{"gene":"BBLN","run_date":"2026-06-09T22:02:44","timeline":{"discoveries":[{"year":2021,"finding":"BBLN-1 (C. elegans ortholog of mammalian BBLN/bublin) interacts with intermediate filament (IF) proteins and localizes to the IF network in an IF-dependent manner; loss of BBLN-1 causes abnormal IF aggregation and bubble-shaped apical membrane invaginations in intestinal cells, establishing a direct role for the IF network in maintaining lumen homeostasis.","method":"Genetic loss-of-function (BBLN-1 mutants in C. elegans), co-localization imaging, protein interaction studies; mammalian BBLN expressed in C. elegans intestine rescued the BBLN-1 loss-of-function phenotype; in mouse intestinal organoids, BBLN localizes subapically with keratin 8","journal":"Current biology : CB","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal genetic rescue, localization with functional consequence, ortholog validation across two model systems, multiple orthogonal methods in one study","pmids":["33857431"],"is_preprint":false},{"year":2023,"finding":"Human BBLN promotes cardiac pathology by activating calcium/calmodulin-dependent protein kinase II delta (CAMK2D); BBLN physically binds CAMK2D, and a BBLN mutant with impaired CAMK2D binding was inert, demonstrating the interaction is required for BBLN-induced cardiac inflammation, fibrosis, and necroptosis. Endogenous BBLN is induced by hypoxia and chronic pressure overload, and its downregulation decreased CAMK2D hyperactivity.","method":"Transgenic mouse overexpression (dosage-dependent mortality), binding-impaired BBLN mutant (mutagenesis), siRNA-mediated CAMK2D knockdown rescuing BBLN-induced phenotypes, co-immunoprecipitation/binding assay implied by mutant inertness, in vivo cardiac pressure overload model","journal":"Nature cardiovascular research","confidence":"High","confidence_rationale":"Tier 2 / Moderate — active-site/binding mutagenesis combined with genetic epistasis (CAMK2D RNAi rescue), in vivo overexpression dosage series, single lab but multiple orthogonal methods","pmids":["38666071"],"is_preprint":false},{"year":2022,"finding":"Fusion of Hero9 (BBLN) in cis strongly protected the activity of firefly luciferase bearing destabilizing mutations against heat and other stress conditions, demonstrating a chaperone-like stabilization function for the protein.","method":"In vitro/cell-based luciferase activity assay with Hero9 fusion constructs under heat and chemical stress; recombinant protein production in E. coli","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro functional assay with direct readout, but single lab, single method, and the focus is on the fusion-tag application rather than deep mechanistic dissection","pmids":["35714106"],"is_preprint":false},{"year":2023,"finding":"In C. elegans, the IF-associated protein BBLN-1 genetically interacts with the cytoskeletal linker IFO-1 and the MAPK SMA-5; removal of the aberrant IF network (via IFB-2 deletion) rescues both structural and functional deficiencies caused by BBLN-1 loss, placing BBLN-1 upstream of IF network organization in the intestinal cytoskeleton.","method":"Genetic epistasis in C. elegans: double mutants of ifb-2 with bbln-1, ifo-1, and sma-5; structural and functional phenotype rescue assays","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean genetic epistasis in C. elegans with multiple allele combinations and functional rescue readout, single study","pmids":["37283438"],"is_preprint":false}],"current_model":"BBLN (bublin/Hero9/C9orf16) is a small coiled-coil protein that associates with intermediate filament networks (interacting with IF proteins and keratin 8 in a subapical compartment) to maintain apical membrane and lumen morphology in epithelial tubes, and in cardiac cells directly binds and activates CAMK2D kinase—a binding required for BBLN-driven inflammation, fibrosis, and necroptosis—while also possessing intrinsic chaperone-like activity that stabilizes client proteins against stress in a cis-fusion context."},"narrative":{"mechanistic_narrative":"BBLN (bublin/Hero9/C9orf16) is a small coiled-coil protein that organizes the intermediate filament (IF) cytoskeleton to maintain epithelial tube and lumen morphology [PMID:33857431]. In C. elegans intestine, the ortholog BBLN-1 interacts with IF proteins and localizes to the IF network in an IF-dependent manner; its loss causes aberrant IF aggregation and bubble-shaped apical membrane invaginations, and mammalian BBLN rescues this phenotype, while in mouse intestinal organoids BBLN localizes subapically with keratin 8 [PMID:33857431]. Genetically, BBLN-1 acts upstream of IF network organization, interacting with the cytoskeletal linker IFO-1 and the MAPK SMA-5, since removing the aberrant IF network by IFB-2 deletion rescues the structural and functional deficits of BBLN-1 loss [PMID:37283438]. In the heart, BBLN is induced by hypoxia and pressure overload and drives cardiac inflammation, fibrosis, and necroptosis by physically binding and activating the kinase CAMK2D; a binding-impaired mutant is inert and CAMK2D knockdown rescues BBLN-induced phenotypes [PMID:38666071]. BBLN additionally possesses an intrinsic chaperone-like activity, stabilizing destabilized client proteins against heat and chemical stress when fused in cis [PMID:35714106].","teleology":[{"year":2021,"claim":"Established BBLN's primary cellular role by showing its ortholog is an IF-network-associated protein required for epithelial lumen homeostasis, answering what biological process this uncharacterized protein serves.","evidence":"Genetic loss-of-function and co-localization in C. elegans intestine, with mammalian BBLN cross-species rescue and keratin 8 co-localization in mouse organoids","pmids":["33857431"],"confidence":"High","gaps":["The biochemical mode of BBLN binding to IF proteins is not resolved","Mammalian epithelial lumen function tested only by ortholog rescue, not in mammalian tissue directly","Whether BBLN nucleates, bundles, or stabilizes IF is undefined"]},{"year":2022,"claim":"Revealed an intrinsic protein-stabilizing capacity, showing BBLN can act as a chaperone-like protector of client protein activity under stress.","evidence":"Cell-based and in vitro luciferase activity assay with cis Hero9/BBLN fusions under heat and chemical stress; recombinant protein from E. coli","pmids":["35714106"],"confidence":"Medium","gaps":["Demonstrated only in a cis-fusion context, not for endogenous trans clients","No physiological client identified","Single lab, single assay focused on fusion-tag application"]},{"year":2023,"claim":"Placed BBLN upstream of IF network assembly in a defined genetic pathway, clarifying that its lumen phenotype arises from disordered IF organization rather than an independent function.","evidence":"Genetic epistasis in C. elegans with ifb-2, ifo-1, and sma-5 double mutants plus structural/functional rescue readouts","pmids":["37283438"],"confidence":"Medium","gaps":["Direct physical interaction with IFO-1 and SMA-5 not biochemically demonstrated","How BBLN-1 mechanistically directs IF network architecture is unknown","Pathway tested in invertebrate intestine only"]},{"year":2023,"claim":"Identified a distinct cardiac function in which BBLN drives pathology through direct kinase activation, expanding its role beyond the cytoskeleton.","evidence":"Transgenic mouse overexpression dosage series, binding-impaired BBLN mutant, siRNA CAMK2D knockdown rescue, and in vivo pressure-overload model","pmids":["38666071"],"confidence":"High","gaps":["Structural basis of the BBLN-CAMK2D interaction not resolved","Whether the cardiac CAMK2D mechanism relates to the IF/chaperone functions is unknown","Mechanism of how binding activates CAMK2D not defined"]},{"year":null,"claim":"How BBLN's three reported activities — IF-network organization, CAMK2D activation, and chaperone-like stabilization — relate within a single molecular framework remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of BBLN exists","No unified biochemical mechanism connecting IF binding, kinase activation, and client stabilization","Endogenous BBLN clients/substrates beyond CAMK2D and IF proteins not catalogued"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[0,3]},{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[1]},{"term_id":"GO:0044183","term_label":"protein folding chaperone","supporting_discovery_ids":[2]}],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[0]},{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[0]}],"pathway":[],"complexes":[],"partners":["CAMK2D","KRT8","IFO-1","SMA-5","IFB-2"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q9BUW7","full_name":"Bublin coiled-coil protein","aliases":["UPF0184 protein C9orf16"],"length_aa":83,"mass_kda":9.1,"function":"Essential for intermediate filament organization in intestinal cells, interacts with intermediate filament and regulates intestinal lumen morphology","subcellular_location":"Cell junction; Cytoplasm, cytoskeleton","url":"https://www.uniprot.org/uniprotkb/Q9BUW7/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/BBLN","classification":"Not Classified","n_dependent_lines":128,"n_total_lines":1208,"dependency_fraction":0.10596026490066225},"opencell":{"profiled":true,"resolved_as":"C9ORF16","ensg_id":"ENSG00000171159","cell_line_id":"CID000395","localizations":[{"compartment":"cytoplasmic","grade":3},{"compartment":"nucleoplasm","grade":3}],"interactors":[{"gene":"ATP6V1F","stoichiometry":10.0},{"gene":"SLC27A4","stoichiometry":0.2},{"gene":"ATP6V1D","stoichiometry":0.2},{"gene":"RNF40","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID000395","total_profiled":1310},"omim":[],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Microtubules","reliability":"Approved"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"brain","ntpm":619.0}],"url":"https://www.proteinatlas.org/search/BBLN"},"hgnc":{"alias_symbol":["Hero9","MGC4639","EST00098","FLJ12823"],"prev_symbol":["C9orf16"]},"alphafold":{"accession":"Q9BUW7","domains":[{"cath_id":"1.20.5","chopping":"27-56","consensus_level":"medium","plddt":96.8917,"start":27,"end":56}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9BUW7","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q9BUW7-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q9BUW7-F1-predicted_aligned_error_v6.png","plddt_mean":80.31},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=BBLN","jax_strain_url":"https://www.jax.org/strain/search?query=BBLN"},"sequence":{"accession":"Q9BUW7","fasta_url":"https://rest.uniprot.org/uniprotkb/Q9BUW7.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q9BUW7/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q9BUW7"}},"corpus_meta":[{"pmid":"29968759","id":"PMC_29968759","title":"Identification of pathways and genes associated with synovitis in osteoarthritis using bioinformatics analyses.","date":"2018","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/29968759","citation_count":42,"is_preprint":false},{"pmid":"33857431","id":"PMC_33857431","title":"BBLN-1 is essential for intermediate filament organization and apical membrane morphology.","date":"2021","source":"Current biology : CB","url":"https://pubmed.ncbi.nlm.nih.gov/33857431","citation_count":14,"is_preprint":false},{"pmid":"35714106","id":"PMC_35714106","title":"Fusion with heat-resistant obscure (Hero) proteins have the potential to improve the molecular property of recombinant proteins.","date":"2022","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/35714106","citation_count":12,"is_preprint":false},{"pmid":"39595169","id":"PMC_39595169","title":"C11orf58 (Hero20) Gene Polymorphism: Contribution to Ischemic Stroke Risk and Interactions with Other Heat-Resistant Obscure Chaperones.","date":"2024","source":"Biomedicines","url":"https://pubmed.ncbi.nlm.nih.gov/39595169","citation_count":8,"is_preprint":false},{"pmid":"38666071","id":"PMC_38666071","title":"BBLN triggers CAMK2D pathology in mice under cardiac pressure overload and potentially in unrepaired hearts with tetralogy of Fallot.","date":"2023","source":"Nature cardiovascular research","url":"https://pubmed.ncbi.nlm.nih.gov/38666071","citation_count":6,"is_preprint":false},{"pmid":"37918265","id":"PMC_37918265","title":"BBLN: A bilateral-branch learning network for unknown protein-protein interaction prediction.","date":"2023","source":"Computers in biology and medicine","url":"https://pubmed.ncbi.nlm.nih.gov/37918265","citation_count":5,"is_preprint":false},{"pmid":"37283438","id":"PMC_37283438","title":"Intermediate filament network perturbation in the C. elegans intestine causes systemic dysfunctions.","date":"2023","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/37283438","citation_count":5,"is_preprint":false},{"pmid":"36307773","id":"PMC_36307773","title":"C9orf16 represents the aberrant genetic programs and drives the progression of PDAC.","date":"2022","source":"BMC cancer","url":"https://pubmed.ncbi.nlm.nih.gov/36307773","citation_count":2,"is_preprint":false},{"pmid":"34102119","id":"PMC_34102119","title":"Intermediate filaments: New insights are bublin up.","date":"2021","source":"Current biology : CB","url":"https://pubmed.ncbi.nlm.nih.gov/34102119","citation_count":0,"is_preprint":false},{"pmid":"40906246","id":"PMC_40906246","title":"When Heroes Fall: Reduced Expression of Heat-Resistant Obscure Proteins in Ischemic Stroke.","date":"2025","source":"Neuromolecular medicine","url":"https://pubmed.ncbi.nlm.nih.gov/40906246","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6227,"output_tokens":1244,"usd":0.01867,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7876,"output_tokens":2019,"usd":0.044928,"stage2_stop_reason":"end_turn"},"total_usd":0.063598,"stage1_batch_id":"msgbatch_0179Z2pxRYBsXi2xADneafRw","stage2_batch_id":"msgbatch_01LaY9ZaVdgjWArcZo9eqQE5","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"BBLN-1 (C. elegans ortholog of mammalian BBLN/bublin) interacts with intermediate filament (IF) proteins and localizes to the IF network in an IF-dependent manner; loss of BBLN-1 causes abnormal IF aggregation and bubble-shaped apical membrane invaginations in intestinal cells, establishing a direct role for the IF network in maintaining lumen homeostasis.\",\n      \"method\": \"Genetic loss-of-function (BBLN-1 mutants in C. elegans), co-localization imaging, protein interaction studies; mammalian BBLN expressed in C. elegans intestine rescued the BBLN-1 loss-of-function phenotype; in mouse intestinal organoids, BBLN localizes subapically with keratin 8\",\n      \"journal\": \"Current biology : CB\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal genetic rescue, localization with functional consequence, ortholog validation across two model systems, multiple orthogonal methods in one study\",\n      \"pmids\": [\"33857431\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Human BBLN promotes cardiac pathology by activating calcium/calmodulin-dependent protein kinase II delta (CAMK2D); BBLN physically binds CAMK2D, and a BBLN mutant with impaired CAMK2D binding was inert, demonstrating the interaction is required for BBLN-induced cardiac inflammation, fibrosis, and necroptosis. Endogenous BBLN is induced by hypoxia and chronic pressure overload, and its downregulation decreased CAMK2D hyperactivity.\",\n      \"method\": \"Transgenic mouse overexpression (dosage-dependent mortality), binding-impaired BBLN mutant (mutagenesis), siRNA-mediated CAMK2D knockdown rescuing BBLN-induced phenotypes, co-immunoprecipitation/binding assay implied by mutant inertness, in vivo cardiac pressure overload model\",\n      \"journal\": \"Nature cardiovascular research\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — active-site/binding mutagenesis combined with genetic epistasis (CAMK2D RNAi rescue), in vivo overexpression dosage series, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"38666071\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Fusion of Hero9 (BBLN) in cis strongly protected the activity of firefly luciferase bearing destabilizing mutations against heat and other stress conditions, demonstrating a chaperone-like stabilization function for the protein.\",\n      \"method\": \"In vitro/cell-based luciferase activity assay with Hero9 fusion constructs under heat and chemical stress; recombinant protein production in E. coli\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro functional assay with direct readout, but single lab, single method, and the focus is on the fusion-tag application rather than deep mechanistic dissection\",\n      \"pmids\": [\"35714106\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"In C. elegans, the IF-associated protein BBLN-1 genetically interacts with the cytoskeletal linker IFO-1 and the MAPK SMA-5; removal of the aberrant IF network (via IFB-2 deletion) rescues both structural and functional deficiencies caused by BBLN-1 loss, placing BBLN-1 upstream of IF network organization in the intestinal cytoskeleton.\",\n      \"method\": \"Genetic epistasis in C. elegans: double mutants of ifb-2 with bbln-1, ifo-1, and sma-5; structural and functional phenotype rescue assays\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean genetic epistasis in C. elegans with multiple allele combinations and functional rescue readout, single study\",\n      \"pmids\": [\"37283438\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"BBLN (bublin/Hero9/C9orf16) is a small coiled-coil protein that associates with intermediate filament networks (interacting with IF proteins and keratin 8 in a subapical compartment) to maintain apical membrane and lumen morphology in epithelial tubes, and in cardiac cells directly binds and activates CAMK2D kinase—a binding required for BBLN-driven inflammation, fibrosis, and necroptosis—while also possessing intrinsic chaperone-like activity that stabilizes client proteins against stress in a cis-fusion context.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"BBLN (bublin/Hero9/C9orf16) is a small coiled-coil protein that organizes the intermediate filament (IF) cytoskeleton to maintain epithelial tube and lumen morphology [#0]. In C. elegans intestine, the ortholog BBLN-1 interacts with IF proteins and localizes to the IF network in an IF-dependent manner; its loss causes aberrant IF aggregation and bubble-shaped apical membrane invaginations, and mammalian BBLN rescues this phenotype, while in mouse intestinal organoids BBLN localizes subapically with keratin 8 [#0]. Genetically, BBLN-1 acts upstream of IF network organization, interacting with the cytoskeletal linker IFO-1 and the MAPK SMA-5, since removing the aberrant IF network by IFB-2 deletion rescues the structural and functional deficits of BBLN-1 loss [#3]. In the heart, BBLN is induced by hypoxia and pressure overload and drives cardiac inflammation, fibrosis, and necroptosis by physically binding and activating the kinase CAMK2D; a binding-impaired mutant is inert and CAMK2D knockdown rescues BBLN-induced phenotypes [#1]. BBLN additionally possesses an intrinsic chaperone-like activity, stabilizing destabilized client proteins against heat and chemical stress when fused in cis [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Established BBLN's primary cellular role by showing its ortholog is an IF-network-associated protein required for epithelial lumen homeostasis, answering what biological process this uncharacterized protein serves.\",\n      \"evidence\": \"Genetic loss-of-function and co-localization in C. elegans intestine, with mammalian BBLN cross-species rescue and keratin 8 co-localization in mouse organoids\",\n      \"pmids\": [\"33857431\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"The biochemical mode of BBLN binding to IF proteins is not resolved\", \"Mammalian epithelial lumen function tested only by ortholog rescue, not in mammalian tissue directly\", \"Whether BBLN nucleates, bundles, or stabilizes IF is undefined\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Revealed an intrinsic protein-stabilizing capacity, showing BBLN can act as a chaperone-like protector of client protein activity under stress.\",\n      \"evidence\": \"Cell-based and in vitro luciferase activity assay with cis Hero9/BBLN fusions under heat and chemical stress; recombinant protein from E. coli\",\n      \"pmids\": [\"35714106\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Demonstrated only in a cis-fusion context, not for endogenous trans clients\", \"No physiological client identified\", \"Single lab, single assay focused on fusion-tag application\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Placed BBLN upstream of IF network assembly in a defined genetic pathway, clarifying that its lumen phenotype arises from disordered IF organization rather than an independent function.\",\n      \"evidence\": \"Genetic epistasis in C. elegans with ifb-2, ifo-1, and sma-5 double mutants plus structural/functional rescue readouts\",\n      \"pmids\": [\"37283438\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct physical interaction with IFO-1 and SMA-5 not biochemically demonstrated\", \"How BBLN-1 mechanistically directs IF network architecture is unknown\", \"Pathway tested in invertebrate intestine only\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Identified a distinct cardiac function in which BBLN drives pathology through direct kinase activation, expanding its role beyond the cytoskeleton.\",\n      \"evidence\": \"Transgenic mouse overexpression dosage series, binding-impaired BBLN mutant, siRNA CAMK2D knockdown rescue, and in vivo pressure-overload model\",\n      \"pmids\": [\"38666071\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of the BBLN-CAMK2D interaction not resolved\", \"Whether the cardiac CAMK2D mechanism relates to the IF/chaperone functions is unknown\", \"Mechanism of how binding activates CAMK2D not defined\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How BBLN's three reported activities — IF-network organization, CAMK2D activation, and chaperone-like stabilization — relate within a single molecular framework remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structural model of BBLN exists\", \"No unified biochemical mechanism connecting IF binding, kinase activation, and client stabilization\", \"Endogenous BBLN clients/substrates beyond CAMK2D and IF proteins not catalogued\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0044183\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [\"CAMK2D\", \"KRT8\", \"IFO-1\", \"SMA-5\", \"IFB-2\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}