{"gene":"SH3YL1","run_date":"2026-06-10T07:46:31","timeline":{"discoveries":[{"year":2020,"finding":"SH3YL1 acts as a cytosolic regulator of NADPH oxidase 4 (Nox4): the SYLF domain and SH3 domain of SH3YL1 form a ternary complex with Nox4 and p22phox, and this complex is required for LPS-triggered H2O2 generation and pro-inflammatory cytokine expression in mouse tubular epithelial cells. SH3YL1 knockout mice show reduced acute kidney injury biomarkers, decreased pro-inflammatory cytokine secretion, decreased macrophage infiltration, and reduced tubular damage after LPS injection.","method":"Co-immunoprecipitation of SH3YL1-Nox4-p22phox complex, domain deletion/mutation analysis, SH3YL1 knockout mouse model with LPS-induced AKI, H2O2 measurement, cytokine assays, histological analysis","journal":"Cell reports","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP establishing ternary complex, domain mapping, genetic KO with multiple orthogonal phenotypic readouts in vivo and in vitro","pmids":["33086058"],"is_preprint":false},{"year":2014,"finding":"SH3YL1 is a phosphoinositide-binding protein that interacts with the C-terminal proline-rich region of Dock4. This interaction promotes Dock4-mediated Rac1 activation and cancer cell migration. Mutations in the SH3YL1 phosphoinositide-binding domain disrupt its ability to promote Dock4-mediated cell migration. Depletion of SH3YL1 in MDA-MB-231 breast cancer cells suppresses cell migration.","method":"Co-immunoprecipitation, domain mutation analysis, Rac1 activity assay (pull-down), siRNA knockdown with migration assay","journal":"Cellular signalling","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP with domain mapping, functional Rac1 assay, and KD phenotype, single lab with multiple orthogonal methods","pmids":["24508479"],"is_preprint":false},{"year":2015,"finding":"SH3YL1 functions as a coregulator of the androgen receptor (AR) by interacting with the N-terminal polyproline domain of AR. This interaction is required for androgen-mediated gene expression (including induction of ubinuclein 1/UBN1), cell growth, and migration of prostate cancer cells. SH3YL1 knockdown attenuates androgen-dependent proliferation and migration.","method":"T7 phage display (identification of interaction), co-immunoprecipitation, siRNA knockdown, RNA expression analysis, cell proliferation and migration assays","journal":"Molecular endocrinology (Baltimore, Md.)","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — phage display identification confirmed by Co-IP, knockdown with multiple functional readouts, single lab","pmids":["26305679"],"is_preprint":false},{"year":2000,"finding":"Mouse Sh3yl1 encodes a novel protein containing a C-terminal SH3 domain with homology to yeast YHRO16c/Ysc84. In mouse skin, Sh3yl1 transcript expression follows the hair-growth cycle, increasing during mid and late anagen phases and decreasing during catagen and telogen. In situ hybridization localized Sh3yl1 transcripts predominantly to the hair bulb, hair shaft, inner root sheath, and outer root sheath during mid/late anagen phases.","method":"Differential cDNA library screening, northern blot, in situ hybridization, sequence homology analysis","journal":"The Journal of investigative dermatology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization by in situ hybridization with hair-cycle correlation, northern blot, single lab; no functional intervention","pmids":["10771491"],"is_preprint":false}],"current_model":"SH3YL1 is a SYLF/SH3 domain-containing scaffold protein that (1) forms a ternary complex with Nox4 and p22phox to regulate LPS-induced H2O2 production and inflammatory signaling in renal tubular cells, (2) binds phosphoinositides and the proline-rich C-terminus of Dock4 to promote Rac1 activation and cancer cell migration, and (3) interacts with the N-terminal polyproline domain of the androgen receptor to co-regulate androgen-dependent gene expression, proliferation, and migration in prostate cancer cells."},"narrative":{"mechanistic_narrative":"SH3YL1 is a SYLF/SH3 domain-containing phosphoinositide-binding scaffold protein that couples to NADPH oxidase signaling, small-GTPase-driven migration, and nuclear receptor transcriptional programs [PMID:33086058, PMID:24508479, PMID:26305679]. In renal tubular epithelial cells, its SYLF and SH3 domains assemble a ternary complex with Nox4 and p22phox that is required for LPS-triggered H2O2 generation and pro-inflammatory cytokine expression; loss of SH3YL1 protects mice from LPS-induced acute kidney injury, reducing macrophage infiltration and tubular damage [PMID:33086058]. Through its phosphoinositide-binding domain SH3YL1 engages the C-terminal proline-rich region of Dock4 to potentiate Dock4-mediated Rac1 activation and cancer cell migration [PMID:24508479]. It additionally acts as an androgen receptor coregulator, binding the AR N-terminal polyproline domain to support androgen-dependent gene expression, proliferation, and migration in prostate cancer cells [PMID:26305679]. The protein was originally identified in mouse skin as a hair-cycle-regulated transcript localized to the hair bulb and root sheaths [PMID:10771491], but its role in hair biology has not been mechanistically connected to its later-defined molecular activities in the available corpus.","teleology":[{"year":2000,"claim":"Established SH3YL1 as a distinct gene product by identifying a novel mouse protein bearing a C-terminal SH3 domain homologous to yeast Ysc84, and tied its expression to a defined physiological program.","evidence":"Differential cDNA screening, northern blot, and in situ hybridization across the hair-growth cycle in mouse skin","pmids":["10771491"],"confidence":"Medium","gaps":["No functional intervention linking the protein to hair biology","Molecular activity of the SH3 domain not tested","No binding partners identified"]},{"year":2014,"claim":"Defined a molecular function for SH3YL1 in cell migration by showing it is a phosphoinositide-binding partner of Dock4 that amplifies Rac1 activation.","evidence":"Co-IP with domain-mutation mapping, Rac1 pull-down activity assay, and siRNA knockdown migration assays in MDA-MB-231 breast cancer cells","pmids":["24508479"],"confidence":"Medium","gaps":["Specific phosphoinositide species bound not resolved","Single-lab evidence without reciprocal in vivo validation","Whether membrane recruitment is the rate-limiting step is unclear"]},{"year":2015,"claim":"Extended SH3YL1's role into transcriptional regulation by identifying it as an androgen receptor coregulator acting through the AR polyproline domain.","evidence":"T7 phage display, Co-IP, siRNA knockdown, RNA expression analysis, and proliferation/migration assays in prostate cancer cells","pmids":["26305679"],"confidence":"Medium","gaps":["Mechanism by which SH3YL1 modulates AR transcriptional output unknown","Direct vs scaffold-mediated AR binding not distinguished","Single-lab finding"]},{"year":2020,"claim":"Provided the strongest mechanistic and in vivo evidence by defining SH3YL1 as an obligate assembly factor for Nox4/p22phox-driven ROS production in inflammation.","evidence":"Reciprocal Co-IP of the SH3YL1-Nox4-p22phox ternary complex, domain deletion mapping, and SH3YL1 knockout mice in an LPS-induced acute kidney injury model with H2O2, cytokine, and histological readouts","pmids":["33086058"],"confidence":"High","gaps":["Structural basis of ternary complex assembly not resolved","Whether SH3YL1 regulates other Nox isoforms untested","Relationship between Nox4 scaffolding and the Dock4/AR roles unexplored"]},{"year":null,"claim":"How SH3YL1's distinct activities — Nox4/p22phox scaffolding, Dock4/Rac1 migration signaling, and AR coregulation — are integrated or context-selected within a single cell remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structural model of the SYLF or SH3 domains in complex","No unified study examining all three functions in one system","Lipid-binding selectivity and its role in partner choice undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,2]},{"term_id":"GO:0008289","term_label":"lipid binding","supporting_discovery_ids":[1]},{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,1]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-168256","term_label":"Immune System","supporting_discovery_ids":[0]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[1]}],"complexes":["Nox4-p22phox-SH3YL1 ternary complex"],"partners":["NOX4","CYBA","DOCK4","AR"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q96HL8","full_name":"SH3 domain-containing YSC84-like protein 1","aliases":[],"length_aa":342,"mass_kda":37.1,"function":"","subcellular_location":"","url":"https://www.uniprot.org/uniprotkb/Q96HL8/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/SH3YL1","classification":"Not Classified","n_dependent_lines":8,"n_total_lines":1208,"dependency_fraction":0.006622516556291391},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/SH3YL1","total_profiled":1310},"omim":[{"mim_id":"617314","title":"SH3 DOMAIN- AND SYLF DOMAIN-CONTAINING PROTEIN 1; SH3YL1","url":"https://www.omim.org/entry/617314"},{"mim_id":"607679","title":"DEDICATOR OF CYTOKINESIS 4; DOCK4","url":"https://www.omim.org/entry/607679"},{"mim_id":"600829","title":"INOSITOL POLYPHOSPHATE PHOSPHATASE-LIKE 1; INPPL1","url":"https://www.omim.org/entry/600829"},{"mim_id":"313700","title":"ANDROGEN RECEPTOR; AR","url":"https://www.omim.org/entry/313700"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/SH3YL1"},"hgnc":{"alias_symbol":["Ray","DKFZP586F1318"],"prev_symbol":[]},"alphafold":{"accession":"Q96HL8","domains":[{"cath_id":"-","chopping":"8-29_37-133_145-214","consensus_level":"high","plddt":83.4828,"start":8,"end":214},{"cath_id":"2.30.30.40","chopping":"285-342","consensus_level":"medium","plddt":80.54,"start":285,"end":342}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q96HL8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q96HL8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q96HL8-F1-predicted_aligned_error_v6.png","plddt_mean":72.94},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SH3YL1","jax_strain_url":"https://www.jax.org/strain/search?query=SH3YL1"},"sequence":{"accession":"Q96HL8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q96HL8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q96HL8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q96HL8"}},"corpus_meta":[{"pmid":"21293373","id":"PMC_21293373","title":"Femtosecond X-ray protein nanocrystallography.","date":"2011","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/21293373","citation_count":1184,"is_preprint":false},{"pmid":"21677752","id":"PMC_21677752","title":"X-ray structure of a bacterial oligosaccharyltransferase.","date":"2011","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/21677752","citation_count":306,"is_preprint":false},{"pmid":"1900938","id":"PMC_1900938","title":"Protein kinase C mediates x-ray inducibility of nuclear signal transducers EGR1 and JUN.","date":"1991","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/1900938","citation_count":273,"is_preprint":false},{"pmid":"25416941","id":"PMC_25416941","title":"A glimpse of structural biology through X-ray crystallography.","date":"2014","source":"Cell","url":"https://pubmed.ncbi.nlm.nih.gov/25416941","citation_count":213,"is_preprint":false},{"pmid":"8421501","id":"PMC_8421501","title":"X-ray structure of a decameric cyclophilin-cyclosporin crystal complex.","date":"1993","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/8421501","citation_count":184,"is_preprint":false},{"pmid":"18235446","id":"PMC_18235446","title":"The X-ray crystal structure of RNA polymerase from Archaea.","date":"2008","source":"Nature","url":"https://pubmed.ncbi.nlm.nih.gov/18235446","citation_count":169,"is_preprint":false},{"pmid":"6876162","id":"PMC_6876162","title":"X-ray studies of water in crystals of lysozyme.","date":"1983","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/6876162","citation_count":144,"is_preprint":false},{"pmid":"10884915","id":"PMC_10884915","title":"x ray crystallography.","date":"2000","source":"Molecular pathology : MP","url":"https://pubmed.ncbi.nlm.nih.gov/10884915","citation_count":142,"is_preprint":false},{"pmid":"20363295","id":"PMC_20363295","title":"X-ray structures of ferritins and related proteins.","date":"2010","source":"Biochimica et biophysica acta","url":"https://pubmed.ncbi.nlm.nih.gov/20363295","citation_count":137,"is_preprint":false},{"pmid":"11104004","id":"PMC_11104004","title":"Automation of X-ray crystallography.","date":"2000","source":"Nature structural biology","url":"https://pubmed.ncbi.nlm.nih.gov/11104004","citation_count":127,"is_preprint":false},{"pmid":"22975810","id":"PMC_22975810","title":"X-ray lasers for structural and dynamic biology.","date":"2012","source":"Reports on progress in physics. 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Section F, Structural biology and crystallization communications","url":"https://pubmed.ncbi.nlm.nih.gov/16582498","citation_count":11,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":38577,"output_tokens":1275,"usd":0.067428,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7900,"output_tokens":2008,"usd":0.04485,"stage2_stop_reason":"end_turn"},"total_usd":0.112278,"stage1_batch_id":"msgbatch_013LWZZT6MWaqB9qyTSeQBmU","stage2_batch_id":"msgbatch_0194ZzQaTGNpruoNJBbEMbt3","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2020,\n      \"finding\": \"SH3YL1 acts as a cytosolic regulator of NADPH oxidase 4 (Nox4): the SYLF domain and SH3 domain of SH3YL1 form a ternary complex with Nox4 and p22phox, and this complex is required for LPS-triggered H2O2 generation and pro-inflammatory cytokine expression in mouse tubular epithelial cells. SH3YL1 knockout mice show reduced acute kidney injury biomarkers, decreased pro-inflammatory cytokine secretion, decreased macrophage infiltration, and reduced tubular damage after LPS injection.\",\n      \"method\": \"Co-immunoprecipitation of SH3YL1-Nox4-p22phox complex, domain deletion/mutation analysis, SH3YL1 knockout mouse model with LPS-induced AKI, H2O2 measurement, cytokine assays, histological analysis\",\n      \"journal\": \"Cell reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP establishing ternary complex, domain mapping, genetic KO with multiple orthogonal phenotypic readouts in vivo and in vitro\",\n      \"pmids\": [\"33086058\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"SH3YL1 is a phosphoinositide-binding protein that interacts with the C-terminal proline-rich region of Dock4. This interaction promotes Dock4-mediated Rac1 activation and cancer cell migration. Mutations in the SH3YL1 phosphoinositide-binding domain disrupt its ability to promote Dock4-mediated cell migration. Depletion of SH3YL1 in MDA-MB-231 breast cancer cells suppresses cell migration.\",\n      \"method\": \"Co-immunoprecipitation, domain mutation analysis, Rac1 activity assay (pull-down), siRNA knockdown with migration assay\",\n      \"journal\": \"Cellular signalling\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP with domain mapping, functional Rac1 assay, and KD phenotype, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"24508479\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"SH3YL1 functions as a coregulator of the androgen receptor (AR) by interacting with the N-terminal polyproline domain of AR. This interaction is required for androgen-mediated gene expression (including induction of ubinuclein 1/UBN1), cell growth, and migration of prostate cancer cells. SH3YL1 knockdown attenuates androgen-dependent proliferation and migration.\",\n      \"method\": \"T7 phage display (identification of interaction), co-immunoprecipitation, siRNA knockdown, RNA expression analysis, cell proliferation and migration assays\",\n      \"journal\": \"Molecular endocrinology (Baltimore, Md.)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — phage display identification confirmed by Co-IP, knockdown with multiple functional readouts, single lab\",\n      \"pmids\": [\"26305679\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2000,\n      \"finding\": \"Mouse Sh3yl1 encodes a novel protein containing a C-terminal SH3 domain with homology to yeast YHRO16c/Ysc84. In mouse skin, Sh3yl1 transcript expression follows the hair-growth cycle, increasing during mid and late anagen phases and decreasing during catagen and telogen. In situ hybridization localized Sh3yl1 transcripts predominantly to the hair bulb, hair shaft, inner root sheath, and outer root sheath during mid/late anagen phases.\",\n      \"method\": \"Differential cDNA library screening, northern blot, in situ hybridization, sequence homology analysis\",\n      \"journal\": \"The Journal of investigative dermatology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct localization by in situ hybridization with hair-cycle correlation, northern blot, single lab; no functional intervention\",\n      \"pmids\": [\"10771491\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SH3YL1 is a SYLF/SH3 domain-containing scaffold protein that (1) forms a ternary complex with Nox4 and p22phox to regulate LPS-induced H2O2 production and inflammatory signaling in renal tubular cells, (2) binds phosphoinositides and the proline-rich C-terminus of Dock4 to promote Rac1 activation and cancer cell migration, and (3) interacts with the N-terminal polyproline domain of the androgen receptor to co-regulate androgen-dependent gene expression, proliferation, and migration in prostate cancer cells.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SH3YL1 is a SYLF/SH3 domain-containing phosphoinositide-binding scaffold protein that couples to NADPH oxidase signaling, small-GTPase-driven migration, and nuclear receptor transcriptional programs [#0, #1, #2]. In renal tubular epithelial cells, its SYLF and SH3 domains assemble a ternary complex with Nox4 and p22phox that is required for LPS-triggered H2O2 generation and pro-inflammatory cytokine expression; loss of SH3YL1 protects mice from LPS-induced acute kidney injury, reducing macrophage infiltration and tubular damage [#0]. Through its phosphoinositide-binding domain SH3YL1 engages the C-terminal proline-rich region of Dock4 to potentiate Dock4-mediated Rac1 activation and cancer cell migration [#1]. It additionally acts as an androgen receptor coregulator, binding the AR N-terminal polyproline domain to support androgen-dependent gene expression, proliferation, and migration in prostate cancer cells [#2]. The protein was originally identified in mouse skin as a hair-cycle-regulated transcript localized to the hair bulb and root sheaths [#3], but its role in hair biology has not been mechanistically connected to its later-defined molecular activities in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2000,\n      \"claim\": \"Established SH3YL1 as a distinct gene product by identifying a novel mouse protein bearing a C-terminal SH3 domain homologous to yeast Ysc84, and tied its expression to a defined physiological program.\",\n      \"evidence\": \"Differential cDNA screening, northern blot, and in situ hybridization across the hair-growth cycle in mouse skin\",\n      \"pmids\": [\"10771491\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No functional intervention linking the protein to hair biology\", \"Molecular activity of the SH3 domain not tested\", \"No binding partners identified\"]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Defined a molecular function for SH3YL1 in cell migration by showing it is a phosphoinositide-binding partner of Dock4 that amplifies Rac1 activation.\",\n      \"evidence\": \"Co-IP with domain-mutation mapping, Rac1 pull-down activity assay, and siRNA knockdown migration assays in MDA-MB-231 breast cancer cells\",\n      \"pmids\": [\"24508479\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Specific phosphoinositide species bound not resolved\", \"Single-lab evidence without reciprocal in vivo validation\", \"Whether membrane recruitment is the rate-limiting step is unclear\"]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"Extended SH3YL1's role into transcriptional regulation by identifying it as an androgen receptor coregulator acting through the AR polyproline domain.\",\n      \"evidence\": \"T7 phage display, Co-IP, siRNA knockdown, RNA expression analysis, and proliferation/migration assays in prostate cancer cells\",\n      \"pmids\": [\"26305679\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism by which SH3YL1 modulates AR transcriptional output unknown\", \"Direct vs scaffold-mediated AR binding not distinguished\", \"Single-lab finding\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Provided the strongest mechanistic and in vivo evidence by defining SH3YL1 as an obligate assembly factor for Nox4/p22phox-driven ROS production in inflammation.\",\n      \"evidence\": \"Reciprocal Co-IP of the SH3YL1-Nox4-p22phox ternary complex, domain deletion mapping, and SH3YL1 knockout mice in an LPS-induced acute kidney injury model with H2O2, cytokine, and histological readouts\",\n      \"pmids\": [\"33086058\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of ternary complex assembly not resolved\", \"Whether SH3YL1 regulates other Nox isoforms untested\", \"Relationship between Nox4 scaffolding and the Dock4/AR roles unexplored\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How SH3YL1's distinct activities — Nox4/p22phox scaffolding, Dock4/Rac1 migration signaling, and AR coregulation — are integrated or context-selected within a single cell remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structural model of the SYLF or SH3 domains in complex\", \"No unified study examining all three functions in one system\", \"Lipid-binding selectivity and its role in partner choice undefined\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0008289\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-168256\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\"Nox4-p22phox-SH3YL1 ternary complex\"],\n    \"partners\": [\"NOX4\", \"CYBA\", \"DOCK4\", \"AR\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":4,"faith_total":4,"faith_pct":100.0}}