{"gene":"UBXN2B","run_date":"2026-06-10T10:51:56","timeline":{"discoveries":[{"year":2017,"finding":"p37/UBXN2B, a cofactor of the p97 AAA ATPase, regulates spindle orientation in mammalian cells by limiting the levels of cortical NuMA. p37 controls cortical NuMA levels via the phosphatase PP1 and its regulatory subunit Repo-Man, acting independently of Gαi, Aurora A kinase, and PP2A phosphatase. In anaphase, PP1/Repo-Man promotes NuMA accumulation at the cortex, while in metaphase p37 negatively regulates this PP1/Repo-Man function to maintain correct spindle orientation.","method":"Loss-of-function (RNAi/KD) with spindle orientation phenotypic readout; genetic epistasis analysis placing p37 upstream of PP1/Repo-Man but independent of Gαi and Aurora A; cortical NuMA quantification by imaging","journal":"The Journal of cell biology","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal pathway placement via multiple epistasis experiments (Gαi, Aurora A, PP2A, PP1/Repo-Man), quantitative imaging of cortical NuMA, defined cellular phenotype in a single rigorous study","pmids":["29222185"],"is_preprint":false},{"year":2024,"finding":"p37/UBXN2B is a major factor regulating VCP/p97 nucleocytoplasmic shuttling. p37-dependent VCP localization is crucial for cytosolic VCP functions (autophagy) and nuclear VCP functions (DNA damage repair). Multisystem proteinopathy-associated VCP mutations enhance association with p37, leading to decreased nuclear VCP localization and increased susceptibility to DNA damage; both defects were normalized by reducing p37 levels.","method":"Subcellular fractionation and live imaging to measure VCP distribution; co-immunoprecipitation to detect p37–VCP interaction; autophagy flux assays; DNA damage sensitivity assays; p37 knockdown rescue experiments in mutant VCP cell lines","journal":"Science advances","confidence":"High","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (fractionation, Co-IP, functional autophagy/DNA-damage assays, rescue by KD) in a single rigorous study establishing mechanistic role","pmids":["38701207"],"is_preprint":false},{"year":2023,"finding":"UBXN2B forms a complex with p97 (VCP) and the FAM104 family proteins VCF1/2. VCF1/2 associate with both p97-UFD1-NPL4 and p97-UBXN2B complexes in cells, and promote nuclear import of p97. Loss of VCF1/2 reduces nuclear p97 levels.","method":"Co-immunoprecipitation and mass spectrometry identifying p97-UBXN2B-VCF1/2 complex; nuclear p97 quantification upon VCF1/2 loss","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP plus functional nuclear localization measurement; single study but two orthogonal methods confirming complex membership","pmids":["37713320"],"is_preprint":false}],"current_model":"UBXN2B (p37) is a cofactor of the p97/VCP AAA-ATPase that (1) regulates mitotic spindle orientation by limiting cortical NuMA levels through negative regulation of PP1/Repo-Man phosphatase activity, and (2) controls p97 nucleocytoplasmic distribution, thereby enabling both cytosolic (autophagy) and nuclear (DNA damage repair) p97 functions; it also participates in a p97–UFD1–NPL4 and p97–UBXN2B–VCF1/2 complex that promotes nuclear p97 import."},"narrative":{"mechanistic_narrative":"UBXN2B (p37) is a cofactor of the p97/VCP AAA-ATPase that couples p97 to mitotic and proteostatic functions across cellular compartments [PMID:29222185, PMID:38701207]. During mitosis, p37 controls spindle orientation by limiting the levels of cortical NuMA: it negatively regulates the PP1 phosphatase and its regulatory subunit Repo-Man, acting independently of Gαi, Aurora A kinase, and PP2A, such that the PP1/Repo-Man-driven cortical NuMA accumulation seen in anaphase is restrained in metaphase [PMID:29222185]. Beyond mitosis, p37 is a major determinant of p97 nucleocytoplasmic shuttling, and this distribution is required for both cytosolic p97 functions (autophagy) and nuclear p97 functions (DNA damage repair); multisystem proteinopathy-associated VCP mutations enhance VCP–p37 association, reducing nuclear VCP and increasing DNA damage susceptibility, defects normalized by lowering p37 [PMID:38701207]. p37 acts within a p97 complex alongside the FAM104 proteins VCF1/2, which associate with both p97-UFD1-NPL4 and p97-UBXN2B assemblies and promote nuclear import of p97 [PMID:37713320].","teleology":[{"year":2017,"claim":"Established that the p97 cofactor p37 has a dedicated mitotic role, defining how spindle orientation is set by restraining cortical NuMA through a specific phosphatase axis.","evidence":"RNAi loss-of-function with spindle-orientation readout and cortical NuMA imaging, plus epistasis placing p37 upstream of PP1/Repo-Man and independent of Gαi, Aurora A, and PP2A","pmids":["29222185"],"confidence":"High","gaps":["Whether p37 regulates PP1/Repo-Man via p97 ATPase activity or independently is not resolved","Direct biochemical demonstration of p37 acting on the PP1/Repo-Man complex is absent","Does not address how this mitotic function relates to p37's interphase p97 roles"]},{"year":2023,"claim":"Identified the molecular machinery delivering p97 to the nucleus, placing UBXN2B in a defined complex with VCF1/2 that promotes p97 nuclear import.","evidence":"Co-immunoprecipitation and mass spectrometry defining the p97-UBXN2B-VCF1/2 complex, with nuclear p97 quantification upon VCF1/2 loss","pmids":["37713320"],"confidence":"Medium","gaps":["Single study with two orthogonal methods; reciprocal validation of complex membership in vitro not shown","Mechanism by which VCF1/2 drives import (carrier vs. retention) is unresolved","Functional consequences of the p37-VCF1/2 axis for downstream p97 activities not tested here"]},{"year":2024,"claim":"Demonstrated that p37 governs p97 nucleocytoplasmic distribution as a control point for both autophagy and DNA damage repair, linking the cofactor to disease-associated VCP dysfunction.","evidence":"Subcellular fractionation, live imaging, Co-IP, autophagy flux and DNA damage sensitivity assays, with p37 knockdown rescue in mutant VCP cell lines","pmids":["38701207"],"confidence":"High","gaps":["Whether p37 acts as a cytoplasmic retention factor or active shuttling carrier is not distinguished","Molecular basis for enhanced p37 association by MSP VCP mutants not structurally defined","Relationship between the mitotic NuMA function and the shuttling function in the same cells unexamined"]},{"year":null,"claim":"How p37's mitotic spindle-orientation role, its control of p97 localization, and the VCF1/2-dependent nuclear import pathway are mechanistically integrated remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the p97-UBXN2B-VCF1/2 complex","Direct substrates processed by p97 under p37 control are not identified","Whether p37 binding to p97 is required for the PP1/Repo-Man regulation is untested"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098772","term_label":"molecular function regulator activity","supporting_discovery_ids":[0,1]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[2]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[1]},{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[1,2]}],"pathway":[{"term_id":"R-HSA-1640170","term_label":"Cell Cycle","supporting_discovery_ids":[0]},{"term_id":"R-HSA-73894","term_label":"DNA Repair","supporting_discovery_ids":[1]},{"term_id":"R-HSA-9612973","term_label":"Autophagy","supporting_discovery_ids":[1]},{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[1,2]}],"complexes":["p97-UBXN2B-VCF1/2","p97-UFD1-NPL4"],"partners":["VCP","VCF1","VCF2"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q14CS0","full_name":"UBX domain-containing protein 2B","aliases":["NSFL1 cofactor p37","p97 cofactor p37"],"length_aa":331,"mass_kda":37.1,"function":"Adapter protein required for Golgi and endoplasmic reticulum biogenesis (PubMed:17141156). Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis (PubMed:17141156). The complex formed with VCP has membrane fusion activity; membrane fusion activity requires USO1-GOLGA2 tethering and BET1L (PubMed:17141156). VCPIP1 is also required, but not its deubiquitinating activity (PubMed:17141156). Together with NSFL1C/p47, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase (PubMed:23649807). Also, regulates spindle orientation during mitosis (PubMed:23649807)","subcellular_location":"Nucleus; Cytoplasm, cytosol; Endoplasmic reticulum; Golgi apparatus; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","url":"https://www.uniprot.org/uniprotkb/Q14CS0/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/UBXN2B","classification":"Not Classified","n_dependent_lines":1,"n_total_lines":1208,"dependency_fraction":0.0008278145695364238},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"VCP","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/UBXN2B","total_profiled":1310},"omim":[{"mim_id":"621109","title":"VCP NUCLEAR COFACTOR FAMILY, MEMBER 1; VCF1","url":"https://www.omim.org/entry/621109"},{"mim_id":"610686","title":"UBX DOMAIN PROTEIN 2B; UBXN2B","url":"https://www.omim.org/entry/610686"},{"mim_id":"601023","title":"VALOSIN-CONTAINING PROTEIN; VCP","url":"https://www.omim.org/entry/601023"},{"mim_id":"301141","title":"VCP NUCLEAR COFACTOR FAMILY, MEMBER 2; VCF2","url":"https://www.omim.org/entry/301141"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoplasm","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/UBXN2B"},"hgnc":{"alias_symbol":["p37"],"prev_symbol":[]},"alphafold":{"accession":"Q14CS0","domains":[{"cath_id":"3.30.420.210","chopping":"79-98_138-208","consensus_level":"medium","plddt":81.5919,"start":79,"end":208},{"cath_id":"3.10.20.90","chopping":"255-329","consensus_level":"high","plddt":84.0803,"start":255,"end":329}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q14CS0","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q14CS0-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q14CS0-F1-predicted_aligned_error_v6.png","plddt_mean":70.31},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=UBXN2B","jax_strain_url":"https://www.jax.org/strain/search?query=UBXN2B"},"sequence":{"accession":"Q14CS0","fasta_url":"https://rest.uniprot.org/uniprotkb/Q14CS0.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q14CS0/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q14CS0"}},"corpus_meta":[{"pmid":"23496005","id":"PMC_23496005","title":"Clinical, polysomnographic and genome-wide association analyses of narcolepsy with cataplexy: a European Narcolepsy Network study.","date":"2013","source":"Journal of sleep research","url":"https://pubmed.ncbi.nlm.nih.gov/23496005","citation_count":171,"is_preprint":false},{"pmid":"37685003","id":"PMC_37685003","title":"Genome-Wide Association Study to Identify QTL for Carcass Traits in Korean Hanwoo Cattle.","date":"2023","source":"Animals : an open access journal from MDPI","url":"https://pubmed.ncbi.nlm.nih.gov/37685003","citation_count":22,"is_preprint":false},{"pmid":"37023829","id":"PMC_37023829","title":"A deep transcriptome meta-analysis reveals sex differences in multiple sclerosis.","date":"2023","source":"Neurobiology of disease","url":"https://pubmed.ncbi.nlm.nih.gov/37023829","citation_count":20,"is_preprint":false},{"pmid":"29222185","id":"PMC_29222185","title":"p37/UBXN2B regulates spindle orientation by limiting cortical NuMA recruitment via PP1/Repo-Man.","date":"2017","source":"The Journal of cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/29222185","citation_count":13,"is_preprint":false},{"pmid":"38701207","id":"PMC_38701207","title":"p37 regulates VCP/p97 shuttling and functions in the nucleus and cytosol.","date":"2024","source":"Science advances","url":"https://pubmed.ncbi.nlm.nih.gov/38701207","citation_count":12,"is_preprint":false},{"pmid":"38778305","id":"PMC_38778305","title":"Genome-wide association study identifies genomic regions associated with key reproductive traits in Korean Hanwoo cows.","date":"2024","source":"BMC genomics","url":"https://pubmed.ncbi.nlm.nih.gov/38778305","citation_count":11,"is_preprint":false},{"pmid":"40452229","id":"PMC_40452229","title":"Genome-wide interaction study with body mass index identifies CYP7A1 and GIPR as genetic modulators of metabolic dysfunction-associated steatotic liver disease.","date":"2025","source":"Clinical and molecular hepatology","url":"https://pubmed.ncbi.nlm.nih.gov/40452229","citation_count":9,"is_preprint":false},{"pmid":"37713320","id":"PMC_37713320","title":"The FAM104 proteins VCF1/2 promote the nuclear localization of p97/VCP.","date":"2023","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/37713320","citation_count":6,"is_preprint":false},{"pmid":"39216264","id":"PMC_39216264","title":"Genome-wide association studies reveal the genetic basis of growth and carcass traits in Sichuan Shelduck.","date":"2024","source":"Poultry science","url":"https://pubmed.ncbi.nlm.nih.gov/39216264","citation_count":5,"is_preprint":false},{"pmid":"41057762","id":"PMC_41057762","title":"Selective sweeps for mutations increasing height impede identification of causative mutations for fertility and other correlated traits in cattle.","date":"2025","source":"Genetics, selection, evolution : GSE","url":"https://pubmed.ncbi.nlm.nih.gov/41057762","citation_count":1,"is_preprint":false},{"pmid":"41772417","id":"PMC_41772417","title":"Full-length transcriptome atlas of porcine skeletal muscle reveals isoform-resolved genetic regulatory mechanisms for muscle growth.","date":"2026","source":"BMC genomics","url":"https://pubmed.ncbi.nlm.nih.gov/41772417","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":8194,"output_tokens":1056,"usd":0.020211,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7623,"output_tokens":2023,"usd":0.044345,"stage2_stop_reason":"end_turn"},"total_usd":0.064556,"stage1_batch_id":"msgbatch_017qqVz33Ga63SCDwzb35XPb","stage2_batch_id":"msgbatch_01Scr2Ei9x4HJMiRGxwrmvLK","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"p37/UBXN2B, a cofactor of the p97 AAA ATPase, regulates spindle orientation in mammalian cells by limiting the levels of cortical NuMA. p37 controls cortical NuMA levels via the phosphatase PP1 and its regulatory subunit Repo-Man, acting independently of Gαi, Aurora A kinase, and PP2A phosphatase. In anaphase, PP1/Repo-Man promotes NuMA accumulation at the cortex, while in metaphase p37 negatively regulates this PP1/Repo-Man function to maintain correct spindle orientation.\",\n      \"method\": \"Loss-of-function (RNAi/KD) with spindle orientation phenotypic readout; genetic epistasis analysis placing p37 upstream of PP1/Repo-Man but independent of Gαi and Aurora A; cortical NuMA quantification by imaging\",\n      \"journal\": \"The Journal of cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal pathway placement via multiple epistasis experiments (Gαi, Aurora A, PP2A, PP1/Repo-Man), quantitative imaging of cortical NuMA, defined cellular phenotype in a single rigorous study\",\n      \"pmids\": [\"29222185\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"p37/UBXN2B is a major factor regulating VCP/p97 nucleocytoplasmic shuttling. p37-dependent VCP localization is crucial for cytosolic VCP functions (autophagy) and nuclear VCP functions (DNA damage repair). Multisystem proteinopathy-associated VCP mutations enhance association with p37, leading to decreased nuclear VCP localization and increased susceptibility to DNA damage; both defects were normalized by reducing p37 levels.\",\n      \"method\": \"Subcellular fractionation and live imaging to measure VCP distribution; co-immunoprecipitation to detect p37–VCP interaction; autophagy flux assays; DNA damage sensitivity assays; p37 knockdown rescue experiments in mutant VCP cell lines\",\n      \"journal\": \"Science advances\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (fractionation, Co-IP, functional autophagy/DNA-damage assays, rescue by KD) in a single rigorous study establishing mechanistic role\",\n      \"pmids\": [\"38701207\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"UBXN2B forms a complex with p97 (VCP) and the FAM104 family proteins VCF1/2. VCF1/2 associate with both p97-UFD1-NPL4 and p97-UBXN2B complexes in cells, and promote nuclear import of p97. Loss of VCF1/2 reduces nuclear p97 levels.\",\n      \"method\": \"Co-immunoprecipitation and mass spectrometry identifying p97-UBXN2B-VCF1/2 complex; nuclear p97 quantification upon VCF1/2 loss\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP plus functional nuclear localization measurement; single study but two orthogonal methods confirming complex membership\",\n      \"pmids\": [\"37713320\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"UBXN2B (p37) is a cofactor of the p97/VCP AAA-ATPase that (1) regulates mitotic spindle orientation by limiting cortical NuMA levels through negative regulation of PP1/Repo-Man phosphatase activity, and (2) controls p97 nucleocytoplasmic distribution, thereby enabling both cytosolic (autophagy) and nuclear (DNA damage repair) p97 functions; it also participates in a p97–UFD1–NPL4 and p97–UBXN2B–VCF1/2 complex that promotes nuclear p97 import.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"UBXN2B (p37) is a cofactor of the p97/VCP AAA-ATPase that couples p97 to mitotic and proteostatic functions across cellular compartments [#0, #1]. During mitosis, p37 controls spindle orientation by limiting the levels of cortical NuMA: it negatively regulates the PP1 phosphatase and its regulatory subunit Repo-Man, acting independently of G\\u03b1i, Aurora A kinase, and PP2A, such that the PP1/Repo-Man-driven cortical NuMA accumulation seen in anaphase is restrained in metaphase [#0]. Beyond mitosis, p37 is a major determinant of p97 nucleocytoplasmic shuttling, and this distribution is required for both cytosolic p97 functions (autophagy) and nuclear p97 functions (DNA damage repair); multisystem proteinopathy-associated VCP mutations enhance VCP\\u2013p37 association, reducing nuclear VCP and increasing DNA damage susceptibility, defects normalized by lowering p37 [#1]. p37 acts within a p97 complex alongside the FAM104 proteins VCF1/2, which associate with both p97-UFD1-NPL4 and p97-UBXN2B assemblies and promote nuclear import of p97 [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2017,\n      \"claim\": \"Established that the p97 cofactor p37 has a dedicated mitotic role, defining how spindle orientation is set by restraining cortical NuMA through a specific phosphatase axis.\",\n      \"evidence\": \"RNAi loss-of-function with spindle-orientation readout and cortical NuMA imaging, plus epistasis placing p37 upstream of PP1/Repo-Man and independent of G\\u03b1i, Aurora A, and PP2A\",\n      \"pmids\": [\"29222185\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether p37 regulates PP1/Repo-Man via p97 ATPase activity or independently is not resolved\",\n        \"Direct biochemical demonstration of p37 acting on the PP1/Repo-Man complex is absent\",\n        \"Does not address how this mitotic function relates to p37's interphase p97 roles\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Identified the molecular machinery delivering p97 to the nucleus, placing UBXN2B in a defined complex with VCF1/2 that promotes p97 nuclear import.\",\n      \"evidence\": \"Co-immunoprecipitation and mass spectrometry defining the p97-UBXN2B-VCF1/2 complex, with nuclear p97 quantification upon VCF1/2 loss\",\n      \"pmids\": [\"37713320\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single study with two orthogonal methods; reciprocal validation of complex membership in vitro not shown\",\n        \"Mechanism by which VCF1/2 drives import (carrier vs. retention) is unresolved\",\n        \"Functional consequences of the p37-VCF1/2 axis for downstream p97 activities not tested here\"\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Demonstrated that p37 governs p97 nucleocytoplasmic distribution as a control point for both autophagy and DNA damage repair, linking the cofactor to disease-associated VCP dysfunction.\",\n      \"evidence\": \"Subcellular fractionation, live imaging, Co-IP, autophagy flux and DNA damage sensitivity assays, with p37 knockdown rescue in mutant VCP cell lines\",\n      \"pmids\": [\"38701207\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Whether p37 acts as a cytoplasmic retention factor or active shuttling carrier is not distinguished\",\n        \"Molecular basis for enhanced p37 association by MSP VCP mutants not structurally defined\",\n        \"Relationship between the mitotic NuMA function and the shuttling function in the same cells unexamined\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How p37's mitotic spindle-orientation role, its control of p97 localization, and the VCF1/2-dependent nuclear import pathway are mechanistically integrated remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of the p97-UBXN2B-VCF1/2 complex\",\n        \"Direct substrates processed by p97 under p37 control are not identified\",\n        \"Whether p37 binding to p97 is required for the PP1/Repo-Man regulation is untested\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098772\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1640170\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-73894\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-9612973\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"complexes\": [\"p97-UBXN2B-VCF1/2\", \"p97-UFD1-NPL4\"],\n    \"partners\": [\"VCP\", \"VCF1\", \"VCF2\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":3,"faith_total":3,"faith_pct":100.0}}