{"gene":"GMNN","run_date":"2026-06-10T01:55:21","timeline":{"discoveries":[{"year":2015,"finding":"De novo heterozygous truncating or missense mutations in GMNN that alter sites 5' to residue Met28 (within the destruction box) result in geminin proteins lacking the destruction box, conferring increased protein stability and prolonged inhibition of DNA replication. The anaphase-promoting complex (APC) normally recognizes the destruction box near the 5' end of geminin to degrade it during the metaphase-anaphase transition; mutations disrupting this sequence prevent APC-mediated degradation, constituting a gain-of-function mechanism causing autosomal-dominant Meier-Gorlin syndrome.","method":"Human genetics (identification of de novo mutations) combined with cell-cycle phase analysis; mechanistic interpretation supported by known APC-destruction box biology and functional data on protein stability","journal":"American journal of human genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — human genetic evidence with mechanistic interpretation of destruction-box loss; single study but multiple mutations converging on same mechanism","pmids":["26637980"],"is_preprint":false},{"year":2025,"finding":"Rare dominant missense mutations in GMNN decrease geminin's binding to CDT1, leading to activation of CHK1, DNA damage, and cell cycle disturbance, resulting in preimplantation embryo arrest. This establishes that geminin prevents DNA re-replication by inhibiting CDT1, and that impaired geminin–CDT1 interaction disrupts correct cell cycle progression in early embryos.","method":"Whole-exome sequencing and Sanger sequencing in patients; RNA sequencing of mouse zygotes and patient one-cell embryo; binding assay (CDT1 interaction) and assessment of CHK1 activation and DNA damage markers","journal":"Science China. Life sciences","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — binding assay plus DNA damage/CHK1 readouts in a single study; multiple orthogonal methods but single lab","pmids":["40455380"],"is_preprint":false},{"year":2018,"finding":"Fusion of Cas9 to the N-terminal peptide of GMNN (geminin) causes the Cas9 fusion protein to be degraded during NHEJ-dominated cell cycle phases (G1), thereby enriching Cas9 activity in S/G2 phases where HDR predominates, resulting in an approximately two-fold increase in homology-directed repair knock-in frequency in porcine fibroblasts.","method":"CRISPR/Cas9-GMNN fusion construct expressed in porcine fetal fibroblasts; point mutation-specific real-time PCR screening for HDR events","journal":"Genes","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional cell-based assay exploiting known cell-cycle-dependent degradation of geminin N-terminal peptide; single lab, single method","pmids":["29899280"],"is_preprint":false},{"year":2025,"finding":"Truncated forms of the human GMNN protein (lacking full-length sequences but retaining degradation signals) are reciprocally degraded relative to CDT1-derived fragments across the cell cycle, allowing fluorescent fusions to distinguish S, G2, and M phases from G1. This confirms that GMNN protein levels are cell-cycle-regulated through phase-specific proteolysis, enabling its use as a biosensor for S/G2/M phases.","method":"Fucci(CA) cell cycle biosensor system using fluorescently tagged truncated GMNN in transgenic chicken line (FuChi); in vitro and in vivo live imaging","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct live-cell imaging with functional validation across multiple tissues; preprint, single study","pmids":[],"is_preprint":true}],"current_model":"Geminin (GMNN) prevents DNA re-replication by binding and inhibiting CDT1; its protein levels are cell-cycle-regulated through APC-mediated destruction-box-dependent degradation at the metaphase-anaphase transition (present in S/G2/M, absent in G1), and mutations that disrupt the destruction box or the CDT1-binding interface cause gain-of-function stabilization, prolonged replication inhibition, and developmental disorders including Meier-Gorlin syndrome and preimplantation embryo arrest."},"narrative":{"mechanistic_narrative":"Geminin (GMNN) is a cell-cycle-regulated inhibitor of DNA re-replication that licenses orderly genome duplication by binding and inhibiting the replication-licensing factor CDT1 [PMID:40455380]. Its activity is controlled at the protein level: geminin carries an N-terminal destruction box near residue Met28 that targets it for anaphase-promoting complex (APC)-mediated degradation at the metaphase-anaphase transition, so the protein accumulates in S/G2/M and is cleared in G1 [PMID:26637980]. This phase-specific proteolysis is sufficiently robust that truncated geminin retaining only its degradation signals can be used as a fluorescent biosensor to mark S/G2/M phases, and the geminin N-terminal degron has been exploited to restrict Cas9 activity to S/G2, biasing repair toward homology-directed repair [PMID:29899280]. Two distinct gain-of-function disease mechanisms have been defined: mutations that delete the destruction box stabilize geminin and prolong replication inhibition, causing autosomal-dominant Meier-Gorlin syndrome [PMID:26637980], whereas missense mutations that weaken the geminin-CDT1 interaction activate CHK1, induce DNA damage, and arrest preimplantation embryos [PMID:40455380].","teleology":[{"year":2015,"claim":"Established that geminin's abundance is set by APC recognition of an N-terminal destruction box, and that loss of this degron is a disease-causing gain-of-function mechanism rather than a loss of function.","evidence":"Human genetics identifying de novo destruction-box-disrupting mutations combined with cell-cycle phase and protein-stability analysis","pmids":["26637980"],"confidence":"Medium","gaps":["Does not directly reconstitute APC-geminin recognition in vitro","Penetrance and tissue-specific consequences of stabilized geminin not resolved"]},{"year":2018,"claim":"Demonstrated that the geminin N-terminal degron is portable and confers cell-cycle-restricted stability on a heterologous protein, confirming the degron is autonomous and functional out of context.","evidence":"Cas9-GMNN N-terminal peptide fusion in porcine fibroblasts with HDR knock-in frequency readout","pmids":["29899280"],"confidence":"Medium","gaps":["Single cell type and single readout","Does not map the minimal degron residues required"]},{"year":2025,"claim":"Defined the CDT1-binding interface as the functional output of geminin, showing that weakened geminin-CDT1 binding triggers CHK1 activation, DNA damage, and embryo arrest.","evidence":"Whole-exome/Sanger sequencing of patients, RNA-seq of zygotes/one-cell embryos, CDT1 binding assay, and CHK1/DNA-damage marker assessment","pmids":["40455380"],"confidence":"Medium","gaps":["Single lab; binding deficit not structurally mapped","Causal chain from reduced binding to CHK1 activation inferred from markers, not dissected step-by-step"]},{"year":2025,"claim":"Confirmed that geminin proteolysis is phase-specific and reciprocal to CDT1 degradation, validating geminin as a live-cell reporter of S/G2/M.","evidence":"Fucci(CA) fluorescent truncated-GMNN biosensor in a transgenic chicken line with in vitro and in vivo live imaging (preprint)","pmids":[],"confidence":"Medium","gaps":["Preprint, single study","Uses truncated protein retaining only degradation signals, not full-length geminin function"]},{"year":null,"claim":"How geminin-CDT1 binding affinity, geminin abundance, and APC-mediated turnover are quantitatively coordinated to enforce single-round replication remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the geminin-CDT1 or geminin-APC interaction in the corpus","Direct biochemical reconstitution of CDT1 inhibition by geminin not present","Tissue-specific thresholds linking degron/binding defects to distinct phenotypes unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[1]}],"localization":[],"pathway":[{"term_id":"R-HSA-69306","term_label":"DNA Replication","supporting_discovery_ids":[0,1]},{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[0,3]}],"complexes":[],"partners":["CDT1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O75496","full_name":"Geminin","aliases":[],"length_aa":209,"mass_kda":23.6,"function":"Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:14993212, PubMed:20129055, PubMed:24064211, PubMed:9635433). It is degraded during the mitotic phase of the cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433). Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle (PubMed:14993212, PubMed:24064211, PubMed:9635433). Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (PubMed:22615398)","subcellular_location":"Cytoplasm; Nucleus","url":"https://www.uniprot.org/uniprotkb/O75496/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/GMNN","classification":"Not Classified","n_dependent_lines":535,"n_total_lines":1208,"dependency_fraction":0.44288079470198677},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"MTMR1","stoichiometry":4.0},{"gene":"CANX","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/GMNN","total_profiled":1310},"omim":[{"mim_id":"620966","title":"TLC DOMAIN-CONTAINING PROTEIN 1; TLCD1","url":"https://www.omim.org/entry/620966"},{"mim_id":"619039","title":"REPLICATION INITIATOR 1; REPIN1","url":"https://www.omim.org/entry/619039"},{"mim_id":"616835","title":"MEIER-GORLIN SYNDROME 6; MGORS6","url":"https://www.omim.org/entry/616835"},{"mim_id":"615414","title":"MICROCEPHALY 11, PRIMARY, AUTOSOMAL RECESSIVE; MCPH11","url":"https://www.omim.org/entry/615414"},{"mim_id":"615167","title":"LEUCINE-RICH REPEATS- AND WD REPEAT DOMAIN-CONTAINING PROTEIN 1; LRWD1","url":"https://www.omim.org/entry/615167"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Nucleoplasm","reliability":"Supported"},{"location":"Basal body","reliability":"Additional"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"pancreas","ntpm":218.1}],"url":"https://www.proteinatlas.org/search/GMNN"},"hgnc":{"alias_symbol":["Gem"],"prev_symbol":[]},"alphafold":{"accession":"O75496","domains":[{"cath_id":"1.20.5","chopping":"84-160","consensus_level":"medium","plddt":93.6404,"start":84,"end":160}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O75496","model_url":"https://alphafold.ebi.ac.uk/files/AF-O75496-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O75496-F1-predicted_aligned_error_v6.png","plddt_mean":69.5},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=GMNN","jax_strain_url":"https://www.jax.org/strain/search?query=GMNN"},"sequence":{"accession":"O75496","fasta_url":"https://rest.uniprot.org/uniprotkb/O75496.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O75496/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O75496"}},"corpus_meta":[{"pmid":"22912832","id":"PMC_22912832","title":"Frequent amplification of CENPF, GMNN and CDK13 genes in hepatocellular carcinomas.","date":"2012","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/22912832","citation_count":81,"is_preprint":false},{"pmid":"26637980","id":"PMC_26637980","title":"De Novo GMNN Mutations Cause Autosomal-Dominant Primordial Dwarfism Associated with Meier-Gorlin Syndrome.","date":"2015","source":"American journal of human genetics","url":"https://pubmed.ncbi.nlm.nih.gov/26637980","citation_count":65,"is_preprint":false},{"pmid":"29899280","id":"PMC_29899280","title":"Efficient Knock-in of a Point Mutation in Porcine Fibroblasts Using the CRISPR/Cas9-GMNN Fusion Gene.","date":"2018","source":"Genes","url":"https://pubmed.ncbi.nlm.nih.gov/29899280","citation_count":20,"is_preprint":false},{"pmid":"30272835","id":"PMC_30272835","title":"Generation of Functional Hepatocytes from Human Adipose-Derived MYC+ KLF4+ GMNN+ Stem Cells Analyzed by Single-Cell RNA-Seq Profiling.","date":"2018","source":"Stem cells translational medicine","url":"https://pubmed.ncbi.nlm.nih.gov/30272835","citation_count":10,"is_preprint":false},{"pmid":"34604412","id":"PMC_34604412","title":"Evaluation of NUF2 and GMNN Expression in Prostate Cancer: Potential Biomarkers for Prostate Cancer Screening.","date":"2021","source":"Reports of biochemistry & molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/34604412","citation_count":7,"is_preprint":false},{"pmid":"40455380","id":"PMC_40455380","title":"GMNN mutations cause female infertility characterized by preimplantation embryo arrest through regulating DNA re-replication.","date":"2025","source":"Science China. Life sciences","url":"https://pubmed.ncbi.nlm.nih.gov/40455380","citation_count":1,"is_preprint":false},{"pmid":"39480819","id":"PMC_39480819","title":"Evaluation of BUBR1, MCM2, and GMNN as oral cancer biomarkers.","date":"2024","source":"European journal of cancer prevention : the official journal of the European Cancer Prevention Organisation (ECP)","url":"https://pubmed.ncbi.nlm.nih.gov/39480819","citation_count":1,"is_preprint":false},{"pmid":"36257233","id":"PMC_36257233","title":"Different expression of DNMT1, PCNA, MCM2, CDT1, EZH2, GMNN and EP300 genes in lymphomagenesis of low vs. high grade lymphoma.","date":"2022","source":"Pathology, research and practice","url":"https://pubmed.ncbi.nlm.nih.gov/36257233","citation_count":1,"is_preprint":false},{"pmid":"17029205","id":"PMC_17029205","title":"The association of polymorphisms of CDT1 and GMNN gene with the risk of breast cancer in Chinese women: a case-control analysis.","date":"2006","source":"Zhonghua yi xue yi chuan xue za zhi = Zhonghua yixue yichuanxue zazhi = Chinese journal of medical genetics","url":"https://pubmed.ncbi.nlm.nih.gov/17029205","citation_count":0,"is_preprint":false},{"pmid":"39659197","id":"PMC_39659197","title":"GMNN and DLL1 mutation-related spondylocarpotarsal synostosis: a case report.","date":"2024","source":"Journal of Yeungnam medical science","url":"https://pubmed.ncbi.nlm.nih.gov/39659197","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.09.24.678103","title":"FuChi: A cell cycle biosensor for investigating cell-cycle kinetics during avian development","date":"2025-09-25","source":"bioRxiv","url":"https://doi.org/10.1101/2025.09.24.678103","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7491,"output_tokens":1180,"usd":0.020087,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7839,"output_tokens":1763,"usd":0.041635,"stage2_stop_reason":"end_turn"},"total_usd":0.061722,"stage1_batch_id":"msgbatch_01DUPACZi7AAWwuZiUjseQF4","stage2_batch_id":"msgbatch_018yt7chE3f48PEFtDwtj6AE","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2015,\n      \"finding\": \"De novo heterozygous truncating or missense mutations in GMNN that alter sites 5' to residue Met28 (within the destruction box) result in geminin proteins lacking the destruction box, conferring increased protein stability and prolonged inhibition of DNA replication. The anaphase-promoting complex (APC) normally recognizes the destruction box near the 5' end of geminin to degrade it during the metaphase-anaphase transition; mutations disrupting this sequence prevent APC-mediated degradation, constituting a gain-of-function mechanism causing autosomal-dominant Meier-Gorlin syndrome.\",\n      \"method\": \"Human genetics (identification of de novo mutations) combined with cell-cycle phase analysis; mechanistic interpretation supported by known APC-destruction box biology and functional data on protein stability\",\n      \"journal\": \"American journal of human genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — human genetic evidence with mechanistic interpretation of destruction-box loss; single study but multiple mutations converging on same mechanism\",\n      \"pmids\": [\"26637980\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Rare dominant missense mutations in GMNN decrease geminin's binding to CDT1, leading to activation of CHK1, DNA damage, and cell cycle disturbance, resulting in preimplantation embryo arrest. This establishes that geminin prevents DNA re-replication by inhibiting CDT1, and that impaired geminin–CDT1 interaction disrupts correct cell cycle progression in early embryos.\",\n      \"method\": \"Whole-exome sequencing and Sanger sequencing in patients; RNA sequencing of mouse zygotes and patient one-cell embryo; binding assay (CDT1 interaction) and assessment of CHK1 activation and DNA damage markers\",\n      \"journal\": \"Science China. Life sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — binding assay plus DNA damage/CHK1 readouts in a single study; multiple orthogonal methods but single lab\",\n      \"pmids\": [\"40455380\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Fusion of Cas9 to the N-terminal peptide of GMNN (geminin) causes the Cas9 fusion protein to be degraded during NHEJ-dominated cell cycle phases (G1), thereby enriching Cas9 activity in S/G2 phases where HDR predominates, resulting in an approximately two-fold increase in homology-directed repair knock-in frequency in porcine fibroblasts.\",\n      \"method\": \"CRISPR/Cas9-GMNN fusion construct expressed in porcine fetal fibroblasts; point mutation-specific real-time PCR screening for HDR events\",\n      \"journal\": \"Genes\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional cell-based assay exploiting known cell-cycle-dependent degradation of geminin N-terminal peptide; single lab, single method\",\n      \"pmids\": [\"29899280\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Truncated forms of the human GMNN protein (lacking full-length sequences but retaining degradation signals) are reciprocally degraded relative to CDT1-derived fragments across the cell cycle, allowing fluorescent fusions to distinguish S, G2, and M phases from G1. This confirms that GMNN protein levels are cell-cycle-regulated through phase-specific proteolysis, enabling its use as a biosensor for S/G2/M phases.\",\n      \"method\": \"Fucci(CA) cell cycle biosensor system using fluorescently tagged truncated GMNN in transgenic chicken line (FuChi); in vitro and in vivo live imaging\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct live-cell imaging with functional validation across multiple tissues; preprint, single study\",\n      \"pmids\": [],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"Geminin (GMNN) prevents DNA re-replication by binding and inhibiting CDT1; its protein levels are cell-cycle-regulated through APC-mediated destruction-box-dependent degradation at the metaphase-anaphase transition (present in S/G2/M, absent in G1), and mutations that disrupt the destruction box or the CDT1-binding interface cause gain-of-function stabilization, prolonged replication inhibition, and developmental disorders including Meier-Gorlin syndrome and preimplantation embryo arrest.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"Geminin (GMNN) is a cell-cycle-regulated inhibitor of DNA re-replication that licenses orderly genome duplication by binding and inhibiting the replication-licensing factor CDT1 [#1]. Its activity is controlled at the protein level: geminin carries an N-terminal destruction box near residue Met28 that targets it for anaphase-promoting complex (APC)-mediated degradation at the metaphase-anaphase transition, so the protein accumulates in S/G2/M and is cleared in G1 [#0]. This phase-specific proteolysis is sufficiently robust that truncated geminin retaining only its degradation signals can be used as a fluorescent biosensor to mark S/G2/M phases [#3], and the geminin N-terminal degron has been exploited to restrict Cas9 activity to S/G2, biasing repair toward homology-directed repair [#2]. Two distinct gain-of-function disease mechanisms have been defined: mutations that delete the destruction box stabilize geminin and prolong replication inhibition, causing autosomal-dominant Meier-Gorlin syndrome [#0], whereas missense mutations that weaken the geminin-CDT1 interaction activate CHK1, induce DNA damage, and arrest preimplantation embryos [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2015,\n      \"claim\": \"Established that geminin's abundance is set by APC recognition of an N-terminal destruction box, and that loss of this degron is a disease-causing gain-of-function mechanism rather than a loss of function.\",\n      \"evidence\": \"Human genetics identifying de novo destruction-box-disrupting mutations combined with cell-cycle phase and protein-stability analysis\",\n      \"pmids\": [\"26637980\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Does not directly reconstitute APC-geminin recognition in vitro\", \"Penetrance and tissue-specific consequences of stabilized geminin not resolved\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Demonstrated that the geminin N-terminal degron is portable and confers cell-cycle-restricted stability on a heterologous protein, confirming the degron is autonomous and functional out of context.\",\n      \"evidence\": \"Cas9-GMNN N-terminal peptide fusion in porcine fibroblasts with HDR knock-in frequency readout\",\n      \"pmids\": [\"29899280\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single cell type and single readout\", \"Does not map the minimal degron residues required\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Defined the CDT1-binding interface as the functional output of geminin, showing that weakened geminin-CDT1 binding triggers CHK1 activation, DNA damage, and embryo arrest.\",\n      \"evidence\": \"Whole-exome/Sanger sequencing of patients, RNA-seq of zygotes/one-cell embryos, CDT1 binding assay, and CHK1/DNA-damage marker assessment\",\n      \"pmids\": [\"40455380\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab; binding deficit not structurally mapped\", \"Causal chain from reduced binding to CHK1 activation inferred from markers, not dissected step-by-step\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Confirmed that geminin proteolysis is phase-specific and reciprocal to CDT1 degradation, validating geminin as a live-cell reporter of S/G2/M.\",\n      \"evidence\": \"Fucci(CA) fluorescent truncated-GMNN biosensor in a transgenic chicken line with in vitro and in vivo live imaging (preprint)\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Preprint, single study\", \"Uses truncated protein retaining only degradation signals, not full-length geminin function\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How geminin-CDT1 binding affinity, geminin abundance, and APC-mediated turnover are quantitatively coordinated to enforce single-round replication remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structural model of the geminin-CDT1 or geminin-APC interaction in the corpus\", \"Direct biochemical reconstitution of CDT1 inhibition by geminin not present\", \"Tissue-specific thresholds linking degron/binding defects to distinct phenotypes unknown\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-69306\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"CDT1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}