{"gene":"NUP93","run_date":"2026-06-10T05:19:52","timeline":{"discoveries":[{"year":1997,"finding":"Nup93 is a vertebrate homologue of yeast Nic96p and localizes to the nuclear basket and near the nuclear entry of the gated channel by immunofluorescence and immunoelectron microscopy. A small fraction physically interacts with nucleoporin p62 (by immunoprecipitation), while a large fraction forms a stable complex with a newly discovered 205-kDa protein (NUP205) in both mammalian and Xenopus extracts. Immunodepletion of the Nup93 complex from Xenopus nuclear reconstitution extracts caused defective nuclear pore assembly, establishing Nup93 as required for correct NPC assembly.","method":"Immunoprecipitation, immunofluorescence, immunoelectron microscopy, mass spectrometry, Xenopus nuclear reconstitution/immunodepletion assay","journal":"Molecular biology of the cell","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — multiple orthogonal methods (Co-IP, IF, IEM, functional reconstitution/depletion) in a single rigorous study with clear functional readout","pmids":["9348540"],"is_preprint":false},{"year":2003,"finding":"In C. elegans, depletion of Nup93 (or Nup205) by RNAi caused failure in nuclear exclusion of non-nuclear macromolecules of ~70 kDa without preventing active nuclear protein import or nuclear envelope assembly, demonstrating that Nup93 and Nup205 are required for normal NPC size-exclusion function in vivo.","method":"RNAi depletion in C. elegans, in vivo nuclear exclusion assays, nuclear import assays","journal":"Molecular biology of the cell","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean in vivo RNAi with specific functional readouts (exclusion vs. import), replicated for two nucleoporins, C. elegans ortholog","pmids":["12937276"],"is_preprint":false},{"year":2005,"finding":"Human Nup53 physically interacts with Nup93, Nup155, and Nup205 (shown by cell fractionation and in vitro binding). siRNA depletion of Nup53 decreases cellular levels of Nup93, Nup155, Nup205, and Mad1, and severely alters nuclear morphology, positioning Nup93 within a Nup53-anchored NPC subcomplex near the pore membrane and lamina.","method":"Cell fractionation, in vitro binding assays, siRNA knockdown, nuclear morphology analysis","journal":"Molecular biology of the cell","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal functional evidence from both Nup53 and Nup93 depletion, two orthogonal methods (fractionation + in vitro binding), single lab","pmids":["15703211"],"is_preprint":false},{"year":2011,"finding":"The C-terminal domain of Nup93 is necessary and sufficient for assembly of a minimal structural backbone of NPCs, while full-length Nup93 is additionally required for recruitment of the Nup62 complex and establishment of transport-competent NPCs, placing Nup93 as a connector between the structural scaffold and the central transport channel.","method":"Domain truncation analysis, NPC assembly assays, functional transport assays","journal":"Molecular biology of the cell","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — domain mutagenesis combined with functional NPC assembly and transport competence assays, single lab but multiple orthogonal readouts","pmids":["22171326"],"is_preprint":false},{"year":2016,"finding":"NUP93 mutations in SRNS patients disrupt NPC assembly. NUP93 knockdown reduced NUP205 presence in the NPC; reciprocally, a NUP205 alteration abrogated NUP93 interaction. NUP93 and exportin 5 (XPO5) interact with SMAD4, and NUP93 mutations abrogated this interaction and interfered with BMP7-induced SMAD transcriptional reporter activity.","method":"Patient genetics, NPC assembly assays, siRNA knockdown, co-immunoprecipitation, SMAD transcriptional reporter assay","journal":"Nature genetics","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP, functional reporter assay, KD phenotype, and patient mutation data converging on NUP93-NUP205-SMAD4 axis; multiple orthogonal methods","pmids":["26878725"],"is_preprint":false},{"year":2016,"finding":"Nup93, together with its interacting partners Nup188 and Nup205, associates with promoters of HOXA1, HOXA3, and HOXA5 (~1 kb upstream of TSS). Depletion of the Nup93 sub-complex upregulates HOXA gene expression, disengages the HOXA locus from the nuclear periphery, increases active histone marks (H3K9ac), decreases repressive marks (H3K27me3) on HOXA1 promoter, and increases elongation marks (H3K36me3) within HOXA1.","method":"ChIP-on-chip/ChIP, siRNA knockdown, 3D-FISH, histone mark analysis","journal":"Epigenetics & chromatin","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — multiple orthogonal methods (ChIP, FISH, histone marks, expression) in single lab; depletion phenotype with mechanistic follow-up","pmids":["27980680"],"is_preprint":false},{"year":2019,"finding":"Nup93 forms a complex with TBK1 (shown by co-immunoprecipitation), and Nup93 overexpression enhances TBK1-mediated IFNβ promoter activation. Nup93-deficient cells show decreased TBK1 activation and impaired IRF3 nuclear translocation during RLR signaling, placing Nup93 as a positive regulator of antiviral innate immunity upstream of IRF3 nuclear entry.","method":"Co-immunoprecipitation, Nup93-deficient RAW264.7 cells (CRISPR or siRNA), IRF3 nuclear translocation assay, IFNβ promoter reporter assay, viral infection","journal":"Biochemical and biophysical research communications","confidence":"Medium","confidence_rationale":"Tier 2–3 / Moderate — Co-IP plus functional assays (reporter, translocation, KD) in single lab; multiple cell types tested","pmids":["31733835"],"is_preprint":false},{"year":2019,"finding":"SARS-CoV nsp1 expression in HEK cells disrupts Nup93 localization at the nuclear envelope (without triggering proteolytic degradation), while nuclear lamina remains unperturbed, and this is accompanied by altered nuclear-cytoplasmic distribution of the RNA-binding protein nucleolin.","method":"Immunofluorescence, co-immunoprecipitation/affinity purification of nsp1-associated proteins, Western blot","journal":"Biochemistry and cell biology","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — localization disruption shown by IF with functional consequence (nucleolin redistribution); single lab, two orthogonal readouts","pmids":["30943371"],"is_preprint":false},{"year":2019,"finding":"A NUP93 intronic variant (c.2137-18G>A) causes exon 20 skipping, demonstrated by RNA sequencing and in vitro minigene splicing assay. The resulting protein shows aberrant subcellular localization with small punctate vesicles in the cytoplasm rather than normal nuclear envelope distribution.","method":"RNA sequencing, in vitro minigene splicing assay, Western blot, immunofluorescence subcellular localization","journal":"Journal of human genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — two orthogonal methods (RNA-seq + minigene) plus protein localization analysis; single lab","pmids":["31015583"],"is_preprint":false},{"year":2019,"finding":"A NUP93 missense variant p.R537W results in a protein that does not localize to NPCs and cannot functionally replace wild-type NUP93, whereas p.F699L apparently supports NPC assembly, indicating domain-specific requirements for NPC incorporation.","method":"Functional complementation assay, immunofluorescence localization of mutant proteins","journal":"Cerebellum","confidence":"Medium","confidence_rationale":"Tier 2–3 / Weak — complementation and localization assay for two specific variants; single lab, limited methodological detail in abstract","pmids":["30741391"],"is_preprint":false},{"year":2020,"finding":"Nup93 depletion in triple-negative breast cancer cells induces stress fiber formation, reduces cell migration and proliferation, and impairs expression of mesenchymal-like genes. ChIP analysis showed Nup93 chromatin interaction partially modulates expression of genes associated with actin cytoskeleton remodeling (including upregulation of LIMCH1). Silencing LIMCH1 partially restored the invasive phenotype, placing Nup93 upstream of LIMCH1 in actin remodeling.","method":"siRNA knockdown, ChIP, functional invasion/migration assays, gene expression analysis, in vivo tumor assay","journal":"Life science alliance","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis (Nup93→LIMCH1) plus ChIP and multiple functional assays; single lab","pmids":["31959624"],"is_preprint":false},{"year":2021,"finding":"Nup93 and CTCF show overlapping chromatin peaks (ChIP-seq) at the HOXA locus, with Nup93 associated with 3′ and CTCF with 5′ HOXA genes. Nup93 depletion disengages the HOXA locus from the nuclear periphery and upregulates 3′ HOXA genes during differentiation, while CTCF depletion has the opposite effect on 5′ HOXA genes, indicating Nup93 and CTCF antagonistically modulate HOXA expression by tethering versus looping mechanisms.","method":"ChIP sequencing, siRNA knockdown, 3D-FISH, gene expression analysis during differentiation","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — ChIP-seq plus 3D-FISH and expression in a differentiation context; single lab, multiple orthogonal methods","pmids":["34746948"],"is_preprint":false},{"year":2023,"finding":"Knockdown of Nup93 in cardiomyocytes does not affect overall mRNA transport from nucleus to cytoplasm but regulates transcription of many mRNAs (mainly oxidative phosphorylation and ribosome genes). Nup93 directly binds promoters of down-regulated genes including YAP1; overexpression of YAP1 partially rescues the cardiomyocyte death phenotype induced by Nup93 knockdown, placing Nup93-YAP1 transcriptional regulation downstream in hypoxia-induced cardiomyocyte injury.","method":"siRNA knockdown, overexpression, RNA-seq, ChIP (promoter binding), YAP1 rescue experiment","journal":"Acta pharmacologica Sinica","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — RNA-seq plus ChIP plus epistatic rescue; single lab, multiple orthogonal methods","pmids":["36807413"],"is_preprint":false},{"year":2025,"finding":"Loss of NUP93 in mature podocytes (conditional knockout mouse) reduces NPC density, causes cytoplasmic redistribution of podocyte-specific transcription factors (reducing their nuclear abundance), and alters transcriptional programs affecting cell adhesion and actin cytoskeleton regulators, leading to progressive FSGS, podocyte loss, and accumulation of genomic damage activating the DNA damage response.","method":"Conditional knockout mouse (NPHS2-Cre), STED microscopy (NPC density), transcriptomics, proteomics, immunofluorescence","journal":"Journal of the American Society of Nephrology","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — in vivo conditional KO with STED microscopy, transcriptomics, and proteomics providing mechanistic detail; multiple orthogonal methods","pmids":["41563289"],"is_preprint":false},{"year":2025,"finding":"Lycorine specifically interferes with de novo synthesis of Nup93, thereby disrupting nuclear export of influenza viral nucleoprotein (NP), defining Nup93 synthesis as required for NPC-mediated viral NP export during influenza replication.","method":"Time-of-addition assays, viral mRNA/titer measurement, protein expression analysis across multiple cell lines","journal":"International journal of molecular sciences","confidence":"Low","confidence_rationale":"Tier 3 / Weak — pharmacological disruption of Nup93 synthesis inferred; mechanistic link to NP export not directly reconstituted; single lab, limited mechanistic detail in abstract","pmids":["40508167"],"is_preprint":false},{"year":2025,"finding":"Reduction of Nup93 in vascular smooth muscle cells under diabetic atherosclerotic stress impairs nuclear import of splicing regulators SRSF1 and SRSF3, leading to abnormal alternative splicing of SerpinE2, enhancing SerpinE2 mRNA stability and promoting VSMC proliferation.","method":"Spatial proteomics, RNA sequencing, siRNA knockdown, nuclear import assay for SRSF1/SRSF3","journal":"Molecular & cellular proteomics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — spatial proteomics plus RNA-seq plus functional nuclear import mechanistic axis; single lab","pmids":["40633766"],"is_preprint":false},{"year":2026,"finding":"METTL3 localizes at NPCs and functionally associates with NUP93 to promote efficient nuclear export of m6A-modified mRNPs; disruption of METTL3–NUP93 association impairs overall mRNP export efficiency. A disease-associated NUP93 variant (p.Arg388Trp) fails to associate with METTL3, causing defective nuclear export of key methylated mRNAs required for kidney function.","method":"Single-molecule imaging of mRNA export, co-immunoprecipitation/functional association assay, mutant NUP93 analysis","journal":"Nature cell biology","confidence":"High","confidence_rationale":"Tier 1–2 / Strong — single-molecule imaging plus functional association plus disease-variant validation; multiple orthogonal methods in single rigorous study","pmids":["41786887"],"is_preprint":false},{"year":2026,"finding":"NUP93 interacts with transcription factor SOX2 (recognizing its nuclear localization sequence) and facilitates SOX2 nuclear import. Nuclear SOX2 transcriptionally activates G3BP1, which stabilizes RAD51 mRNA to promote DNA damage repair and gemcitabine resistance in pancreatic cancer cells. In vivo disruption of the NUP93/SOX2/G3BP1 axis suppressed tumor growth and synergized with gemcitabine.","method":"Co-immunoprecipitation, nuclear import assay, transcriptional activation assay (ChIP/reporter), mRNA stability assay, in vivo tumor model","journal":"Cell death & disease","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Co-IP plus functional nuclear import plus transcriptional and mRNA stability assays; single lab, multiple orthogonal methods","pmids":["41896201"],"is_preprint":false},{"year":2023,"finding":"Loss of Nup93 in endothelial cells leads to nuclear accumulation of YAP and downstream inflammation; endothelial Nup93 protein levels are reduced in aged mouse vasculature, identifying impaired NPC transport via Nup93 loss as a mechanism for endothelial cell senescence.","method":"In vitro Nup93 knockdown, aged mouse vascular analysis, YAP localization assay, NPC transport assay","journal":"bioRxiv","confidence":"Low","confidence_rationale":"Tier 3 / Weak — preprint, single lab, localization/transport assay with limited mechanistic reconstitution detail in abstract","pmids":["38014013"],"is_preprint":true},{"year":2025,"finding":"Targeted loss of endothelial Nup93 significantly reduces Sun1 protein levels, leading to increased RhoA activity, decreased eNOS expression and NO production, and impaired vasodilatory responses. Restoring Sun1 in Nup93-deficient endothelial cells rescues RhoA activity and eNOS/NO levels, establishing a Nup93→Sun1→RhoA→eNOS signaling axis.","method":"Endothelial-specific Nup93 knockout mice, siRNA knockdown in human ECs, Sun1 rescue experiment, RhoA activity assay, eNOS/NO measurement, vasodilation assay","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vivo KO plus in vitro KD plus epistatic rescue; multiple orthogonal functional assays; preprint, single lab","pmids":["40777343"],"is_preprint":true}],"current_model":"NUP93 is a structural scaffold nucleoporin that forms a conserved complex with NUP205 (and NUP188, NUP53, NUP155) at the inner channel of the NPC, where its C-terminal domain is necessary and sufficient for structural backbone assembly while the full-length protein additionally recruits the NUP62 transport complex; beyond structural roles, NUP93 regulates nuclear exclusion/import selectivity, tethers specific genomic loci (e.g., HOXA) to the nuclear periphery to repress transcription, facilitates nuclear import of transcription factors (SOX2, podocyte TFs) and splicing regulators (SRSF1/3), cooperates with METTL3 to promote m6A-dependent mRNA export, positively regulates antiviral TBK1–IRF3 signaling, and modulates YAP activity and actin cytoskeleton gene expression, with disease-causing mutations disrupting NUP205 interaction, SMAD4 interaction, and METTL3 association."},"narrative":{"mechanistic_narrative":"NUP93 is a scaffold nucleoporin that builds the inner architecture of the nuclear pore complex (NPC) and serves as the structural and functional link between the NPC backbone and the central transport channel [PMID:9348540, PMID:22171326]. It localizes near the gated channel and forms a stable subcomplex with NUP205, NUP188, NUP155, and NUP53, and its C-terminal domain is necessary and sufficient to assemble a minimal structural backbone while full-length NUP93 additionally recruits the NUP62 transport complex to establish transport-competent pores [PMID:9348540, PMID:15703211, PMID:22171326]. NUP93 is required for proper NPC assembly and for the size-exclusion selectivity of the pore, since its depletion causes failure in nuclear exclusion of large macromolecules without abolishing active import [PMID:9348540, PMID:12937276]. Beyond structural roles, NUP93 tethers the HOXA locus to the nuclear periphery, where it antagonizes CTCF to repress HOXA transcription through chromatin association and altered histone marks [PMID:27980680, PMID:34746948], and it directly binds gene promoters to regulate transcriptional programs including YAP1 and actin-cytoskeleton genes such as LIMCH1 [PMID:31959624, PMID:36807413]. NUP93 also governs nuclear import of specific factors — SMAD4 in BMP signaling, the splicing regulators SRSF1/SRSF3, and the transcription factor SOX2 — and cooperates with METTL3 at the NPC to promote nuclear export of m6A-modified mRNPs [PMID:26878725, PMID:40633766, PMID:41786887, PMID:41896201]. NUP93 mutations cause steroid-resistant nephrotic syndrome by disrupting NPC assembly and the NUP205 and SMAD4 interactions, and a disease variant abolishes METTL3 association and m6A-mRNA export required for kidney function [PMID:26878725, PMID:41786887], with conditional knockout in podocytes producing progressive FSGS through loss of NPC density, mislocalization of podocyte transcription factors, and accumulation of genomic damage [PMID:41563289].","teleology":[{"year":1997,"claim":"Established NUP93 as an NPC component required for pore assembly, defining its partnership with NUP205 and the central-channel nucleoporin p62.","evidence":"Co-IP, immunofluorescence/immunoEM, and Xenopus nuclear reconstitution with immunodepletion","pmids":["9348540"],"confidence":"High","gaps":["Did not resolve which domains mediate NUP205 versus p62 binding","Structural arrangement within the pore not determined"]},{"year":2003,"claim":"Showed NUP93 contributes specifically to the NPC's size-exclusion barrier rather than active import, separating its structural function from transport selectivity.","evidence":"RNAi depletion in C. elegans with in vivo exclusion versus import assays","pmids":["12937276"],"confidence":"High","gaps":["Molecular basis of the exclusion defect not defined","Ortholog data may not capture vertebrate-specific roles"]},{"year":2005,"claim":"Placed NUP93 within a NUP53-anchored subcomplex at the pore membrane, defining its stable structural interaction network.","evidence":"Cell fractionation, in vitro binding, and siRNA depletion with nuclear morphology readouts","pmids":["15703211"],"confidence":"High","gaps":["Stoichiometry and direct versus indirect contacts not resolved"]},{"year":2011,"claim":"Defined NUP93 as the connector between the structural scaffold and the transport channel, localizing this function to distinct protein domains.","evidence":"Domain truncation analysis with NPC assembly and transport-competence assays","pmids":["22171326"],"confidence":"High","gaps":["Atomic-resolution interface for NUP62-complex recruitment not determined"]},{"year":2016,"claim":"Connected NUP93 mutations to steroid-resistant nephrotic syndrome and revealed a NUP93–NUP205–SMAD4 axis in BMP signaling, linking pore assembly defects to disease.","evidence":"Patient genetics, reciprocal Co-IP, NPC assembly assays, and SMAD transcriptional reporter","pmids":["26878725"],"confidence":"High","gaps":["How SMAD4 transport defect translates to podocyte pathology not fully traced","Whether XPO5 role is direct unresolved"]},{"year":2016,"claim":"Demonstrated a non-structural gene-regulatory role: NUP93 and its partners tether the HOXA locus to the periphery to repress transcription via chromatin marks.","evidence":"ChIP, 3D-FISH, histone mark analysis, and siRNA depletion","pmids":["27980680"],"confidence":"Medium","gaps":["Direct DNA contact versus bridging by other factors not distinguished","Mechanism linking tethering to histone-mark changes unclear"]},{"year":2019,"claim":"Identified NUP93 as a positive regulator of antiviral signaling acting on TBK1–IRF3 nuclear translocation, extending its role to innate immunity.","evidence":"Co-IP, NUP93-deficient macrophages, IRF3 translocation, and IFNβ reporter assays","pmids":["31733835"],"confidence":"Medium","gaps":["Whether NUP93 acts via transport or direct TBK1 scaffolding not resolved","Single lab"]},{"year":2019,"claim":"Showed viral nsp1 and disease-associated splice/missense variants disrupt NUP93 localization, linking proper NPC incorporation to specific sequence requirements.","evidence":"Immunofluorescence, minigene splicing, complementation, and Co-IP across separate studies","pmids":["30943371","31015583","30741391"],"confidence":"Medium","gaps":["Functional consequences of mislocalization at the cellular level limited","Domain-specific assembly requirements only partially mapped"]},{"year":2020,"claim":"Placed NUP93 chromatin binding upstream of actin-cytoskeleton remodeling via LIMCH1 regulation, linking it to cancer cell invasion.","evidence":"siRNA knockdown, ChIP, invasion/migration assays, and in vivo tumor model with LIMCH1 epistasis","pmids":["31959624"],"confidence":"Medium","gaps":["Direct versus indirect promoter regulation unclear","Generalizability beyond TNBC untested"]},{"year":2021,"claim":"Refined the HOXA model by showing NUP93 and CTCF antagonistically regulate HOXA via tethering versus looping during differentiation.","evidence":"ChIP-seq, 3D-FISH, and expression analysis during differentiation","pmids":["34746948"],"confidence":"Medium","gaps":["Mechanistic interplay between tethering and looping not reconstituted"]},{"year":2023,"claim":"Showed NUP93 directly regulates transcription of metabolic and YAP1 genes in cardiomyocytes independent of bulk mRNA transport, defining a transcriptional protective role under hypoxia.","evidence":"siRNA knockdown, RNA-seq, ChIP, and YAP1 rescue experiment","pmids":["36807413"],"confidence":"Medium","gaps":["How promoter binding controls these genes mechanistically unclear","Relationship to NUP93 transport function not addressed"]},{"year":2025,"claim":"Established NUP93 as required for nuclear import of splicing regulators SRSF1/SRSF3, linking its loss to aberrant SerpinE2 splicing and VSMC proliferation.","evidence":"Spatial proteomics, RNA-seq, siRNA, and nuclear import assays","pmids":["40633766"],"confidence":"Medium","gaps":["Whether NUP93 selectively imports SRSF factors or acts globally unclear","Single disease-stress context"]},{"year":2025,"claim":"Demonstrated in vivo that podocyte NUP93 maintains NPC density, transcription-factor nuclear localization, and genome integrity, defining the cellular basis of NUP93-linked FSGS.","evidence":"Conditional knockout mouse, STED microscopy, transcriptomics, and proteomics","pmids":["41563289"],"confidence":"High","gaps":["Specific transcription factors driving FSGS not individually validated","Source of genomic damage not mechanistically defined"]},{"year":2026,"claim":"Revealed a NUP93–METTL3 partnership at the NPC driving m6A-mRNA export, and showed a disease variant abolishes this association, unifying RNA export with NUP93 nephropathy.","evidence":"Single-molecule mRNA export imaging, functional association assay, and mutant NUP93 analysis","pmids":["41786887"],"confidence":"High","gaps":["How NUP93 physically couples METTL3 to export machinery not resolved"]},{"year":2026,"claim":"Defined NUP93 as an import factor for SOX2, driving a SOX2/G3BP1/RAD51 axis underlying DNA repair and chemoresistance in pancreatic cancer.","evidence":"Co-IP, nuclear import assay, transcriptional/mRNA-stability assays, and in vivo tumor model","pmids":["41896201"],"confidence":"Medium","gaps":["NLS-recognition mechanism by NUP93 not structurally defined","Specificity over other NLS-bearing cargoes unclear"]},{"year":null,"claim":"How NUP93 mechanistically partitions between its structural scaffold role, selective cargo import, m6A-mRNA export, and direct chromatin-based transcriptional regulation across different tissues remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No unified structural model linking transport and gene-regulatory functions","Cargo-selectivity determinants for SMAD4/SRSF/SOX2 import undefined","Whether chromatin tethering requires assembled NPCs untested"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0,3]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[3,4,15,17]},{"term_id":"GO:0140110","term_label":"transcription regulator activity","supporting_discovery_ids":[5,10,12]}],"localization":[{"term_id":"GO:0005635","term_label":"nuclear envelope","supporting_discovery_ids":[0,7,8]},{"term_id":"GO:0005634","term_label":"nucleus","supporting_discovery_ids":[5,11]}],"pathway":[{"term_id":"R-HSA-9609507","term_label":"Protein localization","supporting_discovery_ids":[0,1,3]},{"term_id":"R-HSA-8953854","term_label":"Metabolism of RNA","supporting_discovery_ids":[16,15]},{"term_id":"R-HSA-74160","term_label":"Gene expression (Transcription)","supporting_discovery_ids":[5,11,12]},{"term_id":"R-HSA-1643685","term_label":"Disease","supporting_discovery_ids":[4,13,16]}],"complexes":["NPC inner-ring NUP93–NUP205–NUP188–NUP155–NUP53 subcomplex","NUP62 transport complex (recruited)"],"partners":["NUP205","NUP53","NUP155","NUP188","NUP62","SMAD4","METTL3","SOX2"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8N1F7","full_name":"Nuclear pore complex protein Nup93","aliases":["93 kDa nucleoporin","Nucleoporin Nup93"],"length_aa":819,"mass_kda":93.5,"function":"Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:9348540). May anchor nucleoporins, but not NUP153 and TPR, to the NPC. During renal development, regulates podocyte migration and proliferation through SMAD4 signaling (PubMed:26878725)","subcellular_location":"Nucleus membrane; Nucleus, nuclear pore complex; Nucleus envelope","url":"https://www.uniprot.org/uniprotkb/Q8N1F7/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":true,"resolved_as":"","url":"https://depmap.org/portal/gene/NUP93","classification":"Common Essential","n_dependent_lines":1208,"n_total_lines":1208,"dependency_fraction":1.0},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"NUP214","stoichiometry":10.0},{"gene":"CLIP1","stoichiometry":0.2},{"gene":"KPNB1","stoichiometry":0.2},{"gene":"NUMA1","stoichiometry":0.2},{"gene":"NUTF2","stoichiometry":0.2},{"gene":"RAB11A","stoichiometry":0.2},{"gene":"RAN","stoichiometry":0.2},{"gene":"RANBP1","stoichiometry":0.2},{"gene":"RBM14","stoichiometry":0.2},{"gene":"XPO1","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/NUP93","total_profiled":1310},"omim":[{"mim_id":"616893","title":"NEPHROTIC SYNDROME, TYPE 13; NPHS13","url":"https://www.omim.org/entry/616893"},{"mim_id":"616892","title":"NEPHROTIC SYNDROME, TYPE 12; NPHS12","url":"https://www.omim.org/entry/616892"},{"mim_id":"615587","title":"NUCLEOPORIN, 188-KD; NUP188","url":"https://www.omim.org/entry/615587"},{"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"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/NUP93"},"hgnc":{"alias_symbol":["KIAA0095"],"prev_symbol":[]},"alphafold":{"accession":"Q8N1F7","domains":[{"cath_id":"-","chopping":"278-436","consensus_level":"high","plddt":84.196,"start":278,"end":436},{"cath_id":"1.20.5","chopping":"100-150","consensus_level":"medium","plddt":79.7943,"start":100,"end":150},{"cath_id":"1.20.58","chopping":"735-819","consensus_level":"medium","plddt":72.2576,"start":735,"end":819}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N1F7","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N1F7-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8N1F7-F1-predicted_aligned_error_v6.png","plddt_mean":79.88},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=NUP93","jax_strain_url":"https://www.jax.org/strain/search?query=NUP93"},"sequence":{"accession":"Q8N1F7","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8N1F7.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8N1F7/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8N1F7"}},"corpus_meta":[{"pmid":"26878725","id":"PMC_26878725","title":"Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-resistant nephrotic syndrome.","date":"2016","source":"Nature genetics","url":"https://pubmed.ncbi.nlm.nih.gov/26878725","citation_count":160,"is_preprint":false},{"pmid":"12937276","id":"PMC_12937276","title":"Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit of nuclear pore complex size exclusion in vivo.","date":"2003","source":"Molecular biology of the cell","url":"https://pubmed.ncbi.nlm.nih.gov/12937276","citation_count":159,"is_preprint":false},{"pmid":"9348540","id":"PMC_9348540","title":"Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly.","date":"1997","source":"Molecular biology of the cell","url":"https://pubmed.ncbi.nlm.nih.gov/9348540","citation_count":135,"is_preprint":false},{"pmid":"15703211","id":"PMC_15703211","title":"Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex.","date":"2005","source":"Molecular biology of the cell","url":"https://pubmed.ncbi.nlm.nih.gov/15703211","citation_count":113,"is_preprint":false},{"pmid":"22171326","id":"PMC_22171326","title":"The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes.","date":"2011","source":"Molecular biology of the cell","url":"https://pubmed.ncbi.nlm.nih.gov/22171326","citation_count":60,"is_preprint":false},{"pmid":"24572986","id":"PMC_24572986","title":"The diverse roles of the Nup93/Nic96 complex proteins - structural scaffolds of the nuclear pore complex with additional cellular functions.","date":"2014","source":"Biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/24572986","citation_count":49,"is_preprint":false},{"pmid":"30943371","id":"PMC_30943371","title":"SARS coronavirus protein nsp1 disrupts localization of Nup93 from the nuclear pore complex.","date":"2019","source":"Biochemistry and cell biology = Biochimie et biologie cellulaire","url":"https://pubmed.ncbi.nlm.nih.gov/30943371","citation_count":47,"is_preprint":false},{"pmid":"27980680","id":"PMC_27980680","title":"HOXA repression is mediated by nucleoporin Nup93 assisted by its interactors Nup188 and Nup205.","date":"2016","source":"Epigenetics & chromatin","url":"https://pubmed.ncbi.nlm.nih.gov/27980680","citation_count":44,"is_preprint":false},{"pmid":"29869118","id":"PMC_29869118","title":"Genetic diagnosis of steroid-resistant nephrotic syndrome in a longitudinal collection of Czech and Slovak patients: a high proportion of causative variants in NUP93.","date":"2018","source":"Pediatric nephrology (Berlin, Germany)","url":"https://pubmed.ncbi.nlm.nih.gov/29869118","citation_count":44,"is_preprint":false},{"pmid":"31959624","id":"PMC_31959624","title":"Nup93 regulates breast tumor growth by modulating cell proliferation and actin cytoskeleton remodeling.","date":"2020","source":"Life science alliance","url":"https://pubmed.ncbi.nlm.nih.gov/31959624","citation_count":39,"is_preprint":false},{"pmid":"31517150","id":"PMC_31517150","title":"In Vivo Expression of NUP93 and Its Alteration by NUP93 Mutations Causing Focal Segmental Glomerulosclerosis.","date":"2019","source":"Kidney international reports","url":"https://pubmed.ncbi.nlm.nih.gov/31517150","citation_count":22,"is_preprint":false},{"pmid":"31015583","id":"PMC_31015583","title":"Molecular assay for an intronic variant in NUP93 that causes steroid resistant nephrotic syndrome.","date":"2019","source":"Journal of human genetics","url":"https://pubmed.ncbi.nlm.nih.gov/31015583","citation_count":18,"is_preprint":false},{"pmid":"31733835","id":"PMC_31733835","title":"Identification of nucleoporin 93 (Nup93) that mediates antiviral innate immune responses.","date":"2019","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/31733835","citation_count":17,"is_preprint":false},{"pmid":"31774908","id":"PMC_31774908","title":"Expression of Nup93 is associated with the proliferation, migration and invasion capacity of cervical cancer cells.","date":"2019","source":"Acta biochimica et biophysica Sinica","url":"https://pubmed.ncbi.nlm.nih.gov/31774908","citation_count":17,"is_preprint":false},{"pmid":"35211795","id":"PMC_35211795","title":"Exploring the relevance of NUP93 variants in steroid-resistant nephrotic syndrome using next generation sequencing and a fly kidney model.","date":"2022","source":"Pediatric nephrology (Berlin, Germany)","url":"https://pubmed.ncbi.nlm.nih.gov/35211795","citation_count":16,"is_preprint":false},{"pmid":"34746948","id":"PMC_34746948","title":"Nup93 and CTCF modulate spatiotemporal dynamics and function of the HOXA gene locus during differentiation.","date":"2021","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/34746948","citation_count":15,"is_preprint":false},{"pmid":"36807413","id":"PMC_36807413","title":"Downregulation of NUP93 aggravates hypoxia-induced death of cardiomyocytes in vitro through abnormal regulation of gene transcription.","date":"2023","source":"Acta pharmacologica Sinica","url":"https://pubmed.ncbi.nlm.nih.gov/36807413","citation_count":15,"is_preprint":false},{"pmid":"30741391","id":"PMC_30741391","title":"Biallelic Variants in the Nuclear Pore Complex Protein NUP93 Are Associated with Non-progressive Congenital Ataxia.","date":"2019","source":"Cerebellum (London, England)","url":"https://pubmed.ncbi.nlm.nih.gov/30741391","citation_count":14,"is_preprint":false},{"pmid":"30577294","id":"PMC_30577294","title":"First Report of Recurrent Nephrotic Syndrome After Kidney Transplantation in a Patient With NUP93 Gene Mutations: A Case Report.","date":"2018","source":"Transplantation proceedings","url":"https://pubmed.ncbi.nlm.nih.gov/30577294","citation_count":14,"is_preprint":false},{"pmid":"31315584","id":"PMC_31315584","title":"Identification of novel mutations and phenotype in the steroid resistant nephrotic syndrome gene NUP93: a case report.","date":"2019","source":"BMC nephrology","url":"https://pubmed.ncbi.nlm.nih.gov/31315584","citation_count":12,"is_preprint":false},{"pmid":"33578576","id":"PMC_33578576","title":"Steroid-resistant nephrotic syndrome in infants caused by a novel compound heterozygous mutation of the NUP93: A CARE case report.","date":"2021","source":"Medicine","url":"https://pubmed.ncbi.nlm.nih.gov/33578576","citation_count":12,"is_preprint":false},{"pmid":"35874595","id":"PMC_35874595","title":"Collapsing Focal Segmental Glomerulosclerosis in Siblings With Compound Heterozygous Variants in NUP93 Expand the Spectrum of Kidney Phenotypes Associated With Nucleoporin Gene Mutations.","date":"2022","source":"Frontiers in pediatrics","url":"https://pubmed.ncbi.nlm.nih.gov/35874595","citation_count":9,"is_preprint":false},{"pmid":"30001865","id":"PMC_30001865","title":"Visceral leishmaniasis: A novel nuclear envelope protein 'nucleoporins-93 (NUP-93)' from Leishmania donovani prompts macrophage signaling for T-cell activation towards host protective immune response.","date":"2018","source":"Cytokine","url":"https://pubmed.ncbi.nlm.nih.gov/30001865","citation_count":8,"is_preprint":false},{"pmid":"38650033","id":"PMC_38650033","title":"Mutations in the NUP93, NUP107 and NUP160 genes cause steroid-resistant nephrotic syndrome in Chinese children.","date":"2024","source":"Italian journal of pediatrics","url":"https://pubmed.ncbi.nlm.nih.gov/38650033","citation_count":7,"is_preprint":false},{"pmid":"37762751","id":"PMC_37762751","title":"Steroid-Resistant Nephrotic Syndrome Caused by NUP93 Pathogenic Variants.","date":"2023","source":"Journal of clinical medicine","url":"https://pubmed.ncbi.nlm.nih.gov/37762751","citation_count":5,"is_preprint":false},{"pmid":"34815884","id":"PMC_34815884","title":"End-stage renal disease in a child with focal segmental glomerulosclerosis associated with a homozygous NUP93 variant.","date":"2021","source":"Clinical case reports","url":"https://pubmed.ncbi.nlm.nih.gov/34815884","citation_count":5,"is_preprint":false},{"pmid":"40508167","id":"PMC_40508167","title":"Lycorine Inhibits Influenza Virus Replication by Affecting Nascent Nucleoporin Nup93 Synthesis.","date":"2025","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/40508167","citation_count":3,"is_preprint":false},{"pmid":"41786887","id":"PMC_41786887","title":"N6-adenosine methylation enhances nuclear mRNA export through METTL3 and NUP93.","date":"2026","source":"Nature cell biology","url":"https://pubmed.ncbi.nlm.nih.gov/41786887","citation_count":2,"is_preprint":false},{"pmid":"40633766","id":"PMC_40633766","title":"Nup93-Mediated RNA Alternative Splicing Associated With Diabetic Atherosclerosis.","date":"2025","source":"Molecular & cellular proteomics : MCP","url":"https://pubmed.ncbi.nlm.nih.gov/40633766","citation_count":2,"is_preprint":false},{"pmid":"16450586","id":"PMC_16450586","title":"Molecular cloning of the rice field eel Nup93 with predominant expression in gonad and kidney.","date":"2006","source":"Yi chuan xue bao = Acta genetica Sinica","url":"https://pubmed.ncbi.nlm.nih.gov/16450586","citation_count":2,"is_preprint":false},{"pmid":"38014013","id":"PMC_38014013","title":"Nucleoporin93 (Nup93) Limits Yap Activity to Prevent Endothelial Cell Senescence.","date":"2023","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/38014013","citation_count":1,"is_preprint":false},{"pmid":"41563289","id":"PMC_41563289","title":"Mechanisms of Podocyte Injury Due to Loss of the Nucleoporin NUP93.","date":"2025","source":"Journal of the American Society of Nephrology : JASN","url":"https://pubmed.ncbi.nlm.nih.gov/41563289","citation_count":1,"is_preprint":false},{"pmid":"40777343","id":"PMC_40777343","title":"Endothelial Nucleoporin93 (Nup93) Maintains Vascular Function via Sun1-Dependent Regulation of RhoA-eNOS Signaling.","date":"2025","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/40777343","citation_count":1,"is_preprint":false},{"pmid":"30835075","id":"PMC_30835075","title":"Correction to: Biallelic Variants in the Nuclear Pore Complex Protein NUP93 Are Associated with Non-progressive Congenital Ataxia.","date":"2019","source":"Cerebellum (London, England)","url":"https://pubmed.ncbi.nlm.nih.gov/30835075","citation_count":1,"is_preprint":false},{"pmid":"40407330","id":"PMC_40407330","title":"Viral polymerase-host interaction analysis reveals that the association between avian NUP93 and PB1 promotes H5N6 avian influenza virus replication.","date":"2025","source":"Microbiology spectrum","url":"https://pubmed.ncbi.nlm.nih.gov/40407330","citation_count":0,"is_preprint":false},{"pmid":"41129286","id":"PMC_41129286","title":"Black carp Nup93 negatively regulates IRF3- and IRF7-mediated antiviral immune response.","date":"2026","source":"Journal of immunology (Baltimore, Md. : 1950)","url":"https://pubmed.ncbi.nlm.nih.gov/41129286","citation_count":0,"is_preprint":false},{"pmid":"41209161","id":"PMC_41209161","title":"Adult-Onset Nephrotic Syndrome and Optic Nerve Atrophy Associated With NUP93 Mutation.","date":"2025","source":"Kidney medicine","url":"https://pubmed.ncbi.nlm.nih.gov/41209161","citation_count":0,"is_preprint":false},{"pmid":"41896201","id":"PMC_41896201","title":"NUP93 facilitates the nuclear import of SOX2 to activate G3BP1 transcription and impairs gemcitabine response in pancreatic cancer.","date":"2026","source":"Cell death & disease","url":"https://pubmed.ncbi.nlm.nih.gov/41896201","citation_count":0,"is_preprint":false},{"pmid":null,"id":"bio_10.1101_2025.05.05.652162","title":"CRISPR-Cas9 HDR Optimization: RAD52, Denatured and 5’-Modified DNA Templates in Knock-In Mice Generation","date":"2025-05-07","source":"bioRxiv","url":"https://doi.org/10.1101/2025.05.05.652162","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.09.16.613305","title":"Interphase chromosome conformation is specified by distinct folding programs inherited via mitotic chromosomes or through the cytoplasm","date":"2024-09-16","source":"bioRxiv","url":"https://doi.org/10.1101/2024.09.16.613305","citation_count":0,"is_preprint":true},{"pmid":null,"id":"bio_10.1101_2024.08.01.24310552","title":"NXT2 is the key player for nuclear RNA export in the human testis and critical for spermatogenesis","date":"2024-08-02","source":"bioRxiv","url":"https://doi.org/10.1101/2024.08.01.24310552","citation_count":0,"is_preprint":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":21071,"output_tokens":5231,"usd":0.070839,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":13624,"output_tokens":4435,"usd":0.089497,"stage2_stop_reason":"end_turn"},"total_usd":0.160336,"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\": 1997,\n      \"finding\": \"Nup93 is a vertebrate homologue of yeast Nic96p and localizes to the nuclear basket and near the nuclear entry of the gated channel by immunofluorescence and immunoelectron microscopy. A small fraction physically interacts with nucleoporin p62 (by immunoprecipitation), while a large fraction forms a stable complex with a newly discovered 205-kDa protein (NUP205) in both mammalian and Xenopus extracts. Immunodepletion of the Nup93 complex from Xenopus nuclear reconstitution extracts caused defective nuclear pore assembly, establishing Nup93 as required for correct NPC assembly.\",\n      \"method\": \"Immunoprecipitation, immunofluorescence, immunoelectron microscopy, mass spectrometry, Xenopus nuclear reconstitution/immunodepletion assay\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — multiple orthogonal methods (Co-IP, IF, IEM, functional reconstitution/depletion) in a single rigorous study with clear functional readout\",\n      \"pmids\": [\"9348540\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2003,\n      \"finding\": \"In C. elegans, depletion of Nup93 (or Nup205) by RNAi caused failure in nuclear exclusion of non-nuclear macromolecules of ~70 kDa without preventing active nuclear protein import or nuclear envelope assembly, demonstrating that Nup93 and Nup205 are required for normal NPC size-exclusion function in vivo.\",\n      \"method\": \"RNAi depletion in C. elegans, in vivo nuclear exclusion assays, nuclear import assays\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean in vivo RNAi with specific functional readouts (exclusion vs. import), replicated for two nucleoporins, C. elegans ortholog\",\n      \"pmids\": [\"12937276\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2005,\n      \"finding\": \"Human Nup53 physically interacts with Nup93, Nup155, and Nup205 (shown by cell fractionation and in vitro binding). siRNA depletion of Nup53 decreases cellular levels of Nup93, Nup155, Nup205, and Mad1, and severely alters nuclear morphology, positioning Nup93 within a Nup53-anchored NPC subcomplex near the pore membrane and lamina.\",\n      \"method\": \"Cell fractionation, in vitro binding assays, siRNA knockdown, nuclear morphology analysis\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal functional evidence from both Nup53 and Nup93 depletion, two orthogonal methods (fractionation + in vitro binding), single lab\",\n      \"pmids\": [\"15703211\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"The C-terminal domain of Nup93 is necessary and sufficient for assembly of a minimal structural backbone of NPCs, while full-length Nup93 is additionally required for recruitment of the Nup62 complex and establishment of transport-competent NPCs, placing Nup93 as a connector between the structural scaffold and the central transport channel.\",\n      \"method\": \"Domain truncation analysis, NPC assembly assays, functional transport assays\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — domain mutagenesis combined with functional NPC assembly and transport competence assays, single lab but multiple orthogonal readouts\",\n      \"pmids\": [\"22171326\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"NUP93 mutations in SRNS patients disrupt NPC assembly. NUP93 knockdown reduced NUP205 presence in the NPC; reciprocally, a NUP205 alteration abrogated NUP93 interaction. NUP93 and exportin 5 (XPO5) interact with SMAD4, and NUP93 mutations abrogated this interaction and interfered with BMP7-induced SMAD transcriptional reporter activity.\",\n      \"method\": \"Patient genetics, NPC assembly assays, siRNA knockdown, co-immunoprecipitation, SMAD transcriptional reporter assay\",\n      \"journal\": \"Nature genetics\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP, functional reporter assay, KD phenotype, and patient mutation data converging on NUP93-NUP205-SMAD4 axis; multiple orthogonal methods\",\n      \"pmids\": [\"26878725\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Nup93, together with its interacting partners Nup188 and Nup205, associates with promoters of HOXA1, HOXA3, and HOXA5 (~1 kb upstream of TSS). Depletion of the Nup93 sub-complex upregulates HOXA gene expression, disengages the HOXA locus from the nuclear periphery, increases active histone marks (H3K9ac), decreases repressive marks (H3K27me3) on HOXA1 promoter, and increases elongation marks (H3K36me3) within HOXA1.\",\n      \"method\": \"ChIP-on-chip/ChIP, siRNA knockdown, 3D-FISH, histone mark analysis\",\n      \"journal\": \"Epigenetics & chromatin\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — multiple orthogonal methods (ChIP, FISH, histone marks, expression) in single lab; depletion phenotype with mechanistic follow-up\",\n      \"pmids\": [\"27980680\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Nup93 forms a complex with TBK1 (shown by co-immunoprecipitation), and Nup93 overexpression enhances TBK1-mediated IFNβ promoter activation. Nup93-deficient cells show decreased TBK1 activation and impaired IRF3 nuclear translocation during RLR signaling, placing Nup93 as a positive regulator of antiviral innate immunity upstream of IRF3 nuclear entry.\",\n      \"method\": \"Co-immunoprecipitation, Nup93-deficient RAW264.7 cells (CRISPR or siRNA), IRF3 nuclear translocation assay, IFNβ promoter reporter assay, viral infection\",\n      \"journal\": \"Biochemical and biophysical research communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Moderate — Co-IP plus functional assays (reporter, translocation, KD) in single lab; multiple cell types tested\",\n      \"pmids\": [\"31733835\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"SARS-CoV nsp1 expression in HEK cells disrupts Nup93 localization at the nuclear envelope (without triggering proteolytic degradation), while nuclear lamina remains unperturbed, and this is accompanied by altered nuclear-cytoplasmic distribution of the RNA-binding protein nucleolin.\",\n      \"method\": \"Immunofluorescence, co-immunoprecipitation/affinity purification of nsp1-associated proteins, Western blot\",\n      \"journal\": \"Biochemistry and cell biology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — localization disruption shown by IF with functional consequence (nucleolin redistribution); single lab, two orthogonal readouts\",\n      \"pmids\": [\"30943371\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"A NUP93 intronic variant (c.2137-18G>A) causes exon 20 skipping, demonstrated by RNA sequencing and in vitro minigene splicing assay. The resulting protein shows aberrant subcellular localization with small punctate vesicles in the cytoplasm rather than normal nuclear envelope distribution.\",\n      \"method\": \"RNA sequencing, in vitro minigene splicing assay, Western blot, immunofluorescence subcellular localization\",\n      \"journal\": \"Journal of human genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — two orthogonal methods (RNA-seq + minigene) plus protein localization analysis; single lab\",\n      \"pmids\": [\"31015583\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"A NUP93 missense variant p.R537W results in a protein that does not localize to NPCs and cannot functionally replace wild-type NUP93, whereas p.F699L apparently supports NPC assembly, indicating domain-specific requirements for NPC incorporation.\",\n      \"method\": \"Functional complementation assay, immunofluorescence localization of mutant proteins\",\n      \"journal\": \"Cerebellum\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2–3 / Weak — complementation and localization assay for two specific variants; single lab, limited methodological detail in abstract\",\n      \"pmids\": [\"30741391\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Nup93 depletion in triple-negative breast cancer cells induces stress fiber formation, reduces cell migration and proliferation, and impairs expression of mesenchymal-like genes. ChIP analysis showed Nup93 chromatin interaction partially modulates expression of genes associated with actin cytoskeleton remodeling (including upregulation of LIMCH1). Silencing LIMCH1 partially restored the invasive phenotype, placing Nup93 upstream of LIMCH1 in actin remodeling.\",\n      \"method\": \"siRNA knockdown, ChIP, functional invasion/migration assays, gene expression analysis, in vivo tumor assay\",\n      \"journal\": \"Life science alliance\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis (Nup93→LIMCH1) plus ChIP and multiple functional assays; single lab\",\n      \"pmids\": [\"31959624\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Nup93 and CTCF show overlapping chromatin peaks (ChIP-seq) at the HOXA locus, with Nup93 associated with 3′ and CTCF with 5′ HOXA genes. Nup93 depletion disengages the HOXA locus from the nuclear periphery and upregulates 3′ HOXA genes during differentiation, while CTCF depletion has the opposite effect on 5′ HOXA genes, indicating Nup93 and CTCF antagonistically modulate HOXA expression by tethering versus looping mechanisms.\",\n      \"method\": \"ChIP sequencing, siRNA knockdown, 3D-FISH, gene expression analysis during differentiation\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — ChIP-seq plus 3D-FISH and expression in a differentiation context; single lab, multiple orthogonal methods\",\n      \"pmids\": [\"34746948\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Knockdown of Nup93 in cardiomyocytes does not affect overall mRNA transport from nucleus to cytoplasm but regulates transcription of many mRNAs (mainly oxidative phosphorylation and ribosome genes). Nup93 directly binds promoters of down-regulated genes including YAP1; overexpression of YAP1 partially rescues the cardiomyocyte death phenotype induced by Nup93 knockdown, placing Nup93-YAP1 transcriptional regulation downstream in hypoxia-induced cardiomyocyte injury.\",\n      \"method\": \"siRNA knockdown, overexpression, RNA-seq, ChIP (promoter binding), YAP1 rescue experiment\",\n      \"journal\": \"Acta pharmacologica Sinica\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — RNA-seq plus ChIP plus epistatic rescue; single lab, multiple orthogonal methods\",\n      \"pmids\": [\"36807413\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Loss of NUP93 in mature podocytes (conditional knockout mouse) reduces NPC density, causes cytoplasmic redistribution of podocyte-specific transcription factors (reducing their nuclear abundance), and alters transcriptional programs affecting cell adhesion and actin cytoskeleton regulators, leading to progressive FSGS, podocyte loss, and accumulation of genomic damage activating the DNA damage response.\",\n      \"method\": \"Conditional knockout mouse (NPHS2-Cre), STED microscopy (NPC density), transcriptomics, proteomics, immunofluorescence\",\n      \"journal\": \"Journal of the American Society of Nephrology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — in vivo conditional KO with STED microscopy, transcriptomics, and proteomics providing mechanistic detail; multiple orthogonal methods\",\n      \"pmids\": [\"41563289\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Lycorine specifically interferes with de novo synthesis of Nup93, thereby disrupting nuclear export of influenza viral nucleoprotein (NP), defining Nup93 synthesis as required for NPC-mediated viral NP export during influenza replication.\",\n      \"method\": \"Time-of-addition assays, viral mRNA/titer measurement, protein expression analysis across multiple cell lines\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — pharmacological disruption of Nup93 synthesis inferred; mechanistic link to NP export not directly reconstituted; single lab, limited mechanistic detail in abstract\",\n      \"pmids\": [\"40508167\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Reduction of Nup93 in vascular smooth muscle cells under diabetic atherosclerotic stress impairs nuclear import of splicing regulators SRSF1 and SRSF3, leading to abnormal alternative splicing of SerpinE2, enhancing SerpinE2 mRNA stability and promoting VSMC proliferation.\",\n      \"method\": \"Spatial proteomics, RNA sequencing, siRNA knockdown, nuclear import assay for SRSF1/SRSF3\",\n      \"journal\": \"Molecular & cellular proteomics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — spatial proteomics plus RNA-seq plus functional nuclear import mechanistic axis; single lab\",\n      \"pmids\": [\"40633766\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"METTL3 localizes at NPCs and functionally associates with NUP93 to promote efficient nuclear export of m6A-modified mRNPs; disruption of METTL3–NUP93 association impairs overall mRNP export efficiency. A disease-associated NUP93 variant (p.Arg388Trp) fails to associate with METTL3, causing defective nuclear export of key methylated mRNAs required for kidney function.\",\n      \"method\": \"Single-molecule imaging of mRNA export, co-immunoprecipitation/functional association assay, mutant NUP93 analysis\",\n      \"journal\": \"Nature cell biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Strong — single-molecule imaging plus functional association plus disease-variant validation; multiple orthogonal methods in single rigorous study\",\n      \"pmids\": [\"41786887\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"NUP93 interacts with transcription factor SOX2 (recognizing its nuclear localization sequence) and facilitates SOX2 nuclear import. Nuclear SOX2 transcriptionally activates G3BP1, which stabilizes RAD51 mRNA to promote DNA damage repair and gemcitabine resistance in pancreatic cancer cells. In vivo disruption of the NUP93/SOX2/G3BP1 axis suppressed tumor growth and synergized with gemcitabine.\",\n      \"method\": \"Co-immunoprecipitation, nuclear import assay, transcriptional activation assay (ChIP/reporter), mRNA stability assay, in vivo tumor model\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Co-IP plus functional nuclear import plus transcriptional and mRNA stability assays; single lab, multiple orthogonal methods\",\n      \"pmids\": [\"41896201\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Loss of Nup93 in endothelial cells leads to nuclear accumulation of YAP and downstream inflammation; endothelial Nup93 protein levels are reduced in aged mouse vasculature, identifying impaired NPC transport via Nup93 loss as a mechanism for endothelial cell senescence.\",\n      \"method\": \"In vitro Nup93 knockdown, aged mouse vascular analysis, YAP localization assay, NPC transport assay\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — preprint, single lab, localization/transport assay with limited mechanistic reconstitution detail in abstract\",\n      \"pmids\": [\"38014013\"],\n      \"is_preprint\": true\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Targeted loss of endothelial Nup93 significantly reduces Sun1 protein levels, leading to increased RhoA activity, decreased eNOS expression and NO production, and impaired vasodilatory responses. Restoring Sun1 in Nup93-deficient endothelial cells rescues RhoA activity and eNOS/NO levels, establishing a Nup93→Sun1→RhoA→eNOS signaling axis.\",\n      \"method\": \"Endothelial-specific Nup93 knockout mice, siRNA knockdown in human ECs, Sun1 rescue experiment, RhoA activity assay, eNOS/NO measurement, vasodilation assay\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vivo KO plus in vitro KD plus epistatic rescue; multiple orthogonal functional assays; preprint, single lab\",\n      \"pmids\": [\"40777343\"],\n      \"is_preprint\": true\n    }\n  ],\n  \"current_model\": \"NUP93 is a structural scaffold nucleoporin that forms a conserved complex with NUP205 (and NUP188, NUP53, NUP155) at the inner channel of the NPC, where its C-terminal domain is necessary and sufficient for structural backbone assembly while the full-length protein additionally recruits the NUP62 transport complex; beyond structural roles, NUP93 regulates nuclear exclusion/import selectivity, tethers specific genomic loci (e.g., HOXA) to the nuclear periphery to repress transcription, facilitates nuclear import of transcription factors (SOX2, podocyte TFs) and splicing regulators (SRSF1/3), cooperates with METTL3 to promote m6A-dependent mRNA export, positively regulates antiviral TBK1–IRF3 signaling, and modulates YAP activity and actin cytoskeleton gene expression, with disease-causing mutations disrupting NUP205 interaction, SMAD4 interaction, and METTL3 association.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"NUP93 is a scaffold nucleoporin that builds the inner architecture of the nuclear pore complex (NPC) and serves as the structural and functional link between the NPC backbone and the central transport channel [#0, #3]. It localizes near the gated channel and forms a stable subcomplex with NUP205, NUP188, NUP155, and NUP53, and its C-terminal domain is necessary and sufficient to assemble a minimal structural backbone while full-length NUP93 additionally recruits the NUP62 transport complex to establish transport-competent pores [#0, #2, #3]. NUP93 is required for proper NPC assembly and for the size-exclusion selectivity of the pore, since its depletion causes failure in nuclear exclusion of large macromolecules without abolishing active import [#0, #1]. Beyond structural roles, NUP93 tethers the HOXA locus to the nuclear periphery, where it antagonizes CTCF to repress HOXA transcription through chromatin association and altered histone marks [#5, #11], and it directly binds gene promoters to regulate transcriptional programs including YAP1 and actin-cytoskeleton genes such as LIMCH1 [#10, #12]. NUP93 also governs nuclear import of specific factors — SMAD4 in BMP signaling, the splicing regulators SRSF1/SRSF3, and the transcription factor SOX2 — and cooperates with METTL3 at the NPC to promote nuclear export of m6A-modified mRNPs [#4, #15, #16, #17]. NUP93 mutations cause steroid-resistant nephrotic syndrome by disrupting NPC assembly and the NUP205 and SMAD4 interactions, and a disease variant abolishes METTL3 association and m6A-mRNA export required for kidney function [#4, #16], with conditional knockout in podocytes producing progressive FSGS through loss of NPC density, mislocalization of podocyte transcription factors, and accumulation of genomic damage [#13].\"\n,\n  \"teleology\": [\n    {\n      \"year\": 1997,\n      \"claim\": \"Established NUP93 as an NPC component required for pore assembly, defining its partnership with NUP205 and the central-channel nucleoporin p62.\",\n      \"evidence\": \"Co-IP, immunofluorescence/immunoEM, and Xenopus nuclear reconstitution with immunodepletion\",\n      \"pmids\": [\"9348540\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Did not resolve which domains mediate NUP205 versus p62 binding\", \"Structural arrangement within the pore not determined\"]\n    },\n    {\n      \"year\": 2003,\n      \"claim\": \"Showed NUP93 contributes specifically to the NPC's size-exclusion barrier rather than active import, separating its structural function from transport selectivity.\",\n      \"evidence\": \"RNAi depletion in C. elegans with in vivo exclusion versus import assays\",\n      \"pmids\": [\"12937276\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular basis of the exclusion defect not defined\", \"Ortholog data may not capture vertebrate-specific roles\"]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"Placed NUP93 within a NUP53-anchored subcomplex at the pore membrane, defining its stable structural interaction network.\",\n      \"evidence\": \"Cell fractionation, in vitro binding, and siRNA depletion with nuclear morphology readouts\",\n      \"pmids\": [\"15703211\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Stoichiometry and direct versus indirect contacts not resolved\"]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"Defined NUP93 as the connector between the structural scaffold and the transport channel, localizing this function to distinct protein domains.\",\n      \"evidence\": \"Domain truncation analysis with NPC assembly and transport-competence assays\",\n      \"pmids\": [\"22171326\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Atomic-resolution interface for NUP62-complex recruitment not determined\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Connected NUP93 mutations to steroid-resistant nephrotic syndrome and revealed a NUP93\\u2013NUP205\\u2013SMAD4 axis in BMP signaling, linking pore assembly defects to disease.\",\n      \"evidence\": \"Patient genetics, reciprocal Co-IP, NPC assembly assays, and SMAD transcriptional reporter\",\n      \"pmids\": [\"26878725\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How SMAD4 transport defect translates to podocyte pathology not fully traced\", \"Whether XPO5 role is direct unresolved\"]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Demonstrated a non-structural gene-regulatory role: NUP93 and its partners tether the HOXA locus to the periphery to repress transcription via chromatin marks.\",\n      \"evidence\": \"ChIP, 3D-FISH, histone mark analysis, and siRNA depletion\",\n      \"pmids\": [\"27980680\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct DNA contact versus bridging by other factors not distinguished\", \"Mechanism linking tethering to histone-mark changes unclear\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Identified NUP93 as a positive regulator of antiviral signaling acting on TBK1\\u2013IRF3 nuclear translocation, extending its role to innate immunity.\",\n      \"evidence\": \"Co-IP, NUP93-deficient macrophages, IRF3 translocation, and IFN\\u03b2 reporter assays\",\n      \"pmids\": [\"31733835\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether NUP93 acts via transport or direct TBK1 scaffolding not resolved\", \"Single lab\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Showed viral nsp1 and disease-associated splice/missense variants disrupt NUP93 localization, linking proper NPC incorporation to specific sequence requirements.\",\n      \"evidence\": \"Immunofluorescence, minigene splicing, complementation, and Co-IP across separate studies\",\n      \"pmids\": [\"30943371\", \"31015583\", \"30741391\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional consequences of mislocalization at the cellular level limited\", \"Domain-specific assembly requirements only partially mapped\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Placed NUP93 chromatin binding upstream of actin-cytoskeleton remodeling via LIMCH1 regulation, linking it to cancer cell invasion.\",\n      \"evidence\": \"siRNA knockdown, ChIP, invasion/migration assays, and in vivo tumor model with LIMCH1 epistasis\",\n      \"pmids\": [\"31959624\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct versus indirect promoter regulation unclear\", \"Generalizability beyond TNBC untested\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Refined the HOXA model by showing NUP93 and CTCF antagonistically regulate HOXA via tethering versus looping during differentiation.\",\n      \"evidence\": \"ChIP-seq, 3D-FISH, and expression analysis during differentiation\",\n      \"pmids\": [\"34746948\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Mechanistic interplay between tethering and looping not reconstituted\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Showed NUP93 directly regulates transcription of metabolic and YAP1 genes in cardiomyocytes independent of bulk mRNA transport, defining a transcriptional protective role under hypoxia.\",\n      \"evidence\": \"siRNA knockdown, RNA-seq, ChIP, and YAP1 rescue experiment\",\n      \"pmids\": [\"36807413\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"How promoter binding controls these genes mechanistically unclear\", \"Relationship to NUP93 transport function not addressed\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Established NUP93 as required for nuclear import of splicing regulators SRSF1/SRSF3, linking its loss to aberrant SerpinE2 splicing and VSMC proliferation.\",\n      \"evidence\": \"Spatial proteomics, RNA-seq, siRNA, and nuclear import assays\",\n      \"pmids\": [\"40633766\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether NUP93 selectively imports SRSF factors or acts globally unclear\", \"Single disease-stress context\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Demonstrated in vivo that podocyte NUP93 maintains NPC density, transcription-factor nuclear localization, and genome integrity, defining the cellular basis of NUP93-linked FSGS.\",\n      \"evidence\": \"Conditional knockout mouse, STED microscopy, transcriptomics, and proteomics\",\n      \"pmids\": [\"41563289\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Specific transcription factors driving FSGS not individually validated\", \"Source of genomic damage not mechanistically defined\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Revealed a NUP93\\u2013METTL3 partnership at the NPC driving m6A-mRNA export, and showed a disease variant abolishes this association, unifying RNA export with NUP93 nephropathy.\",\n      \"evidence\": \"Single-molecule mRNA export imaging, functional association assay, and mutant NUP93 analysis\",\n      \"pmids\": [\"41786887\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"How NUP93 physically couples METTL3 to export machinery not resolved\"]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Defined NUP93 as an import factor for SOX2, driving a SOX2/G3BP1/RAD51 axis underlying DNA repair and chemoresistance in pancreatic cancer.\",\n      \"evidence\": \"Co-IP, nuclear import assay, transcriptional/mRNA-stability assays, and in vivo tumor model\",\n      \"pmids\": [\"41896201\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"NLS-recognition mechanism by NUP93 not structurally defined\", \"Specificity over other NLS-bearing cargoes unclear\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How NUP93 mechanistically partitions between its structural scaffold role, selective cargo import, m6A-mRNA export, and direct chromatin-based transcriptional regulation across different tissues remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No unified structural model linking transport and gene-regulatory functions\", \"Cargo-selectivity determinants for SMAD4/SRSF/SOX2 import undefined\", \"Whether chromatin tethering requires assembled NPCs untested\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [3, 4, 15, 17]},\n      {\"term_id\": \"GO:0140110\", \"supporting_discovery_ids\": [5, 10, 12]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005643\", \"supporting_discovery_ids\": [0, 2, 3]},\n      {\"term_id\": \"GO:0005635\", \"supporting_discovery_ids\": [0, 7, 8]},\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [5, 11]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-9609507\", \"supporting_discovery_ids\": [0, 1, 3]},\n      {\"term_id\": \"R-HSA-8953854\", \"supporting_discovery_ids\": [16, 15]},\n      {\"term_id\": \"R-HSA-74160\", \"supporting_discovery_ids\": [5, 11, 12]},\n      {\"term_id\": \"R-HSA-1643685\", \"supporting_discovery_ids\": [4, 13, 16]}\n    ],\n    \"complexes\": [\"NPC inner-ring NUP93\\u2013NUP205\\u2013NUP188\\u2013NUP155\\u2013NUP53 subcomplex\", \"NUP62 transport complex (recruited)\"],\n    \"partners\": [\"NUP205\", \"NUP53\", \"NUP155\", \"NUP188\", \"NUP62\", \"SMAD4\", \"METTL3\", \"SOX2\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"tie","faith_supported":6,"faith_total":6,"faith_pct":100.0}}