{"gene":"NUP155","run_date":"2026-06-10T05:19:52","timeline":{"discoveries":[{"year":1993,"finding":"Nup155 is a component of the nuclear pore complex (NPC), localizing to both the nucleoplasmic and cytoplasmic aspects of the NPC by immunoelectron microscopy. In mitotic cells, it assumes a diffuse cytoplasmic distribution. It is among ~30 integral NPC proteins extractable from rat liver nuclear envelopes by 2M urea/1mM EDTA that do not react with WGA.","method":"Molecular cloning, immunoelectron microscopy, subcellular fractionation","journal":"The Journal of Cell Biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — direct immunoelectron microscopy localization with biochemical fractionation, foundational characterization paper","pmids":["8458861"],"is_preprint":false},{"year":2005,"finding":"Nup155 is required for nuclear envelope (NE) formation in C. elegans embryos and Xenopus egg extracts. Its depletion caused failure of nuclear lamina formation, defects in chromosome segregation at anaphase, inhibition of nucleoporin accumulation at the nuclear periphery, and failure to form a continuous nuclear membrane. Nup155 is recruited to chromatin at the time of NE sealing, indicating that NPC assembly must progress to a relatively late stage before NE membrane assembly occurs.","method":"In vivo RNAi depletion (C. elegans), Xenopus egg extract in vitro assay, electron microscopy, time-course chromatin recruitment assay","journal":"The EMBO Journal","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal in vivo and in vitro depletion experiments across two model organisms with EM validation and time-course analysis","pmids":["16193066"],"is_preprint":false},{"year":2003,"finding":"Human Nup155 directly interacts with the mRNA export factor hGle1. The C-terminal 177 amino acids of hNup155 constitute the hGle1-binding domain, and the N-terminal 29 residues of hGle1 mediate binding to hNup155. This interaction is required for nuclear rim localization of hGle1B, indicating that hNup155 anchors hGle1 to the NPC as part of the mRNA export pathway.","method":"Genome-wide yeast two-hybrid screen, in vitro binding confirmation, deletion mapping, HeLa cell localization assay","journal":"Molecular & Cellular Proteomics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — yeast two-hybrid confirmed in vitro with deletion analysis and cellular localization, single lab","pmids":["14645504"],"is_preprint":false},{"year":2008,"finding":"A homozygous R391H mutation in NUP155 causes atrial fibrillation and early sudden cardiac death. The mutation affects nuclear localization of NUP155, reduces nuclear envelope permeability, and inhibits both export of Hsp70 mRNA and nuclear import of Hsp70 protein. Homozygous Nup155-/- mice die before E8.5; heterozygous Nup155+/- mice exhibit the AF phenotype.","method":"Human genetic mapping, co-segregation analysis, mouse knockout, nuclear permeability assay, mRNA/protein transport assay","journal":"Cell","confidence":"High","confidence_rationale":"Tier 2 / Strong — human mutation with cosegregation, mouse KO phenotype, and direct nucleocytoplasmic transport functional assays across multiple orthogonal methods","pmids":["19070573"],"is_preprint":false},{"year":2012,"finding":"Drosophila Nup155 has functionally distinct domains: the β-propeller domain anchors the protein to the NPC (via interactions with Nup93 and Nup53), while the α-solenoid domain is essential for correct localization of inner nuclear membrane (INM) proteins lamin-B receptor (LBR) and otefin, independently of NPC anchoring. The α-solenoid also exhibits chromatin-binding activity that is stronger at the end of mitosis.","method":"RNAi hypomorphic knockdown in Drosophila, protein binding assays, rescue assays with deletion constructs, chromatin extract binding assay from semi-synchronized cells, immunofluorescence","journal":"Journal of Cell Science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — domain dissection with rescue assays in cells and chromatin binding biochemistry, single lab, multiple orthogonal approaches","pmids":["22718353"],"is_preprint":false},{"year":2013,"finding":"The interaction between Nup53 and Nup155 is required for NPC assembly, with Nup53 serving as the main determinant for recruitment of Nup155 to the assembling pore. Separately, the interaction of Nup53 with the integral pore membrane protein Ndc1 is also essential for vertebrate NPC assembly, and the Ndc1-binding site on Nup53 overlaps with its membrane-bending region.","method":"Co-immunoprecipitation, in vitro binding assays, Xenopus egg extract NPC assembly assay, domain deletion analysis","journal":"Journal of Cell Science","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal binding assays combined with reconstituted NPC assembly in Xenopus extracts and domain mapping","pmids":["24363447"],"is_preprint":false},{"year":2018,"finding":"Lamin A/C interacts directly with NUP155 (demonstrated by co-immunoprecipitation and GST pull-down). The AF-associated lamin A/C mutation p.Arg399Cys impairs this interaction, increases extractability of NUP155 from the nuclear envelope, and recapitulates the NUP155 loss-of-function phenotype: inhibition of HSP70 mRNA export and HSP70 protein nuclear import.","method":"Co-immunoprecipitation, GST pull-down, nuclear envelope fractionation, mRNA/protein transport assay","journal":"Human Mutation","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP and pulldown with functional transport assays, single lab","pmids":["30488537"],"is_preprint":false},{"year":2019,"finding":"Nup155 controls mRNA translation of p21 (CDKN1A) by transcriptionally regulating the putative tRNA/rRNA methyltransferase FTSJ1. Both Nup155 and FTSJ1 are p53 repression targets, placing Nup155 within a regulatory network that links translational control to the p53 pathway.","method":"Large-scale proteomics, polysome fractionation, focused RNAi, transcriptional reporter assays in hepatocellular carcinoma cells","journal":"Nature Communications","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (proteomics, polysome fractionation, RNAi) in single lab study","pmids":["31089132"],"is_preprint":false},{"year":2024,"finding":"Loss of Nup155 in podocytes inhibits nuclear export of INO80 mRNA, leading to decreased INO80 protein expression and podocyte senescence. Overexpression of Nup155 or INO80 rescued high fructose-induced senescence. Ferulic acid directly binds Nup155 to stabilize it and enhance its transcription, thereby promoting INO80 mRNA nuclear export.","method":"siRNA knockdown, overexpression rescue, qRT-PCR, Western blot, mRNA nuclear export assay, virtual screening/binding, immunofluorescence, transmission electron microscopy","journal":"Journal of Advanced Research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — loss-of-function and gain-of-function with defined mRNA export readout, single lab, multiple orthogonal methods","pmids":["39111625"],"is_preprint":false},{"year":2024,"finding":"NUP155 knockdown in NSCLC cells upregulates PTEN and downregulates phosphorylated AKT without altering total AKT, placing NUP155 upstream of the PTEN/AKT signaling pathway. Pharmacological PTEN inhibition (SF1670) partially reversed the anti-proliferative and pro-apoptotic effects of NUP155 knockdown, establishing epistasis.","method":"siRNA knockdown, Western blotting, PTEN inhibitor epistasis, proliferation/migration/invasion/apoptosis assays","journal":"Translational Cancer Research","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single epistasis experiment with pharmacological inhibitor, no direct biochemical mechanism established","pmids":["39697746"],"is_preprint":false},{"year":2024,"finding":"TRIM21 E3 ligase ligands induce ubiquitin-proteasome-dependent degradation of NUP155 (identified as the primary target) and secondarily GLE1 (passenger target upon NUP155 degradation). Degradation of NUP155 and GLE1 impairs nuclear envelope integrity and leads to cell death.","method":"DNA-Encoded Library (DEL) screen, crystallography of TRIM21-ligand complex, proteomic profiling, immunofluorescence, proteasome inhibitor rescue","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 1-2 / Moderate — crystallographic confirmation of E3 ligase engagement, proteomic identification of NUP155 as primary degradation target, mechanistic rescue experiments; preprint not yet peer-reviewed","pmids":["bio_10.1101_2024.12.03.626577"],"is_preprint":true}],"current_model":"NUP155 is a structurally essential nucleoporin that localizes symmetrically to both faces of the nuclear pore complex; its β-propeller domain anchors it to the NPC via Nup53-dependent recruitment, while its α-solenoid domain independently organizes inner nuclear membrane proteins and binds chromatin at mitotic exit; NUP155 is required for nuclear envelope membrane sealing and NPC assembly during mitosis, and is functionally critical for bidirectional nucleocytoplasmic transport—including Hsp70 mRNA export and Hsp70 protein import—by scaffolding the mRNA export factor GLE1 at the pore; loss-of-function mutations (human R391H) or disruption of its interaction with lamin A/C cause atrial fibrillation through impaired nucleocytoplasmic transport, while NUP155 also participates in translational regulation of p21 via FTSJ1 transcription and in podocyte homeostasis through INO80 mRNA export."},"narrative":{"mechanistic_narrative":"NUP155 is a structurally essential nucleoporin that localizes symmetrically to both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex (NPC) and disperses to the cytoplasm during mitosis [PMID:8458861]. It is required for nuclear envelope formation and sealing: its depletion blocks nuclear lamina assembly, nucleoporin accumulation at the nuclear periphery, and formation of a continuous nuclear membrane, and it is recruited to chromatin late in NPC assembly at the time of membrane sealing [PMID:16193066]. NUP155 is organized into functionally distinct domains—a β-propeller that anchors it to the assembling pore through Nup53 (with additional Nup93 contacts), and an α-solenoid that independently positions inner nuclear membrane proteins such as LBR and otefin and binds chromatin most strongly at mitotic exit [PMID:22718353, PMID:24363447]. At the pore, NUP155 directly binds and anchors the mRNA export factor GLE1 at the nuclear rim, coupling it to the mRNA export machinery [PMID:14645504]. Through this scaffolding role NUP155 supports bidirectional nucleocytoplasmic transport, including export of HSP70 mRNA and import of HSP70 protein [PMID:19070573]. Its retention at the nuclear envelope and transport function depend on a direct interaction with lamin A/C [PMID:30488537]. A homozygous R391H mutation in NUP155 causes atrial fibrillation and early sudden cardiac death by reducing nuclear localization, lowering nuclear envelope permeability, and impairing HSP70 mRNA/protein transport, a phenotype recapitulated by an AF-associated lamin A/C mutation that disrupts the lamin A/C–NUP155 interaction [PMID:19070573, PMID:30488537]. Beyond its transport scaffolding role, NUP155 has been linked to gene-specific outputs, including translational control of p21 via transcriptional regulation of FTSJ1 within the p53 network [PMID:31089132] and nuclear export of INO80 mRNA in podocyte homeostasis [PMID:39111625].","teleology":[{"year":1993,"claim":"Establishing that NUP155 is a bona fide integral NPC component answered where the protein resides and set it apart from peripheral, WGA-reactive nucleoporins.","evidence":"Molecular cloning, immunoelectron microscopy, and urea/EDTA fractionation of rat liver nuclear envelopes","pmids":["8458861"],"confidence":"High","gaps":["Did not define molecular partners or assembly determinants","Functional role in transport or assembly not yet addressed"]},{"year":2003,"claim":"Identifying GLE1 as a direct NUP155 partner answered how an mRNA export factor is anchored to the pore, linking NUP155 to the mRNA export pathway.","evidence":"Yeast two-hybrid screen with in vitro binding, deletion mapping, and HeLa localization","pmids":["14645504"],"confidence":"Medium","gaps":["Single lab; reciprocal in vivo validation limited","Whether GLE1 anchoring fully accounts for NUP155 transport function not resolved"]},{"year":2005,"claim":"Depletion across two model systems answered whether NUP155 is required for nuclear envelope and NPC biogenesis, placing it at the late, membrane-sealing step of assembly.","evidence":"RNAi in C. elegans, Xenopus egg extract assays, EM, and chromatin-recruitment time course","pmids":["16193066"],"confidence":"High","gaps":["Molecular partners mediating chromatin recruitment not defined here","Domain responsible for membrane sealing not mapped"]},{"year":2008,"claim":"A human R391H mutation and mouse knockout answered whether NUP155 loss causes disease, tying impaired nucleocytoplasmic transport to atrial fibrillation and sudden death.","evidence":"Human genetic mapping with co-segregation, mouse knockout, nuclear permeability and HSP70 mRNA/protein transport assays","pmids":["19070573"],"confidence":"High","gaps":["Mechanism linking transport defect to cardiac electrophysiology not detailed","Why HSP70 cargo specifically is affected not resolved"]},{"year":2012,"claim":"Domain dissection answered how NUP155 partitions its jobs, separating NPC anchoring (β-propeller) from INM protein organization and chromatin binding (α-solenoid).","evidence":"Drosophila hypomorphic RNAi, rescue with deletion constructs, binding and chromatin-extract assays","pmids":["22718353"],"confidence":"Medium","gaps":["Chromatin-binding partner not identified","Single lab in Drosophila; human domain equivalence assumed"]},{"year":2013,"claim":"Mapping the Nup53–NUP155 interaction answered how NUP155 is recruited to the assembling pore, identifying Nup53 as the principal recruitment determinant.","evidence":"Co-IP, in vitro binding, domain deletion, and Xenopus NPC assembly reconstitution","pmids":["24363447"],"confidence":"High","gaps":["Order of recruitment relative to membrane events not fully resolved","Stoichiometry within the assembled pore not defined"]},{"year":2018,"claim":"Demonstrating a direct lamin A/C–NUP155 interaction answered how NUP155 is retained at the nuclear envelope and provided a second genetic route to the AF transport phenotype.","evidence":"Co-IP, GST pull-down, NE fractionation, and HSP70 mRNA/protein transport assays with an AF lamin A/C mutant","pmids":["30488537"],"confidence":"Medium","gaps":["Single lab; structural basis of the interaction unknown","Whether lamin A/C tethering is direct or via other NPC components not fully separated"]},{"year":2019,"claim":"Linking NUP155 to FTSJ1 and p21 translation answered whether NUP155 has gene-regulatory outputs beyond bulk transport, embedding it in the p53 network.","evidence":"Proteomics, polysome fractionation, RNAi, and transcriptional reporters in hepatocellular carcinoma cells","pmids":["31089132"],"confidence":"Medium","gaps":["Mechanism by which a nucleoporin transcriptionally regulates FTSJ1 not defined","Generality beyond HCC cells unknown"]},{"year":2024,"claim":"Podocyte studies answered whether NUP155-dependent mRNA export controls cell fate, linking impaired INO80 mRNA export to senescence.","evidence":"siRNA, overexpression rescue, mRNA export assays, EM, and ferulic acid binding in podocytes","pmids":["39111625"],"confidence":"Medium","gaps":["Selectivity for INO80 mRNA mechanistically unexplained","Direct ferulic acid binding mode not structurally resolved"]},{"year":2024,"claim":"TRIM21-directed degradation answered whether targeted NUP155 destruction is cytotoxic, with GLE1 lost as a passenger and nuclear envelope integrity collapsing.","evidence":"DEL screen, TRIM21-ligand crystallography, proteomics, and proteasome-inhibitor rescue (preprint)","pmids":["bio_10.1101_2024.12.03.626577"],"confidence":"Medium","gaps":["Preprint, not peer-reviewed","Therapeutic window and selectivity not established"]},{"year":null,"claim":"How NUP155 achieves cargo- and transcript-specific outputs (HSP70, INO80 mRNA, FTSJ1/p21) from a structural scaffolding role remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No mechanism connecting NPC scaffolding to selective transcript regulation","Structural model of the human NUP155 β-propeller/α-solenoid in the assembled pore lacking","Direct chromatin-binding partner of the α-solenoid unidentified"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0,1,5]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[2,4]},{"term_id":"GO:0003677","term_label":"DNA binding","supporting_discovery_ids":[4]}],"localization":[{"term_id":"GO:0005635","term_label":"nuclear envelope","supporting_discovery_ids":[0,1,6]},{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[0]}],"pathway":[{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[2,3]},{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[2,3,8]},{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[1,5]}],"complexes":["nuclear pore complex"],"partners":["GLE1","NUP53","NUP93","LMNA","NDC1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O75694","full_name":"Nuclear pore complex protein Nup155","aliases":["155 kDa nucleoporin","Nucleoporin Nup155"],"length_aa":1391,"mass_kda":155.2,"function":"Essential component of nuclear pore complex. Could be essessential for embryogenesis. Nucleoporins may be involved both in binding and translocating proteins during nucleocytoplasmic transport","subcellular_location":"Nucleus, nuclear pore complex; Nucleus membrane; Nucleus membrane","url":"https://www.uniprot.org/uniprotkb/O75694/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/NUP155","classification":"Common Essential","n_dependent_lines":1178,"n_total_lines":1208,"dependency_fraction":0.9751655629139073},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000113569","cell_line_id":"CID001716","localizations":[{"compartment":"nuclear_membrane","grade":3}],"interactors":[{"gene":"MAPRE1","stoichiometry":0.2},{"gene":"NUMA1","stoichiometry":0.2},{"gene":"RAN","stoichiometry":0.2},{"gene":"RANBP1","stoichiometry":0.2},{"gene":"XPO1","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID001716","total_profiled":1310},"omim":[{"mim_id":"615770","title":"ATRIAL FIBRILLATION, FAMILIAL, 15; ATFB15","url":"https://www.omim.org/entry/615770"},{"mim_id":"615753","title":"POM121 TRANSMEMBRANE NUCLEOPORIN; POM121","url":"https://www.omim.org/entry/615753"},{"mim_id":"614352","title":"NUCLEOPORIN, 205-KD; NUP205","url":"https://www.omim.org/entry/614352"},{"mim_id":"614351","title":"NUCLEOPORIN, 93-KD; NUP93","url":"https://www.omim.org/entry/614351"},{"mim_id":"613174","title":"CHROMOSOME 5p13 DUPLICATION SYNDROME","url":"https://www.omim.org/entry/613174"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Enhanced","locations":[{"location":"Nuclear membrane","reliability":"Enhanced"}],"tissue_specificity":"Tissue enriched","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"testis","ntpm":66.2}],"url":"https://www.proteinatlas.org/search/NUP155"},"hgnc":{"alias_symbol":["KIAA0791","N155"],"prev_symbol":[]},"alphafold":{"accession":"O75694","domains":[{"cath_id":"2.130.10.10","chopping":"90-181_196-261_274-278","consensus_level":"medium","plddt":86.8323,"start":90,"end":278},{"cath_id":"-","chopping":"909-989_1013-1058","consensus_level":"medium","plddt":89.8319,"start":909,"end":1058},{"cath_id":"-","chopping":"1073-1212","consensus_level":"medium","plddt":87.3299,"start":1073,"end":1212}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O75694","model_url":"https://alphafold.ebi.ac.uk/files/AF-O75694-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O75694-F1-predicted_aligned_error_v6.png","plddt_mean":83.12},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=NUP155","jax_strain_url":"https://www.jax.org/strain/search?query=NUP155"},"sequence":{"accession":"O75694","fasta_url":"https://rest.uniprot.org/uniprotkb/O75694.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O75694/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O75694"}},"corpus_meta":[{"pmid":"19070573","id":"PMC_19070573","title":"Mutation in nuclear pore component NUP155 leads to atrial fibrillation and early sudden cardiac death.","date":"2008","source":"Cell","url":"https://pubmed.ncbi.nlm.nih.gov/19070573","citation_count":226,"is_preprint":false},{"pmid":"16193066","id":"PMC_16193066","title":"Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates.","date":"2005","source":"The EMBO journal","url":"https://pubmed.ncbi.nlm.nih.gov/16193066","citation_count":93,"is_preprint":false},{"pmid":"8458861","id":"PMC_8458861","title":"Nup155 is a novel nuclear pore complex protein that contains neither repetitive sequence motifs nor reacts with WGA.","date":"1993","source":"The Journal of cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/8458861","citation_count":76,"is_preprint":false},{"pmid":"24363447","id":"PMC_24363447","title":"Interaction of Nup53 with Ndc1 and Nup155 is required for nuclear pore complex assembly.","date":"2013","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/24363447","citation_count":64,"is_preprint":false},{"pmid":"9732281","id":"PMC_9732281","title":"Nup154, a new Drosophila gene essential for male and female gametogenesis is related to the nup155 vertebrate nucleoporin gene.","date":"1998","source":"The Journal of cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/9732281","citation_count":63,"is_preprint":false},{"pmid":"14645504","id":"PMC_14645504","title":"The mRNA export factor human Gle1 interacts with the nuclear pore complex protein Nup155.","date":"2003","source":"Molecular & cellular proteomics : MCP","url":"https://pubmed.ncbi.nlm.nih.gov/14645504","citation_count":55,"is_preprint":false},{"pmid":"19505846","id":"PMC_19505846","title":"Whole genome characterization of reassortant G10P[11] strain (N155) from a neonate with symptomatic rotavirus infection: identification of genes of human and animal rotavirus origin.","date":"2009","source":"Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology","url":"https://pubmed.ncbi.nlm.nih.gov/19505846","citation_count":42,"is_preprint":false},{"pmid":"31089132","id":"PMC_31089132","title":"Nucleoporin Nup155 is part of the p53 network in liver cancer.","date":"2019","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/31089132","citation_count":38,"is_preprint":false},{"pmid":"30488537","id":"PMC_30488537","title":"Lamin A mutation impairs interaction with nucleoporin NUP155 and disrupts nucleocytoplasmic transport in atrial fibrillation.","date":"2018","source":"Human mutation","url":"https://pubmed.ncbi.nlm.nih.gov/30488537","citation_count":34,"is_preprint":false},{"pmid":"29867845","id":"PMC_29867845","title":"Host Interaction Analysis of PA-N155 and PA-N182 in Chicken Cells Reveals an Essential Role of UBA52 for Replication of H5N1 Avian Influenza Virus.","date":"2018","source":"Frontiers in microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/29867845","citation_count":17,"is_preprint":false},{"pmid":"10191094","id":"PMC_10191094","title":"Localization of a human nucleoporin 155 gene (NUP155) to the 5p13 region and cloning of its cDNA.","date":"1999","source":"Genomics","url":"https://pubmed.ncbi.nlm.nih.gov/10191094","citation_count":16,"is_preprint":false},{"pmid":"29848314","id":"PMC_29848314","title":"NUP155 insufficiency recalibrates a pluripotent transcriptome with network remodeling of a cardiogenic signaling module.","date":"2018","source":"BMC systems biology","url":"https://pubmed.ncbi.nlm.nih.gov/29848314","citation_count":15,"is_preprint":false},{"pmid":"22718353","id":"PMC_22718353","title":"The Nup155-mediated organisation of inner nuclear membrane proteins is independent of Nup155 anchoring to the metazoan nuclear pore complex.","date":"2012","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/22718353","citation_count":13,"is_preprint":false},{"pmid":"12034489","id":"PMC_12034489","title":"Genomic organization, transcript variants and comparative analysis of the human nucleoporin 155 (NUP155) gene.","date":"2002","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/12034489","citation_count":9,"is_preprint":false},{"pmid":"39111625","id":"PMC_39111625","title":"Loss of Nup155 promotes high fructose-driven podocyte senescence by inhibiting INO80 mRNA nuclear export.","date":"2024","source":"Journal of advanced research","url":"https://pubmed.ncbi.nlm.nih.gov/39111625","citation_count":6,"is_preprint":false},{"pmid":"38504158","id":"PMC_38504158","title":"Pan-cancer analysis of NUP155 and validation of its role in breast cancer cell proliferation, migration, and apoptosis.","date":"2024","source":"BMC cancer","url":"https://pubmed.ncbi.nlm.nih.gov/38504158","citation_count":6,"is_preprint":false},{"pmid":"32118046","id":"PMC_32118046","title":"Protein Subdomain Enrichment of NUP155 Variants Identify a Novel Predicted Pathogenic Hotspot.","date":"2020","source":"Frontiers in cardiovascular medicine","url":"https://pubmed.ncbi.nlm.nih.gov/32118046","citation_count":4,"is_preprint":false},{"pmid":"39720592","id":"PMC_39720592","title":"NUP155 and NDC1 interaction in NSCLC: a promising target for tumor progression.","date":"2024","source":"Frontiers in pharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/39720592","citation_count":3,"is_preprint":false},{"pmid":"39362331","id":"PMC_39362331","title":"Siwu tablet attenuates high fructose-induced glomerular podocyte senescence in rats through increasing Nup155 to promote INO80 mRNA nuclear export.","date":"2024","source":"Journal of ethnopharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/39362331","citation_count":3,"is_preprint":false},{"pmid":"39697746","id":"PMC_39697746","title":"Postexercise downregulation of NUP155 in regulating non-small cell lung cancer progression via the PTEN/AKT signaling pathway.","date":"2024","source":"Translational cancer research","url":"https://pubmed.ncbi.nlm.nih.gov/39697746","citation_count":0,"is_preprint":false},{"pmid":"40885462","id":"PMC_40885462","title":"MALAT1 elevates the secretion of Th2 cytokines via miR-422a/NUP155 axis in allergic rhinitis mice.","date":"2025","source":"Archives of biochemistry and biophysics","url":"https://pubmed.ncbi.nlm.nih.gov/40885462","citation_count":0,"is_preprint":false},{"pmid":"33381532","id":"PMC_33381532","title":"Corrigendum: Protein Subdomain Enrichment of NUP155 Variants Identify a Novel Predicted Pathogenic Hotspot.","date":"2020","source":"Frontiers in cardiovascular medicine","url":"https://pubmed.ncbi.nlm.nih.gov/33381532","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2024.12.03.626577","title":"Chemically Induced Nuclear Pore Complex Protein Degradation via E3 Ligase TRIM21","date":"2024-12-04","source":"bioRxiv","url":"https://doi.org/10.1101/2024.12.03.626577","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":13104,"output_tokens":2993,"usd":0.042104,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":10411,"output_tokens":3538,"usd":0.070252,"stage2_stop_reason":"end_turn"},"total_usd":0.112356,"stage1_batch_id":"msgbatch_013a8chtv3AWyTqv4z4sEF4C","stage2_batch_id":"msgbatch_01AHsuW63vinsvuTgzmQ3n62","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1993,\n      \"finding\": \"Nup155 is a component of the nuclear pore complex (NPC), localizing to both the nucleoplasmic and cytoplasmic aspects of the NPC by immunoelectron microscopy. In mitotic cells, it assumes a diffuse cytoplasmic distribution. It is among ~30 integral NPC proteins extractable from rat liver nuclear envelopes by 2M urea/1mM EDTA that do not react with WGA.\",\n      \"method\": \"Molecular cloning, immunoelectron microscopy, subcellular fractionation\",\n      \"journal\": \"The Journal of Cell Biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — direct immunoelectron microscopy localization with biochemical fractionation, foundational characterization paper\",\n      \"pmids\": [\"8458861\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2005,\n      \"finding\": \"Nup155 is required for nuclear envelope (NE) formation in C. elegans embryos and Xenopus egg extracts. Its depletion caused failure of nuclear lamina formation, defects in chromosome segregation at anaphase, inhibition of nucleoporin accumulation at the nuclear periphery, and failure to form a continuous nuclear membrane. Nup155 is recruited to chromatin at the time of NE sealing, indicating that NPC assembly must progress to a relatively late stage before NE membrane assembly occurs.\",\n      \"method\": \"In vivo RNAi depletion (C. elegans), Xenopus egg extract in vitro assay, electron microscopy, time-course chromatin recruitment assay\",\n      \"journal\": \"The EMBO Journal\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal in vivo and in vitro depletion experiments across two model organisms with EM validation and time-course analysis\",\n      \"pmids\": [\"16193066\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"Human Nup155 directly interacts with the mRNA export factor hGle1. The C-terminal 177 amino acids of hNup155 constitute the hGle1-binding domain, and the N-terminal 29 residues of hGle1 mediate binding to hNup155. This interaction is required for nuclear rim localization of hGle1B, indicating that hNup155 anchors hGle1 to the NPC as part of the mRNA export pathway.\",\n      \"method\": \"Genome-wide yeast two-hybrid screen, in vitro binding confirmation, deletion mapping, HeLa cell localization assay\",\n      \"journal\": \"Molecular & Cellular Proteomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — yeast two-hybrid confirmed in vitro with deletion analysis and cellular localization, single lab\",\n      \"pmids\": [\"14645504\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2008,\n      \"finding\": \"A homozygous R391H mutation in NUP155 causes atrial fibrillation and early sudden cardiac death. The mutation affects nuclear localization of NUP155, reduces nuclear envelope permeability, and inhibits both export of Hsp70 mRNA and nuclear import of Hsp70 protein. Homozygous Nup155-/- mice die before E8.5; heterozygous Nup155+/- mice exhibit the AF phenotype.\",\n      \"method\": \"Human genetic mapping, co-segregation analysis, mouse knockout, nuclear permeability assay, mRNA/protein transport assay\",\n      \"journal\": \"Cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — human mutation with cosegregation, mouse KO phenotype, and direct nucleocytoplasmic transport functional assays across multiple orthogonal methods\",\n      \"pmids\": [\"19070573\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"Drosophila Nup155 has functionally distinct domains: the β-propeller domain anchors the protein to the NPC (via interactions with Nup93 and Nup53), while the α-solenoid domain is essential for correct localization of inner nuclear membrane (INM) proteins lamin-B receptor (LBR) and otefin, independently of NPC anchoring. The α-solenoid also exhibits chromatin-binding activity that is stronger at the end of mitosis.\",\n      \"method\": \"RNAi hypomorphic knockdown in Drosophila, protein binding assays, rescue assays with deletion constructs, chromatin extract binding assay from semi-synchronized cells, immunofluorescence\",\n      \"journal\": \"Journal of Cell Science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — domain dissection with rescue assays in cells and chromatin binding biochemistry, single lab, multiple orthogonal approaches\",\n      \"pmids\": [\"22718353\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"The interaction between Nup53 and Nup155 is required for NPC assembly, with Nup53 serving as the main determinant for recruitment of Nup155 to the assembling pore. Separately, the interaction of Nup53 with the integral pore membrane protein Ndc1 is also essential for vertebrate NPC assembly, and the Ndc1-binding site on Nup53 overlaps with its membrane-bending region.\",\n      \"method\": \"Co-immunoprecipitation, in vitro binding assays, Xenopus egg extract NPC assembly assay, domain deletion analysis\",\n      \"journal\": \"Journal of Cell Science\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal binding assays combined with reconstituted NPC assembly in Xenopus extracts and domain mapping\",\n      \"pmids\": [\"24363447\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Lamin A/C interacts directly with NUP155 (demonstrated by co-immunoprecipitation and GST pull-down). The AF-associated lamin A/C mutation p.Arg399Cys impairs this interaction, increases extractability of NUP155 from the nuclear envelope, and recapitulates the NUP155 loss-of-function phenotype: inhibition of HSP70 mRNA export and HSP70 protein nuclear import.\",\n      \"method\": \"Co-immunoprecipitation, GST pull-down, nuclear envelope fractionation, mRNA/protein transport assay\",\n      \"journal\": \"Human Mutation\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and pulldown with functional transport assays, single lab\",\n      \"pmids\": [\"30488537\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Nup155 controls mRNA translation of p21 (CDKN1A) by transcriptionally regulating the putative tRNA/rRNA methyltransferase FTSJ1. Both Nup155 and FTSJ1 are p53 repression targets, placing Nup155 within a regulatory network that links translational control to the p53 pathway.\",\n      \"method\": \"Large-scale proteomics, polysome fractionation, focused RNAi, transcriptional reporter assays in hepatocellular carcinoma cells\",\n      \"journal\": \"Nature Communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (proteomics, polysome fractionation, RNAi) in single lab study\",\n      \"pmids\": [\"31089132\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Loss of Nup155 in podocytes inhibits nuclear export of INO80 mRNA, leading to decreased INO80 protein expression and podocyte senescence. Overexpression of Nup155 or INO80 rescued high fructose-induced senescence. Ferulic acid directly binds Nup155 to stabilize it and enhance its transcription, thereby promoting INO80 mRNA nuclear export.\",\n      \"method\": \"siRNA knockdown, overexpression rescue, qRT-PCR, Western blot, mRNA nuclear export assay, virtual screening/binding, immunofluorescence, transmission electron microscopy\",\n      \"journal\": \"Journal of Advanced Research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — loss-of-function and gain-of-function with defined mRNA export readout, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"39111625\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"NUP155 knockdown in NSCLC cells upregulates PTEN and downregulates phosphorylated AKT without altering total AKT, placing NUP155 upstream of the PTEN/AKT signaling pathway. Pharmacological PTEN inhibition (SF1670) partially reversed the anti-proliferative and pro-apoptotic effects of NUP155 knockdown, establishing epistasis.\",\n      \"method\": \"siRNA knockdown, Western blotting, PTEN inhibitor epistasis, proliferation/migration/invasion/apoptosis assays\",\n      \"journal\": \"Translational Cancer Research\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single epistasis experiment with pharmacological inhibitor, no direct biochemical mechanism established\",\n      \"pmids\": [\"39697746\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"TRIM21 E3 ligase ligands induce ubiquitin-proteasome-dependent degradation of NUP155 (identified as the primary target) and secondarily GLE1 (passenger target upon NUP155 degradation). Degradation of NUP155 and GLE1 impairs nuclear envelope integrity and leads to cell death.\",\n      \"method\": \"DNA-Encoded Library (DEL) screen, crystallography of TRIM21-ligand complex, proteomic profiling, immunofluorescence, proteasome inhibitor rescue\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1-2 / Moderate — crystallographic confirmation of E3 ligase engagement, proteomic identification of NUP155 as primary degradation target, mechanistic rescue experiments; preprint not yet peer-reviewed\",\n      \"pmids\": [\"bio_10.1101_2024.12.03.626577\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"NUP155 is a structurally essential nucleoporin that localizes symmetrically to both faces of the nuclear pore complex; its β-propeller domain anchors it to the NPC via Nup53-dependent recruitment, while its α-solenoid domain independently organizes inner nuclear membrane proteins and binds chromatin at mitotic exit; NUP155 is required for nuclear envelope membrane sealing and NPC assembly during mitosis, and is functionally critical for bidirectional nucleocytoplasmic transport—including Hsp70 mRNA export and Hsp70 protein import—by scaffolding the mRNA export factor GLE1 at the pore; loss-of-function mutations (human R391H) or disruption of its interaction with lamin A/C cause atrial fibrillation through impaired nucleocytoplasmic transport, while NUP155 also participates in translational regulation of p21 via FTSJ1 transcription and in podocyte homeostasis through INO80 mRNA export.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"NUP155 is a structurally essential nucleoporin that localizes symmetrically to both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex (NPC) and disperses to the cytoplasm during mitosis [#0]. It is required for nuclear envelope formation and sealing: its depletion blocks nuclear lamina assembly, nucleoporin accumulation at the nuclear periphery, and formation of a continuous nuclear membrane, and it is recruited to chromatin late in NPC assembly at the time of membrane sealing [#1]. NUP155 is organized into functionally distinct domains—a \\u03b2-propeller that anchors it to the assembling pore through Nup53 (with additional Nup93 contacts), and an \\u03b1-solenoid that independently positions inner nuclear membrane proteins such as LBR and otefin and binds chromatin most strongly at mitotic exit [#4, #5]. At the pore, NUP155 directly binds and anchors the mRNA export factor GLE1 at the nuclear rim, coupling it to the mRNA export machinery [#2]. Through this scaffolding role NUP155 supports bidirectional nucleocytoplasmic transport, including export of HSP70 mRNA and import of HSP70 protein [#3]. Its retention at the nuclear envelope and transport function depend on a direct interaction with lamin A/C [#6]. A homozygous R391H mutation in NUP155 causes atrial fibrillation and early sudden cardiac death by reducing nuclear localization, lowering nuclear envelope permeability, and impairing HSP70 mRNA/protein transport, a phenotype recapitulated by an AF-associated lamin A/C mutation that disrupts the lamin A/C\\u2013NUP155 interaction [#3, #6]. Beyond its transport scaffolding role, NUP155 has been linked to gene-specific outputs, including translational control of p21 via transcriptional regulation of FTSJ1 within the p53 network [#7] and nuclear export of INO80 mRNA in podocyte homeostasis [#8].\",\n  \"teleology\": [\n    {\n      \"year\": 1993,\n      \"claim\": \"Establishing that NUP155 is a bona fide integral NPC component answered where the protein resides and set it apart from peripheral, WGA-reactive nucleoporins.\",\n      \"evidence\": \"Molecular cloning, immunoelectron microscopy, and urea/EDTA fractionation of rat liver nuclear envelopes\",\n      \"pmids\": [\"8458861\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not define molecular partners or assembly determinants\", \"Functional role in transport or assembly not yet addressed\"]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"Identifying GLE1 as a direct NUP155 partner answered how an mRNA export factor is anchored to the pore, linking NUP155 to the mRNA export pathway.\",\n      \"evidence\": \"Yeast two-hybrid screen with in vitro binding, deletion mapping, and HeLa localization\",\n      \"pmids\": [\"14645504\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab; reciprocal in vivo validation limited\", \"Whether GLE1 anchoring fully accounts for NUP155 transport function not resolved\"]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"Depletion across two model systems answered whether NUP155 is required for nuclear envelope and NPC biogenesis, placing it at the late, membrane-sealing step of assembly.\",\n      \"evidence\": \"RNAi in C. elegans, Xenopus egg extract assays, EM, and chromatin-recruitment time course\",\n      \"pmids\": [\"16193066\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular partners mediating chromatin recruitment not defined here\", \"Domain responsible for membrane sealing not mapped\"]\n    },\n    {\n      \"year\": 2008,\n      \"claim\": \"A human R391H mutation and mouse knockout answered whether NUP155 loss causes disease, tying impaired nucleocytoplasmic transport to atrial fibrillation and sudden death.\",\n      \"evidence\": \"Human genetic mapping with co-segregation, mouse knockout, nuclear permeability and HSP70 mRNA/protein transport assays\",\n      \"pmids\": [\"19070573\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Mechanism linking transport defect to cardiac electrophysiology not detailed\", \"Why HSP70 cargo specifically is affected not resolved\"]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Domain dissection answered how NUP155 partitions its jobs, separating NPC anchoring (\\u03b2-propeller) from INM protein organization and chromatin binding (\\u03b1-solenoid).\",\n      \"evidence\": \"Drosophila hypomorphic RNAi, rescue with deletion constructs, binding and chromatin-extract assays\",\n      \"pmids\": [\"22718353\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Chromatin-binding partner not identified\", \"Single lab in Drosophila; human domain equivalence assumed\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Mapping the Nup53\\u2013NUP155 interaction answered how NUP155 is recruited to the assembling pore, identifying Nup53 as the principal recruitment determinant.\",\n      \"evidence\": \"Co-IP, in vitro binding, domain deletion, and Xenopus NPC assembly reconstitution\",\n      \"pmids\": [\"24363447\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Order of recruitment relative to membrane events not fully resolved\", \"Stoichiometry within the assembled pore not defined\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Demonstrating a direct lamin A/C\\u2013NUP155 interaction answered how NUP155 is retained at the nuclear envelope and provided a second genetic route to the AF transport phenotype.\",\n      \"evidence\": \"Co-IP, GST pull-down, NE fractionation, and HSP70 mRNA/protein transport assays with an AF lamin A/C mutant\",\n      \"pmids\": [\"30488537\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single lab; structural basis of the interaction unknown\", \"Whether lamin A/C tethering is direct or via other NPC components not fully separated\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Linking NUP155 to FTSJ1 and p21 translation answered whether NUP155 has gene-regulatory outputs beyond bulk transport, embedding it in the p53 network.\",\n      \"evidence\": \"Proteomics, polysome fractionation, RNAi, and transcriptional reporters in hepatocellular carcinoma cells\",\n      \"pmids\": [\"31089132\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanism by which a nucleoporin transcriptionally regulates FTSJ1 not defined\", \"Generality beyond HCC cells unknown\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"Podocyte studies answered whether NUP155-dependent mRNA export controls cell fate, linking impaired INO80 mRNA export to senescence.\",\n      \"evidence\": \"siRNA, overexpression rescue, mRNA export assays, EM, and ferulic acid binding in podocytes\",\n      \"pmids\": [\"39111625\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Selectivity for INO80 mRNA mechanistically unexplained\", \"Direct ferulic acid binding mode not structurally resolved\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"TRIM21-directed degradation answered whether targeted NUP155 destruction is cytotoxic, with GLE1 lost as a passenger and nuclear envelope integrity collapsing.\",\n      \"evidence\": \"DEL screen, TRIM21-ligand crystallography, proteomics, and proteasome-inhibitor rescue (preprint)\",\n      \"pmids\": [\"bio_10.1101_2024.12.03.626577\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Preprint, not peer-reviewed\", \"Therapeutic window and selectivity not established\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How NUP155 achieves cargo- and transcript-specific outputs (HSP70, INO80 mRNA, FTSJ1/p21) from a structural scaffolding role remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No mechanism connecting NPC scaffolding to selective transcript regulation\", \"Structural model of the human NUP155 \\u03b2-propeller/\\u03b1-solenoid in the assembled pore lacking\", \"Direct chromatin-binding partner of the \\u03b1-solenoid unidentified\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 1, 5]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [2, 4]},\n      {\"term_id\": \"GO:0003677\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005643\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0005635\", \"supporting_discovery_ids\": [0, 1, 6]},\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [2, 3]},\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [2, 3, 8]},\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [1, 5]}\n    ],\n    \"complexes\": [\"nuclear pore complex\"],\n    \"partners\": [\"GLE1\", \"NUP53\", \"NUP93\", \"LMNA\", \"NDC1\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":8,"faith_total":8,"faith_pct":100.0}}