{"gene":"SNX30","run_date":"2026-06-10T07:46:37","timeline":{"discoveries":[{"year":2006,"finding":"SNX30 (identified as an ADAM15-binding sorting nexin family member) was discovered as a novel SH3-domain-containing protein that binds ADAM15 via phage display of the complete human SH3 proteome, with nanomolar affinity.","method":"Phage display of human SH3 proteome; binding affinity assay","journal":"EMBO reports","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — systematic phage-display screen identifying binding, single study, no reciprocal validation or mutagenesis reported in abstract","pmids":["16374509"],"is_preprint":false},{"year":2009,"finding":"SNX30 (referred to as SNX33 a.k.a. SNX30 in this paper) co-precipitates with specific ADAM15 isoforms from cell lysates; robust cellular association with SNX30 was observed only for ADAM15 isoforms containing the most carboxyterminal proline cluster, establishing that alternative mRNA splicing of ADAM15 regulates its interaction with SNX30.","method":"Co-precipitation from cell lysates; isoform-specific expression constructs; mutagenesis of proline-rich regions","journal":"Journal of cellular biochemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — co-precipitation with isoform specificity and mutagenesis, single lab but two orthogonal approaches","pmids":["19718658"],"is_preprint":false},{"year":2020,"finding":"SNX30 forms functional heterodimers with SNX4 that associate with tubulovesicular endocytic membranes, as shown by co-immunoprecipitation and imaging; however, the SNX4-SNX7 heterodimer (not SNX4-SNX30) was specifically required for autophagy and ATG9A trafficking, indicating SNX4-SNX30 is not the autophagy-specific complex.","method":"siRNA knockdown, CRISPR-Cas9 deletion, co-immunoprecipitation, fluorescence imaging, autophagosome assembly assays","journal":"Journal of cell science","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal co-IP, CRISPR KO, and imaging with defined cellular phenotype; the specific finding about SNX4-SNX30 heterodimer formation is directly demonstrated","pmids":["32513819"],"is_preprint":false},{"year":2025,"finding":"SNX30 overexpression in lung adenocarcinoma cell lines inhibits cell proliferation, induces ferroptosis (increased ROS, intracellular iron, Ptgs2, Chac1; decreased Cys, GSH, GPX4), and negatively regulates SETDB1 expression; rescue of SETDB1 reversed SNX30-induced ferroptosis, placing SNX30 upstream of SETDB1 in a ferroptosis pathway.","method":"Plasmid overexpression, CCK8 proliferation assay, flow cytometry (apoptosis/ROS), iron assay kits, RT-qPCR, western blotting, ferrostatin-1 rescue experiment","journal":"Journal of cardiothoracic surgery","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — defined cellular phenotype with pathway placement via rescue experiment (SETDB1 overexpression reversal), single lab, single study","pmids":["39780196"],"is_preprint":false}],"current_model":"SNX30 is a sorting nexin family member that forms heterodimers with SNX4 on tubulovesicular endocytic membranes, interacts with ADAM15 in an isoform-specific (SH3-proline cluster-dependent) manner, and in lung adenocarcinoma cells functions upstream of SETDB1 to suppress proliferation and induce ferroptosis."},"narrative":{"mechanistic_narrative":"SNX30 is a sorting nexin family member that operates on endocytic membranes and engages in selective protein-protein interactions through its SH3 domain [PMID:16374509, PMID:32513819]. It binds the metalloproteinase-disintegrin ADAM15 with nanomolar affinity, and this association is governed by alternative mRNA splicing of ADAM15: robust cellular binding occurs only for ADAM15 isoforms retaining the most carboxyterminal proline cluster, establishing splice-dependent control of the SNX30–ADAM15 interaction [PMID:16374509, PMID:19718658]. SNX30 also forms heterodimers with SNX4 that localize to tubulovesicular endocytic membranes, distinguishing it from the SNX4–SNX7 heterodimer that mediates autophagy and ATG9A trafficking [PMID:32513819]. In lung adenocarcinoma cells, SNX30 overexpression suppresses proliferation and drives ferroptosis—raising ROS and intracellular iron while depleting cysteine, glutathione, and GPX4—by acting upstream of and negatively regulating SETDB1, since restoring SETDB1 reverses the ferroptotic phenotype [PMID:39780196]. The structural basis of these functions and the connection between SNX30's membrane-trafficking activity and its tumor-suppressive role have not been resolved in the available corpus.","teleology":[{"year":2006,"claim":"Establishing whether SNX30 has defined binding partners, an unbiased SH3-proteome screen identified ADAM15 as a high-affinity SNX30 ligand, defining its first molecular interaction.","evidence":"Phage display of the complete human SH3 proteome with binding affinity measurement","pmids":["16374509"],"confidence":"Medium","gaps":["No reciprocal validation or mutagenesis in the original report","Functional consequence of the ADAM15 interaction not addressed","No cellular context for the interaction"]},{"year":2009,"claim":"To test whether the ADAM15 interaction occurs in cells and how it is regulated, co-precipitation across ADAM15 splice isoforms showed binding requires the most C-terminal proline cluster, establishing alternative splicing as the regulatory switch for the SNX30–ADAM15 association.","evidence":"Co-precipitation from cell lysates with isoform-specific constructs and proline-cluster mutagenesis","pmids":["19718658"],"confidence":"Medium","gaps":["Biological output of the SNX30–ADAM15 complex not defined","Single lab without independent confirmation","Subcellular site of the interaction not mapped"]},{"year":2020,"claim":"To place SNX30 within sorting nexin membrane assemblies, reciprocal co-IP, CRISPR deletion, and imaging demonstrated SNX30 forms SNX4 heterodimers on tubulovesicular endocytic membranes but, unlike SNX4–SNX7, is dispensable for autophagy and ATG9A trafficking, defining the specificity of SNX4-based complexes.","evidence":"siRNA, CRISPR-Cas9 deletion, reciprocal co-immunoprecipitation, fluorescence imaging, and autophagosome assays","pmids":["32513819"],"confidence":"High","gaps":["The cargo trafficked by the SNX4–SNX30 heterodimer is not identified","Physiological pathway served by SNX4–SNX30 not defined","Relationship to the ADAM15 interaction not explored"]},{"year":2025,"claim":"To assign a disease-relevant cellular function, SNX30 overexpression in lung adenocarcinoma cells was shown to suppress proliferation and induce ferroptosis by negatively regulating SETDB1, with SETDB1 rescue reversing the phenotype, placing SNX30 upstream of SETDB1 in a ferroptosis pathway.","evidence":"Plasmid overexpression, proliferation and ROS/iron assays, RT-qPCR, western blot, and SETDB1 rescue with ferrostatin-1 control","pmids":["39780196"],"confidence":"Medium","gaps":["Mechanism linking SNX30 to SETDB1 regulation is unknown","Overexpression-based, single lab and single study","Connection to SNX30's membrane-trafficking activity not established"]},{"year":null,"claim":"How SNX30's endocytic membrane-trafficking activity mechanistically connects to its ADAM15 interaction and its SETDB1-dependent tumor-suppressive role remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of SNX30 or its complexes","No identified cargo for the SNX4–SNX30 heterodimer","Molecular mechanism of SETDB1 regulation undefined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1,2]}],"localization":[{"term_id":"GO:0031410","term_label":"cytoplasmic vesicle","supporting_discovery_ids":[2]}],"pathway":[],"complexes":["SNX4-SNX30 heterodimer"],"partners":["SNX4","ADAM15"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8WV41","full_name":"Sorting nexin-33","aliases":["SH3 and PX domain-containing protein 3"],"length_aa":574,"mass_kda":65.3,"function":"Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes","subcellular_location":"Cytoplasm, cytosol; Membrane; Cytoplasmic vesicle membrane","url":"https://www.uniprot.org/uniprotkb/Q8WV41/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/SNX30","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"SNX4","stoichiometry":10.0},{"gene":"CAPZB","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/SNX30","total_profiled":1310},"omim":[{"mim_id":"620955","title":"SORTING NEXIN 30; SNX30","url":"https://www.omim.org/entry/620955"},{"mim_id":"605931","title":"SORTING NEXIN 4; SNX4","url":"https://www.omim.org/entry/605931"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"},{"location":"Nucleoli","reliability":"Approved"},{"location":"Cytosol","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/SNX30"},"hgnc":{"alias_symbol":["ATG24A"],"prev_symbol":[]},"alphafold":{"accession":"Q8WV41","domains":[{"cath_id":"2.30.30.40","chopping":"4-59","consensus_level":"high","plddt":88.5418,"start":4,"end":59},{"cath_id":"3.30.1520.10","chopping":"233-364","consensus_level":"medium","plddt":92.1494,"start":233,"end":364},{"cath_id":"1.20.1270.60","chopping":"372-571","consensus_level":"medium","plddt":96.7934,"start":372,"end":571}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8WV41","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8WV41-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8WV41-F1-predicted_aligned_error_v6.png","plddt_mean":81.44},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=SNX30","jax_strain_url":"https://www.jax.org/strain/search?query=SNX30"},"sequence":{"accession":"Q8WV41","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8WV41.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8WV41/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8WV41"}},"corpus_meta":[{"pmid":"16374509","id":"PMC_16374509","title":"Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome.","date":"2006","source":"EMBO reports","url":"https://pubmed.ncbi.nlm.nih.gov/16374509","citation_count":99,"is_preprint":false},{"pmid":"35763030","id":"PMC_35763030","title":"Genome-wide meta-analysis and omics integration identifies novel genes associated with diabetic kidney disease.","date":"2022","source":"Diabetologia","url":"https://pubmed.ncbi.nlm.nih.gov/35763030","citation_count":50,"is_preprint":false},{"pmid":"32513819","id":"PMC_32513819","title":"A heterodimeric SNX4--SNX7 SNX-BAR autophagy complex coordinates ATG9A trafficking for efficient autophagosome assembly.","date":"2020","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/32513819","citation_count":37,"is_preprint":false},{"pmid":"34515027","id":"PMC_34515027","title":"Epigenome-wide analysis of DNA methylation and coronary heart disease: a nested case-control study.","date":"2021","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/34515027","citation_count":24,"is_preprint":false},{"pmid":"19718658","id":"PMC_19718658","title":"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins.","date":"2009","source":"Journal of cellular biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/19718658","citation_count":18,"is_preprint":false},{"pmid":"31750732","id":"PMC_31750732","title":"Distinct Patterns of mRNA and lncRNA Expression Differences Between Lung Squamous Cell Carcinoma and Adenocarcinoma.","date":"2019","source":"Journal of computational biology : a journal of computational molecular cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/31750732","citation_count":17,"is_preprint":false},{"pmid":"40798960","id":"PMC_40798960","title":"Transcriptomic Signatures in TP53 Positive and Negative Tumor Samples in NSCLC.","date":"2025","source":"Current gene therapy","url":"https://pubmed.ncbi.nlm.nih.gov/40798960","citation_count":6,"is_preprint":false},{"pmid":"39780196","id":"PMC_39780196","title":"SNX30 inhibits lung adenocarcinoma cell proliferation and induces cell ferroptosis through regulating SETDB1.","date":"2025","source":"Journal of cardiothoracic surgery","url":"https://pubmed.ncbi.nlm.nih.gov/39780196","citation_count":0,"is_preprint":false},{"pmid":"41076048","id":"PMC_41076048","title":"Susceptibility and protective genes in diabetic retinopathy: A comprehensive single-cell RNA sequencing analysis.","date":"2025","source":"Experimental eye research","url":"https://pubmed.ncbi.nlm.nih.gov/41076048","citation_count":0,"is_preprint":false},{"pmid":"40431640","id":"PMC_40431640","title":"Anthraquinone-2-Carboxylic Acid Is a Potential Antiviral Candidate Against Influenza Viruses In Vitro and In Vivo.","date":"2025","source":"Viruses","url":"https://pubmed.ncbi.nlm.nih.gov/40431640","citation_count":0,"is_preprint":false},{"pmid":"41605412","id":"PMC_41605412","title":"Integrated miRNA-proteomic profiling identifies chronic vesicle-trafficking and proteostasis disruptions after mild traumatic brain injury.","date":"2026","source":"Experimental neurology","url":"https://pubmed.ncbi.nlm.nih.gov/41605412","citation_count":0,"is_preprint":false},{"pmid":"42059218","id":"PMC_42059218","title":"Integrative eQTL and Mendelian Randomization Analyses with Experimental Validation Prioritize Genetic Candidate Biomarkers for Crohn's Disease.","date":"2026","source":"Endocrine, metabolic & immune disorders drug targets","url":"https://pubmed.ncbi.nlm.nih.gov/42059218","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":9052,"output_tokens":1082,"usd":0.021693,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7624,"output_tokens":2054,"usd":0.044735,"stage2_stop_reason":"end_turn"},"total_usd":0.066428,"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\": 2006,\n      \"finding\": \"SNX30 (identified as an ADAM15-binding sorting nexin family member) was discovered as a novel SH3-domain-containing protein that binds ADAM15 via phage display of the complete human SH3 proteome, with nanomolar affinity.\",\n      \"method\": \"Phage display of human SH3 proteome; binding affinity assay\",\n      \"journal\": \"EMBO reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — systematic phage-display screen identifying binding, single study, no reciprocal validation or mutagenesis reported in abstract\",\n      \"pmids\": [\"16374509\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"SNX30 (referred to as SNX33 a.k.a. SNX30 in this paper) co-precipitates with specific ADAM15 isoforms from cell lysates; robust cellular association with SNX30 was observed only for ADAM15 isoforms containing the most carboxyterminal proline cluster, establishing that alternative mRNA splicing of ADAM15 regulates its interaction with SNX30.\",\n      \"method\": \"Co-precipitation from cell lysates; isoform-specific expression constructs; mutagenesis of proline-rich regions\",\n      \"journal\": \"Journal of cellular biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — co-precipitation with isoform specificity and mutagenesis, single lab but two orthogonal approaches\",\n      \"pmids\": [\"19718658\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"SNX30 forms functional heterodimers with SNX4 that associate with tubulovesicular endocytic membranes, as shown by co-immunoprecipitation and imaging; however, the SNX4-SNX7 heterodimer (not SNX4-SNX30) was specifically required for autophagy and ATG9A trafficking, indicating SNX4-SNX30 is not the autophagy-specific complex.\",\n      \"method\": \"siRNA knockdown, CRISPR-Cas9 deletion, co-immunoprecipitation, fluorescence imaging, autophagosome assembly assays\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal co-IP, CRISPR KO, and imaging with defined cellular phenotype; the specific finding about SNX4-SNX30 heterodimer formation is directly demonstrated\",\n      \"pmids\": [\"32513819\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"SNX30 overexpression in lung adenocarcinoma cell lines inhibits cell proliferation, induces ferroptosis (increased ROS, intracellular iron, Ptgs2, Chac1; decreased Cys, GSH, GPX4), and negatively regulates SETDB1 expression; rescue of SETDB1 reversed SNX30-induced ferroptosis, placing SNX30 upstream of SETDB1 in a ferroptosis pathway.\",\n      \"method\": \"Plasmid overexpression, CCK8 proliferation assay, flow cytometry (apoptosis/ROS), iron assay kits, RT-qPCR, western blotting, ferrostatin-1 rescue experiment\",\n      \"journal\": \"Journal of cardiothoracic surgery\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — defined cellular phenotype with pathway placement via rescue experiment (SETDB1 overexpression reversal), single lab, single study\",\n      \"pmids\": [\"39780196\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"SNX30 is a sorting nexin family member that forms heterodimers with SNX4 on tubulovesicular endocytic membranes, interacts with ADAM15 in an isoform-specific (SH3-proline cluster-dependent) manner, and in lung adenocarcinoma cells functions upstream of SETDB1 to suppress proliferation and induce ferroptosis.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SNX30 is a sorting nexin family member that operates on endocytic membranes and engages in selective protein-protein interactions through its SH3 domain [#0, #2]. It binds the metalloproteinase-disintegrin ADAM15 with nanomolar affinity, and this association is governed by alternative mRNA splicing of ADAM15: robust cellular binding occurs only for ADAM15 isoforms retaining the most carboxyterminal proline cluster, establishing splice-dependent control of the SNX30–ADAM15 interaction [#0, #1]. SNX30 also forms heterodimers with SNX4 that localize to tubulovesicular endocytic membranes, distinguishing it from the SNX4–SNX7 heterodimer that mediates autophagy and ATG9A trafficking [#2]. In lung adenocarcinoma cells, SNX30 overexpression suppresses proliferation and drives ferroptosis—raising ROS and intracellular iron while depleting cysteine, glutathione, and GPX4—by acting upstream of and negatively regulating SETDB1, since restoring SETDB1 reverses the ferroptotic phenotype [#3]. The structural basis of these functions and the connection between SNX30's membrane-trafficking activity and its tumor-suppressive role have not been resolved in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"Establishing whether SNX30 has defined binding partners, an unbiased SH3-proteome screen identified ADAM15 as a high-affinity SNX30 ligand, defining its first molecular interaction.\",\n      \"evidence\": \"Phage display of the complete human SH3 proteome with binding affinity measurement\",\n      \"pmids\": [\n        \"16374509\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No reciprocal validation or mutagenesis in the original report\",\n        \"Functional consequence of the ADAM15 interaction not addressed\",\n        \"No cellular context for the interaction\"\n      ]\n    },\n    {\n      \"year\": 2009,\n      \"claim\": \"To test whether the ADAM15 interaction occurs in cells and how it is regulated, co-precipitation across ADAM15 splice isoforms showed binding requires the most C-terminal proline cluster, establishing alternative splicing as the regulatory switch for the SNX30–ADAM15 association.\",\n      \"evidence\": \"Co-precipitation from cell lysates with isoform-specific constructs and proline-cluster mutagenesis\",\n      \"pmids\": [\n        \"19718658\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Biological output of the SNX30–ADAM15 complex not defined\",\n        \"Single lab without independent confirmation\",\n        \"Subcellular site of the interaction not mapped\"\n      ]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"To place SNX30 within sorting nexin membrane assemblies, reciprocal co-IP, CRISPR deletion, and imaging demonstrated SNX30 forms SNX4 heterodimers on tubulovesicular endocytic membranes but, unlike SNX4–SNX7, is dispensable for autophagy and ATG9A trafficking, defining the specificity of SNX4-based complexes.\",\n      \"evidence\": \"siRNA, CRISPR-Cas9 deletion, reciprocal co-immunoprecipitation, fluorescence imaging, and autophagosome assays\",\n      \"pmids\": [\n        \"32513819\"\n      ],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"The cargo trafficked by the SNX4–SNX30 heterodimer is not identified\",\n        \"Physiological pathway served by SNX4–SNX30 not defined\",\n        \"Relationship to the ADAM15 interaction not explored\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"To assign a disease-relevant cellular function, SNX30 overexpression in lung adenocarcinoma cells was shown to suppress proliferation and induce ferroptosis by negatively regulating SETDB1, with SETDB1 rescue reversing the phenotype, placing SNX30 upstream of SETDB1 in a ferroptosis pathway.\",\n      \"evidence\": \"Plasmid overexpression, proliferation and ROS/iron assays, RT-qPCR, western blot, and SETDB1 rescue with ferrostatin-1 control\",\n      \"pmids\": [\n        \"39780196\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanism linking SNX30 to SETDB1 regulation is unknown\",\n        \"Overexpression-based, single lab and single study\",\n        \"Connection to SNX30's membrane-trafficking activity not established\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How SNX30's endocytic membrane-trafficking activity mechanistically connects to its ADAM15 interaction and its SETDB1-dependent tumor-suppressive role remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of SNX30 or its complexes\",\n        \"No identified cargo for the SNX4–SNX30 heterodimer\",\n        \"Molecular mechanism of SETDB1 regulation undefined\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\n        \"term_id\": \"GO:0060090\",\n        \"supporting_discovery_ids\": [\n          0,\n          1,\n          2\n        ]\n      }\n    ],\n    \"localization\": [\n      {\n        \"term_id\": \"GO:0031410\",\n        \"supporting_discovery_ids\": [\n          2\n        ]\n      }\n    ],\n    \"pathway\": [],\n    \"complexes\": [\n      \"SNX4-SNX30 heterodimer\"\n    ],\n    \"partners\": [\n      \"SNX4\",\n      \"ADAM15\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":3,"faith_total":4,"faith_pct":75.0}}