{"gene":"RINL","run_date":"2026-06-10T06:43:36","timeline":{"discoveries":[{"year":2011,"finding":"RINL (Rin-like) functions as a guanine nucleotide exchange factor (GEF) for Rab5a and Rab22, preferentially binding nucleotide-free Rab5a and GDP-bound Rab22 to catalyze GDP-for-GTP exchange, with a higher catalytic rate for Rab22 than Rab5a.","method":"In vitro GEF activity assays (nucleotide exchange assays), binding studies","journal":"Biochimica et biophysica acta","confidence":"High","confidence_rationale":"Tier 1 / Moderate — direct in vitro biochemical reconstitution of GEF activity with kinetic measurements, replicated in a second independent study (PMID:22291991)","pmids":["21419809"],"is_preprint":false},{"year":2011,"finding":"RINL interacts with the receptor tyrosine kinase MuSK and localizes to neuromuscular synapses, associating closely with the cytoskeleton at actin-positive compartments.","method":"Interaction studies (binding/pulldown), immunolocalization at neuromuscular junctions","journal":"Biochimica et biophysica acta","confidence":"Medium","confidence_rationale":"Tier 3 / Weak — single lab, single paper; binding and localization shown but no functional epistasis or structural validation","pmids":["21419809"],"is_preprint":false},{"year":2011,"finding":"Overexpression of RINL affects fluid-phase endocytosis and EGFR endocytosis, implicating RINL in endocytic processes.","method":"Overexpression in cultured cells with functional endocytosis assays","journal":"Biochimica et biophysica acta","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — defined cellular phenotype with loss/gain-of-function, single lab, single method","pmids":["21419809"],"is_preprint":false},{"year":2012,"finding":"RINL has GEF activity for Rab5 subfamily proteins in cultured cells (confirmed by measuring GTP-bound forms), and interacts with the ankyrin-repeat and SAM domain-containing protein odin to form a ternary complex with EphA8.","method":"GTP-loading assays in cultured cells, co-immunoprecipitation","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — GEF activity confirmed in cells and by in vitro data from prior study; co-IP for complex; two orthogonal methods in single lab","pmids":["22291991"],"is_preprint":false},{"year":2012,"finding":"RINL expression reduces EphA8 protein levels in a manner dependent on both its GEF activity (VPS9 domain) and its interaction with odin; RINL knockdown increases EphA8 levels, placing RINL in the EphA8 degradation pathway.","method":"Overexpression and knockdown in HeLa cells, GEF-activity-dead mutants, western blot for EphA8 levels","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — loss-of-function and gain-of-function with domain mutants, single lab, two orthogonal approaches","pmids":["22291991"],"is_preprint":false},{"year":2023,"finding":"RINL acts as a negative regulator of T follicular helper (Tfh) cell differentiation in a GEF-activity-dependent, T cell-intrinsic manner; mechanistically, RINL regulates CD28 internalization and downstream CD28 signaling, thereby shaping CD4+ T cell activation and differentiation.","method":"Rinl knockout mice, adoptive transfer of WT vs Rinl-KO naïve CD4+ T cells, in vivo immunization and LCMV infection models, human CD4+ T cell in vitro cultures, CD28 internalization assays","journal":"The Journal of experimental medicine","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal loss-of-function (KO) with adoptive transfer establishing T cell-intrinsic function, GEF-dependence tested, replicated across mouse and human systems with multiple orthogonal methods","pmids":["37703004"],"is_preprint":false}],"current_model":"RINL is a VPS9-domain-containing guanine nucleotide exchange factor (GEF) for Rab5 subfamily GTPases (Rab5a and Rab22) that localizes to actin-positive endocytic compartments and neuromuscular synapses; it interacts with MuSK and forms a ternary complex with odin and EphA8 to promote EphA8 lysosomal degradation via Rab5-dependent endocytosis, and in CD4+ T cells it negatively regulates Tfh differentiation by controlling CD28 internalization and signaling in a GEF-activity-dependent manner."},"narrative":{"mechanistic_narrative":"RINL is a VPS9-domain guanine nucleotide exchange factor (GEF) for Rab5-subfamily GTPases that links receptor endocytic trafficking to cellular signaling outcomes [PMID:21419809, PMID:22291991]. In vitro it preferentially engages nucleotide-free Rab5a and GDP-bound Rab22 to catalyze GDP-for-GTP exchange, with higher catalytic efficiency toward Rab22, and this GEF activity is confirmed in cells by elevated GTP-loading of Rab5-subfamily proteins [PMID:21419809, PMID:22291991]. RINL associates with actin-positive endocytic compartments and neuromuscular synapses, where it binds the receptor tyrosine kinase MuSK, and its overexpression perturbs fluid-phase and EGFR endocytosis [PMID:21419809]. Through interaction with the ankyrin-repeat/SAM-domain adaptor odin, RINL forms a ternary complex with EphA8 and drives EphA8 down-regulation in a manner requiring both its VPS9 GEF activity and the odin interaction [PMID:22291991]. In CD4+ T cells, RINL is a T cell-intrinsic negative regulator of T follicular helper differentiation, acting through GEF-activity-dependent control of CD28 internalization and downstream CD28 signaling [PMID:37703004].","teleology":[{"year":2011,"claim":"Establishing that RINL is an enzyme rather than a passive scaffold, this work defined its catalytic activity as a GEF selective for Rab5-subfamily GTPases.","evidence":"In vitro nucleotide exchange and binding assays with Rab5a and Rab22","pmids":["21419809"],"confidence":"High","gaps":["No structural basis for Rab5a-versus-Rab22 selectivity","Physiological substrate preference in vivo not resolved"]},{"year":2011,"claim":"To place the GEF in a cellular context, RINL was shown to bind MuSK and localize to actin-positive neuromuscular synapses, suggesting a site of action.","evidence":"Binding/pulldown and immunolocalization at neuromuscular junctions","pmids":["21419809"],"confidence":"Medium","gaps":["No functional epistasis linking MuSK binding to GEF output","Single lab, no reciprocal validation"]},{"year":2011,"claim":"Connecting GEF activity to membrane traffic, overexpression of RINL altered fluid-phase and EGFR endocytosis, implicating it in endocytic flux.","evidence":"Overexpression endocytosis assays in cultured cells","pmids":["21419809"],"confidence":"Medium","gaps":["Overexpression-only; endogenous loss-of-function not tested","Whether effects are direct or Rab-mediated unclear"]},{"year":2012,"claim":"Identifying a specific receptor cargo, RINL was found to form a ternary complex with odin and EphA8 and to confirm GEF activity in cells by Rab5-subfamily GTP-loading.","evidence":"Cellular GTP-loading assays and co-immunoprecipitation","pmids":["22291991"],"confidence":"Medium","gaps":["Direct versus bridged nature of the ternary complex not resolved","Single lab co-IP"]},{"year":2012,"claim":"Demonstrating functional consequence, RINL was shown to reduce EphA8 levels dependent on both its VPS9 GEF activity and odin interaction, placing it in the EphA8 degradation pathway.","evidence":"Overexpression/knockdown in HeLa cells with GEF-dead mutants and EphA8 western blots","pmids":["22291991"],"confidence":"Medium","gaps":["Lysosomal route inferred rather than directly traced","Single cell line"]},{"year":2023,"claim":"Extending RINL to immune physiology, knockout and adoptive-transfer studies established a T cell-intrinsic role in restraining Tfh differentiation via GEF-dependent control of CD28 internalization.","evidence":"Rinl-KO mice, adoptive transfer, immunization/LCMV models, human CD4+ T cell cultures, CD28 internalization assays","pmids":["37703004"],"confidence":"High","gaps":["Which Rab effector links CD28 trafficking to signaling not pinpointed","Connection between CD28 trafficking and the EphA8/odin axis unknown"]},{"year":null,"claim":"How RINL's GEF activity is recruited and regulated at specific receptor compartments, and whether a unifying mechanism connects its roles at synapses, EphA8 degradation, and CD28 trafficking, remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structure of RINL or its complexes","Upstream regulators of RINL activity unknown","No shared effector mechanism across its reported contexts"]}],"mechanism_profile":{"molecular_activity":[],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[1]},{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[2]}],"pathway":[{"term_id":"R-HSA-5653656","term_label":"Vesicle-mediated transport","supporting_discovery_ids":[2,4]},{"term_id":"R-HSA-168256","term_label":"Immune System","supporting_discovery_ids":[5]}],"complexes":[],"partners":["RAB5A","RAB22A","MUSK","ANKS1A","EPHA8","CD28"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q6ZS11","full_name":"Ras and Rab interactor-like protein","aliases":[],"length_aa":566,"mass_kda":62.5,"function":"Guanine nucleotide exchange factor (GEF) for RAB5A and RAB22A that activates RAB5A and RAB22A by exchanging bound GDP for free GTP. Plays a role in endocytosis via its role in activating Rab family members (By similarity)","subcellular_location":"Cell projection, ruffle; Cytoplasmic vesicle","url":"https://www.uniprot.org/uniprotkb/Q6ZS11/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/RINL","classification":"Not Classified","n_dependent_lines":2,"n_total_lines":1208,"dependency_fraction":0.0016556291390728477},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/RINL","total_profiled":1310},"omim":[{"mim_id":"620678","title":"RAS AND RAB INTERACTOR-LIKE PROTEIN; RINL","url":"https://www.omim.org/entry/620678"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"},{"location":"Vesicles","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in many","driving_tissues":[],"url":"https://www.proteinatlas.org/search/RINL"},"hgnc":{"alias_symbol":["FLJ45909"],"prev_symbol":[]},"alphafold":{"accession":"Q6ZS11","domains":[{"cath_id":"3.30.505.10","chopping":"38-128","consensus_level":"high","plddt":79.6951,"start":38,"end":128},{"cath_id":"-","chopping":"256-329_341-356","consensus_level":"high","plddt":85.9308,"start":256,"end":356},{"cath_id":"1.20.1050.80","chopping":"372-387_402-512_522-537","consensus_level":"high","plddt":85.0852,"start":372,"end":537}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6ZS11","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q6ZS11-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q6ZS11-F1-predicted_aligned_error_v6.png","plddt_mean":66.06},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=RINL","jax_strain_url":"https://www.jax.org/strain/search?query=RINL"},"sequence":{"accession":"Q6ZS11","fasta_url":"https://rest.uniprot.org/uniprotkb/Q6ZS11.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q6ZS11/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q6ZS11"}},"corpus_meta":[{"pmid":"8035228","id":"PMC_8035228","title":"Effects of chronic spinalization on ankle extensor motoneurons. II. Motoneuron electrical properties.","date":"1994","source":"Journal of neurophysiology","url":"https://pubmed.ncbi.nlm.nih.gov/8035228","citation_count":71,"is_preprint":false},{"pmid":"21419809","id":"PMC_21419809","title":"Rin-like, a novel regulator of endocytosis, acts as guanine nucleotide exchange factor for Rab5a and Rab22.","date":"2011","source":"Biochimica et biophysica acta","url":"https://pubmed.ncbi.nlm.nih.gov/21419809","citation_count":14,"is_preprint":false},{"pmid":"22291991","id":"PMC_22291991","title":"RINL, guanine nucleotide exchange factor Rab5-subfamily, is involved in the EphA8-degradation pathway with odin.","date":"2012","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/22291991","citation_count":12,"is_preprint":false},{"pmid":"37703004","id":"PMC_37703004","title":"The guanine nucleotide exchange factor Rin-like controls Tfh cell differentiation via CD28 signaling.","date":"2023","source":"The Journal of experimental medicine","url":"https://pubmed.ncbi.nlm.nih.gov/37703004","citation_count":4,"is_preprint":false},{"pmid":"38612491","id":"PMC_38612491","title":"Unveiling the Genetic Mechanism of Meat Color in Pigs through GWAS, Multi-Tissue, and Single-Cell Transcriptome Signatures Exploration.","date":"2024","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/38612491","citation_count":4,"is_preprint":false},{"pmid":"41098063","id":"PMC_41098063","title":"Molecular Atlas of PM2.5 Chemical Constituents on Cardiac Conduction: A Multiomics Landscape in Older Adults.","date":"2025","source":"Environmental science & technology","url":"https://pubmed.ncbi.nlm.nih.gov/41098063","citation_count":2,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5251,"output_tokens":1431,"usd":0.018609,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8054,"output_tokens":2148,"usd":0.046985,"stage2_stop_reason":"end_turn"},"total_usd":0.065594,"stage1_batch_id":"msgbatch_01CNoDbkChHEkgrJnL7BwtGJ","stage2_batch_id":"msgbatch_016Y4x9E9Wg5VQDANj9quSQD","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2011,\n      \"finding\": \"RINL (Rin-like) functions as a guanine nucleotide exchange factor (GEF) for Rab5a and Rab22, preferentially binding nucleotide-free Rab5a and GDP-bound Rab22 to catalyze GDP-for-GTP exchange, with a higher catalytic rate for Rab22 than Rab5a.\",\n      \"method\": \"In vitro GEF activity assays (nucleotide exchange assays), binding studies\",\n      \"journal\": \"Biochimica et biophysica acta\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — direct in vitro biochemical reconstitution of GEF activity with kinetic measurements, replicated in a second independent study (PMID:22291991)\",\n      \"pmids\": [\"21419809\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"RINL interacts with the receptor tyrosine kinase MuSK and localizes to neuromuscular synapses, associating closely with the cytoskeleton at actin-positive compartments.\",\n      \"method\": \"Interaction studies (binding/pulldown), immunolocalization at neuromuscular junctions\",\n      \"journal\": \"Biochimica et biophysica acta\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single paper; binding and localization shown but no functional epistasis or structural validation\",\n      \"pmids\": [\"21419809\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"Overexpression of RINL affects fluid-phase endocytosis and EGFR endocytosis, implicating RINL in endocytic processes.\",\n      \"method\": \"Overexpression in cultured cells with functional endocytosis assays\",\n      \"journal\": \"Biochimica et biophysica acta\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — defined cellular phenotype with loss/gain-of-function, single lab, single method\",\n      \"pmids\": [\"21419809\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"RINL has GEF activity for Rab5 subfamily proteins in cultured cells (confirmed by measuring GTP-bound forms), and interacts with the ankyrin-repeat and SAM domain-containing protein odin to form a ternary complex with EphA8.\",\n      \"method\": \"GTP-loading assays in cultured cells, co-immunoprecipitation\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — GEF activity confirmed in cells and by in vitro data from prior study; co-IP for complex; two orthogonal methods in single lab\",\n      \"pmids\": [\"22291991\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"RINL expression reduces EphA8 protein levels in a manner dependent on both its GEF activity (VPS9 domain) and its interaction with odin; RINL knockdown increases EphA8 levels, placing RINL in the EphA8 degradation pathway.\",\n      \"method\": \"Overexpression and knockdown in HeLa cells, GEF-activity-dead mutants, western blot for EphA8 levels\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function and gain-of-function with domain mutants, single lab, two orthogonal approaches\",\n      \"pmids\": [\"22291991\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"RINL acts as a negative regulator of T follicular helper (Tfh) cell differentiation in a GEF-activity-dependent, T cell-intrinsic manner; mechanistically, RINL regulates CD28 internalization and downstream CD28 signaling, thereby shaping CD4+ T cell activation and differentiation.\",\n      \"method\": \"Rinl knockout mice, adoptive transfer of WT vs Rinl-KO naïve CD4+ T cells, in vivo immunization and LCMV infection models, human CD4+ T cell in vitro cultures, CD28 internalization assays\",\n      \"journal\": \"The Journal of experimental medicine\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal loss-of-function (KO) with adoptive transfer establishing T cell-intrinsic function, GEF-dependence tested, replicated across mouse and human systems with multiple orthogonal methods\",\n      \"pmids\": [\"37703004\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"RINL is a VPS9-domain-containing guanine nucleotide exchange factor (GEF) for Rab5 subfamily GTPases (Rab5a and Rab22) that localizes to actin-positive endocytic compartments and neuromuscular synapses; it interacts with MuSK and forms a ternary complex with odin and EphA8 to promote EphA8 lysosomal degradation via Rab5-dependent endocytosis, and in CD4+ T cells it negatively regulates Tfh differentiation by controlling CD28 internalization and signaling in a GEF-activity-dependent manner.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"RINL is a VPS9-domain guanine nucleotide exchange factor (GEF) for Rab5-subfamily GTPases that links receptor endocytic trafficking to cellular signaling outcomes [#0, #4]. In vitro it preferentially engages nucleotide-free Rab5a and GDP-bound Rab22 to catalyze GDP-for-GTP exchange, with higher catalytic efficiency toward Rab22, and this GEF activity is confirmed in cells by elevated GTP-loading of Rab5-subfamily proteins [#0, #3]. RINL associates with actin-positive endocytic compartments and neuromuscular synapses, where it binds the receptor tyrosine kinase MuSK, and its overexpression perturbs fluid-phase and EGFR endocytosis [#1, #2]. Through interaction with the ankyrin-repeat/SAM-domain adaptor odin, RINL forms a ternary complex with EphA8 and drives EphA8 down-regulation in a manner requiring both its VPS9 GEF activity and the odin interaction [#3, #4]. In CD4+ T cells, RINL is a T cell-intrinsic negative regulator of T follicular helper differentiation, acting through GEF-activity-dependent control of CD28 internalization and downstream CD28 signaling [#5].\",\n  \"teleology\": [\n    {\n      \"year\": 2011,\n      \"claim\": \"Establishing that RINL is an enzyme rather than a passive scaffold, this work defined its catalytic activity as a GEF selective for Rab5-subfamily GTPases.\",\n      \"evidence\": \"In vitro nucleotide exchange and binding assays with Rab5a and Rab22\",\n      \"pmids\": [\"21419809\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No structural basis for Rab5a-versus-Rab22 selectivity\", \"Physiological substrate preference in vivo not resolved\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"To place the GEF in a cellular context, RINL was shown to bind MuSK and localize to actin-positive neuromuscular synapses, suggesting a site of action.\",\n      \"evidence\": \"Binding/pulldown and immunolocalization at neuromuscular junctions\",\n      \"pmids\": [\"21419809\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No functional epistasis linking MuSK binding to GEF output\", \"Single lab, no reciprocal validation\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Connecting GEF activity to membrane traffic, overexpression of RINL altered fluid-phase and EGFR endocytosis, implicating it in endocytic flux.\",\n      \"evidence\": \"Overexpression endocytosis assays in cultured cells\",\n      \"pmids\": [\"21419809\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Overexpression-only; endogenous loss-of-function not tested\", \"Whether effects are direct or Rab-mediated unclear\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Identifying a specific receptor cargo, RINL was found to form a ternary complex with odin and EphA8 and to confirm GEF activity in cells by Rab5-subfamily GTP-loading.\",\n      \"evidence\": \"Cellular GTP-loading assays and co-immunoprecipitation\",\n      \"pmids\": [\"22291991\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct versus bridged nature of the ternary complex not resolved\", \"Single lab co-IP\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Demonstrating functional consequence, RINL was shown to reduce EphA8 levels dependent on both its VPS9 GEF activity and odin interaction, placing it in the EphA8 degradation pathway.\",\n      \"evidence\": \"Overexpression/knockdown in HeLa cells with GEF-dead mutants and EphA8 western blots\",\n      \"pmids\": [\"22291991\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Lysosomal route inferred rather than directly traced\", \"Single cell line\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Extending RINL to immune physiology, knockout and adoptive-transfer studies established a T cell-intrinsic role in restraining Tfh differentiation via GEF-dependent control of CD28 internalization.\",\n      \"evidence\": \"Rinl-KO mice, adoptive transfer, immunization/LCMV models, human CD4+ T cell cultures, CD28 internalization assays\",\n      \"pmids\": [\"37703004\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Which Rab effector links CD28 trafficking to signaling not pinpointed\", \"Connection between CD28 trafficking and the EphA8/odin axis unknown\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How RINL's GEF activity is recruited and regulated at specific receptor compartments, and whether a unifying mechanism connects its roles at synapses, EphA8 degradation, and CD28 trafficking, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structure of RINL or its complexes\", \"Upstream regulators of RINL activity unknown\", \"No shared effector mechanism across its reported contexts\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005085\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-5653656\", \"supporting_discovery_ids\": [2, 4]},\n      {\"term_id\": \"R-HSA-168256\", \"supporting_discovery_ids\": [5]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"RAB5A\", \"RAB22A\", \"MUSK\", \"ANKS1A\", \"EPHA8\", \"CD28\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"tie","faith_supported":5,"faith_total":5,"faith_pct":100.0}}