{"gene":"CCDC102B","run_date":"2026-04-28T17:28:52","timeline":{"discoveries":[{"year":2018,"finding":"CCDC102B is a centrosome linker protein required for centrosome cohesion. It localizes to the centrosome via recruitment by C-Nap1 (CEP250), physically interacts with the centrosome linker components rootletin and LRRC45, and decorates and facilitates the formation of rootletin filaments. At the onset of mitosis, CCDC102B is phosphorylated by Nek2A and dissociates from the centrosome, thereby enabling centrosome separation.","method":"Co-immunoprecipitation, immunofluorescence localization, loss-of-function (knockdown) with centrosome cohesion phenotype readout, in vitro phosphorylation assay (Nek2A), rootletin filament formation assay","journal":"Journal of cell science","confidence":"High","confidence_rationale":"Tier 2 — multiple orthogonal methods (Co-IP, localization, KD phenotype, kinase assay, filament formation) in a single rigorous study","pmids":["30404835"],"is_preprint":false},{"year":2022,"finding":"CCDC102B promotes breast cancer metastasis by interacting with RACK1 and positively regulating the NF-κB pathway. RACK1 promotes lysosomal degradation of CCDC102B via chaperone-mediated autophagy (CMA); loss of RACK1 stabilizes CCDC102B. Overexpression of CCDC102B reduces interaction between RACK1 and IKKα, thereby activating NF-κB signaling and driving metastatic behavior in vitro and in vivo.","method":"Co-immunoprecipitation, mass spectrometry, RNA sequencing (pathway enrichment), CRISPR/Cas9 loss-of-function in vivo screen, tail vein and xenograft tumor models, nuclear protein extraction, immunofluorescence, cell migration/invasion assays","journal":"Frontiers in oncology","confidence":"Medium","confidence_rationale":"Tier 2 — multiple orthogonal methods (Co-IP, MS, in vivo models, CMA pathway validation) from a single lab","pmids":["35957886"],"is_preprint":false}],"current_model":"CCDC102B functions as a centrosome linker protein that is recruited by C-Nap1, interacts with rootletin and LRRC45 to facilitate centrosome linker filament assembly and cohesion, and is released at mitosis onset via Nek2A-mediated phosphorylation; additionally, CCDC102B promotes breast cancer metastasis by interacting with RACK1 to activate NF-κB signaling, while RACK1 targets CCDC102B for chaperone-mediated autophagic degradation."},"narrative":{"teleology":[{"year":2018,"claim":"Established CCDC102B as a centrosome linker component, resolving how rootletin filaments are assembled and how centrosome cohesion is maintained and then released at mitosis via Nek2A phosphorylation.","evidence":"Co-immunoprecipitation, immunofluorescence, knockdown-induced centrosome splitting, in vitro Nek2A phosphorylation assay, and rootletin filament formation assay in human cells","pmids":["30404835"],"confidence":"High","gaps":["Exact phosphorylation sites on CCDC102B by Nek2A are not mapped at residue resolution","No structural model of the CCDC102B–rootletin or CCDC102B–LRRC45 interfaces","Whether CCDC102B has linker-independent functions was unexplored"]},{"year":2022,"claim":"Revealed a non-centrosomal role for CCDC102B in cancer, showing it activates NF-κB by sequestering RACK1 away from IKKα and is itself degraded by RACK1-directed chaperone-mediated autophagy, linking centrosome biology to metastatic signaling.","evidence":"Co-IP, mass spectrometry, RNA-seq pathway analysis, CRISPR screen, xenograft and tail-vein metastasis models in breast cancer cell lines","pmids":["35957886"],"confidence":"Medium","gaps":["Findings originate from a single laboratory; independent replication is lacking","Whether the RACK1–CCDC102B axis operates in non-breast cancer contexts is unknown","Relationship between centrosome linker function and NF-κB activation has not been dissected"]},{"year":null,"claim":"It remains unknown how the centrosome-linker and NF-κB-signaling functions of CCDC102B are coordinated, whether CCDC102B possesses intrinsic enzymatic activity, and what post-translational modifications beyond Nek2A phosphorylation regulate its stability and localization.","evidence":"","pmids":[],"confidence":"Low","gaps":["No enzymatic activity has been attributed to CCDC102B","No high-resolution structure exists","In vivo animal models of CCDC102B loss for centrosome cohesion phenotypes are absent"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[0]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[1]}],"complexes":[],"partners":["CEP250","CROCC","LRRC45","RACK1"],"other_free_text":[]},"mechanistic_narrative":"CCDC102B is a centrosome linker protein that is recruited to the centrosome by C-Nap1 (CEP250), where it physically interacts with rootletin and LRRC45 to facilitate linker filament assembly and maintain centrosome cohesion during interphase; at mitosis onset, Nek2A-mediated phosphorylation causes CCDC102B to dissociate, enabling centrosome separation [PMID:30404835]. CCDC102B also interacts with RACK1 and, when overexpressed, competitively reduces RACK1–IKKα association, thereby activating NF-κB signaling and promoting breast cancer metastasis in xenograft models; RACK1 in turn targets CCDC102B for lysosomal degradation via chaperone-mediated autophagy [PMID:35957886]."},"prefetch_data":{"uniprot":{"accession":"Q68D86","full_name":"Coiled-coil domain-containing protein 102B","aliases":[],"length_aa":513,"mass_kda":60.4,"function":"During interphase, forms fibers at the proximal ends of centrioles to maintain centrosome cohesion (PubMed:30404835). During mitosis, dissociates from the centrosome following phosphorylation to allow centrosome separation (PubMed:30404835). Contributes to CROCC/rootletin filament formation (PubMed:30404835)","subcellular_location":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole","url":"https://www.uniprot.org/uniprotkb/Q68D86/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CCDC102B","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/CCDC102B","total_profiled":1310},"omim":[{"mim_id":"621147","title":"COILED-COIL DOMAIN-CONTAINING PROTEIN 102B; CCDC102B","url":"https://www.omim.org/entry/621147"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"placenta","ntpm":26.6}],"url":"https://www.proteinatlas.org/search/CCDC102B"},"hgnc":{"alias_symbol":["FLJ23594","HsT1731","AN"],"prev_symbol":["C18orf14","ACY1L"]},"alphafold":{"accession":"Q68D86","domains":[],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q68D86","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q68D86-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q68D86-F1-predicted_aligned_error_v6.png","plddt_mean":75.88},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CCDC102B","jax_strain_url":"https://www.jax.org/strain/search?query=CCDC102B"},"sequence":{"accession":"Q68D86","fasta_url":"https://rest.uniprot.org/uniprotkb/Q68D86.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q68D86/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q68D86"}},"corpus_meta":[{"pmid":"27337627","id":"PMC_27337627","title":"Development of a methylation marker set for forensic age estimation using analysis of public methylation data and the Agena Bioscience EpiTYPER system.","date":"2016","source":"Forensic science international. 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mutations.","date":"2025","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/41338459","citation_count":0,"is_preprint":false,"source_track":"gene2pubmed"}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":13136,"output_tokens":895,"usd":0.026416},"stage2":{"model":"claude-opus-4-6","input_tokens":4095,"output_tokens":1217,"usd":0.07635},"total_usd":0.216552,"stage1_batch_id":"msgbatch_011kfMfE81o6CTcyhVUqumuW","stage2_batch_id":"msgbatch_01DTputS6WNkH745x1nVSoBo","note":"batch pricing = 50% of standard","round2_stage1":{"model":"claude-sonnet-4-6","input_tokens":22197,"output_tokens":1178,"usd":0.042131},"round2_rules_fired":"R3","round2_stage2":{"model":"claude-opus-4-6","input_tokens":4179,"output_tokens":1075,"usd":0.071655}},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2018,\n      \"finding\": \"CCDC102B is a centrosome linker protein required for centrosome cohesion. It is recruited to the centrosome by C-Nap1 (CEP250), interacts with centrosome linker components rootletin and LRRC45, decorates and facilitates formation of rootletin filaments, and is phosphorylated by Nek2A causing its disassociation from the centrosome at the onset of mitosis.\",\n      \"method\": \"Co-immunoprecipitation, immunofluorescence localization, rootletin filament assembly assay, phosphorylation assay, loss-of-function centrosome cohesion readout\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (Co-IP, localization, filament assembly, phosphorylation assay) in a single study with specific functional readouts\",\n      \"pmids\": [\"30404835\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"CCDC102B promotes breast cancer metastasis via activation of the NF-κB pathway. RACK1 targets CCDC102B for lysosomal degradation through chaperone-mediated autophagy (CMA). Overexpression of CCDC102B reduces interaction between RACK1 and IKKα, thereby positively regulating NF-κB pathway activity.\",\n      \"method\": \"Co-immunoprecipitation, mass spectrometry, CRISPR/Cas9 in vivo screening, RNA sequencing, nuclear protein extraction, immunofluorescence, tail vein metastasis model, wound healing/migration/invasion assays\",\n      \"journal\": \"Frontiers in oncology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods including Co-IP, MS, in vivo models, and mechanistic pathway validation\",\n      \"pmids\": [\"35957886\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"CCDC102B gene is located at chromosome 18q22.1; a 2.7 Mb deletion at this locus disrupts CCDC102B (deletion breakpoint falls within the gene), placing it in a genomic region associated with diaphragmatic hernia and microphthalmia, though no direct functional role for CCDC102B was established.\",\n      \"method\": \"Affymetrix GeneChip SNP array, fluorescence in situ hybridization (FISH)\",\n      \"journal\": \"American journal of medical genetics. Part A\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 — genomic mapping only, no functional mechanistic data for CCDC102B itself\",\n      \"pmids\": [\"20358601\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CCDC102B is a centrosome linker protein recruited by C-Nap1 that interacts with rootletin and LRRC45 to facilitate rootletin filament formation and centrosome cohesion in interphase, is released from centrosomes at mitosis onset via Nek2A phosphorylation, and in a cancer context is stabilized by loss of RACK1 (which normally promotes its CMA-mediated lysosomal degradation) to activate the NF-κB pathway by competing with RACK1 for IKKα interaction, thereby promoting metastasis.\"\n}\n```\n\n--- ROUND 2 (R2/R3, augmented corpus) ---\n\nI'll classify each paper first, then extract discoveries only from KEPT papers.\n\n**Classification:**\n\n- Papers [1]-[7] (forensic methylation/age estimation), [9] (18q22 deletion/DSEL), [10]-[11] (forensic methylation), [13] (forensic methylation), [14] (myopia GWAS — genetic association only, no mechanism), [15] (CRC biomarker — expression/ML only), [16] (cardiac fibrosis — expression only), [17]-[21] (various: myopia GWAS, interactome screens, cDNA collections, smoking cessation, etc.) from main corpus — mostly EXCLUDE (expression/biomarker/GWAS, no mechanistic findings about CCDC102B protein function)\n\n- Paper [8] **KEEP** — direct mechanistic study of CCDC102B protein function\n\n- Paper [12] **KEEP** — direct mechanistic study of CCDC102B in breast cancer metastasis\n\n- From gene2pubmed list: BioPlex papers [2],[3],[8] are interactome screens that may list CCDC102B interactions; paper [18] is GWAS (EXCLUDE — association only); others are cDNA/interactome resources.\n\n- BioPlex [2] PMID:26186194, [3] PMID:28514442, [8] PMID:33961781 — high-throughput AP-MS screens; CCDC102B interactions listed but not specifically characterized. These are Tier 3 at best and don't add specific mechanistic findings beyond what paper [8] establishes.\n\n**KEEP for extraction:** PMID:30404835 (Xia et al. 2018) and PMID:35957886 (Si et al. 2022)\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2018,\n      \"finding\": \"CCDC102B is a centrosome linker protein required for centrosome cohesion. It localizes to the centrosome via recruitment by C-Nap1 (CEP250), physically interacts with the centrosome linker components rootletin and LRRC45, and decorates and facilitates the formation of rootletin filaments. At the onset of mitosis, CCDC102B is phosphorylated by Nek2A and dissociates from the centrosome, thereby enabling centrosome separation.\",\n      \"method\": \"Co-immunoprecipitation, immunofluorescence localization, loss-of-function (knockdown) with centrosome cohesion phenotype readout, in vitro phosphorylation assay (Nek2A), rootletin filament formation assay\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (Co-IP, localization, KD phenotype, kinase assay, filament formation) in a single rigorous study\",\n      \"pmids\": [\"30404835\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"CCDC102B promotes breast cancer metastasis by interacting with RACK1 and positively regulating the NF-κB pathway. RACK1 promotes lysosomal degradation of CCDC102B via chaperone-mediated autophagy (CMA); loss of RACK1 stabilizes CCDC102B. Overexpression of CCDC102B reduces interaction between RACK1 and IKKα, thereby activating NF-κB signaling and driving metastatic behavior in vitro and in vivo.\",\n      \"method\": \"Co-immunoprecipitation, mass spectrometry, RNA sequencing (pathway enrichment), CRISPR/Cas9 loss-of-function in vivo screen, tail vein and xenograft tumor models, nuclear protein extraction, immunofluorescence, cell migration/invasion assays\",\n      \"journal\": \"Frontiers in oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — multiple orthogonal methods (Co-IP, MS, in vivo models, CMA pathway validation) from a single lab\",\n      \"pmids\": [\"35957886\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CCDC102B functions as a centrosome linker protein that is recruited by C-Nap1, interacts with rootletin and LRRC45 to facilitate centrosome linker filament assembly and cohesion, and is released at mitosis onset via Nek2A-mediated phosphorylation; additionally, CCDC102B promotes breast cancer metastasis by interacting with RACK1 to activate NF-κB signaling, while RACK1 targets CCDC102B for chaperone-mediated autophagic degradation.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"CCDC102B is a centrosome linker protein that is recruited to the centrosome by C-Nap1 (CEP250), where it interacts with rootletin and LRRC45 to decorate and facilitate rootletin filament formation, thereby maintaining centrosome cohesion during interphase; at the onset of mitosis, Nek2A phosphorylates CCDC102B, triggering its dissociation from the centrosome to permit centrosome separation [PMID:30404835]. In breast cancer cells, RACK1 normally targets CCDC102B for lysosomal degradation via chaperone-mediated autophagy, and when CCDC102B is stabilized it competitively displaces RACK1 from IKKα, activating the NF-κB pathway and promoting metastasis [PMID:35957886].\",\n  \"teleology\": [\n    {\n      \"year\": 2018,\n      \"claim\": \"The fundamental question of what CCDC102B does at the centrosome was resolved: it functions as a linker protein recruited by C-Nap1 that facilitates rootletin filament assembly and centrosome cohesion, and is released upon Nek2A phosphorylation at mitosis onset, establishing CCDC102B as a cell-cycle-regulated structural component of the centrosome linker.\",\n      \"evidence\": \"Co-immunoprecipitation, immunofluorescence, rootletin filament assembly assay, phosphorylation assay, and centrosome cohesion loss-of-function readout in cultured cells\",\n      \"pmids\": [\"30404835\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Specific Nek2A phosphorylation sites on CCDC102B have not been mapped\",\n        \"No structural model exists for the CCDC102B–rootletin or CCDC102B–LRRC45 interface\",\n        \"Whether CCDC102B has additional non-centrosomal functions during interphase is unexplored\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"An unexpected oncogenic role was uncovered: CCDC102B promotes breast cancer metastasis by activating NF-κB signaling, and its steady-state abundance is controlled by RACK1-mediated chaperone-mediated autophagy, linking centrosome biology to cancer signaling via a competitive interaction with IKKα.\",\n      \"evidence\": \"Co-IP, mass spectrometry, CRISPR/Cas9 in vivo screening, RNA-seq, tail vein metastasis model, and migration/invasion assays in breast cancer cells\",\n      \"pmids\": [\"35957886\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether the NF-κB–activating function operates independently of centrosome localization is unknown\",\n        \"The CMA-targeting motif on CCDC102B has not been identified\",\n        \"Relevance of the CCDC102B–IKKα axis beyond breast cancer has not been tested\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Key unresolved questions include the structural basis of CCDC102B interactions, the identity of Nek2A phosphosites, and whether the centrosomal and NF-κB signaling functions are mechanistically coupled or represent independent roles in distinct subcellular compartments.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No crystal or cryo-EM structure of CCDC102B or its complexes exists\",\n        \"Relationship between centrosome linker function and metastatic signaling is uncharacterized\",\n        \"In vivo physiological roles beyond cancer models remain unexplored\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-9612973\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"CEP250\", \"CROCC\", \"LRRC45\", \"NEK2\", \"RACK1\", \"CHUK\"],\n    \"other_free_text\": []\n  }\n}\n```\n\n--- ROUND 2 (R2/R3, augmented corpus) ---\n\n```json\n{\n  \"mechanistic_narrative\": \"CCDC102B is a centrosome linker protein that is recruited to the centrosome by C-Nap1 (CEP250), where it physically interacts with rootletin and LRRC45 to facilitate linker filament assembly and maintain centrosome cohesion during interphase; at mitosis onset, Nek2A-mediated phosphorylation causes CCDC102B to dissociate, enabling centrosome separation [PMID:30404835]. CCDC102B also interacts with RACK1 and, when overexpressed, competitively reduces RACK1–IKKα association, thereby activating NF-κB signaling and promoting breast cancer metastasis in xenograft models; RACK1 in turn targets CCDC102B for lysosomal degradation via chaperone-mediated autophagy [PMID:35957886].\",\n  \"teleology\": [\n    {\n      \"year\": 2018,\n      \"claim\": \"Established CCDC102B as a centrosome linker component, resolving how rootletin filaments are assembled and how centrosome cohesion is maintained and then released at mitosis via Nek2A phosphorylation.\",\n      \"evidence\": \"Co-immunoprecipitation, immunofluorescence, knockdown-induced centrosome splitting, in vitro Nek2A phosphorylation assay, and rootletin filament formation assay in human cells\",\n      \"pmids\": [\"30404835\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Exact phosphorylation sites on CCDC102B by Nek2A are not mapped at residue resolution\",\n        \"No structural model of the CCDC102B–rootletin or CCDC102B–LRRC45 interfaces\",\n        \"Whether CCDC102B has linker-independent functions was unexplored\"\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Revealed a non-centrosomal role for CCDC102B in cancer, showing it activates NF-κB by sequestering RACK1 away from IKKα and is itself degraded by RACK1-directed chaperone-mediated autophagy, linking centrosome biology to metastatic signaling.\",\n      \"evidence\": \"Co-IP, mass spectrometry, RNA-seq pathway analysis, CRISPR screen, xenograft and tail-vein metastasis models in breast cancer cell lines\",\n      \"pmids\": [\"35957886\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Findings originate from a single laboratory; independent replication is lacking\",\n        \"Whether the RACK1–CCDC102B axis operates in non-breast cancer contexts is unknown\",\n        \"Relationship between centrosome linker function and NF-κB activation has not been dissected\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown how the centrosome-linker and NF-κB-signaling functions of CCDC102B are coordinated, whether CCDC102B possesses intrinsic enzymatic activity, and what post-translational modifications beyond Nek2A phosphorylation regulate its stability and localization.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No enzymatic activity has been attributed to CCDC102B\",\n        \"No high-resolution structure exists\",\n        \"In vivo animal models of CCDC102B loss for centrosome cohesion phenotypes are absent\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"CEP250\", \"CROCC\", \"LRRC45\", \"RACK1\"],\n    \"other_free_text\": []\n  }\n}\n```"}