{"gene":"IGFN1","run_date":"2026-04-28T18:06:53","timeline":{"discoveries":[{"year":2010,"finding":"IGFN1 was identified as a Z-band associated protein in skeletal muscle that forms a complex with KY and filamin C (FLNC). The three N-terminal globular domains of IGFN1 are sufficient for Z-band targeting, and interaction with KY was identified through a KY interacting protein fragment screen, while FLNC was identified as an IGFN1 binding partner by yeast two-hybrid.","method":"Yeast two-hybrid, immunofluorescence, co-immunoprecipitation, recombinant fragment expression in C2C12 myotubes and neonatal cardiomyocytes","journal":"Experimental cell research","confidence":"High","confidence_rationale":"Tier 2 — reciprocal interaction validation by multiple orthogonal methods (Y2H, biochemical, IF localization) in a single study","pmids":["20206623"],"is_preprint":false},{"year":2008,"finding":"IGFN1 was identified as a binding partner of eukaryotic translation elongation factor eEF1A in skeletal muscle. The interaction was discovered by yeast two-hybrid screening of a human skeletal muscle cDNA library and confirmed in vitro. IGFN1 shows structural homology to myosin binding protein-C, is specifically expressed in skeletal muscle, and is substantially upregulated during muscle denervation, suggesting it may downregulate protein synthesis via interaction with eEF1A.","method":"Yeast two-hybrid screen, in vitro binding assay confirmation","journal":"Journal of cellular biochemistry","confidence":"Medium","confidence_rationale":"Tier 2 — Y2H plus in vitro validation, single lab","pmids":["18756455"],"is_preprint":false},{"year":2017,"finding":"IGFN1 is required for myoblast fusion and differentiation. Knockdown of Igfn1 via shRNAs targeting the common 3'-UTR caused complete blunting of myoblast fusion without preventing differentiation marker expression. CRISPR/Cas9-mediated deletion of exon 13 also caused fusion defects. Expression of IGFN1_v1 partially rescued fusion and myotube morphology in the exon 13 knockout cell line.","method":"shRNA knockdown, CRISPR/Cas9 knockout, rescue by IGFN1_v1 overexpression in C2C12 cells","journal":"PloS one","confidence":"High","confidence_rationale":"Tier 2 — loss-of-function with specific phenotypic readout replicated by two independent methods plus rescue experiment","pmids":["28665998"],"is_preprint":false},{"year":2020,"finding":"IGFN1 interacts with, stabilizes, and colocalizes with the actin nucleating protein COBL at the Z-disc. IGFN1-deficient C2C12 myoblasts show significantly higher G:F actin ratios during differentiation, indicating deficient actin remodeling underlies the fusion and differentiation defects. IGFN1 prevents COBL from forming actin ruffles in COS7 cells. Proteomics of IGFN1 pull-downs from skeletal muscle identified cytoskeleton and proteasome as main interaction networks.","method":"Co-immunoprecipitation, proteomics/mass spectrometry pull-down from skeletal muscle, G:F actin ratio measurement, colocalization by immunofluorescence, COS7 cell overexpression assay, COBL loss-of-function clones","journal":"Experimental cell research","confidence":"High","confidence_rationale":"Tier 2 — multiple orthogonal methods (proteomics, Co-IP, actin ratio, functional overexpression assay, KO), single lab with rigorous follow-up","pmids":["32768501"],"is_preprint":false},{"year":2018,"finding":"An intronic G-quadruplex-forming sequence (PQS) in IGFN1 intron 15 folds into a stable G-quadruplex structure that regulates alternative splicing of IGFN1. Stabilization of the G-quadruplex by pyridostatin (PDS) altered splicing isoforms of IGFN1 in renal cell carcinoma cells. The G-quadruplex inhibits reverse transcriptase and Taq polymerase in stop assays, and its formation site was mapped at single-base resolution.","method":"Gel shift assay, circular dichroism spectroscopy, reverse transcriptase stop assay, PCR stop assay, Sanger sequencing of plasmid constructs, PDS treatment of UOK146 cell line","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 1-2 — multiple in vitro biophysical assays and cell-based splicing assay, single lab","pmids":["30335789"],"is_preprint":false}],"current_model":"IGFN1 is a multi-domain (Ig-like and fibronectin type III) skeletal muscle protein that localizes to the Z-disc via its three N-terminal globular domains, where it forms a complex with KY and filamin C (FLNC); it binds and inhibits the actin nucleating protein COBL to regulate actin dynamics, interacts with translation elongation factor eEF1A to potentially modulate protein synthesis, and is required for myoblast fusion and differentiation, with its expression upregulated upon muscle denervation."},"narrative":{"teleology":[{"year":2008,"claim":"Establishing that IGFN1 is a skeletal-muscle-specific protein that physically engages the translational machinery answered the question of what molecular partners this uncharacterized multi-domain protein interacts with, implicating it in regulation of protein synthesis during muscle atrophy.","evidence":"Yeast two-hybrid screen of human skeletal muscle cDNA library with in vitro binding validation; denervation expression profiling","pmids":["18756455"],"confidence":"Medium","gaps":["Interaction with eEF1A confirmed only by Y2H and in vitro binding without in vivo validation","Functional consequence on translation not directly measured","Whether upregulation during denervation is causally linked to atrophy remains untested"]},{"year":2010,"claim":"Determining that IGFN1 localizes to the Z-disc through its N-terminal domains and forms a ternary complex with KY and FLNC established its role as a sarcomeric scaffolding protein rather than a diffuse cytoplasmic factor.","evidence":"Yeast two-hybrid, co-immunoprecipitation, and immunofluorescence in C2C12 myotubes and neonatal cardiomyocytes; domain-deletion constructs","pmids":["20206623"],"confidence":"High","gaps":["Stoichiometry and architecture of the KY–IGFN1–FLNC complex are unknown","Whether the complex is required for Z-disc integrity or is regulatory has not been tested"]},{"year":2017,"claim":"Demonstrating that IGFN1 loss blocks myoblast fusion while preserving differentiation marker expression resolved whether the protein is needed for general differentiation or specifically for the cell fusion step of myogenesis.","evidence":"shRNA knockdown and CRISPR/Cas9 exon 13 deletion in C2C12 cells with rescue by IGFN1_v1 overexpression","pmids":["28665998"],"confidence":"High","gaps":["In vivo validation in animal models is absent","Which IGFN1 domain(s) are critical for the fusion function has not been mapped"]},{"year":2018,"claim":"Identifying a stable intronic G-quadruplex that regulates IGFN1 alternative splicing revealed a cis-regulatory mechanism controlling isoform diversity, though the physiological relevance in muscle was tested only in a renal carcinoma cell line.","evidence":"Biophysical assays (CD, gel shift, RT/PCR stop assays) and pyridostatin treatment of UOK146 cells","pmids":["30335789"],"confidence":"Medium","gaps":["Splicing regulation by the G-quadruplex has not been confirmed in skeletal muscle cells","Which IGFN1 isoforms are functionally distinct remains unresolved"]},{"year":2020,"claim":"Showing that IGFN1 binds and inhibits the actin nucleator COBL at the Z-disc, with IGFN1 loss causing elevated G:F actin ratios, provided a mechanistic explanation for how IGFN1 controls actin remodeling during myoblast fusion.","evidence":"Co-IP, proteomics pull-downs from skeletal muscle, G:F actin ratio measurements in IGFN1-deficient C2C12 cells, COS7 overexpression assay","pmids":["32768501"],"confidence":"High","gaps":["Direct binding domains between IGFN1 and COBL have not been mapped","Whether COBL re-expression rescues fusion in IGFN1-null cells is untested","Proteasome interactions identified by proteomics have not been functionally explored"]},{"year":null,"claim":"It remains unknown whether IGFN1 functions in vivo as a required fusion factor, how its interactions with eEF1A and COBL are coordinated, and whether its isoforms have distinct sarcomeric functions.","evidence":"","pmids":[],"confidence":"Low","gaps":["No in vivo knockout or disease-associated mutation data exist","Relationship between eEF1A binding and COBL inhibition is unexplored","No structural information on any IGFN1 domain or complex is available"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[0,3]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[3]}],"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":[2,3]}],"complexes":["KY–IGFN1–FLNC Z-disc complex"],"partners":["KY","FLNC","COBL","EEF1A1"],"other_free_text":[]},"mechanistic_narrative":"IGFN1 is a multi-domain skeletal muscle protein that localizes to the Z-disc and functions as a critical regulator of actin dynamics during myoblast fusion and differentiation. Its three N-terminal globular domains mediate Z-disc targeting, where it forms a complex with KY and filamin C (FLNC) and interacts with the actin nucleating protein COBL, stabilizing COBL and inhibiting its actin-ruffling activity to control the G:F actin ratio required for proper myotube formation [PMID:20206623, PMID:32768501]. Loss of IGFN1 completely blocks myoblast fusion without abolishing differentiation marker expression, and re-expression of the IGFN1_v1 isoform partially rescues fusion defects [PMID:28665998]. IGFN1 also binds eukaryotic translation elongation factor eEF1A and is markedly upregulated upon muscle denervation, linking it to translational regulation under atrophic conditions [PMID:18756455]."},"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 Profile of Metastatic Breast Cancers: A Retrospective Analysis.","date":"2016","source":"PLoS medicine","url":"https://pubmed.ncbi.nlm.nih.gov/28027327","citation_count":309,"is_preprint":false},{"pmid":"36516485","id":"PMC_36516485","title":"Single nuclei profiling identifies cell specific markers of skeletal muscle aging, frailty, and senescence.","date":"2022","source":"Aging","url":"https://pubmed.ncbi.nlm.nih.gov/36516485","citation_count":106,"is_preprint":false},{"pmid":"35726356","id":"PMC_35726356","title":"Decoding the transcriptome of denervated muscle at single-nucleus resolution.","date":"2022","source":"Journal of cachexia, sarcopenia and muscle","url":"https://pubmed.ncbi.nlm.nih.gov/35726356","citation_count":48,"is_preprint":false},{"pmid":"20206623","id":"PMC_20206623","title":"Identification of a Z-band associated protein complex involving KY, FLNC and IGFN1.","date":"2010","source":"Experimental cell 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{\n      \"year\": 2010,\n      \"finding\": \"IGFN1 was identified as a Z-band associated protein in skeletal muscle that forms a complex with KY and filamin C (FLNC). The three N-terminal globular domains of IGFN1 are sufficient for Z-band targeting, and interaction with KY was identified through a KY interacting protein fragment screen, while FLNC was identified as an IGFN1 binding partner by yeast two-hybrid.\",\n      \"method\": \"Yeast two-hybrid, immunofluorescence, co-immunoprecipitation, recombinant fragment expression in C2C12 myotubes and neonatal cardiomyocytes\",\n      \"journal\": \"Experimental cell research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal interaction validation by multiple orthogonal methods (Y2H, biochemical, IF localization) in a single study\",\n      \"pmids\": [\"20206623\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"IGFN1 was identified as a binding partner of eukaryotic translation elongation factor eEF1A in skeletal muscle. The interaction was discovered by yeast two-hybrid screening of a human skeletal muscle cDNA library and confirmed in vitro. IGFN1 shows structural homology to myosin binding protein-C, is specifically expressed in skeletal muscle, and is substantially upregulated during muscle denervation, suggesting it may downregulate protein synthesis via interaction with eEF1A.\",\n      \"method\": \"Yeast two-hybrid screen, in vitro binding assay confirmation\",\n      \"journal\": \"Journal of cellular biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — Y2H plus in vitro validation, single lab\",\n      \"pmids\": [\"18756455\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"IGFN1 is required for myoblast fusion and differentiation. Knockdown of Igfn1 via shRNAs targeting the common 3'-UTR caused complete blunting of myoblast fusion without preventing differentiation marker expression. CRISPR/Cas9-mediated deletion of exon 13 also caused fusion defects. Expression of IGFN1_v1 partially rescued fusion and myotube morphology in the exon 13 knockout cell line.\",\n      \"method\": \"shRNA knockdown, CRISPR/Cas9 knockout, rescue by IGFN1_v1 overexpression in C2C12 cells\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — loss-of-function with specific phenotypic readout replicated by two independent methods plus rescue experiment\",\n      \"pmids\": [\"28665998\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"IGFN1 interacts with, stabilizes, and colocalizes with the actin nucleating protein COBL at the Z-disc. IGFN1-deficient C2C12 myoblasts show significantly higher G:F actin ratios during differentiation, indicating deficient actin remodeling underlies the fusion and differentiation defects. IGFN1 prevents COBL from forming actin ruffles in COS7 cells. Proteomics of IGFN1 pull-downs from skeletal muscle identified cytoskeleton and proteasome as main interaction networks.\",\n      \"method\": \"Co-immunoprecipitation, proteomics/mass spectrometry pull-down from skeletal muscle, G:F actin ratio measurement, colocalization by immunofluorescence, COS7 cell overexpression assay, COBL loss-of-function clones\",\n      \"journal\": \"Experimental cell research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (proteomics, Co-IP, actin ratio, functional overexpression assay, KO), single lab with rigorous follow-up\",\n      \"pmids\": [\"32768501\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"An intronic G-quadruplex-forming sequence (PQS) in IGFN1 intron 15 folds into a stable G-quadruplex structure that regulates alternative splicing of IGFN1. Stabilization of the G-quadruplex by pyridostatin (PDS) altered splicing isoforms of IGFN1 in renal cell carcinoma cells. The G-quadruplex inhibits reverse transcriptase and Taq polymerase in stop assays, and its formation site was mapped at single-base resolution.\",\n      \"method\": \"Gel shift assay, circular dichroism spectroscopy, reverse transcriptase stop assay, PCR stop assay, Sanger sequencing of plasmid constructs, PDS treatment of UOK146 cell line\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1-2 — multiple in vitro biophysical assays and cell-based splicing assay, single lab\",\n      \"pmids\": [\"30335789\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"IGFN1 is a multi-domain (Ig-like and fibronectin type III) skeletal muscle protein that localizes to the Z-disc via its three N-terminal globular domains, where it forms a complex with KY and filamin C (FLNC); it binds and inhibits the actin nucleating protein COBL to regulate actin dynamics, interacts with translation elongation factor eEF1A to potentially modulate protein synthesis, and is required for myoblast fusion and differentiation, with its expression upregulated upon muscle denervation.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"IGFN1 is a multi-domain skeletal muscle protein that localizes to the Z-disc and functions as a critical regulator of actin dynamics during myoblast fusion and differentiation. Its three N-terminal globular domains mediate Z-disc targeting, where it forms a complex with KY and filamin C (FLNC) and interacts with the actin nucleating protein COBL, stabilizing COBL and inhibiting its actin-ruffling activity to control the G:F actin ratio required for proper myotube formation [PMID:20206623, PMID:32768501]. Loss of IGFN1 completely blocks myoblast fusion without abolishing differentiation marker expression, and re-expression of the IGFN1_v1 isoform partially rescues fusion defects [PMID:28665998]. IGFN1 also binds eukaryotic translation elongation factor eEF1A and is markedly upregulated upon muscle denervation, linking it to translational regulation under atrophic conditions [PMID:18756455].\",\n  \"teleology\": [\n    {\n      \"year\": 2008,\n      \"claim\": \"Establishing that IGFN1 is a skeletal-muscle-specific protein that physically engages the translational machinery answered the question of what molecular partners this uncharacterized multi-domain protein interacts with, implicating it in regulation of protein synthesis during muscle atrophy.\",\n      \"evidence\": \"Yeast two-hybrid screen of human skeletal muscle cDNA library with in vitro binding validation; denervation expression profiling\",\n      \"pmids\": [\"18756455\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Interaction with eEF1A confirmed only by Y2H and in vitro binding without in vivo validation\",\n        \"Functional consequence on translation not directly measured\",\n        \"Whether upregulation during denervation is causally linked to atrophy remains untested\"\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Determining that IGFN1 localizes to the Z-disc through its N-terminal domains and forms a ternary complex with KY and FLNC established its role as a sarcomeric scaffolding protein rather than a diffuse cytoplasmic factor.\",\n      \"evidence\": \"Yeast two-hybrid, co-immunoprecipitation, and immunofluorescence in C2C12 myotubes and neonatal cardiomyocytes; domain-deletion constructs\",\n      \"pmids\": [\"20206623\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Stoichiometry and architecture of the KY–IGFN1–FLNC complex are unknown\",\n        \"Whether the complex is required for Z-disc integrity or is regulatory has not been tested\"\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Demonstrating that IGFN1 loss blocks myoblast fusion while preserving differentiation marker expression resolved whether the protein is needed for general differentiation or specifically for the cell fusion step of myogenesis.\",\n      \"evidence\": \"shRNA knockdown and CRISPR/Cas9 exon 13 deletion in C2C12 cells with rescue by IGFN1_v1 overexpression\",\n      \"pmids\": [\"28665998\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"In vivo validation in animal models is absent\",\n        \"Which IGFN1 domain(s) are critical for the fusion function has not been mapped\"\n      ]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Identifying a stable intronic G-quadruplex that regulates IGFN1 alternative splicing revealed a cis-regulatory mechanism controlling isoform diversity, though the physiological relevance in muscle was tested only in a renal carcinoma cell line.\",\n      \"evidence\": \"Biophysical assays (CD, gel shift, RT/PCR stop assays) and pyridostatin treatment of UOK146 cells\",\n      \"pmids\": [\"30335789\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Splicing regulation by the G-quadruplex has not been confirmed in skeletal muscle cells\",\n        \"Which IGFN1 isoforms are functionally distinct remains unresolved\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Showing that IGFN1 binds and inhibits the actin nucleator COBL at the Z-disc, with IGFN1 loss causing elevated G:F actin ratios, provided a mechanistic explanation for how IGFN1 controls actin remodeling during myoblast fusion.\",\n      \"evidence\": \"Co-IP, proteomics pull-downs from skeletal muscle, G:F actin ratio measurements in IGFN1-deficient C2C12 cells, COS7 overexpression assay\",\n      \"pmids\": [\"32768501\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct binding domains between IGFN1 and COBL have not been mapped\",\n        \"Whether COBL re-expression rescues fusion in IGFN1-null cells is untested\",\n        \"Proteasome interactions identified by proteomics have not been functionally explored\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown whether IGFN1 functions in vivo as a required fusion factor, how its interactions with eEF1A and COBL are coordinated, and whether its isoforms have distinct sarcomeric functions.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No in vivo knockout or disease-associated mutation data exist\",\n        \"Relationship between eEF1A binding and COBL inhibition is unexplored\",\n        \"No structural information on any IGFN1 domain or complex is available\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [3]}\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, 3]}\n    ],\n    \"complexes\": [\n      \"KY–IGFN1–FLNC Z-disc complex\"\n    ],\n    \"partners\": [\n      \"KY\",\n      \"FLNC\",\n      \"COBL\",\n      \"EEF1A1\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}