{"gene":"LIAT1","run_date":"2026-04-28T18:30:27","timeline":{"discoveries":[{"year":2014,"finding":"LIAT1 (Ligand of Ate1) was identified as a binding partner of the arginyltransferase Ate1, with higher affinity for Ate1 isoforms 1A7A and 1B7A, and a ~30-residue conserved region of LIAT1 was shown to be required for this binding.","method":"Co-immunoprecipitation / pulldown; deletion mapping of the conserved ~30-residue region","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 2 — reciprocal interaction demonstrated with domain mapping and isoform specificity characterization in a rigorous study","pmids":["25369936"],"is_preprint":false},{"year":2014,"finding":"LIAT1 stimulates the in vitro N-terminal arginylation of a model substrate by Ate1, indicating it functions as a positive regulator of Ate1 enzymatic activity.","method":"In vitro arginylation assay with purified components","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 1 — direct in vitro reconstituted enzymatic assay demonstrating stimulation of Ate1 activity","pmids":["25369936"],"is_preprint":false},{"year":2020,"finding":"LIAT1's N-terminal half comprises an intrinsically disordered region (IDR) containing a low-complexity poly-K region that targets LIAT1 to the nucleolus, where it undergoes liquid-liquid phase separation (LLPS).","method":"Bimolecular fluorescence complementation, immunocytochemistry, domain deletion analysis","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 2 — direct localization with functional domain mapping using multiple orthogonal imaging methods","pmids":["33443146"],"is_preprint":false},{"year":2020,"finding":"The lysyl-hydroxylase Jumonji Domain Containing 6 (Jmjd6) modifies LIAT1 in a manner dependent on the poly-K region within its IDR, and this modification inhibits LIAT1's nucleolar targeting.","method":"Immunocytochemistry, bimolecular fluorescence complementation, Jmjd6 activity assays","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"Medium","confidence_rationale":"Tier 2 — direct cellular experiment linking a specific PTM writer (Jmjd6) to LIAT1 localization, single study","pmids":["33443146"],"is_preprint":false},{"year":2024,"finding":"Human tRNA-Arg directly binds recombinant mouse LIAT1 in vitro, identifying LIAT1 as an RNA-binding protein.","method":"In vitro RNA-protein binding assay with recombinant LIAT1 and in vitro-transcribed tRNA-Arg","journal":"microPublication biology","confidence":"Medium","confidence_rationale":"Tier 2 — direct in vitro binding assay; single study, novel finding without mutagenesis confirmation","pmids":["39081859"],"is_preprint":false}],"current_model":"LIAT1 is an intrinsically disordered protein that binds and stimulates the arginyltransferase Ate1 (via a conserved ~30-residue region), localizes to the nucleolus through liquid-liquid phase separation driven by its poly-K IDR, is regulated by Jmjd6-mediated lysyl-hydroxylation that inhibits its nucleolar targeting, and also binds tRNA-Arg directly, suggesting an additional role in tRNA/RNA metabolism."},"narrative":{"teleology":[{"year":2014,"claim":"Identification of LIAT1 as a direct binding partner and enzymatic activator of Ate1 established the first known regulatory cofactor for N-terminal arginylation, revealing that arginylation is subject to accessory-protein control rather than being solely dictated by Ate1 itself.","evidence":"Co-immunoprecipitation, deletion mapping of a conserved ~30-residue binding region, and reconstituted in vitro arginylation assay with purified components","pmids":["25369936"],"confidence":"High","gaps":["Structural basis of the LIAT1–Ate1 interaction is undefined","In vivo substrates whose arginylation depends on LIAT1 have not been identified","Mechanism by which LIAT1 stimulates Ate1 catalytic activity (allosteric vs. tRNA delivery) is unknown"]},{"year":2020,"claim":"Demonstration that LIAT1's poly-K IDR drives nucleolar localization through liquid–liquid phase separation, and that Jmjd6-mediated lysyl hydroxylation of this region inhibits nucleolar targeting, linked LIAT1 to regulated biomolecular condensate biology and provided the first post-translational control mechanism for LIAT1 localization.","evidence":"Bimolecular fluorescence complementation, immunocytochemistry, domain deletion analysis, and Jmjd6 activity assays in cells","pmids":["33443146"],"confidence":"High","gaps":["Functional consequence of nucleolar LIAT1 condensates (e.g., ribosome biogenesis, rRNA processing) is unknown","Whether Jmjd6-mediated regulation of LIAT1 affects Ate1-dependent arginylation has not been tested","The precise hydroxylated residues within the poly-K region have not been mapped at single-residue resolution"]},{"year":2024,"claim":"Discovery that LIAT1 directly binds tRNA-Arg in vitro expanded its functional repertoire beyond protein–protein interaction to RNA binding, raising the possibility that LIAT1 couples tRNA delivery to Ate1-mediated arginylation.","evidence":"In vitro RNA–protein binding assay using recombinant mouse LIAT1 and in vitro–transcribed human tRNA-Arg","pmids":["39081859"],"confidence":"Medium","gaps":["Binding specificity (tRNA-Arg vs. other tRNAs or RNAs) has not been assessed","No mutagenesis to identify the RNA-binding determinant within LIAT1","Whether tRNA-Arg binding is relevant to LIAT1's stimulation of Ate1 activity is untested"]},{"year":null,"claim":"The central open question is how LIAT1's three activities — Ate1 activation, nucleolar phase separation, and tRNA-Arg binding — are integrated in vivo to regulate N-terminal arginylation and/or nucleolar function.","evidence":"","pmids":[],"confidence":"Low","gaps":["No loss-of-function phenotype for LIAT1 has been reported in any organism","Whether LIAT1 acts as a tRNA carrier that delivers Arg-charged tRNA to Ate1 is untested","Physiological substrates of the LIAT1–Ate1 axis remain unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,1]},{"term_id":"GO:0003723","term_label":"RNA binding","supporting_discovery_ids":[4]}],"localization":[{"term_id":"GO:0005730","term_label":"nucleolus","supporting_discovery_ids":[2]}],"pathway":[],"complexes":[],"partners":["ATE1","JMJD6"],"other_free_text":[]},"mechanistic_narrative":"LIAT1 is an intrinsically disordered protein that functions as a positive regulator of the arginyltransferase Ate1, binding Ate1 through a conserved ~30-residue region with isoform-selective affinity and stimulating N-terminal arginylation of substrates in vitro [PMID:25369936]. Its N-terminal low-complexity poly-K intrinsically disordered region drives nucleolar targeting through liquid–liquid phase separation, a process negatively regulated by Jmjd6-mediated lysyl hydroxylation of the same poly-K region [PMID:33443146]. LIAT1 also directly binds tRNA-Arg in vitro, indicating an additional role in RNA metabolism [PMID:39081859]."},"prefetch_data":{"uniprot":{"accession":"Q6ZQX7","full_name":"Protein LIAT1","aliases":["Ligand of ATE1 protein"],"length_aa":453,"mass_kda":49.7,"function":"Participates in nucleolar liquid-liquid phase separation (LLPS) through its N-terminal intrinsically disordered region (IDR). May be involved in ATE1-mediated N-terminal arginylation","subcellular_location":"Nucleus, nucleolus; Cytoplasm","url":"https://www.uniprot.org/uniprotkb/Q6ZQX7/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/LIAT1","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/LIAT1","total_profiled":1310},"omim":[],"hpa":{"profiled":true,"resolved_as":"C17ORF97","reliability":"Approved","locations":[{"location":"Nucleoli","reliability":"Approved"},{"location":"Cytosol","reliability":"Additional"}],"tissue_specificity":"Tissue enriched","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"testis","ntpm":55.1}],"url":"https://www.proteinatlas.org/search/C17ORF97"},"hgnc":{"alias_symbol":["LOC400566"],"prev_symbol":["C17orf97"]},"alphafold":{"accession":"Q6ZQX7","domains":[],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6ZQX7","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q6ZQX7-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q6ZQX7-F1-predicted_aligned_error_v6.png","plddt_mean":46.41},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=LIAT1","jax_strain_url":"https://www.jax.org/strain/search?query=LIAT1"},"sequence":{"accession":"Q6ZQX7","fasta_url":"https://rest.uniprot.org/uniprotkb/Q6ZQX7.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q6ZQX7/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6ZQX7"}},"corpus_meta":[{"pmid":"25369936","id":"PMC_25369936","title":"Liat1, an arginyltransferase-binding protein whose evolution among primates involved changes in the numbers of its 10-residue repeats.","date":"2014","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/25369936","citation_count":20,"is_preprint":false},{"pmid":"33443146","id":"PMC_33443146","title":"The Ligand of Ate1 is intrinsically disordered and participates in nucleolar phase separation regulated by Jumonji Domain Containing 6.","date":"2020","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/33443146","citation_count":6,"is_preprint":false},{"pmid":"39081859","id":"PMC_39081859","title":"tRNA Arg binds in vitro TDP-43 RNA recognition motifs and ligand of Ate1 protein LIAT1.","date":"2024","source":"microPublication biology","url":"https://pubmed.ncbi.nlm.nih.gov/39081859","citation_count":3,"is_preprint":false},{"pmid":"28865488","id":"PMC_28865488","title":"Distinct transcriptional and metabolic profiles associated with empathy in Buddhist priests: a pilot study.","date":"2017","source":"Human genomics","url":"https://pubmed.ncbi.nlm.nih.gov/28865488","citation_count":3,"is_preprint":false},{"pmid":"39897169","id":"PMC_39897169","title":"Erratum: Corrigendum: tRNA Arg binds in vitro TDP-43 RNA recognition motifs and ligand of Ate1 protein LIAT1.","date":"2025","source":"microPublication biology","url":"https://pubmed.ncbi.nlm.nih.gov/39897169","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3741,"output_tokens":1093,"usd":0.013809},"stage2":{"model":"claude-opus-4-6","input_tokens":4310,"output_tokens":2637,"usd":0.131213},"total_usd":0.145022,"stage1_batch_id":"msgbatch_01Mgbec4vM6c9vXht7JVJzss","stage2_batch_id":"msgbatch_01JkuuH5RB2BdJNsgnhjbC6s","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"LIAT1 (Ligand of Ate1) was identified as a binding partner of the arginyltransferase Ate1, with higher affinity for Ate1 isoforms 1A7A and 1B7A, and a ~30-residue conserved region of LIAT1 was shown to be required for this binding.\",\n      \"method\": \"Co-immunoprecipitation / pulldown; deletion mapping of the conserved ~30-residue region\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal interaction demonstrated with domain mapping and isoform specificity characterization in a rigorous study\",\n      \"pmids\": [\"25369936\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"LIAT1 stimulates the in vitro N-terminal arginylation of a model substrate by Ate1, indicating it functions as a positive regulator of Ate1 enzymatic activity.\",\n      \"method\": \"In vitro arginylation assay with purified components\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — direct in vitro reconstituted enzymatic assay demonstrating stimulation of Ate1 activity\",\n      \"pmids\": [\"25369936\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"LIAT1's N-terminal half comprises an intrinsically disordered region (IDR) containing a low-complexity poly-K region that targets LIAT1 to the nucleolus, where it undergoes liquid-liquid phase separation (LLPS).\",\n      \"method\": \"Bimolecular fluorescence complementation, immunocytochemistry, domain deletion analysis\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — direct localization with functional domain mapping using multiple orthogonal imaging methods\",\n      \"pmids\": [\"33443146\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"The lysyl-hydroxylase Jumonji Domain Containing 6 (Jmjd6) modifies LIAT1 in a manner dependent on the poly-K region within its IDR, and this modification inhibits LIAT1's nucleolar targeting.\",\n      \"method\": \"Immunocytochemistry, bimolecular fluorescence complementation, Jmjd6 activity assays\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — direct cellular experiment linking a specific PTM writer (Jmjd6) to LIAT1 localization, single study\",\n      \"pmids\": [\"33443146\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Human tRNA-Arg directly binds recombinant mouse LIAT1 in vitro, identifying LIAT1 as an RNA-binding protein.\",\n      \"method\": \"In vitro RNA-protein binding assay with recombinant LIAT1 and in vitro-transcribed tRNA-Arg\",\n      \"journal\": \"microPublication biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — direct in vitro binding assay; single study, novel finding without mutagenesis confirmation\",\n      \"pmids\": [\"39081859\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"LIAT1 is an intrinsically disordered protein that binds and stimulates the arginyltransferase Ate1 (via a conserved ~30-residue region), localizes to the nucleolus through liquid-liquid phase separation driven by its poly-K IDR, is regulated by Jmjd6-mediated lysyl-hydroxylation that inhibits its nucleolar targeting, and also binds tRNA-Arg directly, suggesting an additional role in tRNA/RNA metabolism.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"LIAT1 is an intrinsically disordered protein that functions as a positive regulator of the arginyltransferase Ate1, binding Ate1 through a conserved ~30-residue region with isoform-selective affinity and stimulating N-terminal arginylation of substrates in vitro [PMID:25369936]. Its N-terminal low-complexity poly-K intrinsically disordered region drives nucleolar targeting through liquid–liquid phase separation, a process negatively regulated by Jmjd6-mediated lysyl hydroxylation of the same poly-K region [PMID:33443146]. LIAT1 also directly binds tRNA-Arg in vitro, indicating an additional role in RNA metabolism [PMID:39081859].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Identification of LIAT1 as a direct binding partner and enzymatic activator of Ate1 established the first known regulatory cofactor for N-terminal arginylation, revealing that arginylation is subject to accessory-protein control rather than being solely dictated by Ate1 itself.\",\n      \"evidence\": \"Co-immunoprecipitation, deletion mapping of a conserved ~30-residue binding region, and reconstituted in vitro arginylation assay with purified components\",\n      \"pmids\": [\"25369936\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of the LIAT1–Ate1 interaction is undefined\",\n        \"In vivo substrates whose arginylation depends on LIAT1 have not been identified\",\n        \"Mechanism by which LIAT1 stimulates Ate1 catalytic activity (allosteric vs. tRNA delivery) is unknown\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Demonstration that LIAT1's poly-K IDR drives nucleolar localization through liquid–liquid phase separation, and that Jmjd6-mediated lysyl hydroxylation of this region inhibits nucleolar targeting, linked LIAT1 to regulated biomolecular condensate biology and provided the first post-translational control mechanism for LIAT1 localization.\",\n      \"evidence\": \"Bimolecular fluorescence complementation, immunocytochemistry, domain deletion analysis, and Jmjd6 activity assays in cells\",\n      \"pmids\": [\"33443146\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Functional consequence of nucleolar LIAT1 condensates (e.g., ribosome biogenesis, rRNA processing) is unknown\",\n        \"Whether Jmjd6-mediated regulation of LIAT1 affects Ate1-dependent arginylation has not been tested\",\n        \"The precise hydroxylated residues within the poly-K region have not been mapped at single-residue resolution\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Discovery that LIAT1 directly binds tRNA-Arg in vitro expanded its functional repertoire beyond protein–protein interaction to RNA binding, raising the possibility that LIAT1 couples tRNA delivery to Ate1-mediated arginylation.\",\n      \"evidence\": \"In vitro RNA–protein binding assay using recombinant mouse LIAT1 and in vitro–transcribed human tRNA-Arg\",\n      \"pmids\": [\"39081859\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Binding specificity (tRNA-Arg vs. other tRNAs or RNAs) has not been assessed\",\n        \"No mutagenesis to identify the RNA-binding determinant within LIAT1\",\n        \"Whether tRNA-Arg binding is relevant to LIAT1's stimulation of Ate1 activity is untested\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The central open question is how LIAT1's three activities — Ate1 activation, nucleolar phase separation, and tRNA-Arg binding — are integrated in vivo to regulate N-terminal arginylation and/or nucleolar function.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No loss-of-function phenotype for LIAT1 has been reported in any organism\",\n        \"Whether LIAT1 acts as a tRNA carrier that delivers Arg-charged tRNA to Ate1 is untested\",\n        \"Physiological substrates of the LIAT1–Ate1 axis remain unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005730\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0392499\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"ATE1\", \"JMJD6\"],\n    \"other_free_text\": []\n  }\n}\n```\n\nWait — I need to fix the pathway term_id. Let me correct:\n\n```json\n{\n  \"mechanistic_narrative\": \"LIAT1 is an intrinsically disordered protein that functions as a positive regulator of the arginyltransferase Ate1, binding Ate1 through a conserved ~30-residue region with isoform-selective affinity and stimulating N-terminal arginylation of substrates in vitro [PMID:25369936]. Its N-terminal low-complexity poly-K intrinsically disordered region drives nucleolar targeting through liquid–liquid phase separation, a process negatively regulated by Jmjd6-mediated lysyl hydroxylation of the same poly-K region [PMID:33443146]. LIAT1 also directly binds tRNA-Arg in vitro, indicating an additional role in RNA metabolism [PMID:39081859].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Identification of LIAT1 as a direct binding partner and enzymatic activator of Ate1 established the first known regulatory cofactor for N-terminal arginylation, revealing that arginylation is subject to accessory-protein control rather than being solely dictated by Ate1 itself.\",\n      \"evidence\": \"Co-immunoprecipitation, deletion mapping of a conserved ~30-residue binding region, and reconstituted in vitro arginylation assay with purified components\",\n      \"pmids\": [\"25369936\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of the LIAT1–Ate1 interaction is undefined\",\n        \"In vivo substrates whose arginylation depends on LIAT1 have not been identified\",\n        \"Mechanism by which LIAT1 stimulates Ate1 catalytic activity (allosteric vs. tRNA delivery) is unknown\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Demonstration that LIAT1's poly-K IDR drives nucleolar localization through liquid–liquid phase separation, and that Jmjd6-mediated lysyl hydroxylation of this region inhibits nucleolar targeting, linked LIAT1 to regulated biomolecular condensate biology and provided the first post-translational control mechanism for LIAT1 localization.\",\n      \"evidence\": \"Bimolecular fluorescence complementation, immunocytochemistry, domain deletion analysis, and Jmjd6 activity assays in cells\",\n      \"pmids\": [\"33443146\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Functional consequence of nucleolar LIAT1 condensates (e.g., ribosome biogenesis, rRNA processing) is unknown\",\n        \"Whether Jmjd6-mediated regulation of LIAT1 affects Ate1-dependent arginylation has not been tested\",\n        \"The precise hydroxylated residues within the poly-K region have not been mapped at single-residue resolution\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Discovery that LIAT1 directly binds tRNA-Arg in vitro expanded its functional repertoire beyond protein–protein interaction to RNA binding, raising the possibility that LIAT1 couples tRNA delivery to Ate1-mediated arginylation.\",\n      \"evidence\": \"In vitro RNA–protein binding assay using recombinant mouse LIAT1 and in vitro–transcribed human tRNA-Arg\",\n      \"pmids\": [\"39081859\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Binding specificity (tRNA-Arg vs. other tRNAs or RNAs) has not been assessed\",\n        \"No mutagenesis to identify the RNA-binding determinant within LIAT1\",\n        \"Whether tRNA-Arg binding is relevant to LIAT1's stimulation of Ate1 activity is untested\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The central open question is how LIAT1's three activities — Ate1 activation, nucleolar phase separation, and tRNA-Arg binding — are integrated in vivo to regulate N-terminal arginylation and/or nucleolar function.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No loss-of-function phenotype for LIAT1 has been reported in any organism\",\n        \"Whether LIAT1 acts as a tRNA carrier that delivers Arg-charged tRNA to Ate1 is untested\",\n        \"Physiological substrates of the LIAT1–Ate1 axis remain unknown\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005730\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"ATE1\", \"JMJD6\"],\n    \"other_free_text\": []\n  }\n}\n```"}