{"gene":"CCIN","run_date":"2026-04-28T17:28:52","timeline":{"discoveries":[{"year":2022,"finding":"Calicin (CCIN) interacts with itself (self-association) and many other perinuclear theca (PT) components, suggesting it serves as an organizing center of PT assembly. It also interacts with inner acrosomal membrane (IAM) protein SPACA1 and nuclear envelope (NE) components to form an 'IAM-PT-NE' structure. Loss of Calicin (Ccin-knockout) causes surface subsidence of sperm heads during nuclear condensation, DNA damage, and failure of fertilization.","method":"Co-immunoprecipitation, immunofluorescence, live imaging/fractionation, knockout mouse model with defined phenotypic readout","journal":"Cell reports","confidence":"High","confidence_rationale":"Tier 2 — reciprocal Co-IP, KO mouse with multiple defined phenotypes (head shaping, DNA damage, fertilization failure), multiple orthogonal methods in single study","pmids":["35793634"],"is_preprint":false},{"year":2022,"finding":"Homozygous missense and compound heterozygous mutations in CCIN cause teratozoospermia with severe sperm head malformation and markedly reduced Calicin protein levels. Mutant spermatozoa (human and mouse models) fail to adhere to the zona pellucida, identified as the major mechanistic reason for CCIN-mutant sperm-derived infertility. ICSI bypasses this defect and restores fertility.","method":"Patient exome sequencing, Sanger sequencing, immunofluorescence, ultrastructural analysis, mouse knock-in models expressing disease-associated variants, zona adhesion assay, ICSI rescue","journal":"Science bulletin","confidence":"High","confidence_rationale":"Tier 2 — human mutations validated in mouse models with multiple orthogonal methods and functional rescue by ICSI","pmids":["36546111"],"is_preprint":false},{"year":2025,"finding":"FNDC8 (a testis-enriched PT protein) physically interacts with CCIN and ACTL7A during spermiogenesis; depletion of FNDC8 destabilizes both CCIN and ACTL7A proteins, leading to acrosome detachment and sperm head surface collapse, placing CCIN within a PT protein-interaction network essential for sperm head morphogenesis.","method":"Co-immunoprecipitation, knockout mouse model, immunofluorescence, Western blot","journal":"Zoological research","confidence":"Medium","confidence_rationale":"Tier 2 — Co-IP and KO phenotype from single study; CCIN interaction confirmed but CCIN itself not directly manipulated","pmids":["41169243"],"is_preprint":false},{"year":2021,"finding":"CCIN (Calicin) is among bull sperm actin cytoskeleton proteins that undergo oxidative post-translational modifications (oxPTMs) mediated by 2-Cys peroxiredoxins (PRDXs) under basal conditions, as revealed by inhibition of 2-Cys PRDXs with Conoidin A.","method":"Proteomic/mass spectrometry analysis of oxPTMs after pharmacological inhibition of 2-Cys PRDXs in sperm","journal":"International journal of molecular sciences","confidence":"Low","confidence_rationale":"Tier 3 — single proteomics study without functional follow-up on CCIN specifically","pmids":["34884692"],"is_preprint":false},{"year":2022,"finding":"FSIP2 mutations in asthenoteratozoospermic patients are associated with downregulated expression of CCIN in spermatozoa, placing CCIN downstream of FSIP2 in acrosome biogenesis and sperm morphogenesis.","method":"Whole exome sequencing of patients, immunofluorescence, proteomics (LC-MS/MS), co-immunoprecipitation for FSIP2 interactors","journal":"Journal of medical genetics","confidence":"Low","confidence_rationale":"Tier 3 — CCIN downregulation is an indirect finding in an FSIP2 study; no direct manipulation of CCIN","pmids":["35654582"],"is_preprint":false},{"year":2023,"finding":"A novel homozygous missense variant in CCIN causes male infertility with an abnormal sperm head nuclear subsidence phenotype, consistent with Calicin's role in maintaining sperm nuclear structure.","method":"Sanger sequencing of patient, sperm morphological analysis","journal":"Clinical genetics","confidence":"Low","confidence_rationale":"Tier 3 — single patient case report with limited mechanistic follow-up","pmids":["36527329"],"is_preprint":false}],"current_model":"CCIN encodes Calicin, a perinuclear theca (PT) cytoskeletal protein that self-associates and interacts with IAM protein SPACA1, nuclear envelope components, ACTL7A, and FNDC8 to form a structural scaffold (IAM-PT-NE) that shapes the sperm head during nuclear condensation, maintains nuclear integrity, and is required for sperm-zona pellucida adhesion; loss-of-function mutations cause teratozoospermia with sperm head deformation, DNA damage, and fertilization failure."},"narrative":{"teleology":[{"year":2021,"claim":"Identifying that Calicin undergoes oxidative post-translational modifications mediated by 2-Cys peroxiredoxins placed CCIN within the redox-regulated sperm cytoskeletal proteome, though its functional significance remained unclear.","evidence":"Mass spectrometry-based oxPTM profiling of bull sperm after pharmacological PRDX inhibition","pmids":["34884692"],"confidence":"Low","gaps":["Single proteomics study without functional follow-up on CCIN specifically","Role of oxidative modifications on Calicin function not tested","Not confirmed in human sperm"]},{"year":2022,"claim":"Direct demonstration that Calicin self-associates and bridges the inner acrosomal membrane (via SPACA1) to the nuclear envelope established CCIN as a central organizer of the perinuclear theca scaffold, and Ccin-knockout mice revealed its necessity for sperm head shaping, DNA integrity, and fertilization.","evidence":"Reciprocal Co-IP, immunofluorescence, live imaging, and Ccin-knockout mouse phenotyping","pmids":["35793634"],"confidence":"High","gaps":["Structural basis of Calicin self-association unknown","Mechanism linking PT disruption to DNA damage not resolved","Whether Calicin directly contacts the zona pellucida or acts indirectly is unclear"]},{"year":2022,"claim":"Human genetic evidence confirmed that CCIN mutations cause teratozoospermia and male infertility, and zona adhesion assays pinpointed failure of sperm-zona binding as the proximate cause, with ICSI providing functional rescue.","evidence":"Patient exome sequencing, mouse knock-in models of disease variants, zona adhesion assays, ICSI rescue experiments","pmids":["36546111"],"confidence":"High","gaps":["Identity of the zona receptor engaged by Calicin-dependent surface structures unknown","Whether PT structural defects alter other surface proteins mediating zona binding not determined"]},{"year":2023,"claim":"An additional patient harboring a homozygous CCIN missense variant with sperm head nuclear subsidence reinforced the genotype–phenotype relationship but did not add new mechanistic insight.","evidence":"Sanger sequencing and sperm morphological analysis in a single patient","pmids":["36527329"],"confidence":"Low","gaps":["Single case report without functional validation of variant pathogenicity","No protein-level or rescue data provided"]},{"year":2025,"claim":"Placing CCIN in a ternary interaction network with FNDC8 and ACTL7A showed that upstream PT factors stabilize Calicin protein levels, and their loss phenocopies CCIN deficiency with acrosome detachment and head collapse.","evidence":"Co-immunoprecipitation and Fndc8-knockout mouse model with immunofluorescence and Western blot","pmids":["41169243"],"confidence":"Medium","gaps":["Whether FNDC8 directly stabilizes CCIN or acts via ACTL7A is unresolved","Stoichiometry and assembly order of the FNDC8-CCIN-ACTL7A complex unknown"]},{"year":null,"claim":"The structural basis of Calicin self-association, the mechanism by which PT disruption causes DNA damage, and the identity of zona pellucida receptors dependent on Calicin-organized surface architecture remain unresolved.","evidence":"","pmids":[],"confidence":"High","gaps":["No structural model of Calicin or its oligomeric assembly exists","Causal link between PT scaffold loss and DNA damage is correlative","Downstream zona-binding partners not identified"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0,1,2]},{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[0,2]}],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[0,2]},{"term_id":"GO:0005635","term_label":"nuclear envelope","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-1474165","term_label":"Reproduction","supporting_discovery_ids":[0,1,2]}],"complexes":[],"partners":["SPACA1","ACTL7A","FNDC8"],"other_free_text":[]},"mechanistic_narrative":"CCIN encodes Calicin, a structural cytoskeletal protein of the sperm perinuclear theca (PT) that self-associates and interacts with inner acrosomal membrane protein SPACA1, nuclear envelope components, ACTL7A, and FNDC8 to form an IAM-PT-NE scaffold essential for sperm head morphogenesis during spermiogenesis [PMID:35793634, PMID:41169243]. Calicin is required for proper nuclear condensation and head shaping; loss of CCIN in knockout mice causes surface subsidence of sperm heads, DNA damage, and fertilization failure due to inability to adhere to the zona pellucida [PMID:35793634, PMID:36546111]. Homozygous and compound heterozygous loss-of-function mutations in CCIN cause human teratozoospermia with severe sperm head malformation and male infertility, which can be bypassed by ICSI [PMID:36546111, PMID:36527329]."},"prefetch_data":{"uniprot":{"accession":"Q13939","full_name":"Calicin","aliases":[],"length_aa":588,"mass_kda":66.6,"function":"Required for both nuclear and acrosomal shaping during spermiogenesis","subcellular_location":"Cytoplasm, cytoskeleton, perinuclear theca, calyx","url":"https://www.uniprot.org/uniprotkb/Q13939/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CCIN","classification":"Not Classified","n_dependent_lines":20,"n_total_lines":1208,"dependency_fraction":0.016556291390728478},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/CCIN","total_profiled":1310},"omim":[{"mim_id":"620838","title":"SPERMATOGENIC FAILURE 91; SPGF91","url":"https://www.omim.org/entry/620838"},{"mim_id":"604035","title":"CYLICIN 2; CYLC2","url":"https://www.omim.org/entry/604035"},{"mim_id":"603960","title":"CALICIN; CCIN","url":"https://www.omim.org/entry/603960"},{"mim_id":"301119","title":"SPERMATOGENIC FAILURE, X-LINKED, 8; SPGFX8","url":"https://www.omim.org/entry/301119"},{"mim_id":"300768","title":"CYLICIN 1; CYLC1","url":"https://www.omim.org/entry/300768"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Calyx","reliability":"Supported"},{"location":"Nucleoplasm","reliability":"Additional"},{"location":"Perinuclear theca","reliability":"Additional"}],"tissue_specificity":"Tissue enriched","tissue_distribution":"Detected in some","driving_tissues":[{"tissue":"testis","ntpm":70.2}],"url":"https://www.proteinatlas.org/search/CCIN"},"hgnc":{"alias_symbol":["KBTBD14","BTBD20"],"prev_symbol":[]},"alphafold":{"accession":"Q13939","domains":[{"cath_id":"3.30.710.10","chopping":"9-127","consensus_level":"high","plddt":92.9732,"start":9,"end":127},{"cath_id":"1.25.40.420","chopping":"145-270","consensus_level":"medium","plddt":92.0334,"start":145,"end":270},{"cath_id":"2.120.10.80","chopping":"302-584","consensus_level":"high","plddt":90.5402,"start":302,"end":584}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q13939","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q13939-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q13939-F1-predicted_aligned_error_v6.png","plddt_mean":90.44},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CCIN","jax_strain_url":"https://www.jax.org/strain/search?query=CCIN"},"sequence":{"accession":"Q13939","fasta_url":"https://rest.uniprot.org/uniprotkb/Q13939.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q13939/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q13939"}},"corpus_meta":[{"pmid":"9400769","id":"PMC_9400769","title":"Mitomycin 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player.","date":"2020","source":"Human genetics","url":"https://pubmed.ncbi.nlm.nih.gov/33108537","citation_count":30,"is_preprint":false},{"pmid":"35793634","id":"PMC_35793634","title":"The perinuclear theca protein Calicin helps shape the sperm head and maintain the nuclear structure in mice.","date":"2022","source":"Cell reports","url":"https://pubmed.ncbi.nlm.nih.gov/35793634","citation_count":28,"is_preprint":false},{"pmid":"14701965","id":"PMC_14701965","title":"A case of conjunctiva-cornea intraepithelial neoplasia successfully treated with topical mitomycin C and interferon alfa-2b in cycles.","date":"2004","source":"Cornea","url":"https://pubmed.ncbi.nlm.nih.gov/14701965","citation_count":26,"is_preprint":false},{"pmid":"36546111","id":"PMC_36546111","title":"Mutations in CCIN cause teratozoospermia and male infertility.","date":"2022","source":"Science 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research","url":"https://pubmed.ncbi.nlm.nih.gov/41169243","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":13798,"output_tokens":1472,"usd":0.031737},"stage2":{"model":"claude-opus-4-6","input_tokens":4706,"output_tokens":1497,"usd":0.091432},"total_usd":0.123169,"stage1_batch_id":"msgbatch_011kfMfE81o6CTcyhVUqumuW","stage2_batch_id":"msgbatch_01DTputS6WNkH745x1nVSoBo","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2022,\n      \"finding\": \"Calicin (CCIN) interacts with itself (self-association) and many other perinuclear theca (PT) components, suggesting it serves as an organizing center of PT assembly. It also interacts with inner acrosomal membrane (IAM) protein SPACA1 and nuclear envelope (NE) components to form an 'IAM-PT-NE' structure. Loss of Calicin (Ccin-knockout) causes surface subsidence of sperm heads during nuclear condensation, DNA damage, and failure of fertilization.\",\n      \"method\": \"Co-immunoprecipitation, immunofluorescence, live imaging/fractionation, knockout mouse model with defined phenotypic readout\",\n      \"journal\": \"Cell reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal Co-IP, KO mouse with multiple defined phenotypes (head shaping, DNA damage, fertilization failure), multiple orthogonal methods in single study\",\n      \"pmids\": [\"35793634\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Homozygous missense and compound heterozygous mutations in CCIN cause teratozoospermia with severe sperm head malformation and markedly reduced Calicin protein levels. Mutant spermatozoa (human and mouse models) fail to adhere to the zona pellucida, identified as the major mechanistic reason for CCIN-mutant sperm-derived infertility. ICSI bypasses this defect and restores fertility.\",\n      \"method\": \"Patient exome sequencing, Sanger sequencing, immunofluorescence, ultrastructural analysis, mouse knock-in models expressing disease-associated variants, zona adhesion assay, ICSI rescue\",\n      \"journal\": \"Science bulletin\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — human mutations validated in mouse models with multiple orthogonal methods and functional rescue by ICSI\",\n      \"pmids\": [\"36546111\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"FNDC8 (a testis-enriched PT protein) physically interacts with CCIN and ACTL7A during spermiogenesis; depletion of FNDC8 destabilizes both CCIN and ACTL7A proteins, leading to acrosome detachment and sperm head surface collapse, placing CCIN within a PT protein-interaction network essential for sperm head morphogenesis.\",\n      \"method\": \"Co-immunoprecipitation, knockout mouse model, immunofluorescence, Western blot\",\n      \"journal\": \"Zoological research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — Co-IP and KO phenotype from single study; CCIN interaction confirmed but CCIN itself not directly manipulated\",\n      \"pmids\": [\"41169243\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"CCIN (Calicin) is among bull sperm actin cytoskeleton proteins that undergo oxidative post-translational modifications (oxPTMs) mediated by 2-Cys peroxiredoxins (PRDXs) under basal conditions, as revealed by inhibition of 2-Cys PRDXs with Conoidin A.\",\n      \"method\": \"Proteomic/mass spectrometry analysis of oxPTMs after pharmacological inhibition of 2-Cys PRDXs in sperm\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 — single proteomics study without functional follow-up on CCIN specifically\",\n      \"pmids\": [\"34884692\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"FSIP2 mutations in asthenoteratozoospermic patients are associated with downregulated expression of CCIN in spermatozoa, placing CCIN downstream of FSIP2 in acrosome biogenesis and sperm morphogenesis.\",\n      \"method\": \"Whole exome sequencing of patients, immunofluorescence, proteomics (LC-MS/MS), co-immunoprecipitation for FSIP2 interactors\",\n      \"journal\": \"Journal of medical genetics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 — CCIN downregulation is an indirect finding in an FSIP2 study; no direct manipulation of CCIN\",\n      \"pmids\": [\"35654582\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"A novel homozygous missense variant in CCIN causes male infertility with an abnormal sperm head nuclear subsidence phenotype, consistent with Calicin's role in maintaining sperm nuclear structure.\",\n      \"method\": \"Sanger sequencing of patient, sperm morphological analysis\",\n      \"journal\": \"Clinical genetics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 — single patient case report with limited mechanistic follow-up\",\n      \"pmids\": [\"36527329\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CCIN encodes Calicin, a perinuclear theca (PT) cytoskeletal protein that self-associates and interacts with IAM protein SPACA1, nuclear envelope components, ACTL7A, and FNDC8 to form a structural scaffold (IAM-PT-NE) that shapes the sperm head during nuclear condensation, maintains nuclear integrity, and is required for sperm-zona pellucida adhesion; loss-of-function mutations cause teratozoospermia with sperm head deformation, DNA damage, and fertilization failure.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"CCIN encodes Calicin, a structural cytoskeletal protein of the sperm perinuclear theca (PT) that self-associates and interacts with inner acrosomal membrane protein SPACA1, nuclear envelope components, ACTL7A, and FNDC8 to form an IAM-PT-NE scaffold essential for sperm head morphogenesis during spermiogenesis [PMID:35793634, PMID:41169243]. Calicin is required for proper nuclear condensation and head shaping; loss of CCIN in knockout mice causes surface subsidence of sperm heads, DNA damage, and fertilization failure due to inability to adhere to the zona pellucida [PMID:35793634, PMID:36546111]. Homozygous and compound heterozygous loss-of-function mutations in CCIN cause human teratozoospermia with severe sperm head malformation and male infertility, which can be bypassed by ICSI [PMID:36546111, PMID:36527329].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Identifying that Calicin undergoes oxidative post-translational modifications mediated by 2-Cys peroxiredoxins placed CCIN within the redox-regulated sperm cytoskeletal proteome, though its functional significance remained unclear.\",\n      \"evidence\": \"Mass spectrometry-based oxPTM profiling of bull sperm after pharmacological PRDX inhibition\",\n      \"pmids\": [\"34884692\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single proteomics study without functional follow-up on CCIN specifically\", \"Role of oxidative modifications on Calicin function not tested\", \"Not confirmed in human sperm\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Direct demonstration that Calicin self-associates and bridges the inner acrosomal membrane (via SPACA1) to the nuclear envelope established CCIN as a central organizer of the perinuclear theca scaffold, and Ccin-knockout mice revealed its necessity for sperm head shaping, DNA integrity, and fertilization.\",\n      \"evidence\": \"Reciprocal Co-IP, immunofluorescence, live imaging, and Ccin-knockout mouse phenotyping\",\n      \"pmids\": [\"35793634\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of Calicin self-association unknown\", \"Mechanism linking PT disruption to DNA damage not resolved\", \"Whether Calicin directly contacts the zona pellucida or acts indirectly is unclear\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Human genetic evidence confirmed that CCIN mutations cause teratozoospermia and male infertility, and zona adhesion assays pinpointed failure of sperm-zona binding as the proximate cause, with ICSI providing functional rescue.\",\n      \"evidence\": \"Patient exome sequencing, mouse knock-in models of disease variants, zona adhesion assays, ICSI rescue experiments\",\n      \"pmids\": [\"36546111\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Identity of the zona receptor engaged by Calicin-dependent surface structures unknown\", \"Whether PT structural defects alter other surface proteins mediating zona binding not determined\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"An additional patient harboring a homozygous CCIN missense variant with sperm head nuclear subsidence reinforced the genotype–phenotype relationship but did not add new mechanistic insight.\",\n      \"evidence\": \"Sanger sequencing and sperm morphological analysis in a single patient\",\n      \"pmids\": [\"36527329\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single case report without functional validation of variant pathogenicity\", \"No protein-level or rescue data provided\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Placing CCIN in a ternary interaction network with FNDC8 and ACTL7A showed that upstream PT factors stabilize Calicin protein levels, and their loss phenocopies CCIN deficiency with acrosome detachment and head collapse.\",\n      \"evidence\": \"Co-immunoprecipitation and Fndc8-knockout mouse model with immunofluorescence and Western blot\",\n      \"pmids\": [\"41169243\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether FNDC8 directly stabilizes CCIN or acts via ACTL7A is unresolved\", \"Stoichiometry and assembly order of the FNDC8-CCIN-ACTL7A complex unknown\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The structural basis of Calicin self-association, the mechanism by which PT disruption causes DNA damage, and the identity of zona pellucida receptors dependent on Calicin-organized surface architecture remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No structural model of Calicin or its oligomeric assembly exists\", \"Causal link between PT scaffold loss and DNA damage is correlative\", \"Downstream zona-binding partners not identified\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0005635\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1474165\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"SPACA1\", \"ACTL7A\", \"FNDC8\"],\n    \"other_free_text\": []\n  }\n}\n```"}