{"gene":"FSCB","run_date":"2026-06-09T23:54:44","timeline":{"discoveries":[{"year":2007,"finding":"FSCB (fibrous sheath CABYR binding protein) is a testis- and sperm-specific protein that binds CABYR (a calcium-binding protein tyrosine-phosphorylated during capacitation), as demonstrated by co-immunoprecipitation/binding assays. FSCB is phosphorylated by protein kinase A (PKA) in vitro and at native phosphorylation sites in mouse sperm. FSCB itself is a calcium-binding protein as shown by calcium overlay assay. It localizes ultrastructurally to a cortical layer at the surface of the ribs and longitudinal columns of the fibrous sheath principal piece in mouse sperm flagella, and is first expressed at step 11 of spermatogenesis in elongating spermatids.","method":"Co-immunoprecipitation/binding assay (CABYR interaction), in vitro PKA phosphorylation assay with native phosphorylation site mapping, calcium overlay assay, immunofluorescence and electron microscopy localization","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — multiple orthogonal methods in a single focused study: in vitro kinase assay, native phosphosite mapping, calcium overlay, ultrastructural localization, and binding partner identification","pmids":["17855365"],"is_preprint":false},{"year":2011,"finding":"FSCB undergoes both tyrosine and Ser/Thr phosphorylation during mouse spermatozoa capacitation, detectable as early as 1 min after capacitation onset and increasing over 60 min. Phosphorylation is induced by the PKA agonist db-cAMP and blocked by the PKA antagonist H-89, confirming PKA-dependence. The extent of FSCB phosphorylation correlates with PKA activity and sperm motility characteristics.","method":"Immunoprecipitation with anti-phosphotyrosine and anti-phosphoSer/Thr antibodies, pharmacological manipulation (db-cAMP, H-89), time-course analysis during in vitro capacitation","journal":"BMB reports","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — reciprocal immunoprecipitation with pharmacological validation in a single lab; multiple orthogonal approaches but no in vitro reconstitution","pmids":["21871179"],"is_preprint":false},{"year":2013,"finding":"FSCB protein levels are reduced in sperm from ROPN1 knockout (RKO) mice, indicating that ROPN1 is required for normal FSCB incorporation or stability in the fibrous sheath. Separately, sperm from ROPN1L knockout (RLKO) mice show reduced PKA phosphorylation of a 270-kDa protein identified as FSCB, linking ROPN1L to FSCB phosphorylation signaling.","method":"Genetic knockout mouse models (RKO, RLKO, DKO), Western blotting for FSCB protein levels and PKA phosphorylation substrates","journal":"Biology of reproduction","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean knockout mouse models with specific molecular readouts (protein levels, phosphorylation), single lab","pmids":["23303679"],"is_preprint":false},{"year":2016,"finding":"Phosphorylated FSCB suppresses SUMOylation of ROPN1 and ROPN1L during mouse spermatozoa capacitation. Immunoprecipitation showed that phosphorylated FSCB has significantly higher binding affinity to ROPN1/ROPN1L than non-phosphorylated FSCB. Suppression of ROPN1/ROPN1L SUMOylation mimicked the pro-motility effects of FSCB phosphorylation.","method":"Immunoprecipitation assay comparing phosphorylated vs. non-phosphorylated FSCB binding to ROPN1/ROPN1L; SUMOylation assays; sperm motility analysis","journal":"American journal of translational research","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — immunoprecipitation with functional rescue experiment (mimicking FSCB phosphorylation by suppressing SUMOylation), single lab, no in vitro reconstitution","pmids":["27398160"],"is_preprint":false}],"current_model":"FSCB is a testis/sperm-specific, PKA-phosphorylated calcium-binding protein that localizes to the cortical layer of the fibrous sheath principal piece; it binds CABYR and, upon PKA-mediated phosphorylation during capacitation, increases its affinity for ROPN1/ROPN1L and suppresses their SUMOylation, thereby promoting sperm motility—a pathway that also requires ROPN1 for proper FSCB incorporation into the fibrous sheath."},"narrative":{"mechanistic_narrative":"FSCB (fibrous sheath CABYR binding protein) is a testis- and sperm-specific calcium-binding protein that operates in a PKA-driven signaling module controlling sperm flagellar motility during capacitation [PMID:17855365]. It is first expressed at step 11 of spermatogenesis in elongating spermatids and localizes ultrastructurally to a cortical layer at the surface of the ribs and longitudinal columns of the fibrous sheath principal piece, where it binds the calcium-binding protein CABYR [PMID:17855365]. During capacitation, FSCB is rapidly phosphorylated on both tyrosine and Ser/Thr residues in a strictly PKA-dependent manner, with the extent of phosphorylation tracking PKA activity and sperm motility [PMID:17855365, PMID:21871179]. Phosphorylated FSCB binds ROPN1 and ROPN1L with markedly increased affinity and suppresses their SUMOylation, an effect that recapitulates the pro-motility consequence of FSCB phosphorylation; reciprocally, ROPN1 is required for normal FSCB incorporation/stability in the fibrous sheath and ROPN1L is required for FSCB phosphorylation [PMID:23303679, PMID:27398160]. Beyond this PKA–FSCB–ROPN1/ROPN1L motility axis, no further mechanistic detail has been characterized in the available corpus.","teleology":[{"year":2007,"claim":"Established FSCB as a distinct sperm structural-signaling protein by defining its identity, binding partner, post-translational regulation, and precise location in the flagellum.","evidence":"Co-IP/binding assay for CABYR interaction, in vitro PKA phosphorylation with native phosphosite mapping, calcium overlay, and immunofluorescence/EM localization in mouse sperm","pmids":["17855365"],"confidence":"High","gaps":["Functional consequence of CABYR binding not tested","Role of calcium binding not defined","No loss-of-function phenotype established"]},{"year":2011,"claim":"Connected FSCB phosphorylation to the capacitation program, showing it is an early PKA-dependent event whose magnitude correlates with motility.","evidence":"Reciprocal phospho-specific immunoprecipitation, pharmacological PKA manipulation (db-cAMP, H-89), and time-course during in vitro capacitation in mouse sperm","pmids":["21871179"],"confidence":"Medium","gaps":["Correlation with motility not shown to be causal","Kinase acting on tyrosine residues not identified","No in vitro reconstitution"]},{"year":2013,"claim":"Placed FSCB within a reciprocal dependency with ROPN1/ROPN1L, showing ROPN1 controls FSCB incorporation/stability and ROPN1L controls FSCB phosphorylation.","evidence":"ROPN1, ROPN1L, and double knockout mouse models with Western blotting for FSCB protein levels and PKA phosphorylation substrates","pmids":["23303679"],"confidence":"Medium","gaps":["Mechanism of ROPN1-dependent FSCB incorporation not resolved","Direct vs indirect effect on phosphorylation not distinguished","Single lab"]},{"year":2016,"claim":"Defined the downstream output of FSCB phosphorylation: phospho-dependent high-affinity binding to ROPN1/ROPN1L that suppresses their SUMOylation and drives motility.","evidence":"Immunoprecipitation comparing phospho vs non-phospho FSCB binding, SUMOylation assays, and motility analysis showing SUMOylation suppression mimics FSCB phosphorylation","pmids":["27398160"],"confidence":"Medium","gaps":["SUMO ligase/site on ROPN1/ROPN1L not mapped","No in vitro reconstitution of the binding-SUMOylation link","Single lab"]},{"year":null,"claim":"How FSCB integrates its calcium binding and CABYR interaction with the PKA-ROPN1/ROPN1L SUMOylation axis, and whether FSCB loss itself impairs fertility, remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No FSCB knockout phenotype reported","Functional role of calcium binding unknown","Structural basis of phospho-dependent ROPN1 binding undetermined"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[3]}],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-1474165","term_label":"Reproduction","supporting_discovery_ids":[0,2]}],"complexes":["fibrous sheath"],"partners":["CABYR","ROPN1","ROPN1L"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q5H9T9","full_name":"Fibrous sheath CABYR-binding protein","aliases":[],"length_aa":825,"mass_kda":88.0,"function":"May be involved in the later stages of fibrous sheath biogenesis and spermatozoa capacitation. Inhibits ROPN1 and ROPN1L SUMOylation. Binds calcium","subcellular_location":"Cell projection, cilium, flagellum","url":"https://www.uniprot.org/uniprotkb/Q5H9T9/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/FSCB","classification":"Not Classified","n_dependent_lines":4,"n_total_lines":1208,"dependency_fraction":0.0033112582781456954},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/FSCB","total_profiled":1310},"omim":[{"mim_id":"611779","title":"FIBROUS SHEATH CABYR-BINDING PROTEIN; FSCB","url":"https://www.omim.org/entry/611779"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Flagellar centriole","reliability":"Approved"},{"location":"Mid piece","reliability":"Additional"},{"location":"Principal piece","reliability":"Additional"},{"location":"End piece","reliability":"Additional"}],"tissue_specificity":"Tissue enriched","tissue_distribution":"Detected in single","driving_tissues":[{"tissue":"testis","ntpm":28.7}],"url":"https://www.proteinatlas.org/search/FSCB"},"hgnc":{"alias_symbol":["DKFZP434F1017"],"prev_symbol":["C14orf155"]},"alphafold":{"accession":"Q5H9T9","domains":[],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5H9T9","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q5H9T9-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q5H9T9-F1-predicted_aligned_error_v6.png","plddt_mean":46.25},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=FSCB","jax_strain_url":"https://www.jax.org/strain/search?query=FSCB"},"sequence":{"accession":"Q5H9T9","fasta_url":"https://rest.uniprot.org/uniprotkb/Q5H9T9.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q5H9T9/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5H9T9"}},"corpus_meta":[{"pmid":"23303679","id":"PMC_23303679","title":"Loss of R2D2 proteins ROPN1 and ROPN1L causes defects in murine sperm motility, phosphorylation, and fibrous sheath integrity.","date":"2013","source":"Biology of reproduction","url":"https://pubmed.ncbi.nlm.nih.gov/23303679","citation_count":83,"is_preprint":false},{"pmid":"22006429","id":"PMC_22006429","title":"High-throughput genotyping in osteosarcoma identifies multiple mutations in phosphoinositide-3-kinase and other oncogenes.","date":"2011","source":"Cancer","url":"https://pubmed.ncbi.nlm.nih.gov/22006429","citation_count":58,"is_preprint":false},{"pmid":"17855365","id":"PMC_17855365","title":"FSCB, a novel protein kinase A-phosphorylated calcium-binding protein, is a CABYR-binding partner involved in late steps of fibrous sheath biogenesis.","date":"2007","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/17855365","citation_count":38,"is_preprint":false},{"pmid":"25575546","id":"PMC_25575546","title":"Production of the antibiotic FR-008/candicidin in Streptomyces sp. FR-008 is co-regulated by two regulators, FscRI and FscRIV, from different transcription factor families.","date":"2015","source":"Microbiology (Reading, England)","url":"https://pubmed.ncbi.nlm.nih.gov/25575546","citation_count":26,"is_preprint":false},{"pmid":"27398160","id":"PMC_27398160","title":"FSCB phosphorylation regulates mouse spermatozoa capacitation through suppressing SUMOylation of ROPN1/ROPN1L.","date":"2016","source":"American journal of translational research","url":"https://pubmed.ncbi.nlm.nih.gov/27398160","citation_count":16,"is_preprint":false},{"pmid":"21871179","id":"PMC_21871179","title":"FSCB phosphorylation in mouse spermatozoa capacitation.","date":"2011","source":"BMB reports","url":"https://pubmed.ncbi.nlm.nih.gov/21871179","citation_count":11,"is_preprint":false},{"pmid":"27440996","id":"PMC_27440996","title":"Variation in PTCHD2, CRISP3, NAP1L4, FSCB, and AP3B2 associated with spherical equivalent.","date":"2016","source":"Molecular vision","url":"https://pubmed.ncbi.nlm.nih.gov/27440996","citation_count":9,"is_preprint":false},{"pmid":"36054039","id":"PMC_36054039","title":"Tomato spotted wilt orthotospovirus shifts sex ratio toward males in the western flower thrips, Frankliniella occidentalis, by down-regulating a FSCB-like gene.","date":"2022","source":"Pest management science","url":"https://pubmed.ncbi.nlm.nih.gov/36054039","citation_count":5,"is_preprint":false},{"pmid":"39651266","id":"PMC_39651266","title":"An updated reference genome sequence and annotation reveals gene losses and gains underlying naked mole-rat biology.","date":"2024","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/39651266","citation_count":4,"is_preprint":false},{"pmid":"39336733","id":"PMC_39336733","title":"Genomic Regions Associated with Growth and Reproduction Traits in Pink-Eyed White Mink.","date":"2024","source":"Genes","url":"https://pubmed.ncbi.nlm.nih.gov/39336733","citation_count":1,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.07.09.663517","title":"Surprising effects of stimulus repetition on neuronal firing rates and gamma-band synchronization in awake macaque V1","date":"2025-07-11","source":"bioRxiv","url":"https://doi.org/10.1101/2025.07.09.663517","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":8451,"output_tokens":1361,"usd":0.022884,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7991,"output_tokens":1858,"usd":0.043202,"stage2_stop_reason":"end_turn"},"total_usd":0.066086,"stage1_batch_id":"msgbatch_01AsR7g8dGTEiEw9U83bJeWn","stage2_batch_id":"msgbatch_01YV5ZyxtFNUZEjxRcpd9jzb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2007,\n      \"finding\": \"FSCB (fibrous sheath CABYR binding protein) is a testis- and sperm-specific protein that binds CABYR (a calcium-binding protein tyrosine-phosphorylated during capacitation), as demonstrated by co-immunoprecipitation/binding assays. FSCB is phosphorylated by protein kinase A (PKA) in vitro and at native phosphorylation sites in mouse sperm. FSCB itself is a calcium-binding protein as shown by calcium overlay assay. It localizes ultrastructurally to a cortical layer at the surface of the ribs and longitudinal columns of the fibrous sheath principal piece in mouse sperm flagella, and is first expressed at step 11 of spermatogenesis in elongating spermatids.\",\n      \"method\": \"Co-immunoprecipitation/binding assay (CABYR interaction), in vitro PKA phosphorylation assay with native phosphorylation site mapping, calcium overlay assay, immunofluorescence and electron microscopy localization\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — multiple orthogonal methods in a single focused study: in vitro kinase assay, native phosphosite mapping, calcium overlay, ultrastructural localization, and binding partner identification\",\n      \"pmids\": [\"17855365\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"FSCB undergoes both tyrosine and Ser/Thr phosphorylation during mouse spermatozoa capacitation, detectable as early as 1 min after capacitation onset and increasing over 60 min. Phosphorylation is induced by the PKA agonist db-cAMP and blocked by the PKA antagonist H-89, confirming PKA-dependence. The extent of FSCB phosphorylation correlates with PKA activity and sperm motility characteristics.\",\n      \"method\": \"Immunoprecipitation with anti-phosphotyrosine and anti-phosphoSer/Thr antibodies, pharmacological manipulation (db-cAMP, H-89), time-course analysis during in vitro capacitation\",\n      \"journal\": \"BMB reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — reciprocal immunoprecipitation with pharmacological validation in a single lab; multiple orthogonal approaches but no in vitro reconstitution\",\n      \"pmids\": [\"21871179\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"FSCB protein levels are reduced in sperm from ROPN1 knockout (RKO) mice, indicating that ROPN1 is required for normal FSCB incorporation or stability in the fibrous sheath. Separately, sperm from ROPN1L knockout (RLKO) mice show reduced PKA phosphorylation of a 270-kDa protein identified as FSCB, linking ROPN1L to FSCB phosphorylation signaling.\",\n      \"method\": \"Genetic knockout mouse models (RKO, RLKO, DKO), Western blotting for FSCB protein levels and PKA phosphorylation substrates\",\n      \"journal\": \"Biology of reproduction\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean knockout mouse models with specific molecular readouts (protein levels, phosphorylation), single lab\",\n      \"pmids\": [\"23303679\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Phosphorylated FSCB suppresses SUMOylation of ROPN1 and ROPN1L during mouse spermatozoa capacitation. Immunoprecipitation showed that phosphorylated FSCB has significantly higher binding affinity to ROPN1/ROPN1L than non-phosphorylated FSCB. Suppression of ROPN1/ROPN1L SUMOylation mimicked the pro-motility effects of FSCB phosphorylation.\",\n      \"method\": \"Immunoprecipitation assay comparing phosphorylated vs. non-phosphorylated FSCB binding to ROPN1/ROPN1L; SUMOylation assays; sperm motility analysis\",\n      \"journal\": \"American journal of translational research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — immunoprecipitation with functional rescue experiment (mimicking FSCB phosphorylation by suppressing SUMOylation), single lab, no in vitro reconstitution\",\n      \"pmids\": [\"27398160\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"FSCB is a testis/sperm-specific, PKA-phosphorylated calcium-binding protein that localizes to the cortical layer of the fibrous sheath principal piece; it binds CABYR and, upon PKA-mediated phosphorylation during capacitation, increases its affinity for ROPN1/ROPN1L and suppresses their SUMOylation, thereby promoting sperm motility—a pathway that also requires ROPN1 for proper FSCB incorporation into the fibrous sheath.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"FSCB (fibrous sheath CABYR binding protein) is a testis- and sperm-specific calcium-binding protein that operates in a PKA-driven signaling module controlling sperm flagellar motility during capacitation [#0]. It is first expressed at step 11 of spermatogenesis in elongating spermatids and localizes ultrastructurally to a cortical layer at the surface of the ribs and longitudinal columns of the fibrous sheath principal piece, where it binds the calcium-binding protein CABYR [#0]. During capacitation, FSCB is rapidly phosphorylated on both tyrosine and Ser/Thr residues in a strictly PKA-dependent manner, with the extent of phosphorylation tracking PKA activity and sperm motility [#0, #1]. Phosphorylated FSCB binds ROPN1 and ROPN1L with markedly increased affinity and suppresses their SUMOylation, an effect that recapitulates the pro-motility consequence of FSCB phosphorylation; reciprocally, ROPN1 is required for normal FSCB incorporation/stability in the fibrous sheath and ROPN1L is required for FSCB phosphorylation [#2, #3]. Beyond this PKA–FSCB–ROPN1/ROPN1L motility axis, no further mechanistic detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2007,\n      \"claim\": \"Established FSCB as a distinct sperm structural-signaling protein by defining its identity, binding partner, post-translational regulation, and precise location in the flagellum.\",\n      \"evidence\": \"Co-IP/binding assay for CABYR interaction, in vitro PKA phosphorylation with native phosphosite mapping, calcium overlay, and immunofluorescence/EM localization in mouse sperm\",\n      \"pmids\": [\"17855365\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Functional consequence of CABYR binding not tested\", \"Role of calcium binding not defined\", \"No loss-of-function phenotype established\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Connected FSCB phosphorylation to the capacitation program, showing it is an early PKA-dependent event whose magnitude correlates with motility.\",\n      \"evidence\": \"Reciprocal phospho-specific immunoprecipitation, pharmacological PKA manipulation (db-cAMP, H-89), and time-course during in vitro capacitation in mouse sperm\",\n      \"pmids\": [\"21871179\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Correlation with motility not shown to be causal\", \"Kinase acting on tyrosine residues not identified\", \"No in vitro reconstitution\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Placed FSCB within a reciprocal dependency with ROPN1/ROPN1L, showing ROPN1 controls FSCB incorporation/stability and ROPN1L controls FSCB phosphorylation.\",\n      \"evidence\": \"ROPN1, ROPN1L, and double knockout mouse models with Western blotting for FSCB protein levels and PKA phosphorylation substrates\",\n      \"pmids\": [\"23303679\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism of ROPN1-dependent FSCB incorporation not resolved\", \"Direct vs indirect effect on phosphorylation not distinguished\", \"Single lab\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Defined the downstream output of FSCB phosphorylation: phospho-dependent high-affinity binding to ROPN1/ROPN1L that suppresses their SUMOylation and drives motility.\",\n      \"evidence\": \"Immunoprecipitation comparing phospho vs non-phospho FSCB binding, SUMOylation assays, and motility analysis showing SUMOylation suppression mimics FSCB phosphorylation\",\n      \"pmids\": [\"27398160\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"SUMO ligase/site on ROPN1/ROPN1L not mapped\", \"No in vitro reconstitution of the binding-SUMOylation link\", \"Single lab\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How FSCB integrates its calcium binding and CABYR interaction with the PKA-ROPN1/ROPN1L SUMOylation axis, and whether FSCB loss itself impairs fertility, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No FSCB knockout phenotype reported\", \"Functional role of calcium binding unknown\", \"Structural basis of phospho-dependent ROPN1 binding undetermined\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1474165\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"complexes\": [\"fibrous sheath\"],\n    \"partners\": [\"CABYR\", \"ROPN1\", \"ROPN1L\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":4,"faith_total":4,"faith_pct":100.0}}