Affinage

NUP210

Nuclear pore membrane glycoprotein 210 · UniProt Q8TEM1

Length
1887 aa
Mass
205.1 kDa
Annotated
2026-06-10
44 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NUP210 (gp210) is a single-pass transmembrane nucleoporin that anchors in the pore membrane of the nuclear envelope and contributes to nuclear pore complex (NPC) assembly, nuclear envelope dynamics, and mechanosensing (PMID:1281815, PMID:14517331). Its single transmembrane segment is sufficient for sorting to the pore membrane domain, while its massive luminal/cisternal domain carries no localization information, and it assembles into SDS-resistant dimers and higher-order oligomers distributed with eightfold radial symmetry around the NPC ring (PMID:1281815, PMID:11453980, PMID:22389396). The cytoplasmic C-terminal tail drives nuclear pore dilation and NPC maturation, with its loss arresting assembly at 'mini-pore' intermediates that fail to incorporate downstream nucleoporins; depletion is lethal and produces clustered NPCs and aberrant nuclear membranes across human cells and C. elegans (PMID:12093788, PMID:14517331). Cell-cycle control operates through this tail: cyclin B-cdc2 phosphorylates Ser1880 during mitosis, and a phosphomimetic substitution blocks NPC incorporation, coupling NUP210 to NPC disassembly and nuclear envelope breakdown (PMID:8672508, PMID:17559836, PMID:18216332). Independently of its NPC role, the conserved N-terminal luminal domain maintains nuclear envelope/ER homeostasis and is sufficient to drive muscle cell differentiation by limiting ER-stress apoptosis, and NUP210 is required for neural fate reprogramming via SoxB1 activation (PMID:25778917, PMID:30067988). At the nuclear periphery NUP210 acts as a mechanosensor, bridging the LINC component SUN2 to chromatin through the short isoform of BRD4 and histones H3.1/H3.2, such that its loss drives PRC2-dependent H3K27me3 accumulation and repositioning of mechanosensitive genes, and an endogenous tension biosensor confirms that gp210 itself bears mechanical force (PMID:34903738, PMID:40463170). NUP210 also engages importin-α/β to regulate nucleoplasmic transport and NPC density and modulates late steps of HIV-1 nuclear entry and proviral integration (PMID:39393532, PMID:40202922).

Mechanistic history

Synthesis pass · year-by-year structured walk · 21 steps
  1. 1992 High

    Established which part of gp210 directs it to the nuclear pore, answering how a large luminal protein is targeted to the pore membrane domain.

    Evidence cDNA mutagenesis and chimeric protein expression with immunofluorescence in 3T3 cells

    PMID:1281815

    Open questions at the time
    • Does not define the luminal domain's function
    • Mechanism of the weaker cytoplasmic-tail sorting determinant unresolved
  2. 1996 High

    Identified Ser1880 in the cytoplasmic tail as a mitosis-specific phosphosite, linking gp210 to cell-cycle-regulated kinase activity.

    Evidence In vitro kinase assays with mutant fusion proteins, phosphopeptide mapping, cell cycle fractionation

    PMID:8672508

    Open questions at the time
    • Kinase identity inferred but not directly proven in this study
    • Functional consequence of phosphorylation not yet shown
  3. 2001 High

    Showed gp210 self-associates into stable dimers and oligomers, indicating it is an oligomeric building block at the pore membrane.

    Evidence Immunoprecipitation, velocity sedimentation, gel filtration, and crosslinking from rat liver nuclear envelopes

    PMID:11453980

    Open questions at the time
    • Stoichiometry and interface of oligomers undefined
    • Whether oligomerization is regulated unknown
  4. 2002 High

    Demonstrated the cytoplasmic tail is required for nuclear pore dilation and NPC assembly, placing gp210 at a defined step of pore maturation.

    Evidence Xenopus nuclear assembly extract with recombinant peptide and antibody inhibition, EM and immunofluorescence

    PMID:12093788

    Open questions at the time
    • Direct partners mediating dilation not identified
    • How the tail couples to membrane curvature unknown
  5. 2003 Medium

    Characterized the disordered, PII-rich conformation of the cytoplasmic domain around the Ser1880 SPXX motif, providing structural context for its regulation.

    Evidence CD, FTIR, and fluorescence spectroscopy on recombinant C-terminal domain

    PMID:12653556

    Open questions at the time
    • No functional mutagenesis in this study
    • Conformational changes shown only under non-physiological perturbations (TFE, pH)
  6. 2003 High

    Established that gp210 loss is lethal and disrupts NPC and nuclear membrane structure across species, defining it as essential and evolutionarily conserved.

    Evidence RNAi in HeLa cells and C. elegans with EM and immunofluorescence

    PMID:14517331

    Open questions at the time
    • Does not separate NPC-assembly role from membrane-homeostasis role
    • Molecular cause of NPC clustering unresolved
  7. 2004 Medium

    Refined the assembly model by showing gp210 is dispensable for POM121 and NUP107 incorporation and NPC stability, narrowing its mechanistic role.

    Evidence FRAP and immunofluorescence in gp210-deficient NIH/3T3 cells

    PMID:15304359

    Open questions at the time
    • Negative finding in one cell model
    • Does not identify which nucleoporins depend on gp210
  8. 2006 High

    Revealed functional redundancy between gp210 and POM121 for membrane anchorage of NPCs, implying additional integral nucleoporins exist.

    Evidence siRNA double knockdown and ectopic assembly assays in HeLa and human fibroblasts

    PMID:16702234

    Open questions at the time
    • Identity of the inferred additional integral nucleoporins not established here
    • Conditions where gp210 is non-redundant undefined
  9. 2008 High

    Connected Ser1880 phosphorylation status to NPC retention, showing mitotic phosphorylation dissociates gp210 from the pore.

    Evidence S1880A/S1880E mutagenesis with live imaging and FRAP

    PMID:17559836

    Open questions at the time
    • Does not identify the phosphatase reversing the modification
    • Single cell system
  10. 2008 High

    Established gp210 as required for nuclear envelope breakdown and linked its hyperphosphorylation to cyclin B-cdc2 via genetic epistasis.

    Evidence RNAi and antibody inhibition in C. elegans embryos with cyclin B depletion epistasis

    PMID:18216332

    Open questions at the time
    • Direct demonstration of cdc2 acting on Ser1880 in vivo not shown
    • How NEBD failure causes nuclear twinning mechanistically unclear
  11. 2012 High

    Positioned gp210 spatially at each of the eight NPC subunits, anchoring structural models of its arrangement around the pore.

    Evidence dSTORM super-resolution imaging of Xenopus oocyte nuclear envelopes

    PMID:22389396

    Open questions at the time
    • Copy number per spoke not quantified
    • Does not address dynamics or conformational state
  12. 2015 High

    Uncovered an NPC-independent function: the luminal N-terminal domain drives muscle differentiation by maintaining ER/NE homeostasis and limiting ER-stress apoptosis.

    Evidence Domain-deletion mutagenesis, C2C12 differentiation, caspase assays, and ER-stress inhibitor rescue

    PMID:25778917

    Open questions at the time
    • Luminal-domain binding partners unidentified
    • Molecular trigger of ER stress upon depletion unknown
  13. 2018 Medium

    Extended the differentiation role to neural fate, showing Nup210 acts upstream of SoxB1 transcription factors during reprogramming.

    Evidence Knockdown/overexpression during chemical reprogramming with transcriptome/epigenome analysis and growth factor epistasis

    PMID:30067988

    Open questions at the time
    • Direct versus indirect activation of SoxB1 not resolved
    • Single lab
  14. 2021 High

    Defined NUP210 as a mechanosensor coupling the LINC complex (SUN2) to chromatin through BRD4 and H3.1/H3.2, regulating PRC2 heterochromatin and gene positioning.

    Evidence Reciprocal Co-IP, H3K27me3 ChIP-seq, DNA FISH, focal adhesion assays, and mouse metastasis models in Nup210-knockout cells

    PMID:34903738

    Open questions at the time
    • How a luminal/membrane nucleoporin physically reaches chromatin not fully resolved
    • Direct versus indirect SUN2-BRD4 bridging unclear
  15. 2021 Medium

    Tested the muscle role in vivo, showing Nup210 is dispensable for muscle formation but required for repair, fiber-type balance, and endurance.

    Evidence Nup210 knockout mouse with injury/repair, histology, and voluntary running assays

    PMID:34911810

    Open questions at the time
    • Reconciliation with the essential C2C12 differentiation phenotype incomplete
    • Cell-autonomous versus systemic effects unresolved
  16. 2022 Medium

    Linked BRD4 to NUP210 expression in cancer, with NUP210 controlling nuclear size and cell growth.

    Evidence BRD4 inhibitor treatment, NUP210 siRNA, nuclear size and growth assays in colorectal cancer cells

    PMID:35159127

    Open questions at the time
    • Mechanism linking NUP210 to nuclear size not defined
    • Single lab
  17. 2024 Medium

    Showed NUP210 uses NLS-dependent localization and importin-α/β binding to regulate nucleoplasmic transport and NPC density.

    Evidence NLS mutagenesis, importin Co-IP, NPC density and transport assays, xenografts in CRC cells

    PMID:39393532

    Open questions at the time
    • Mechanistic depth limited
    • Relationship to canonical transmembrane targeting unclear
  18. 2025 Medium

    Provided direct evidence that gp210 bears mechanical force, identifying nuclear strain as the predominant force source at the NPC.

    Evidence CRISPR knock-in FRET tension biosensor with osmotic and pharmacological perturbations (preprint)

    PMID:40463170

    Open questions at the time
    • Preprint, single lab
    • Functional consequence of gp210 tension not established
  19. 2025 Medium

    Implicated Nup210 in late HIV-1 nuclear entry/integration and viral mRNA splicing, with Vpr as a potential antagonist.

    Evidence Knockdown/overexpression, qPCR for viral intermediates, integrase inhibitor epistasis, viral mRNA RT-qPCR

    PMID:40202922

    Open questions at the time
    • Direct interaction with viral or host integration machinery not shown
    • Mechanism of splicing regulation undefined
  20. 2026 Medium

    Identified TMEM209 as a transmembrane nucleoporin that binds Nup210 and controls its retention at the nuclear envelope.

    Evidence Proximity labeling, Co-IP, immunofluorescence, depletion/overexpression with cell cycle analysis

    PMID:41582553

    Open questions at the time
    • Functional consequence of Nup210 dissociation by TMEM209 unclear
    • Single lab
  21. 2026 Medium

    Placed NUP210 downstream of m6A regulation, with METTL3 stabilizing NUP210 mRNA to promote cancer metastasis.

    Evidence MeRIP, RIP, mRNA stability and rescue assays, transwell and in vivo metastasis models in prostate cancer

    PMID:41775163

    Open questions at the time
    • Direct m6A site mapping not detailed
    • Single lab

Open questions

Synthesis pass · forward-looking unresolved questions
  • How NUP210's distinct domains coordinate its NPC-assembly, ER/NE-homeostasis, mechanosensing, and transport-regulatory functions within a single protein remains unresolved.
  • No structure integrating luminal, transmembrane, and cytoplasmic domains
  • Luminal-domain interactome unidentified
  • Mechanism coupling membrane anchorage to chromatin regulation undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 4 GO:0140299 molecular sensor activity 2 GO:0060090 molecular adaptor activity 1
Localization
GO:0005635 nuclear envelope 3 GO:0005783 endoplasmic reticulum 1
Pathway
R-HSA-1640170 Cell Cycle 3 R-HSA-1266738 Developmental Biology 2 R-HSA-9609507 Protein localization 2 R-HSA-4839726 Chromatin organization 1
Partners
BRD4H3.1/H3.2IMPORTIN-ΑIMPORTIN-ΒPOM121SUN2TMEM209
Complex memberships
LINC complex (via SUN2)nuclear pore complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1992 The single transmembrane segment (TM) of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope, as demonstrated by expression of wild-type, mutant, and chimeric gp210 constructs in 3T3 cells; the cytoplasmic tail (CT) also contains a weaker sorting determinant. The large cisternal domain (95% of gp210's mass) contains no sorting determinants. cDNA mutagenesis, chimeric protein expression, immunofluorescence microscopy in 3T3 cells The Journal of cell biology High 1281815
1996 Gp210 is specifically phosphorylated during mitosis (not in interphase) at Ser1880 in its cytoplasmic tail, consistent with phosphorylation by cyclin B-p34cdc2 or a related kinase, as determined by cell cycle-specific phosphorylation assays and in vitro phosphorylation mapping of mutant fusion proteins containing the cytoplasmic domain. In vitro kinase assay with mutant and wild-type fusion proteins, phosphopeptide mapping, cell cycle fractionation Biochemistry High 8672508
2001 Gp210 forms SDS-resistant dimers and larger oligomers in the nuclear pore membrane, as shown by immunoprecipitation from cell extracts and velocity sedimentation/gel filtration from purified rat liver nuclear envelopes; cross-linking prior to solubilization dramatically increased the proportion of dimers. Immunoprecipitation, velocity sedimentation, gel filtration, cross-linking, denaturing electrophoresis European journal of biochemistry High 11453980
2002 The cytoplasmic tail of gp210 is required for nuclear pore dilation and NPC assembly: adding recombinant tail polypeptides or anti-tail antibodies to Xenopus nuclear assembly extracts blocked NPC assembly and nuclear growth without affecting membrane fusion, and inhibited nuclei failed to incorporate Nup214/CAN, Nup153, and Nup98. EM revealed arrested 'mini-pore' structures and a lack of 'closely apposed' inner and outer nuclear membranes. Xenopus nuclear assembly extract assay, recombinant protein addition, antibody inhibition, scanning and transmission EM, immunofluorescence The Journal of cell biology High 12093788
2003 The C-terminal domain (CTD) of human gp210 adopts a largely unordered conformation with significant polyproline type II (PII) helical structure in solution; the conformation is altered by high pH, charged detergents, and TFE, and TFE induces a conformational change around the SPXX motif containing Ser1880 (the mitotically phosphorylated serine). Solution NMR/spectroscopy (circular dichroism, FTIR, fluorescence), biochemical structure determination of recombinant CTD Biochemistry Medium 12653556
2003 RNAi-mediated depletion of gp210 in HeLa cells is lethal and causes accumulation of clustered NPCs and aberrant nuclear membrane structures, indicating gp210 is required for nuclear pore formation/dilation and structural integrity of NPCs. In C. elegans, gp210 RNAi causes embryonic lethality with similar nuclear membrane aberrations, demonstrating evolutionary conservation of function. RNAi knockdown in HeLa cells and C. elegans, electron microscopy, immunofluorescence Molecular biology of the cell High 14517331
2004 In NIH/3T3 cells lacking gp210, POM121 and NUP107 are correctly distributed at nuclear pores and remain stably associated as assessed by FRAP, indicating that gp210 is not required for incorporation of POM121 or NUP107 or for maintaining NPC stability. FRAP, immunofluorescence in gp210-deficient NIH/3T3 cells FEBS letters Medium 15304359
2006 POM121 can recruit nucleoporins (Nup62, Nup358) to ectopic assembly sites and acts as a nucleation site for NPC substructures. Double knockdown of gp210 and POM121 in HeLa cells, and depletion of POM121 in human fibroblasts (which do not express gp210), still permits functional NPC assembly, indicating extensive redundancy and that additional membrane-integral nucleoporins exist for NE anchorage. siRNA double knockdown in HeLa cells, functional NPC assay, ectopic assembly site assay The Journal of cell biology High 16702234
2007 Phosphomimetic substitution S1880E of gp210 specifically interferes with incorporation of gp210 into NPCs and compromises its post-mitotic recruitment to daughter nuclei, while the alanine substitution S1880A makes gp210 more dynamic at the NPC (faster FRAP), suggesting that mitotic phosphorylation at Ser1880 acts to dissociate gp210 from the NPC. Site-directed mutagenesis (S1880A, S1880E), live cell imaging, time-lapse microscopy, FRAP Experimental cell research High 17559836
2008 Gp210 is required for nuclear envelope breakdown (NEBD) in mitosis: RNAi depletion or mutation of C. elegans gp210 prevents lamin depolymerization and causes nuclear twinning after mitosis. Anti-gp210 C-terminal tail antibodies added to in vitro assembled nuclei completely blocked NEBD and inhibited mitotic hyperphosphorylation of gp210. Depletion of cyclin B from C. elegans embryos also causes nuclear twinning, consistent with cyclin B-cdc2 being the relevant kinase. RNAi in C. elegans embryos, in vitro nuclear assembly antibody inhibition, cyclin B depletion epistasis Journal of cell science High 18216332
2012 Super-resolution dSTORM imaging of isolated Xenopus laevis oocyte nuclear envelopes demonstrates that gp210 is distributed with eightfold radial symmetry around the NPC, placing it at each of the eight subunits of the NPC ring; the central NPC channel diameter was determined to be 41 ± 7 nm. Direct stochastic optical reconstruction microscopy (dSTORM), super-resolution imaging of Xenopus oocyte nuclear envelopes Journal of cell science High 22389396
2015 Gp210/Nup210 mediates muscle cell differentiation via its conserved N-terminal luminal domain; the C-terminal domain (which targets gp210 to NPCs) is dispensable and a mutant lacking both the transmembrane and C-terminal domains is sufficient for C2C12 myoblast differentiation. ER stress-specific caspase cascade is exacerbated during Nup210 depletion, and blocking ER stress-mediated apoptosis rescues differentiation of Nup210-deficient cells, indicating the luminal domain maintains nuclear envelope/ER homeostasis. Domain deletion mutagenesis, C2C12 myoblast differentiation assay, caspase activity assay, ER stress inhibitor rescue, knockdown/rescue experiments The Journal of cell biology High 25778917
2018 Nup210 is required during chemical reprogramming of mouse fibroblasts into neural stem cells (NSCs): Nup210 activates SoxB1 transcription factors to initiate NSC fate, and its activity is required for both chemical cocktail- and growth factor (IL-6, FGF5, LIF)-driven reprogramming. Nup210 knockdown/overexpression during chemical reprogramming, transcriptome and epigenome analysis, growth factor treatment experiments Cell reports Medium 30067988
2021 NUP210 interacts with LINC complex protein SUN2 (connecting nucleus to cytoskeleton), and the NUP210/SUN2 complex further interacts with chromatin via the short isoform of BRD4 and histone H3.1/H3.2 at the nuclear periphery. Nup210 depletion causes accumulation of H3K27me3 heterochromatin (mediated by PRC2) at mechanosensitive genes, repositioning of these genes within the nucleus, and defective mechanotransduction and focal adhesion. Co-immunoprecipitation (NUP210-SUN2, NUP210-BRD4 interactions), ChIP-seq (H3K27me3), DNA FISH (gene repositioning), focal adhesion assays, mouse metastasis models, Nup210 knockout cells Nature communications High 34903738
2021 Ablation of Nup210 in mice does not prevent skeletal muscle formation or growth, but Nup210 knockout mice show delayed muscle repair after injury, increased centrally nucleated fibers with age, abnormal fiber type distribution, and reduced muscle endurance during voluntary running. Nup210 knockout mouse model, muscle injury/repair assay, histology, voluntary running assay Life science alliance Medium 34911810
2022 NUP210 expression is driven by BRD4 in colorectal cancer cells; BRD4 inhibition by ACP-1n reduces NUP210 levels and decreases nuclear size, and NUP210 silencing alone is sufficient to decrease nucleus size and cellular growth. BRD4 inhibitor treatment, NUP210 siRNA knockdown, nuclear size measurement, cell growth assay, phase separation assay Cells Medium 35159127
2024 Nup210 requires nuclear localization sequences (NLS) to localize to the nuclear membrane surface and interacts with importin-α/β, thereby regulating nucleoplasmic transport capacity and NPC density on CRC cell surfaces; Nup210 knockdown reduces nuclear size, NPC density, and nucleoplasmic transport. Nup210 knockdown, NLS mutagenesis, co-immunoprecipitation (importin-α/β), NPC density measurement, nuclear transport assay, in vivo xenograft Laboratory investigation Medium 39393532
2025 A FRET-based tension biosensor inserted into gp210 (at endogenous levels via CRISPR knock-in) reveals that gp210 and the NPC experience mechanical tension. Forces on gp210 increase with osmotically induced nuclear swelling and are influenced by ECM stiffness, the LINC complex, chromatin condensation, and actomyosin contractility; chromatin relaxation and MLCK inhibition increase gp210 forces, suggesting nuclear strain (rather than cytoskeletal forces) is the predominant source of NPC forces. FRET-force biosensor (TSmod), CRISPR knock-in at endogenous locus, osmotic swelling, pharmacological perturbations, live cell imaging bioRxivpreprint Medium 40463170
2025 Nup210 knockdown promotes HIV-1 infection by increasing accumulation of integrated proviral DNA, while levels of reverse transcription products and 2-LTR circles (nuclear entry intermediates) are unaffected, indicating Nup210 acts at late steps of viral nuclear entry (post-nuclear entry, affecting integration). Nup210 also regulates viral mRNA alternative splicing; knockdown increases singly spliced Vpr mRNA, and elevated Vpr may act as a viral antagonist of Nup210. Nup210 knockdown/overexpression, luciferase infectivity assay, qPCR for RT products/2-LTR circles/integrated DNA, RT-qPCR for viral mRNA species, Raltegravir integrase inhibitor epistasis AIDS Medium 40202922
2026 TMEM209 is a fourth transmembrane nucleoporin that biochemically interacts with Nup210 via a region containing its two transmembrane domains; TMEM209 localizes to NPCs by proximity labeling and immunofluorescence, and overexpression of TMEM209 specifically dissociates Nup210 from the nuclear envelope. TMEM209 depletion impairs cell growth and delays S, G2 and M phase entry. Proximity labeling, co-immunoprecipitation, immunofluorescence, siRNA depletion, overexpression, cell cycle analysis Journal of cell science Medium 41582553
2026 METTL3-mediated N6-methyladenosine (m6A) modification stabilizes NUP210 mRNA; METTL3 silencing reduces NUP210 expression, and NUP210 overexpression reverses the inhibitory effects of METTL3 silencing on prostate cancer cell metastasis and EMT in vitro and in vivo. MeRIP (m6A-IP), RNA-binding protein immunoprecipitation (RIP), mRNA stability assay, rescue experiments, transwell assay, in vivo metastasis model Mutation research Medium 41775163

Source papers

Stage 0 corpus · 44 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Super-resolution imaging visualizes the eightfold symmetry of gp210 proteins around the nuclear pore complex and resolves the central channel with nanometer resolution. Journal of cell science 226 22389396
1996 Cell cycle-dependent phosphorylation of nucleoporins and nuclear pore membrane protein Gp210. Biochemistry 131 8672508
1992 The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope. The Journal of cell biology 108 1281815
1996 Specificity and sensitivity of gp210 autoantibodies detected using an enzyme-linked immunosorbent assay and a synthetic polypeptide in the diagnosis of primary biliary cirrhosis. Hepatology (Baltimore, Md.) 89 8621127
1993 Autoantibodies from patients with primary biliary cirrhosis recognize a restricted region within the cytoplasmic tail of nuclear pore membrane glycoprotein Gp210. The Journal of experimental medicine 76 7504063
2008 A role for gp210 in mitotic nuclear-envelope breakdown. Journal of cell science 67 18216332
2006 Nuclear pore complex assembly and maintenance in POM121- and gp210-deficient cells. The Journal of cell biology 61 16702234
2003 Nuclear pore protein gp210 is essential for viability in HeLa cells and Caenorhabditis elegans. Molecular biology of the cell 51 14517331
2021 Nuclear pore protein NUP210 depletion suppresses metastasis through heterochromatin-mediated disruption of tumor cell mechanical response. Nature communications 50 34903738
1995 Autoantibodies from patients with primary biliary cirrhosis preferentially react with the amino-terminal domain of nuclear pore complex glycoprotein gp210. The Journal of experimental medicine 49 7561689
2015 The nucleoporin gp210/Nup210 controls muscle differentiation by regulating nuclear envelope/ER homeostasis. The Journal of cell biology 48 25778917
2002 Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation. The Journal of cell biology 48 12093788
2005 Increased expression of nuclear envelope gp210 antigen in small bile ducts in primary biliary cirrhosis. Journal of autoimmunity 41 16337775
2009 The nuclear pore complex protein ALADIN is anchored via NDC1 but not via POM121 and GP210 in the nuclear envelope. Biochemical and biophysical research communications 34 19782045
1998 The antinuclear autoantibodies Sp100 and gp210 persist after orthotopic liver transplantation in patients with primary biliary cirrhosis. Journal of hepatology 34 9625318
1995 Detection of Gp210 autoantibodies in primary biliary cirrhosis using a recombinant protein containing the predominant autoepitope. Hepatology (Baltimore, Md.) 33 7531172
1996 Primary biliary cirrhosis sera recognize not only gp210 but also proteins of the p62 complex bearing N-acetylglucosamine residues from rat liver nuclear envelope. Anti-p62 complex antibody in PBC. Molecular biology reports 31 9112233
2007 Predictive role of anti-gp210 and anticentromere antibodies in long-term outcome of primary biliary cirrhosis. Hepatology research : the official journal of the Japan Society of Hepatology 29 17931196
2004 Dynamic properties of nuclear pore complex proteins in gp210 deficient cells. FEBS letters 27 15304359
2001 Biochemical characterization of nuclear pore complex protein gp210 oligomers. European journal of biochemistry 22 11453980
2018 Direct Conversion of Mouse Fibroblasts into Neural Stem Cells by Chemical Cocktail Requires Stepwise Activation of Growth Factors and Nup210. Cell reports 20 30067988
2022 Discovery of a Novel Aminocyclopropenone Compound That Inhibits BRD4-Driven Nucleoporin NUP210 Expression and Attenuates Colorectal Cancer Growth. Cells 17 35159127
1995 Drosophila gp210, an invertebrate nuclear pore complex glycoprotein. European journal of cell biology 16 7641726
2020 NUP210 and MicroRNA-22 Modulate Fas to Elicit HeLa Cell Cycle Arrest. Yonsei medical journal 10 32390360
1996 Anti-gp210 antibodies in sera of patients with primary biliary cirrhosis. Identification of a 64 kD fragment of gp210 as a major epitope. Human antibodies and hybridomas 10 9140728
2018 Mice Deficient in Nucleoporin Nup210 Develop Peripheral T Cell Alterations. Frontiers in immunology 9 30323813
2022 Long Non-coding RNA LINC01224 Promotes the Malignant Behaviors of Triple Negative Breast Cancer Cells via Regulating the miR-193a-5p/NUP210 Axis. Molecular biotechnology 8 36127622
2007 Phosphomimetic mutation of the mitotically phosphorylated serine 1880 compromises the interaction of the transmembrane nucleoporin gp210 with the nuclear pore complex. Experimental cell research 8 17559836
2003 Polyproline type II conformation in the C-terminal domain of the nuclear pore complex protein gp210. Biochemistry 8 12653556
2012 TRAF1 gene polymorphism correlates with the titre of Gp210 antibody in patients with primary biliary cirrhosis. Clinical & developmental immunology 7 23125866
2019 Functional polymorphism within NUP210 encoding for nucleoporin GP210 is associated with the risk of endometriosis. Fertility and sterility 6 31256999
1999 Oxalate-induced and cell-cycle-dependent expression of nuclear pore complex oxalate binding protein gp210. Biochemical and biophysical research communications 6 10581167
2021 Loss of Nup210 results in muscle repair delays and age-associated alterations in muscle integrity. Life science alliance 5 34911810
2005 [The significance of anti-nuclear envelope (gp210) antibody in primary biliary cirrhosis]. Nihon Rinsho Men'eki Gakkai kaishi = Japanese journal of clinical immunology 3 15997174
2004 Despite WT1 binding sites in the promoter region of human and mouse nucleoporin glycoprotein 210, WT1 does not influence expression of GP210. Journal of negative results in biomedicine 3 15613247
2025 The transmembrane nucleoporin Nup210 weakens HIV-1 infection via modulating late events of viral nuclear import. AIDS (London, England) 1 40202922
2025 A novel FRET-force biosensor for nucleoporin gp210 reveals that the nuclear pore complex experiences mechanical tension. bioRxiv : the preprint server for biology 1 40463170
2024 Nup210 Promotes Colorectal Cancer Progression by Regulating Nuclear Plasma Transport. Laboratory investigation; a journal of technical methods and pathology 1 39393532
2021 Increased sensitivity of gp210 autoantibody detection using a newly designed gp210 antigen. Journal of immunological methods 1 34971632
2020 Fluctuations of antimitochondrial antibodies and anti-gp210 antibody in a patient with primary biliary cholangitis and Sjögren syndrome with subsequent autoimmune hemolytic anemia: A case report. Medicine 1 32011506
2026 The nuclear envelope protein TMEM209 is an integral component of the nuclear pore complex and interacts with Nup210. Journal of cell science 0 41582553
2026 METTL3 promotes prostate cancer cell metastasis and EMT by mediating NUP210 m6A modification. Mutation research 0 41775163
2026 Super-enhancer-associated lncRNA HDAC11-AS1 aggravates hepatocellular carcinoma progression by modulating HDAC11 and NUP210 expression via promoting super-enhancer activity. Cellular oncology (Dordrecht, Netherlands) 0 42126774
2025 Evaluating the diagnostic efficacy of anti-M2-3E, anti-gp210, and anti-sp100 antibodies in primary biliary cirrhosis. Laboratory medicine 0 40973111

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