{"gene":"TBC1D22B","run_date":"2026-06-10T10:51:54","timeline":{"discoveries":[{"year":2013,"finding":"TBC1D22B (and paralog TBC1D22A) were identified as ACBD3-interacting proteins via affinity purification-mass spectrometry. Fine-scale mapping showed that the binding domains for TBC1D22A/B and PI4KB on ACBD3 are identical, and affinity purification confirmed that PI4KB and TBC1D22A/B interactions with ACBD3 are mutually exclusive, suggesting TBC1D22B competes with PI4KB for ACBD3 binding.","method":"Affinity purification-mass spectrometry, fine-scale domain mapping, competitive binding assays","journal":"mBio","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal affinity purification with MS and domain-mapping, single lab, two orthogonal methods","pmids":["23572552"],"is_preprint":false},{"year":2025,"finding":"TBC1D22B functions as a GTPase-activating protein (GAP) for RAB1B; overexpression of TBC1D22B inhibits ER-to-Golgi transport in a GAP-activity-dependent manner, RAB1B silencing phenocopies the trafficking defects caused by TBC1D22B overexpression, and TBC1D22B overexpression represses a module of extracellular matrix and adhesion-related genes consistent with altered secretory activity.","method":"RUSH (Retention Using Selective Hooks) trafficking assay, proximity-labeling and co-immunoprecipitation proteomics, siRNA knockdown, transcriptomic profiling, GAP-dead mutant analysis","journal":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — functional trafficking assay (RUSH), GAP-activity-dependent mutagenesis, direct substrate identification (RAB1B), and phenocopy by RAB1B silencing, all in single rigorous study with multiple orthogonal methods","pmids":["40878439"],"is_preprint":false},{"year":2024,"finding":"Elevated TBC1D22B expression is causally linked to a glycolytic phenotype in triple-negative breast cancer (TNBC) cell lines, as demonstrated by in-depth functional investigations.","method":"Gene knockdown/overexpression in TNBC cell lines with metabolic phenotype readout; orthogonal transcriptomics/metabolomics","journal":"Cell death & disease","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional knockdown/overexpression with metabolic readout plus transcriptomics/metabolomics, single lab","pmids":["39231952"],"is_preprint":false},{"year":2025,"finding":"TBC1D22B is required for tubular endosome formation in HeLa cells; both knockdown and overexpression of TBC1D22B reduce tubular endosome structures, and this effect is dependent on GAP activity.","method":"Comprehensive TBC/Rab-GAP siRNA knockdown screening, overexpression experiments, tubular endosome morphology quantification","journal":"Traffic (Copenhagen, Denmark)","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — systematic knockdown and overexpression screen with morphological phenotype readout and GAP-activity dependence, single lab","pmids":["40241313"],"is_preprint":false},{"year":2026,"finding":"RAB30, a Golgi-resident Rab GTPase, is a direct target of TBC1D22B's GAP activity and is involved in tubular endosome formation and clathrin-independent endocytosis (CIE) cargo trafficking; a Rab30-BICD2-KIF5B axis is implicated downstream.","method":"Comprehensive Rab knockdown screening, dominant-negative Rab expression, co-functional epistasis with TBC1D22B in HeLa cells","journal":"Cell structure and function","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — systematic Rab knockdown/dominant-negative screen combined with TBC1D22B loss-of-function, single lab, single study","pmids":["41833373"],"is_preprint":false}],"current_model":"TBC1D22B is a Golgi-associated RAB-GTPase-activating protein (GAP) that directly inactivates RAB1B to inhibit ER-to-Golgi trafficking and also targets RAB30 to regulate tubular endosome formation and CIE cargo recycling; it interacts with the Golgi adaptor ACBD3 in a manner mutually exclusive with PI4KB binding, is required for normal tubular endosome structures in a GAP-activity-dependent manner, and its overexpression in breast cancer cells drives a glycolytic phenotype and represses extracellular matrix/adhesion gene programs."},"narrative":{"mechanistic_narrative":"TBC1D22B is a Golgi-associated RAB-GTPase-activating protein (GAP) that controls membrane trafficking by inactivating specific RAB GTPases [PMID:40878439, PMID:41833373]. It acts as a GAP for RAB1B, and its overexpression inhibits ER-to-Golgi transport in a manner dependent on intact GAP activity; silencing RAB1B phenocopies this trafficking defect, and the resulting altered secretory state represses a module of extracellular matrix and adhesion genes [PMID:40878439]. TBC1D22B additionally targets the Golgi-resident GTPase RAB30, and through this activity it is required for normal tubular endosome formation and clathrin-independent endocytic cargo trafficking, with a downstream RAB30-BICD2-KIF5B axis implicated; both loss and excess of TBC1D22B disrupt tubular endosome structures in a GAP-dependent manner [PMID:40241313, PMID:41833373]. TBC1D22B associates with the Golgi adaptor ACBD3, binding the same region used by PI4KB such that the two interactions are mutually exclusive [PMID:23572552]. In triple-negative breast cancer cells, elevated TBC1D22B expression drives a glycolytic phenotype [PMID:39231952].","teleology":[{"year":2013,"claim":"Established the first physical interactor of TBC1D22B, placing it at the Golgi adaptor ACBD3 and revealing it competes with the lipid kinase PI4KB for the same binding site.","evidence":"Affinity purification-mass spectrometry with fine-scale domain mapping and competitive binding assays","pmids":["23572552"],"confidence":"Medium","gaps":["Functional consequence of TBC1D22B-ACBD3 binding not tested","GAP substrate and enzymatic role not yet defined here","Whether competition with PI4KB regulates PI4P signaling unaddressed"]},{"year":2024,"claim":"Linked TBC1D22B expression to cellular metabolism, showing its elevation drives a glycolytic phenotype in cancer cells.","evidence":"Knockdown/overexpression in TNBC cell lines with metabolic and transcriptomic/metabolomic readouts","pmids":["39231952"],"confidence":"Medium","gaps":["Mechanistic connection between GAP/trafficking activity and glycolysis not resolved","Single cancer context (TNBC); generality unknown"]},{"year":2025,"claim":"Defined TBC1D22B as a GAP for RAB1B that gates ER-to-Golgi trafficking, providing the first direct enzymatic substrate and a secretory-pathway role tied to ECM/adhesion gene regulation.","evidence":"RUSH trafficking assay, proximity-labeling and co-IP proteomics, siRNA, GAP-dead mutagenesis, and transcriptomics","pmids":["40878439"],"confidence":"High","gaps":["Direct biochemical GAP kinetics on RAB1B not quantified in narrative terms","How ECM/adhesion gene repression couples mechanistically to trafficking unresolved"]},{"year":2025,"claim":"Identified a role for TBC1D22B in endosomal membrane shaping, showing it is required for tubular endosome formation via its GAP activity.","evidence":"Systematic TBC/Rab-GAP siRNA screen with overexpression and tubular endosome morphology quantification in HeLa cells","pmids":["40241313"],"confidence":"Medium","gaps":["The relevant Rab substrate for this endosomal phenotype not identified in this study","Bidirectional (knockdown and overexpression) disruption mechanism unexplained"]},{"year":2026,"claim":"Identified RAB30 as a second GAP substrate of TBC1D22B and placed it in a motor-based axis controlling tubular endosomes and CIE cargo recycling.","evidence":"Comprehensive Rab knockdown and dominant-negative screen with TBC1D22B epistasis in HeLa cells","pmids":["41833373"],"confidence":"Medium","gaps":["Direct biochemical GAP activity on RAB30 vs RAB1B selectivity not dissected","RAB30-BICD2-KIF5B axis is implicated but not biochemically reconstituted","Relationship between RAB1B and RAB30 regulation by the same GAP unclear"]},{"year":null,"claim":"How TBC1D22B selects among RAB substrates (RAB1B vs RAB30) across compartments, and how its trafficking function connects to the glycolytic and ECM phenotypes, remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of GAP-substrate or ACBD3 interaction","Mechanistic link between trafficking control and metabolic reprogramming undefined","Physiological/in vivo role not established"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[1,3,4]},{"term_id":"GO:0060089","term_label":"molecular transducer activity","supporting_discovery_ids":[1,4]}],"localization":[{"term_id":"GO:0005794","term_label":"Golgi apparatus","supporting_discovery_ids":[0,1]},{"term_id":"GO:0005768","term_label":"endosome","supporting_discovery_ids":[3,4]}],"pathway":[{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[1,3,4]},{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[1,4]}],"complexes":[],"partners":["ACBD3","RAB1B","RAB30"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9NU19","full_name":"TBC1 domain family member 22B","aliases":[],"length_aa":505,"mass_kda":59.1,"function":"May act as a GTPase-activating protein for Rab family protein(s)","subcellular_location":"","url":"https://www.uniprot.org/uniprotkb/Q9NU19/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/TBC1D22B","classification":"Not Classified","n_dependent_lines":14,"n_total_lines":1208,"dependency_fraction":0.011589403973509934},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/TBC1D22B","total_profiled":1310},"omim":[{"mim_id":"616880","title":"TBC1 DOMAIN FAMILY, MEMBER 22B; TBC1D22B","url":"https://www.omim.org/entry/616880"},{"mim_id":"616879","title":"TBC1 DOMAIN FAMILY, MEMBER 22A; TBC1D22A","url":"https://www.omim.org/entry/616879"},{"mim_id":"606809","title":"ACYL-CoA-BINDING DOMAIN-CONTAINING PROTEIN 3; ACBD3","url":"https://www.omim.org/entry/606809"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Uncertain","locations":[{"location":"Nucleoplasm","reliability":"Uncertain"},{"location":"Cytosol","reliability":"Uncertain"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/TBC1D22B"},"hgnc":{"alias_symbol":["FLJ20337","dJ744I24.2"],"prev_symbol":["C6orf197"]},"alphafold":{"accession":"Q9NU19","domains":[{"cath_id":"1.10.8","chopping":"181-362","consensus_level":"high","plddt":95.9635,"start":181,"end":362},{"cath_id":"1.10.472.80","chopping":"372-498","consensus_level":"high","plddt":96.852,"start":372,"end":498}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NU19","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NU19-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9NU19-F1-predicted_aligned_error_v6.png","plddt_mean":75.88},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=TBC1D22B","jax_strain_url":"https://www.jax.org/strain/search?query=TBC1D22B"},"sequence":{"accession":"Q9NU19","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9NU19.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9NU19/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9NU19"}},"corpus_meta":[{"pmid":"23572552","id":"PMC_23572552","title":"ACBD3 interaction with TBC1 domain 22 protein is differentially affected by enteroviral and kobuviral 3A protein binding.","date":"2013","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/23572552","citation_count":57,"is_preprint":false},{"pmid":"32341752","id":"PMC_32341752","title":"Association of germline genetic variants with TMPRSS2-ERG fusion status in prostate cancer.","date":"2020","source":"Oncotarget","url":"https://pubmed.ncbi.nlm.nih.gov/32341752","citation_count":13,"is_preprint":false},{"pmid":"39231952","id":"PMC_39231952","title":"TBC1 domain-containing proteins are frequently involved in triple-negative breast cancers in connection with the induction of a glycolytic phenotype.","date":"2024","source":"Cell death & disease","url":"https://pubmed.ncbi.nlm.nih.gov/39231952","citation_count":4,"is_preprint":false},{"pmid":"40878439","id":"PMC_40878439","title":"TBC1D22B Regulates ER-to-Golgi Trafficking via RAB1B Inactivation and Promotes Oncogenic Programs in Breast Cancer.","date":"2025","source":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","url":"https://pubmed.ncbi.nlm.nih.gov/40878439","citation_count":3,"is_preprint":false},{"pmid":"40241313","id":"PMC_40241313","title":"Identification of Rab GTPase-Activating Proteins Required for Tubular Endosome Formation.","date":"2025","source":"Traffic (Copenhagen, Denmark)","url":"https://pubmed.ncbi.nlm.nih.gov/40241313","citation_count":1,"is_preprint":false},{"pmid":"39848545","id":"PMC_39848545","title":"Sex-specific DNA methylation marks associated with sex-biased risk of recurrence in unprovoked venous thromboembolism.","date":"2025","source":"Journal of thrombosis and haemostasis : JTH","url":"https://pubmed.ncbi.nlm.nih.gov/39848545","citation_count":1,"is_preprint":false},{"pmid":"41833373","id":"PMC_41833373","title":"Identification of Rab30 as a novel regulator of tubular endosomes.","date":"2026","source":"Cell structure and function","url":"https://pubmed.ncbi.nlm.nih.gov/41833373","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6309,"output_tokens":1357,"usd":0.019641,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8038,"output_tokens":2196,"usd":0.047545,"stage2_stop_reason":"end_turn"},"total_usd":0.067186,"stage1_batch_id":"msgbatch_017qqVz33Ga63SCDwzb35XPb","stage2_batch_id":"msgbatch_01Scr2Ei9x4HJMiRGxwrmvLK","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2013,\n      \"finding\": \"TBC1D22B (and paralog TBC1D22A) were identified as ACBD3-interacting proteins via affinity purification-mass spectrometry. Fine-scale mapping showed that the binding domains for TBC1D22A/B and PI4KB on ACBD3 are identical, and affinity purification confirmed that PI4KB and TBC1D22A/B interactions with ACBD3 are mutually exclusive, suggesting TBC1D22B competes with PI4KB for ACBD3 binding.\",\n      \"method\": \"Affinity purification-mass spectrometry, fine-scale domain mapping, competitive binding assays\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal affinity purification with MS and domain-mapping, single lab, two orthogonal methods\",\n      \"pmids\": [\"23572552\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TBC1D22B functions as a GTPase-activating protein (GAP) for RAB1B; overexpression of TBC1D22B inhibits ER-to-Golgi transport in a GAP-activity-dependent manner, RAB1B silencing phenocopies the trafficking defects caused by TBC1D22B overexpression, and TBC1D22B overexpression represses a module of extracellular matrix and adhesion-related genes consistent with altered secretory activity.\",\n      \"method\": \"RUSH (Retention Using Selective Hooks) trafficking assay, proximity-labeling and co-immunoprecipitation proteomics, siRNA knockdown, transcriptomic profiling, GAP-dead mutant analysis\",\n      \"journal\": \"Advanced science (Weinheim, Baden-Wurttemberg, Germany)\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — functional trafficking assay (RUSH), GAP-activity-dependent mutagenesis, direct substrate identification (RAB1B), and phenocopy by RAB1B silencing, all in single rigorous study with multiple orthogonal methods\",\n      \"pmids\": [\"40878439\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Elevated TBC1D22B expression is causally linked to a glycolytic phenotype in triple-negative breast cancer (TNBC) cell lines, as demonstrated by in-depth functional investigations.\",\n      \"method\": \"Gene knockdown/overexpression in TNBC cell lines with metabolic phenotype readout; orthogonal transcriptomics/metabolomics\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional knockdown/overexpression with metabolic readout plus transcriptomics/metabolomics, single lab\",\n      \"pmids\": [\"39231952\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"TBC1D22B is required for tubular endosome formation in HeLa cells; both knockdown and overexpression of TBC1D22B reduce tubular endosome structures, and this effect is dependent on GAP activity.\",\n      \"method\": \"Comprehensive TBC/Rab-GAP siRNA knockdown screening, overexpression experiments, tubular endosome morphology quantification\",\n      \"journal\": \"Traffic (Copenhagen, Denmark)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — systematic knockdown and overexpression screen with morphological phenotype readout and GAP-activity dependence, single lab\",\n      \"pmids\": [\"40241313\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"RAB30, a Golgi-resident Rab GTPase, is a direct target of TBC1D22B's GAP activity and is involved in tubular endosome formation and clathrin-independent endocytosis (CIE) cargo trafficking; a Rab30-BICD2-KIF5B axis is implicated downstream.\",\n      \"method\": \"Comprehensive Rab knockdown screening, dominant-negative Rab expression, co-functional epistasis with TBC1D22B in HeLa cells\",\n      \"journal\": \"Cell structure and function\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — systematic Rab knockdown/dominant-negative screen combined with TBC1D22B loss-of-function, single lab, single study\",\n      \"pmids\": [\"41833373\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"TBC1D22B is a Golgi-associated RAB-GTPase-activating protein (GAP) that directly inactivates RAB1B to inhibit ER-to-Golgi trafficking and also targets RAB30 to regulate tubular endosome formation and CIE cargo recycling; it interacts with the Golgi adaptor ACBD3 in a manner mutually exclusive with PI4KB binding, is required for normal tubular endosome structures in a GAP-activity-dependent manner, and its overexpression in breast cancer cells drives a glycolytic phenotype and represses extracellular matrix/adhesion gene programs.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TBC1D22B is a Golgi-associated RAB-GTPase-activating protein (GAP) that controls membrane trafficking by inactivating specific RAB GTPases [#1, #4]. It acts as a GAP for RAB1B, and its overexpression inhibits ER-to-Golgi transport in a manner dependent on intact GAP activity; silencing RAB1B phenocopies this trafficking defect, and the resulting altered secretory state represses a module of extracellular matrix and adhesion genes [#1]. TBC1D22B additionally targets the Golgi-resident GTPase RAB30, and through this activity it is required for normal tubular endosome formation and clathrin-independent endocytic cargo trafficking, with a downstream RAB30-BICD2-KIF5B axis implicated; both loss and excess of TBC1D22B disrupt tubular endosome structures in a GAP-dependent manner [#3, #4]. TBC1D22B associates with the Golgi adaptor ACBD3, binding the same region used by PI4KB such that the two interactions are mutually exclusive [#0]. In triple-negative breast cancer cells, elevated TBC1D22B expression drives a glycolytic phenotype [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Established the first physical interactor of TBC1D22B, placing it at the Golgi adaptor ACBD3 and revealing it competes with the lipid kinase PI4KB for the same binding site.\",\n      \"evidence\": \"Affinity purification-mass spectrometry with fine-scale domain mapping and competitive binding assays\",\n      \"pmids\": [\"23572552\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional consequence of TBC1D22B-ACBD3 binding not tested\",\n        \"GAP substrate and enzymatic role not yet defined here\",\n        \"Whether competition with PI4KB regulates PI4P signaling unaddressed\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Linked TBC1D22B expression to cellular metabolism, showing its elevation drives a glycolytic phenotype in cancer cells.\",\n      \"evidence\": \"Knockdown/overexpression in TNBC cell lines with metabolic and transcriptomic/metabolomic readouts\",\n      \"pmids\": [\"39231952\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanistic connection between GAP/trafficking activity and glycolysis not resolved\",\n        \"Single cancer context (TNBC); generality unknown\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Defined TBC1D22B as a GAP for RAB1B that gates ER-to-Golgi trafficking, providing the first direct enzymatic substrate and a secretory-pathway role tied to ECM/adhesion gene regulation.\",\n      \"evidence\": \"RUSH trafficking assay, proximity-labeling and co-IP proteomics, siRNA, GAP-dead mutagenesis, and transcriptomics\",\n      \"pmids\": [\"40878439\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct biochemical GAP kinetics on RAB1B not quantified in narrative terms\",\n        \"How ECM/adhesion gene repression couples mechanistically to trafficking unresolved\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Identified a role for TBC1D22B in endosomal membrane shaping, showing it is required for tubular endosome formation via its GAP activity.\",\n      \"evidence\": \"Systematic TBC/Rab-GAP siRNA screen with overexpression and tubular endosome morphology quantification in HeLa cells\",\n      \"pmids\": [\"40241313\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The relevant Rab substrate for this endosomal phenotype not identified in this study\",\n        \"Bidirectional (knockdown and overexpression) disruption mechanism unexplained\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Identified RAB30 as a second GAP substrate of TBC1D22B and placed it in a motor-based axis controlling tubular endosomes and CIE cargo recycling.\",\n      \"evidence\": \"Comprehensive Rab knockdown and dominant-negative screen with TBC1D22B epistasis in HeLa cells\",\n      \"pmids\": [\"41833373\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct biochemical GAP activity on RAB30 vs RAB1B selectivity not dissected\",\n        \"RAB30-BICD2-KIF5B axis is implicated but not biochemically reconstituted\",\n        \"Relationship between RAB1B and RAB30 regulation by the same GAP unclear\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How TBC1D22B selects among RAB substrates (RAB1B vs RAB30) across compartments, and how its trafficking function connects to the glycolytic and ECM phenotypes, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of GAP-substrate or ACBD3 interaction\",\n        \"Mechanistic link between trafficking control and metabolic reprogramming undefined\",\n        \"Physiological/in vivo role not established\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [1, 3, 4]},\n      {\"term_id\": \"GO:0060089\", \"supporting_discovery_ids\": [1, 4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0005768\", \"supporting_discovery_ids\": [3, 4]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [1, 3, 4]},\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [1, 4]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"ACBD3\", \"RAB1B\", \"RAB30\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}