{"gene":"IGFN1","run_date":"2026-06-10T01:55:22","timeline":{"discoveries":[{"year":2010,"finding":"IGFN1 was identified as a Z-band associated protein in skeletal muscle that forms a protein complex with KY and filamin C (FLNC). Yeast two-hybrid screening identified FLNC as an IGFN1 interacting partner, and the three N-terminal globular domains of IGFN1 are sufficient for Z-band targeting. KY co-localizes with IGFN1 at the Z-band in C2C12-derived myotubes and neonatal cardiomyocytes.","method":"Yeast two-hybrid screening, immunofluorescence, recombinant protein expression, immunodetection in C2C12-derived myotubes and neonatal cardiomyocytes","journal":"Experimental cell research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — yeast two-hybrid plus biochemical and immunofluorescence data in multiple cell types, single lab","pmids":["20206623"],"is_preprint":false},{"year":2008,"finding":"IGFN1 was identified as a novel binding partner of eukaryotic translation elongation factor 1A (eEF1A) via yeast two-hybrid screening of a human skeletal muscle cDNA library, with the interaction confirmed in vitro. IGFN1 shows sequence and structural homology to myosin binding protein-C (fast and slow-type skeletal muscle isoforms) and is substantially upregulated during muscle denervation.","method":"Yeast two-hybrid screening of human skeletal muscle cDNA library, in vitro binding confirmation","journal":"Journal of cellular biochemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — yeast two-hybrid plus in vitro confirmation, single lab, two orthogonal methods","pmids":["18756455"],"is_preprint":false},{"year":2017,"finding":"IGFN1_v1 is required for myoblast fusion and differentiation. shRNA-mediated knockdown of all Igfn1 variants completely blocked myoblast fusion without preventing expression of differentiation markers. CRISPR/Cas9 deletion of exon 13 (encoding N-terminal domains) caused fusion defects and abnormal large multinucleated cells. Expression of IGFN1_v1 partially rescued fusion and myotube morphology in the exon 13 knockout cell line.","method":"shRNA knockdown, CRISPR/Cas9 homologous recombination (exon 13 deletion), rescue by IGFN1_v1 overexpression in C2C12 cells","journal":"PloS one","confidence":"High","confidence_rationale":"Tier 2 / Strong — two independent loss-of-function approaches (shRNA and CRISPR/Cas9) with specific phenotypic readout plus rescue experiment, single lab but multiple orthogonal methods","pmids":["28665998"],"is_preprint":false},{"year":2020,"finding":"IGFN1-deficient C2C12 myoblasts show elevated G:F actin ratios during differentiation, indicating deficient actin remodelling underlies fusion and differentiation defects. Proteomic pull-down from skeletal muscle with IGFN1 fragments identified the actin nucleating protein COBL as a binding partner; IGFN1 interacts with, stabilizes, and co-localizes with COBL at the Z-disc, and prevents COBL from forming actin ruffles in COS7 cells. The proteasome was also identified as a main network in IGFN1 complexes. COBL loss-of-function C2C12 clones retain the ability to fuse, indicating COBL or the IGFN1/COBL interaction is not essential for myoblast fusion.","method":"G:F actin ratio assay in IGFN1-deficient C2C12 cells, IGFN1 fragment pull-down from skeletal muscle with proteomics, co-immunoprecipitation/co-localization of IGFN1 and COBL, actin ruffle assay in COS7 cells, COBL loss-of-function clones","journal":"Experimental cell research","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (proteomics pull-down, co-IP, co-localization, functional actin assay, loss-of-function) in single rigorous study","pmids":["32768501"],"is_preprint":false},{"year":2018,"finding":"A stable G-quadruplex structure forms in intron 15 of the IGFN1 gene (confirmed by gel shift assay and circular dichroism spectroscopy with G-quadruplex stabilizing agents PDS and KCl) and inhibits reverse transcriptase and Taq polymerase in stop assays. Treatment with the G-quadruplex stabilizer pyridostatin (PDS) alters IGFN1 splicing isoforms in UOK146 renal cell carcinoma cells, implicating intronic G-quadruplex formation in IGFN1 aberrant splicing.","method":"Gel shift assay, circular dichroism spectroscopy, reverse transcriptase and PCR stop assays, Sanger sequencing of PQS and mutant plasmid constructs, PDS treatment in UOK146 cells","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 1 / Moderate — multiple in vitro biochemical assays (CD, gel shift, polymerase stop) plus cell-based splicing assay, single lab","pmids":["30335789"],"is_preprint":false}],"current_model":"IGFN1 is a skeletal muscle Z-band protein that forms a complex with KY and filamin C (FLNC), interacts with eEF1A (potentially modulating protein synthesis during denervation), and is required for myoblast fusion and differentiation through regulation of actin dynamics—partly via interaction with and stabilization of the actin nucleating protein COBL; additionally, a stable intronic G-quadruplex in IGFN1 intron 15 regulates alternative splicing of the locus."},"narrative":{"mechanistic_narrative":"IGFN1 is a skeletal muscle Z-band/Z-disc-associated protein that scaffolds the contractile apparatus and governs myoblast fusion and differentiation through control of actin dynamics [PMID:20206623, PMID:28665998, PMID:32768501]. Its three N-terminal globular domains are sufficient for Z-band targeting, where it assembles into a complex with KY and filamin C (FLNC) [PMID:20206623]. Loss of all IGFN1 variants by shRNA, or deletion of exon 13 encoding N-terminal domains, completely blocks myoblast fusion and produces abnormal large multinucleated cells without preventing differentiation-marker expression, and re-expression of IGFN1_v1 partially rescues these defects [PMID:28665998]. Mechanistically, IGFN1-deficient myoblasts show elevated G:F actin ratios indicative of deficient actin remodelling; IGFN1 binds, stabilizes, and co-localizes at the Z-disc with the actin-nucleating protein COBL and restrains COBL-driven actin ruffling [PMID:32768501]. IGFN1 also binds eukaryotic translation elongation factor eEF1A and is strongly upregulated during muscle denervation, linking it to protein-synthesis regulation in muscle [PMID:18756455]. At the gene level, a stable G-quadruplex in intron 15 modulates alternative splicing of the locus [PMID:30335789].","teleology":[{"year":2008,"claim":"Established a first molecular partner and regulatory context for IGFN1 by identifying it as an eEF1A-binding muscle protein induced during denervation, hinting at a role coupling muscle state to translational machinery.","evidence":"Yeast two-hybrid screening of a human skeletal muscle cDNA library with in vitro binding confirmation","pmids":["18756455"],"confidence":"Medium","gaps":["Functional consequence of the eEF1A interaction on translation not demonstrated","Denervation upregulation correlative, not mechanistically tied to eEF1A binding","No structural mapping of the interaction interface"]},{"year":2010,"claim":"Placed IGFN1 at the Z-band as part of a defined sarcomeric complex, defining where in muscle architecture it operates.","evidence":"Yeast two-hybrid, recombinant domain mapping, and immunofluorescence in C2C12 myotubes and neonatal cardiomyocytes","pmids":["20206623"],"confidence":"Medium","gaps":["Functional role of the IGFN1/KY/FLNC complex not tested","Single-lab interaction data without in vivo validation","Stoichiometry and assembly order of the complex unknown"]},{"year":2017,"claim":"Demonstrated that IGFN1 is functionally required for myoblast fusion, moving it from a structural component to a determinant of muscle cell morphogenesis.","evidence":"shRNA knockdown and CRISPR/Cas9 exon 13 deletion with IGFN1_v1 rescue in C2C12 cells","pmids":["28665998"],"confidence":"High","gaps":["Molecular mechanism downstream of IGFN1 not resolved in this study","Only partial rescue achieved","In vivo muscle phenotype not addressed"]},{"year":2020,"claim":"Identified the mechanistic basis of the fusion defect as deficient actin remodelling and linked IGFN1 to the actin nucleator COBL, explaining how a Z-disc scaffold controls cytoskeletal dynamics.","evidence":"G:F actin assays, IGFN1 fragment pull-down proteomics, co-IP/co-localization, actin ruffle assay in COS7, and COBL loss-of-function clones","pmids":["32768501"],"confidence":"High","gaps":["COBL loss-of-function clones still fuse, so COBL is not essential for fusion","The fusion-relevant actin effector downstream of IGFN1 remains unidentified","Role of the proteasome network found in IGFN1 complexes not defined"]},{"year":2018,"claim":"Showed that gene-level regulation of IGFN1 isoforms is controlled by an intronic G-quadruplex, adding a transcript-processing layer to its biology.","evidence":"Gel shift, circular dichroism, polymerase stop assays, and pyridostatin-induced splicing changes in UOK146 cells","pmids":["30335789"],"confidence":"Medium","gaps":["Splicing effect shown in a renal carcinoma line, not skeletal muscle","Endogenous splicing factors reading the G-quadruplex not identified","Physiological relevance of isoform switching not established"]},{"year":null,"claim":"The effector pathway by which IGFN1-dependent actin remodelling drives myoblast fusion, and how its Z-disc, eEF1A, and splicing functions integrate in vivo, remain unresolved.","evidence":"No single study in the corpus connects IGFN1's scaffolding, translational, and splicing roles in an intact muscle model","pmids":[],"confidence":"Low","gaps":["No in vivo (animal) loss-of-function phenotype in the corpus","Fusion-essential actin effector unidentified","Functional consequence of eEF1A binding undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[3]},{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[0,3]}],"pathway":[{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[2]},{"term_id":"R-HSA-397014","term_label":"Muscle contraction","supporting_discovery_ids":[0]}],"complexes":[],"partners":["FLNC","KY","EEF1A1","COBL"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q86VF2","full_name":"Immunoglobulin-like and fibronectin type III domain-containing protein 1","aliases":["EEF1A2-binding protein 1","KY-interacting protein 1"],"length_aa":1251,"mass_kda":137.8,"function":"","subcellular_location":"Nucleus; Cytoplasm, myofibril, sarcomere, Z line","url":"https://www.uniprot.org/uniprotkb/Q86VF2/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/IGFN1","classification":"Not Classified","n_dependent_lines":12,"n_total_lines":1208,"dependency_fraction":0.009933774834437087},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/IGFN1","total_profiled":1310},"omim":[{"mim_id":"617309","title":"IMMUNOGLOBULIN-LIKE AND FIBRONECTIN TYPE III DOMAINS-CONTAINING PROTEIN 1; IGFN1","url":"https://www.omim.org/entry/617309"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Midbody ring","reliability":"Approved"}],"tissue_specificity":"Tissue enriched","tissue_distribution":"Detected in some","driving_tissues":[{"tissue":"skeletal muscle","ntpm":174.5}],"url":"https://www.proteinatlas.org/search/IGFN1"},"hgnc":{"alias_symbol":["DKFZp434B1231","EEF1A2BP1"],"prev_symbol":[]},"alphafold":{"accession":"Q86VF2","domains":[{"cath_id":"2.60.40.10","chopping":"6-122","consensus_level":"high","plddt":77.79,"start":6,"end":122},{"cath_id":"2.60.40.10","chopping":"164-307","consensus_level":"medium","plddt":74.1779,"start":164,"end":307},{"cath_id":"2.60.40.10","chopping":"312-395","consensus_level":"high","plddt":83.9689,"start":312,"end":395},{"cath_id":"2.60.40.10","chopping":"464-541","consensus_level":"high","plddt":83.3423,"start":464,"end":541},{"cath_id":"2.60.40.10","chopping":"546-642","consensus_level":"high","plddt":85.3868,"start":546,"end":642},{"cath_id":"2.60.40.10","chopping":"653-736","consensus_level":"high","plddt":87.9833,"start":653,"end":736},{"cath_id":"2.60.40.10","chopping":"752-839","consensus_level":"medium","plddt":87.7067,"start":752,"end":839},{"cath_id":"2.60.40.10","chopping":"853-943","consensus_level":"medium","plddt":87.9908,"start":853,"end":943},{"cath_id":"2.60.40.10","chopping":"1153-1251","consensus_level":"medium","plddt":77.1135,"start":1153,"end":1251}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q86VF2","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q86VF2-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q86VF2-F1-predicted_aligned_error_v6.png","plddt_mean":77.38},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=IGFN1","jax_strain_url":"https://www.jax.org/strain/search?query=IGFN1"},"sequence":{"accession":"Q86VF2","fasta_url":"https://rest.uniprot.org/uniprotkb/Q86VF2.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q86VF2/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q86VF2"}},"corpus_meta":[{"pmid":"28027327","id":"PMC_28027327","title":"Mutational 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associated protein in skeletal muscle that forms a protein complex with KY and filamin C (FLNC). Yeast two-hybrid screening identified FLNC as an IGFN1 interacting partner, and the three N-terminal globular domains of IGFN1 are sufficient for Z-band targeting. KY co-localizes with IGFN1 at the Z-band in C2C12-derived myotubes and neonatal cardiomyocytes.\",\n      \"method\": \"Yeast two-hybrid screening, immunofluorescence, recombinant protein expression, immunodetection in C2C12-derived myotubes and neonatal cardiomyocytes\",\n      \"journal\": \"Experimental cell research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — yeast two-hybrid plus biochemical and immunofluorescence data in multiple cell types, single lab\",\n      \"pmids\": [\"20206623\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"IGFN1 was identified as a novel binding partner of eukaryotic translation elongation factor 1A (eEF1A) via yeast two-hybrid screening of a human skeletal muscle cDNA library, with the interaction confirmed in vitro. IGFN1 shows sequence and structural homology to myosin binding protein-C (fast and slow-type skeletal muscle isoforms) and is substantially upregulated during muscle denervation.\",\n      \"method\": \"Yeast two-hybrid screening of human skeletal muscle cDNA library, in vitro binding confirmation\",\n      \"journal\": \"Journal of cellular biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — yeast two-hybrid plus in vitro confirmation, single lab, two orthogonal methods\",\n      \"pmids\": [\"18756455\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"IGFN1_v1 is required for myoblast fusion and differentiation. shRNA-mediated knockdown of all Igfn1 variants completely blocked myoblast fusion without preventing expression of differentiation markers. CRISPR/Cas9 deletion of exon 13 (encoding N-terminal domains) caused fusion defects and abnormal large multinucleated cells. Expression of IGFN1_v1 partially rescued fusion and myotube morphology in the exon 13 knockout cell line.\",\n      \"method\": \"shRNA knockdown, CRISPR/Cas9 homologous recombination (exon 13 deletion), rescue by IGFN1_v1 overexpression in C2C12 cells\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — two independent loss-of-function approaches (shRNA and CRISPR/Cas9) with specific phenotypic readout plus rescue experiment, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"28665998\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"IGFN1-deficient C2C12 myoblasts show elevated G:F actin ratios during differentiation, indicating deficient actin remodelling underlies fusion and differentiation defects. Proteomic pull-down from skeletal muscle with IGFN1 fragments identified the actin nucleating protein COBL as a binding partner; IGFN1 interacts with, stabilizes, and co-localizes with COBL at the Z-disc, and prevents COBL from forming actin ruffles in COS7 cells. The proteasome was also identified as a main network in IGFN1 complexes. COBL loss-of-function C2C12 clones retain the ability to fuse, indicating COBL or the IGFN1/COBL interaction is not essential for myoblast fusion.\",\n      \"method\": \"G:F actin ratio assay in IGFN1-deficient C2C12 cells, IGFN1 fragment pull-down from skeletal muscle with proteomics, co-immunoprecipitation/co-localization of IGFN1 and COBL, actin ruffle assay in COS7 cells, COBL loss-of-function clones\",\n      \"journal\": \"Experimental cell research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (proteomics pull-down, co-IP, co-localization, functional actin assay, loss-of-function) in single rigorous study\",\n      \"pmids\": [\"32768501\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"A stable G-quadruplex structure forms in intron 15 of the IGFN1 gene (confirmed by gel shift assay and circular dichroism spectroscopy with G-quadruplex stabilizing agents PDS and KCl) and inhibits reverse transcriptase and Taq polymerase in stop assays. Treatment with the G-quadruplex stabilizer pyridostatin (PDS) alters IGFN1 splicing isoforms in UOK146 renal cell carcinoma cells, implicating intronic G-quadruplex formation in IGFN1 aberrant splicing.\",\n      \"method\": \"Gel shift assay, circular dichroism spectroscopy, reverse transcriptase and PCR stop assays, Sanger sequencing of PQS and mutant plasmid constructs, PDS treatment in UOK146 cells\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — multiple in vitro biochemical assays (CD, gel shift, polymerase stop) plus cell-based splicing assay, single lab\",\n      \"pmids\": [\"30335789\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"IGFN1 is a skeletal muscle Z-band protein that forms a complex with KY and filamin C (FLNC), interacts with eEF1A (potentially modulating protein synthesis during denervation), and is required for myoblast fusion and differentiation through regulation of actin dynamics—partly via interaction with and stabilization of the actin nucleating protein COBL; additionally, a stable intronic G-quadruplex in IGFN1 intron 15 regulates alternative splicing of the locus.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"IGFN1 is a skeletal muscle Z-band/Z-disc-associated protein that scaffolds the contractile apparatus and governs myoblast fusion and differentiation through control of actin dynamics [#0, #2, #3]. Its three N-terminal globular domains are sufficient for Z-band targeting, where it assembles into a complex with KY and filamin C (FLNC) [#0]. Loss of all IGFN1 variants by shRNA, or deletion of exon 13 encoding N-terminal domains, completely blocks myoblast fusion and produces abnormal large multinucleated cells without preventing differentiation-marker expression, and re-expression of IGFN1_v1 partially rescues these defects [#2]. Mechanistically, IGFN1-deficient myoblasts show elevated G:F actin ratios indicative of deficient actin remodelling; IGFN1 binds, stabilizes, and co-localizes at the Z-disc with the actin-nucleating protein COBL and restrains COBL-driven actin ruffling [#3]. IGFN1 also binds eukaryotic translation elongation factor eEF1A and is strongly upregulated during muscle denervation, linking it to protein-synthesis regulation in muscle [#1]. At the gene level, a stable G-quadruplex in intron 15 modulates alternative splicing of the locus [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2008,\n      \"claim\": \"Established a first molecular partner and regulatory context for IGFN1 by identifying it as an eEF1A-binding muscle protein induced during denervation, hinting at a role coupling muscle state to translational machinery.\",\n      \"evidence\": \"Yeast two-hybrid screening of a human skeletal muscle cDNA library with in vitro binding confirmation\",\n      \"pmids\": [\"18756455\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional consequence of the eEF1A interaction on translation not demonstrated\",\n        \"Denervation upregulation correlative, not mechanistically tied to eEF1A binding\",\n        \"No structural mapping of the interaction interface\"\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Placed IGFN1 at the Z-band as part of a defined sarcomeric complex, defining where in muscle architecture it operates.\",\n      \"evidence\": \"Yeast two-hybrid, recombinant domain mapping, and immunofluorescence in C2C12 myotubes and neonatal cardiomyocytes\",\n      \"pmids\": [\"20206623\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional role of the IGFN1/KY/FLNC complex not tested\",\n        \"Single-lab interaction data without in vivo validation\",\n        \"Stoichiometry and assembly order of the complex unknown\"\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Demonstrated that IGFN1 is functionally required for myoblast fusion, moving it from a structural component to a determinant of muscle cell morphogenesis.\",\n      \"evidence\": \"shRNA knockdown and CRISPR/Cas9 exon 13 deletion with IGFN1_v1 rescue in C2C12 cells\",\n      \"pmids\": [\"28665998\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Molecular mechanism downstream of IGFN1 not resolved in this study\",\n        \"Only partial rescue achieved\",\n        \"In vivo muscle phenotype not addressed\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Identified the mechanistic basis of the fusion defect as deficient actin remodelling and linked IGFN1 to the actin nucleator COBL, explaining how a Z-disc scaffold controls cytoskeletal dynamics.\",\n      \"evidence\": \"G:F actin assays, IGFN1 fragment pull-down proteomics, co-IP/co-localization, actin ruffle assay in COS7, and COBL loss-of-function clones\",\n      \"pmids\": [\"32768501\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"COBL loss-of-function clones still fuse, so COBL is not essential for fusion\",\n        \"The fusion-relevant actin effector downstream of IGFN1 remains unidentified\",\n        \"Role of the proteasome network found in IGFN1 complexes not defined\"\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Showed that gene-level regulation of IGFN1 isoforms is controlled by an intronic G-quadruplex, adding a transcript-processing layer to its biology.\",\n      \"evidence\": \"Gel shift, circular dichroism, polymerase stop assays, and pyridostatin-induced splicing changes in UOK146 cells\",\n      \"pmids\": [\"30335789\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Splicing effect shown in a renal carcinoma line, not skeletal muscle\",\n        \"Endogenous splicing factors reading the G-quadruplex not identified\",\n        \"Physiological relevance of isoform switching not established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The effector pathway by which IGFN1-dependent actin remodelling drives myoblast fusion, and how its Z-disc, eEF1A, and splicing functions integrate in vivo, remain unresolved.\",\n      \"evidence\": \"No single study in the corpus connects IGFN1's scaffolding, translational, and splicing roles in an intact muscle model\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No in vivo (animal) loss-of-function phenotype in the corpus\",\n        \"Fusion-essential actin effector unidentified\",\n        \"Functional consequence of eEF1A binding undefined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [2]},\n      {\"term_id\": \"R-HSA-397014\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"FLNC\", \"KY\", \"EEF1A1\", \"COBL\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":6,"faith_total":6,"faith_pct":100.0}}