{"gene":"STK11IP","run_date":"2026-04-28T20:42:08","timeline":{"discoveries":[{"year":2001,"finding":"LIP1 (STK11IP) was identified as a novel leucine-rich repeat-containing cytoplasmic protein that interacts with LKB1. Co-expression of LKB1 and LIP1 dramatically increases the proportion of cytoplasmic LKB1, suggesting LIP1 regulates LKB1 function by controlling its subcellular localization.","method":"Co-immunoprecipitation, subcellular localization by imaging, ectopic co-expression in Xenopus embryos","journal":"Human molecular genetics","confidence":"High","confidence_rationale":"Tier 2 — reciprocal interaction, localization shift, and in vivo functional phenotype (secondary body axis) in a single study","pmids":["11741830"],"is_preprint":false},{"year":2001,"finding":"LIP1 (STK11IP) interacts with the TGFβ-regulated transcription factor SMAD4, forming a LKB1-LIP1-SMAD4 ternary complex, suggesting a mechanistic link between LKB1/Peutz-Jeghers syndrome and TGFβ/SMAD4 signaling.","method":"Co-immunoprecipitation, ternary complex pulldown","journal":"Human molecular genetics","confidence":"Medium","confidence_rationale":"Tier 3 — single lab, co-IP showing ternary complex but limited functional follow-up of the SMAD4 interaction","pmids":["11741830"],"is_preprint":false},{"year":2010,"finding":"LKB1 phosphorylates SMAD4 on Thr77 of its DNA-binding domain, and LIP1 self-oligomerizes and scaffolds the LKB1-LIP1-SMAD4 complex. LKB1 inhibits SMAD4 binding to TGFβ- and BMP-responsive promoters, negatively regulating TGFβ-induced transcription and epithelial-mesenchymal transition.","method":"In vitro kinase assay, mutagenesis, promoter-binding assays, reporter assays, Co-IP","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1–2 — in vitro phosphorylation assay with site identification, promoter binding, and transcriptional readout in a single study","pmids":["20974850"],"is_preprint":false},{"year":2022,"finding":"STK11IP is a lysosome-specific substrate of mTORC1; mTORC1 phosphorylates STK11IP at Ser404. STK11IP binds to V-ATPase and regulates its activity to control lysosomal acidification. Knockout of STK11IP increases autophagy flux, and dephosphorylation of STK11IP at Ser404 represses its role as an autophagy inhibitor.","method":"Quantitative phosphoproteomics, lysosome proteome cross-reference, genetic knockout (in vitro and in vivo mouse models), Co-IP with V-ATPase, autophagy flux assays","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1–2 — mass spectrometry-identified phosphosite, validated by KO with defined cellular and in vivo phenotype, V-ATPase binding confirmed by Co-IP, multiple orthogonal methods","pmids":["35365663"],"is_preprint":false},{"year":2021,"finding":"LKB1IP (STK11IP) promotes pathological cardiac hypertrophy by directly targeting PTEN and inhibiting its phosphatase activity, thereby activating Akt signaling.","method":"LKB1IP knockout mice, isoproterenol/TAC-induced hypertrophy models, in vitro PTEN phosphatase activity assay, Co-IP","journal":"Journal of cellular and molecular medicine","confidence":"Medium","confidence_rationale":"Tier 2 — KO with defined phenotype and direct in vitro PTEN phosphatase inhibition assay, single lab","pmids":["33486894"],"is_preprint":false}],"current_model":"STK11IP (LIP1) is a leucine-rich repeat scaffold protein that (1) controls LKB1 subcellular localization by retaining it in the cytoplasm, (2) bridges LKB1 and SMAD4 into a ternary complex through which LKB1 phosphorylates SMAD4-Thr77 to negatively regulate TGFβ transcriptional responses, (3) serves as a lysosome-specific mTORC1 substrate (phosphorylated at Ser404) that binds V-ATPase to regulate lysosomal acidification and suppress autophagy flux, and (4) promotes cardiac hypertrophy by inhibiting PTEN phosphatase activity to activate Akt signaling."},"narrative":{"teleology":[{"year":2001,"claim":"The identity of LKB1-interacting partners that control its localization was unknown; discovery of LIP1/STK11IP as a leucine-rich repeat protein that retains LKB1 in the cytoplasm established the first mechanism for regulated LKB1 subcellular distribution and linked it to SMAD4 via a ternary complex.","evidence":"Co-immunoprecipitation, subcellular imaging after co-expression, Xenopus ectopic axis assay, and ternary complex pulldown","pmids":["11741830"],"confidence":"High","gaps":["Endogenous stoichiometry and physiological triggers for LKB1 cytoplasmic retention were not determined","Functional consequence of the SMAD4 interaction on transcription was not addressed in this initial study"]},{"year":2010,"claim":"How LKB1 regulates TGFβ signaling through STK11IP was resolved: LKB1 phosphorylates SMAD4 on Thr77 within the DNA-binding domain, disrupting promoter occupancy and thereby negatively regulating TGFβ/BMP-driven transcription and EMT, with STK11IP serving as the obligate scaffold via self-oligomerization.","evidence":"In vitro kinase assay with site-directed mutagenesis, promoter-binding assays, transcriptional reporter assays, co-immunoprecipitation","pmids":["20974850"],"confidence":"High","gaps":["Whether STK11IP scaffolding is rate-limiting for SMAD4 phosphorylation in vivo is untested","Relevance to Peutz–Jeghers syndrome tumor suppression has not been directly demonstrated"]},{"year":2021,"claim":"Whether STK11IP has LKB1-independent signaling roles was unclear; demonstration that STK11IP directly inhibits PTEN phosphatase activity to activate Akt signaling identified a distinct pro-hypertrophic function in the heart.","evidence":"STK11IP knockout mice subjected to isoproterenol/TAC-induced hypertrophy, in vitro PTEN phosphatase activity assay, co-immunoprecipitation","pmids":["33486894"],"confidence":"Medium","gaps":["Molecular basis of PTEN inhibition (binding site, stoichiometry) is uncharacterized","Whether this PTEN-inhibitory function occurs outside cardiac tissue is unknown","Single-lab finding; independent replication is lacking"]},{"year":2022,"claim":"STK11IP's relationship to mTORC1 and lysosomal biology was unknown; identification of STK11IP as a lysosome-specific mTORC1 substrate (Ser404) that binds V-ATPase and controls lysosomal acidification repositioned the protein as a direct autophagy suppressor downstream of mTORC1.","evidence":"Quantitative phosphoproteomics, lysosome proteome cross-referencing, genetic knockout in cells and mice, V-ATPase co-immunoprecipitation, autophagy flux assays","pmids":["35365663"],"confidence":"High","gaps":["How phospho-Ser404 alters STK11IP–V-ATPase binding or V-ATPase assembly is mechanistically undefined","Structural basis of the STK11IP–V-ATPase interaction is lacking","Whether lysosomal and cytoplasmic LKB1-scaffolding functions of STK11IP are coordinated or independent is unresolved"]},{"year":null,"claim":"A unified model integrating STK11IP's lysosomal mTORC1-effector role, cytoplasmic LKB1-scaffolding role, and PTEN-inhibitory role — and whether these functions are spatially or temporally segregated — remains to be constructed.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural model of STK11IP exists","The relationship between STK11IP oligomerization and its distinct partner interactions is unexplored","Tissue-specific versus universal functions of STK11IP are not delineated"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1,2]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[3,4]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0]},{"term_id":"GO:0005764","term_label":"lysosome","supporting_discovery_ids":[3]}],"pathway":[{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[2,3,4]},{"term_id":"R-HSA-9612973","term_label":"Autophagy","supporting_discovery_ids":[3]}],"complexes":["LKB1–STK11IP–SMAD4 ternary complex"],"partners":["STK11","SMAD4","PTEN","ATP6V1A"],"other_free_text":[]},"mechanistic_narrative":"STK11IP (LIP1) is a leucine-rich repeat scaffold protein that integrates LKB1/AMPK, TGFβ/SMAD, and mTORC1/lysosome signaling axes. It was originally identified as a cytoplasmic anchor for the LKB1 kinase: co-expression shifts LKB1 from the nucleus to the cytoplasm, and STK11IP self-oligomerizes to scaffold a ternary LKB1–STK11IP–SMAD4 complex in which LKB1 phosphorylates SMAD4-Thr77, thereby suppressing SMAD4 binding to TGFβ/BMP-responsive promoters and inhibiting epithelial–mesenchymal transition [PMID:11741830, PMID:20974850]. At the lysosome, STK11IP is phosphorylated at Ser404 by mTORC1 and binds V-ATPase to regulate lysosomal acidification; its genetic ablation increases autophagy flux, establishing STK11IP as a lysosome-specific mTORC1 effector that restrains autophagy [PMID:35365663]. STK11IP also directly inhibits PTEN phosphatase activity to activate Akt signaling, promoting pathological cardiac hypertrophy in mouse models of pressure overload [PMID:33486894]."},"prefetch_data":{"uniprot":{"accession":"Q8N1F8","full_name":"Serine/threonine-protein kinase 11-interacting protein","aliases":["LKB1-interacting protein 1"],"length_aa":1088,"mass_kda":120.3,"function":"May regulate STK11/LKB1 function by controlling its subcellular localization","subcellular_location":"Cytoplasm","url":"https://www.uniprot.org/uniprotkb/Q8N1F8/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/STK11IP","classification":"Not Classified","n_dependent_lines":1,"n_total_lines":1208,"dependency_fraction":0.0008278145695364238},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"TMEM106B","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/STK11IP","total_profiled":1310},"omim":[{"mim_id":"607172","title":"SERINE/THREONINE KINASE 11-INTERACTING PROTEIN; STK11IP","url":"https://www.omim.org/entry/607172"},{"mim_id":"175200","title":"PEUTZ-JEGHERS SYNDROME; PJS","url":"https://www.omim.org/entry/175200"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Vesicles","reliability":"Enhanced"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/STK11IP"},"hgnc":{"alias_symbol":["LIP1","KIAA1898","LKB1IP","STK11IP1"],"prev_symbol":[]},"alphafold":{"accession":"Q8N1F8","domains":[{"cath_id":"3.80.10.10","chopping":"2-53_71-263","consensus_level":"medium","plddt":85.4658,"start":2,"end":263},{"cath_id":"2.30.29.30","chopping":"537-592_611-659","consensus_level":"high","plddt":84.479,"start":537,"end":659},{"cath_id":"2.30.29.30","chopping":"783-924","consensus_level":"high","plddt":84.1563,"start":783,"end":924},{"cath_id":"2.30.29.30","chopping":"939-981_1008-1082","consensus_level":"high","plddt":85.8332,"start":939,"end":1082}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N1F8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N1F8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N1F8-F1-predicted_aligned_error_v6.png","plddt_mean":67.94},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=STK11IP","jax_strain_url":"https://www.jax.org/strain/search?query=STK11IP"},"sequence":{"accession":"Q8N1F8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8N1F8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8N1F8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N1F8"}},"corpus_meta":[{"pmid":"11161219","id":"PMC_11161219","title":"Notch 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agriculture","url":"https://pubmed.ncbi.nlm.nih.gov/40159693","citation_count":0,"is_preprint":false},{"pmid":"40521868","id":"PMC_40521868","title":"Structural and Functional Analysis of Plant Oil-Body Lipase Eg LIP1 From Elaeis guineensis.","date":"2025","source":"Proteins","url":"https://pubmed.ncbi.nlm.nih.gov/40521868","citation_count":0,"is_preprint":false},{"pmid":"40936029","id":"PMC_40936029","title":"Protecting DNA and improving freeze-drying survival rate of Lactiplantibacillus plantarum LIP-1 through metabolism of hypoxanthine.","date":"2025","source":"World journal of microbiology & biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/40936029","citation_count":0,"is_preprint":false},{"pmid":"40073550","id":"PMC_40073550","title":"Sucrose improve Lactiplantibacillus plantarum LIP-1's tolerance to heat by increasing biofilm production.","date":"2025","source":"International journal of food microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/40073550","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":26464,"output_tokens":1353,"usd":0.049843},"stage2":{"model":"claude-opus-4-6","input_tokens":4590,"output_tokens":1792,"usd":0.101625},"total_usd":0.151468,"stage1_batch_id":"msgbatch_011rkcQdVV1RaFq9XhcG6df6","stage2_batch_id":"msgbatch_01RzgrJafdF4EWHhj5mNi6dh","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2001,\n      \"finding\": \"LIP1 (STK11IP) was identified as a novel leucine-rich repeat-containing cytoplasmic protein that interacts with LKB1. Co-expression of LKB1 and LIP1 dramatically increases the proportion of cytoplasmic LKB1, suggesting LIP1 regulates LKB1 function by controlling its subcellular localization.\",\n      \"method\": \"Co-immunoprecipitation, subcellular localization by imaging, ectopic co-expression in Xenopus embryos\",\n      \"journal\": \"Human molecular genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal interaction, localization shift, and in vivo functional phenotype (secondary body axis) in a single study\",\n      \"pmids\": [\"11741830\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2001,\n      \"finding\": \"LIP1 (STK11IP) interacts with the TGFβ-regulated transcription factor SMAD4, forming a LKB1-LIP1-SMAD4 ternary complex, suggesting a mechanistic link between LKB1/Peutz-Jeghers syndrome and TGFβ/SMAD4 signaling.\",\n      \"method\": \"Co-immunoprecipitation, ternary complex pulldown\",\n      \"journal\": \"Human molecular genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 — single lab, co-IP showing ternary complex but limited functional follow-up of the SMAD4 interaction\",\n      \"pmids\": [\"11741830\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"LKB1 phosphorylates SMAD4 on Thr77 of its DNA-binding domain, and LIP1 self-oligomerizes and scaffolds the LKB1-LIP1-SMAD4 complex. LKB1 inhibits SMAD4 binding to TGFβ- and BMP-responsive promoters, negatively regulating TGFβ-induced transcription and epithelial-mesenchymal transition.\",\n      \"method\": \"In vitro kinase assay, mutagenesis, promoter-binding assays, reporter assays, Co-IP\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — in vitro phosphorylation assay with site identification, promoter binding, and transcriptional readout in a single study\",\n      \"pmids\": [\"20974850\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"STK11IP is a lysosome-specific substrate of mTORC1; mTORC1 phosphorylates STK11IP at Ser404. STK11IP binds to V-ATPase and regulates its activity to control lysosomal acidification. Knockout of STK11IP increases autophagy flux, and dephosphorylation of STK11IP at Ser404 represses its role as an autophagy inhibitor.\",\n      \"method\": \"Quantitative phosphoproteomics, lysosome proteome cross-reference, genetic knockout (in vitro and in vivo mouse models), Co-IP with V-ATPase, autophagy flux assays\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 — mass spectrometry-identified phosphosite, validated by KO with defined cellular and in vivo phenotype, V-ATPase binding confirmed by Co-IP, multiple orthogonal methods\",\n      \"pmids\": [\"35365663\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"LKB1IP (STK11IP) promotes pathological cardiac hypertrophy by directly targeting PTEN and inhibiting its phosphatase activity, thereby activating Akt signaling.\",\n      \"method\": \"LKB1IP knockout mice, isoproterenol/TAC-induced hypertrophy models, in vitro PTEN phosphatase activity assay, Co-IP\",\n      \"journal\": \"Journal of cellular and molecular medicine\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — KO with defined phenotype and direct in vitro PTEN phosphatase inhibition assay, single lab\",\n      \"pmids\": [\"33486894\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"STK11IP (LIP1) is a leucine-rich repeat scaffold protein that (1) controls LKB1 subcellular localization by retaining it in the cytoplasm, (2) bridges LKB1 and SMAD4 into a ternary complex through which LKB1 phosphorylates SMAD4-Thr77 to negatively regulate TGFβ transcriptional responses, (3) serves as a lysosome-specific mTORC1 substrate (phosphorylated at Ser404) that binds V-ATPase to regulate lysosomal acidification and suppress autophagy flux, and (4) promotes cardiac hypertrophy by inhibiting PTEN phosphatase activity to activate Akt signaling.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"STK11IP (LIP1) is a leucine-rich repeat scaffold protein that integrates LKB1/AMPK, TGFβ/SMAD, and mTORC1/lysosome signaling axes. It was originally identified as a cytoplasmic anchor for the LKB1 kinase: co-expression shifts LKB1 from the nucleus to the cytoplasm, and STK11IP self-oligomerizes to scaffold a ternary LKB1–STK11IP–SMAD4 complex in which LKB1 phosphorylates SMAD4-Thr77, thereby suppressing SMAD4 binding to TGFβ/BMP-responsive promoters and inhibiting epithelial–mesenchymal transition [PMID:11741830, PMID:20974850]. At the lysosome, STK11IP is phosphorylated at Ser404 by mTORC1 and binds V-ATPase to regulate lysosomal acidification; its genetic ablation increases autophagy flux, establishing STK11IP as a lysosome-specific mTORC1 effector that restrains autophagy [PMID:35365663]. STK11IP also directly inhibits PTEN phosphatase activity to activate Akt signaling, promoting pathological cardiac hypertrophy in mouse models of pressure overload [PMID:33486894].\",\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"The identity of LKB1-interacting partners that control its localization was unknown; discovery of LIP1/STK11IP as a leucine-rich repeat protein that retains LKB1 in the cytoplasm established the first mechanism for regulated LKB1 subcellular distribution and linked it to SMAD4 via a ternary complex.\",\n      \"evidence\": \"Co-immunoprecipitation, subcellular imaging after co-expression, Xenopus ectopic axis assay, and ternary complex pulldown\",\n      \"pmids\": [\"11741830\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Endogenous stoichiometry and physiological triggers for LKB1 cytoplasmic retention were not determined\",\n        \"Functional consequence of the SMAD4 interaction on transcription was not addressed in this initial study\"\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"How LKB1 regulates TGFβ signaling through STK11IP was resolved: LKB1 phosphorylates SMAD4 on Thr77 within the DNA-binding domain, disrupting promoter occupancy and thereby negatively regulating TGFβ/BMP-driven transcription and EMT, with STK11IP serving as the obligate scaffold via self-oligomerization.\",\n      \"evidence\": \"In vitro kinase assay with site-directed mutagenesis, promoter-binding assays, transcriptional reporter assays, co-immunoprecipitation\",\n      \"pmids\": [\"20974850\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether STK11IP scaffolding is rate-limiting for SMAD4 phosphorylation in vivo is untested\",\n        \"Relevance to Peutz–Jeghers syndrome tumor suppression has not been directly demonstrated\"\n      ]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Whether STK11IP has LKB1-independent signaling roles was unclear; demonstration that STK11IP directly inhibits PTEN phosphatase activity to activate Akt signaling identified a distinct pro-hypertrophic function in the heart.\",\n      \"evidence\": \"STK11IP knockout mice subjected to isoproterenol/TAC-induced hypertrophy, in vitro PTEN phosphatase activity assay, co-immunoprecipitation\",\n      \"pmids\": [\"33486894\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Molecular basis of PTEN inhibition (binding site, stoichiometry) is uncharacterized\",\n        \"Whether this PTEN-inhibitory function occurs outside cardiac tissue is unknown\",\n        \"Single-lab finding; independent replication is lacking\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"STK11IP's relationship to mTORC1 and lysosomal biology was unknown; identification of STK11IP as a lysosome-specific mTORC1 substrate (Ser404) that binds V-ATPase and controls lysosomal acidification repositioned the protein as a direct autophagy suppressor downstream of mTORC1.\",\n      \"evidence\": \"Quantitative phosphoproteomics, lysosome proteome cross-referencing, genetic knockout in cells and mice, V-ATPase co-immunoprecipitation, autophagy flux assays\",\n      \"pmids\": [\"35365663\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"How phospho-Ser404 alters STK11IP–V-ATPase binding or V-ATPase assembly is mechanistically undefined\",\n        \"Structural basis of the STK11IP–V-ATPase interaction is lacking\",\n        \"Whether lysosomal and cytoplasmic LKB1-scaffolding functions of STK11IP are coordinated or independent is unresolved\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"A unified model integrating STK11IP's lysosomal mTORC1-effector role, cytoplasmic LKB1-scaffolding role, and PTEN-inhibitory role — and whether these functions are spatially or temporally segregated — remains to be constructed.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No structural model of STK11IP exists\",\n        \"The relationship between STK11IP oligomerization and its distinct partner interactions is unexplored\",\n        \"Tissue-specific versus universal functions of STK11IP are not delineated\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [3, 4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005764\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [2, 3, 4]},\n      {\"term_id\": \"R-HSA-9612973\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [\n      \"LKB1–STK11IP–SMAD4 ternary complex\"\n    ],\n    \"partners\": [\n      \"STK11\",\n      \"SMAD4\",\n      \"PTEN\",\n      \"ATP6V1A\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}