interacts with the homeodomain transcription factor PITX1 through PITX1's homeodomain, and the resulting complex cooperatively represses transcription from the hTERT promoter [PMID:31404068]. ZCCHC10 expression is itself subject to negative regulation: miR-410-3p directly targets its 3′UTR to lower ZCCHC10 protein, and loss of ZCCHC10 derepresses NF-κB signaling to drive epithelial–mesenchymal transition, migration, and invasion in colorectal cancer cells [PMID:33517196]; in acute myeloid leukemia, the lncRNA SNHG1 silences ZCCHC10 by recruiting DNMT1 and DNMT3B to its promoter CpG island for hypermethylation, and restoring ZCCHC10 raises p53 levels, suppresses proliferation, and sensitizes cells to venetoclax [PMID:37052262]. The biochemical activity of the ZCCHC10 protein itself beyond these binding-mediated functions has not been characterized in the available corpus.","teleology":[{"year":2019,"claim":"Established ZCCHC10 as a direct p53-stabilizing tumor suppressor, defining its first mechanistic role by showing it physically guards p53 from MDM2-driven degradation.","evidence":"Co-IP, overexpression/knockdown in lung cancer lines, pifithrin-α/Nutlin3 epistasis rescue, and xenograft assays","pmids":["31138778"],"confidence":"High","gaps":["Does not map which ZCCHC10 domain or residues mediate p53 binding or MDM2 displacement","No structural model of the ZCCHC10–p53 complex","Whether ZCCHC10 itself has enzymatic activity is unaddressed"]},{"year":2019,"claim":"Revealed a second, p53-independent output by showing ZCCHC10 partners with PITX1 to transcriptionally repress hTERT, linking it to telomerase control.","evidence":"FLAG pull-down, transcriptional reporter assays, and PITX1 homeodomain deletion mutagenesis in melanoma cells","pmids":["31404068"],"confidence":"Medium","gaps":["Reciprocal interaction shown in a single lab","How ZCCHC10 contributes mechanistically to repression (DNA binding vs. cofactor recruitment) is unresolved","Relationship between hTERT repression and the p53 axis is not integrated"]},{"year":2021,"claim":"Identified an upstream silencing mechanism and a downstream invasion phenotype, showing miR-410-3p suppresses ZCCHC10 to unleash NF-κB-driven EMT.","evidence":"Dual-luciferase 3′UTR reporter, miRNA mimic/siRNA, BAY 11-7082 NF-κB inhibitor rescue, and migration/invasion assays in colorectal cancer cells","pmids":["33517196"],"confidence":"Medium","gaps":["How ZCCHC10 loss mechanistically activates NF-κB is not defined","Whether NF-κB regulation depends on the p53 axis is untested","Single-lab validation"]},{"year":2023,"claim":"Demonstrated epigenetic silencing of ZCCHC10 in AML and connected its restoration to p53 elevation and drug sensitivity, reinforcing the tumor-suppressor model therapeutically.","evidence":"Promoter methylation/ChIP, SNHG1–DNMT1/DNMT3B RNA-IP, SNHG1 deletion mutants, ZCCHC10 overexpression, and venetoclax sensitization in AML lines and xenografts","pmids":["37052262"],"confidence":"Medium","gaps":["Does not establish whether the p53 increase is direct or secondary to proliferation arrest","Single-lab study","Generality of SNHG1-driven silencing across other cancers unknown"]},{"year":null,"claim":"The intrinsic biochemical activity of the ZCCHC10 protein and how its multiple binding-mediated roles (p53 stabilization, PITX1/hTERT repression, NF-κB restraint) are coordinated remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No defined catalytic or nucleic-acid-binding activity for ZCCHC10","No structural characterization of any ZCCHC10 complex","Whether the p53, telomerase, and NF-κB functions operate in the same cells or are tissue-specific is unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[1]}],"localization":[],"pathway":[{"term_id":"R-HSA-5357801","term_label":"Programmed Cell Death","supporting_discovery_ids":[0]}],"complexes":[],"partners":["TP53","PITX1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8TBK6","full_name":"Zinc finger CCHC domain-containing protein 10","aliases":[],"length_aa":192,"mass_kda":21.0,"function":"","subcellular_location":"","url":"https://www.uniprot.org/uniprotkb/Q8TBK6/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/ZCCHC10","classification":"Not Classified","n_dependent_lines":4,"n_total_lines":1208,"dependency_fraction":0.0033112582781456954},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"CPSF6","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/ZCCHC10","total_profiled":1310},"omim":[],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoli rim","reliability":"Approved"},{"location":"Nucleoplasm","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/ZCCHC10"},"hgnc":{"alias_symbol":["FLJ20094"],"prev_symbol":[]},"alphafold":{"accession":"Q8TBK6","domains":[{"cath_id":"-","chopping":"39-95","consensus_level":"medium","plddt":81.9133,"start":39,"end":95}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8TBK6","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8TBK6-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8TBK6-F1-predicted_aligned_error_v6.png","plddt_mean":62.84},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=ZCCHC10","jax_strain_url":"https://www.jax.org/strain/search?query=ZCCHC10"},"sequence":{"accession":"Q8TBK6","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8TBK6.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8TBK6/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8TBK6"}},"corpus_meta":[{"pmid":"24243566","id":"PMC_24243566","title":"Maternal preconception body mass index and offspring cord blood DNA methylation: exploration of early life origins of disease.","date":"2013","source":"Environmental and molecular mutagenesis","url":"https://pubmed.ncbi.nlm.nih.gov/24243566","citation_count":101,"is_preprint":false},{"pmid":"33517196","id":"PMC_33517196","title":"MiR-410-3p activates the NF-κB pathway by targeting ZCCHC10 to promote migration, invasion and EMT of colorectal cancer.","date":"2021","source":"Cytokine","url":"https://pubmed.ncbi.nlm.nih.gov/33517196","citation_count":26,"is_preprint":false},{"pmid":"31138778","id":"PMC_31138778","title":"ZCCHC10 suppresses lung cancer progression and cisplatin resistance by attenuating MDM2-mediated p53 ubiquitination and degradation.","date":"2019","source":"Cell death & disease","url":"https://pubmed.ncbi.nlm.nih.gov/31138778","citation_count":24,"is_preprint":false},{"pmid":"31404068","id":"PMC_31404068","title":"PITX1 protein interacts with ZCCHC10 to regulate hTERT mRNA transcription.","date":"2019","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/31404068","citation_count":20,"is_preprint":false},{"pmid":"30984102","id":"PMC_30984102","title":"Identification of Shared Genes Between Ischemic Stroke and Parkinson's Disease Using Genome-Wide Association Studies.","date":"2019","source":"Frontiers in neurology","url":"https://pubmed.ncbi.nlm.nih.gov/30984102","citation_count":14,"is_preprint":false},{"pmid":"37052262","id":"PMC_37052262","title":"Epigenetic silencing of ZCCHC10 by the lncRNA SNHG1 promotes progression and venetoclax resistance of acute myeloid leukemia.","date":"2023","source":"International journal of oncology","url":"https://pubmed.ncbi.nlm.nih.gov/37052262","citation_count":11,"is_preprint":false},{"pmid":"37511041","id":"PMC_37511041","title":"Epigenomics Analysis of the Suppression Role of SIRT1 via H3K9 Deacetylation in Preadipocyte Differentiation.","date":"2023","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/37511041","citation_count":11,"is_preprint":false},{"pmid":"28842203","id":"PMC_28842203","title":"Analysis of the peptides detected in atopic dermatitis and various inflammatory diseases patients-derived sera.","date":"2017","source":"International journal of biological macromolecules","url":"https://pubmed.ncbi.nlm.nih.gov/28842203","citation_count":7,"is_preprint":false},{"pmid":"41143260","id":"PMC_41143260","title":"Iso-seq and RNA-seq data from ML-2 acute myeloid leukemia cells overexpressing the ZCCHC10 gene.","date":"2025","source":"Data in brief","url":"https://pubmed.ncbi.nlm.nih.gov/41143260","citation_count":1,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7127,"output_tokens":1411,"usd":0.021273,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8078,"output_tokens":2075,"usd":0.046132,"stage2_stop_reason":"end_turn"},"total_usd":0.067405,"stage1_batch_id":"msgbatch_01UT1AahFPCAyn2uVweS7A9z","stage2_batch_id":"msgbatch_01HuKWtKNT4Pqj1bc8eEP5RV","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2019,\n      \"finding\": \"ZCCHC10 physically binds p53 and disrupts the p53-MDM2 interaction, thereby blocking MDM2-mediated ubiquitination and degradation of p53 and stabilizing the p53 protein. This activity requires wild-type p53, as ZCCHC10 had no effect on p53-null or p53-mutant lung cancer cells.\",\n      \"method\": \"Co-immunoprecipitation, overexpression/knockdown in lung cancer cell lines, p53 inhibitor (pifithrin-α) and activator (Nutlin3) rescue experiments, in vivo tumor xenograft assays\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal co-IP demonstrating protein-protein interaction, epistasis via pharmacological rescue (pifithrin-α and Nutlin3), orthogonal in vitro and in vivo validation in a single study\",\n      \"pmids\": [\"31138778\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"ZCCHC10 interacts with the homeodomain transcription factor PITX1 (identified by FLAG pull-down assay), and the ZCCHC10–PITX1 complex cooperatively suppresses transcription of the hTERT gene promoter in melanoma cells. Deletion of the homeodomain region of PITX1 that mediates interaction with ZCCHC10 abolished hTERT transcriptional repression.\",\n      \"method\": \"FLAG pull-down assay, co-expression rescue, luciferase/transcriptional reporter assays, homeodomain deletion mutagenesis of PITX1\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal pull-down and mutagenesis in a single lab, two orthogonal methods (pull-down + transcription assay with deletion mutant)\",\n      \"pmids\": [\"31404068\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"miR-410-3p directly targets the ZCCHC10 3′UTR (validated by dual-luciferase reporter assay), reducing ZCCHC10 protein levels. Loss of ZCCHC10 activates the NF-κB signaling pathway, promoting epithelial-mesenchymal transition (EMT), cell migration, and invasion in colorectal cancer cells. NF-κB inhibitor BAY 11-7082 rescued the pro-invasive phenotype caused by ZCCHC10 knockdown, and ZCCHC10 overexpression reversed miR-410-3p-driven effects.\",\n      \"method\": \"Dual-luciferase reporter assay, siRNA knockdown, miRNA mimic overexpression, NF-κB inhibitor rescue, wound-healing and Transwell invasion assays, western blot\",\n      \"journal\": \"Cytokine\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — dual-luciferase validation of direct miRNA targeting, pharmacological epistasis, and rescue by ZCCHC10 overexpression in single lab\",\n      \"pmids\": [\"33517196\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"The lncRNA SNHG1 epigenetically silences ZCCHC10 by binding simultaneously to the ZCCHC10 promoter CpG island and to DNA methyltransferases DNMT1 and DNMT3B, thereby recruiting them to the promoter and inducing hypermethylation. Overexpression of SNHG1 with deletion of its ZCCHC10-promoter binding motif failed to induce methylation, confirming sequence-specificity. Suppression of SNHG1 decreased ZCCHC10 promoter methylation and restored ZCCHC10 expression, which in turn increased p53 levels, suppressed AML cell proliferation, and sensitized cells to venetoclax.\",\n      \"method\": \"ChIP/promoter methylation assays, SNHG1 deletion mutant overexpression, RNA immunoprecipitation (SNHG1–DNMT1/DNMT3B interaction), ZCCHC10 overexpression in AML cell lines, xenograft mouse model\",\n      \"journal\": \"International journal of oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (promoter methylation, RNA-IP, deletion mutagenesis, in vivo xenograft) in a single lab\",\n      \"pmids\": [\"37052262\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"ZCCHC10 is a tumor suppressor that stabilizes p53 by directly binding p53 and competitively disrupting the p53–MDM2 interaction to block ubiquitin-mediated degradation; it also forms a complex with the transcription factor PITX1 to repress hTERT transcription, is targeted for silencing by miR-410-3p (leading to NF-κB-dependent EMT) and by SNHG1-recruited DNMT1/DNMT3B-mediated promoter hypermethylation, collectively placing ZCCHC10 at the intersection of p53 stabilization, telomerase regulation, and NF-κB-driven invasion.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ZCCHC10 is a tumor suppressor that converges on p53 stabilization and telomerase repression to restrain cancer cell proliferation and invasion [#0, #1]. It directly binds p53 and competitively disrupts the p53–MDM2 interaction, blocking MDM2-mediated ubiquitination and degradation and thereby stabilizing p53 protein; this activity is strictly dependent on wild-type p53, as ZCCHC10 has no effect in p53-null or p53-mutant lung cancer cells [#0]. Independently, ZCCHC10 interacts with the homeodomain transcription factor PITX1 through PITX1's homeodomain, and the resulting complex cooperatively represses transcription from the hTERT promoter [#1]. ZCCHC10 expression is itself subject to negative regulation: miR-410-3p directly targets its 3′UTR to lower ZCCHC10 protein, and loss of ZCCHC10 derepresses NF-κB signaling to drive epithelial–mesenchymal transition, migration, and invasion in colorectal cancer cells [#2]; in acute myeloid leukemia, the lncRNA SNHG1 silences ZCCHC10 by recruiting DNMT1 and DNMT3B to its promoter CpG island for hypermethylation, and restoring ZCCHC10 raises p53 levels, suppresses proliferation, and sensitizes cells to venetoclax [#3]. The biochemical activity of the ZCCHC10 protein itself beyond these binding-mediated functions has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2019,\n      \"claim\": \"Established ZCCHC10 as a direct p53-stabilizing tumor suppressor, defining its first mechanistic role by showing it physically guards p53 from MDM2-driven degradation.\",\n      \"evidence\": \"Co-IP, overexpression/knockdown in lung cancer lines, pifithrin-α/Nutlin3 epistasis rescue, and xenograft assays\",\n      \"pmids\": [\"31138778\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Does not map which ZCCHC10 domain or residues mediate p53 binding or MDM2 displacement\",\n        \"No structural model of the ZCCHC10–p53 complex\",\n        \"Whether ZCCHC10 itself has enzymatic activity is unaddressed\"\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Revealed a second, p53-independent output by showing ZCCHC10 partners with PITX1 to transcriptionally repress hTERT, linking it to telomerase control.\",\n      \"evidence\": \"FLAG pull-down, transcriptional reporter assays, and PITX1 homeodomain deletion mutagenesis in melanoma cells\",\n      \"pmids\": [\"31404068\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Reciprocal interaction shown in a single lab\",\n        \"How ZCCHC10 contributes mechanistically to repression (DNA binding vs. cofactor recruitment) is unresolved\",\n        \"Relationship between hTERT repression and the p53 axis is not integrated\"\n      ]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Identified an upstream silencing mechanism and a downstream invasion phenotype, showing miR-410-3p suppresses ZCCHC10 to unleash NF-κB-driven EMT.\",\n      \"evidence\": \"Dual-luciferase 3′UTR reporter, miRNA mimic/siRNA, BAY 11-7082 NF-κB inhibitor rescue, and migration/invasion assays in colorectal cancer cells\",\n      \"pmids\": [\"33517196\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"How ZCCHC10 loss mechanistically activates NF-κB is not defined\",\n        \"Whether NF-κB regulation depends on the p53 axis is untested\",\n        \"Single-lab validation\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Demonstrated epigenetic silencing of ZCCHC10 in AML and connected its restoration to p53 elevation and drug sensitivity, reinforcing the tumor-suppressor model therapeutically.\",\n      \"evidence\": \"Promoter methylation/ChIP, SNHG1–DNMT1/DNMT3B RNA-IP, SNHG1 deletion mutants, ZCCHC10 overexpression, and venetoclax sensitization in AML lines and xenografts\",\n      \"pmids\": [\"37052262\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Does not establish whether the p53 increase is direct or secondary to proliferation arrest\",\n        \"Single-lab study\",\n        \"Generality of SNHG1-driven silencing across other cancers unknown\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The intrinsic biochemical activity of the ZCCHC10 protein and how its multiple binding-mediated roles (p53 stabilization, PITX1/hTERT repression, NF-κB restraint) are coordinated remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No defined catalytic or nucleic-acid-binding activity for ZCCHC10\",\n        \"No structural characterization of any ZCCHC10 complex\",\n        \"Whether the p53, telomerase, and NF-κB functions operate in the same cells or are tissue-specific is unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5357801\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"TP53\", \"PITX1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":4,"faith_total":4,"faith_pct":100.0}}