Affinage

NSMCE1

Non-structural maintenance of chromosomes element 1 homolog · UniProt Q8WV22

Round 2 corrected
Length
266 aa
Mass
30.9 kDa
Annotated
2026-04-29
42 papers in source corpus 17 papers cited in narrative 17 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NSMCE1 (NSE1) is an essential non-SMC subunit of the SMC5/6 complex that functions as both a structural scaffold and a ubiquitin E3 ligase critical for DNA repair, replication fork stability, and chromosome segregation during mitosis and meiosis (PMID:11927594, PMID:12966087, PMID:15331764). Its RING-like domain mediates assembly of the Nse1–Nse3–Nse4 subcomplex, which adopts a closed dimer conformation that forces Nse4 into a Z-shaped architecture coordinating DNA binding; disruption of this domain destabilizes the entire SMC5/6 holocomplex and impairs recruitment to DNA lesions (PMID:18667531, PMID:33676928, PMID:38847937). NSMCE1 possesses bona fide E3 ligase activity utilizing Ubc13/Mms2 as its cognate E2, stimulated by Nse3 and Nse4, and ubiquitinates Nse4-K181 to regulate the replication stress response through the homologous recombination pathway (PMID:35011726, PMID:17923688). In human cells, RING domain mutations reduce replication fork rates and increase genomic instability, and NSMCE1 displays a synthetic sick interaction with FANCM (PMID:38847937).

Mechanistic history

Synthesis pass · year-by-year structured walk · 11 steps
  1. 2002 High

    Identification of Nse1 as a novel non-SMC subunit of the SMC5/6 complex established that this large chromosomal complex contains dedicated accessory proteins essential for viability and DNA damage tolerance.

    Evidence Co-immunoprecipitation of Nse1p with SMC5-SMC6, nuclear localization microscopy, and DNA damage sensitivity of nse1 mutants in budding yeast

    PMID:11927594

    Open questions at the time
    • Biochemical function of Nse1 unknown
    • No structural information
    • No mammalian ortholog characterized
  2. 2003 High

    Confirmation that Nse1 is conserved from yeast to humans and functions epistatically with Rhp51 placed it squarely within the homologous recombination repair pathway, defining the biological context of its DNA repair role.

    Evidence Mass spectrometry identification after Smc5 purification, genetic epistasis with Rhp51 in fission yeast

    PMID:12966087

    Open questions at the time
    • Mechanism of Nse1 contribution to HR undefined
    • Physical basis of Nse1 interaction with other subunits unknown
  3. 2004 High

    Functional studies revealed that Nse1 is required not for DNA damage checkpoint initiation but for maintaining checkpoint arrest and enabling repair completion, and that it contributes to meiotic recombination and replication fork stability.

    Evidence Chk1 phosphorylation and checkpoint maintenance assays, meiotic segregation analysis, epistasis with Rhp51 in fission yeast

    PMID:14701739 PMID:15331764

    Open questions at the time
    • Molecular mechanism of checkpoint maintenance role unclear
    • Direct substrates or activities of Nse1 not identified
  4. 2007 High

    Characterization of the human SMC5/6 complex showed that NSE1 depletion destabilizes all other subunits and confers genotoxin sensitivity, while the complex localizes to ALT-associated PML bodies for telomere HR, extending Nse1's roles to human genome maintenance and telomere biology.

    Evidence RNAi knockdown with western blotting for complex stability, MMS sensitivity, immunofluorescence for ALT-PML co-localization, telomere length analysis in human cells

    PMID:17589526 PMID:18086888

    Open questions at the time
    • Whether NSE1 has enzymatic activity in mammalian cells untested
    • Mechanism of complex destabilization upon NSE1 loss unclear
  5. 2008 High

    Dissection of the RING-like domain showed it is dispensable for viability but essential for DNA repair; initial in vitro assays failed to detect E3 ligase activity, instead revealing the RING domain as a protein–protein interaction platform required for Nse1–Nse3–Nse4 trimer formation and damage-induced recruitment of the complex to lesion sites.

    Evidence RING domain mutagenesis, in vitro E3 ligase assays (negative), in vitro trimer reconstitution, immunofluorescence foci analysis in fission yeast

    PMID:18667531

    Open questions at the time
    • E3 ligase activity could not be demonstrated — assay conditions may have been suboptimal
    • Structural basis of trimer assembly unknown
  6. 2010 High

    The crystal structure of the MAGE-G1–NSE1 complex revealed the structural basis for RING E3 ligase activity and showed that MAGE proteins enhance NSE1 ubiquitin ligase activity, resolving the earlier negative biochemical results.

    Evidence X-ray crystallography of mammalian MAGE-G1–NSE1 complex, biochemical ubiquitin ligase assays

    PMID:20864041

    Open questions at the time
    • Physiological substrates of NSE1 E3 ligase activity unidentified
    • No structure of the full Nse1–Nse3–Nse4 trimer
  7. 2011 High

    RING domain mutations that abolish lesion recruitment can paradoxically suppress DNA damage sensitivity of Smc5/6 hypomorphs, revealing that recruitment of dysfunctional complexes to lesions is itself toxic and that repair can be rerouted through alternative error-free pathways.

    Evidence Site-directed RING mutagenesis, ChIP for lesion recruitment, genetic suppression analysis in fission yeast

    PMID:21976700

    Open questions at the time
    • Whether this suppression mechanism operates in mammalian cells unknown
    • Molecular basis of toxicity from dysfunctional complex recruitment unclear
  8. 2017 Medium

    In budding yeast, the Nse1 RING domain mediates interactions with Nse3, Nse4, and Smc5, and RING mutants display replication defects that are partially suppressed by deletion of the Mph1 helicase, linking Nse1 to the restraint of helicase activity at stalled replication forks.

    Evidence Co-immunoprecipitation, chromosome loss assay, BrdU replication assay, genetic epistasis with mph1Δ and rrm3Δ in budding yeast

    PMID:29119272

    Open questions at the time
    • Direct physical interaction between Nse1 and Mph1 not demonstrated
    • Mechanism of Mph1 restraint by Smc5/6 unresolved
  9. 2021 High

    The 1.7 Å crystal structure of the Xenopus Nse1–Nse3–Nse4 subcomplex revealed how the Nse1–Nse3 dimer imposes a Z-shaped conformation on the kleisin Nse4, organizing its DNA-binding regions and explaining how disease-causing mutations dislodge Nse4 from the complex.

    Evidence X-ray crystallography at 1.7 Å resolution, DNA binding assays, mutational analysis of disease-associated residues

    PMID:33676928

    Open questions at the time
    • Structure of the full holocomplex with SMC5/6 arms not solved
    • How Z-shaped Nse4 conformation regulates ATPase activity mechanistically unclear
  10. 2022 High

    Reconstituted biochemistry definitively established Nse1 as a ubiquitin E3 ligase using Ubc13/Mms2 as the cognate E2, identified Nse4-K181 as the first physiological substrate, and showed that Nse1 ligase activity is stimulated by Nse3/Nse4 and is critical under replication stress.

    Evidence In vitro ubiquitination with purified fission yeast proteins, E2 specificity panel, R188E mutagenesis, mass spectrometry identification of Nse4-K181, genetic suppression analysis

    PMID:35011726

    Open questions at the time
    • Whether Nse4-K181 ubiquitination is the sole functionally relevant modification unknown
    • No mammalian substrate identified
    • Downstream effectors reading the ubiquitin mark unidentified
  11. 2024 High

    In human cells, RING domain mutations confirmed that NSE1 is essential for SMC5/6 stability, replication fork progression, and genome integrity, and uncovered a synthetic sick interaction with FANCM that is not conserved from yeast, while C. elegans studies demonstrated NSE1 is required for meiotic recombination and proper chromosomal loading of the Nse1–Nse3–Nse4 subcomplex.

    Evidence RING domain point mutations/truncations in human cell lines with western blot, DNA fiber assay, genomic instability assays, FANCM epistasis; nse-1 mutant analysis with genotoxic sensitivity, RAD-51 foci, chromosome fragmentation, NSE-4/MAGE-1 localization in C. elegans

    PMID:38507953 PMID:38847937

    Open questions at the time
    • No human disease-causing mutations in NSMCE1 itself reported
    • Whether FANCM synthetic interaction reflects a shared substrate or parallel pathway is unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the identity of mammalian NSMCE1 ubiquitin substrates, how Nse4 ubiquitination at K181 mechanistically modulates SMC5/6 function, the structure of the complete SMC5/6 holocomplex bound to DNA, and the molecular basis of the NSMCE1–FANCM genetic interaction.
  • No mammalian Nse1 E3 substrate identified
  • Holocomplex structure with DNA not solved
  • FANCM interaction mechanism uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0005198 structural molecule activity 3 GO:0016874 ligase activity 2 GO:0140096 catalytic activity, acting on a protein 2
Localization
GO:0005634 nucleus 2 GO:0005694 chromosome 2
Pathway
R-HSA-73894 DNA Repair 6 R-HSA-1640170 Cell Cycle 3 R-HSA-69306 DNA Replication 2
Partners
FANCMMMS2NSE2NSE3NSE4SMC5SMC6UBC13
Complex memberships
Nse1-Nse3-Nse4 subcomplexSMC5/6 complex

Evidence

Reading pass · 17 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 NSE1 (Nse1p) was identified as a novel non-SMC component of the budding yeast SMC5-SMC6 complex (~2-3 MDa). Nse1p is essential for cell proliferation, localizes primarily to the nucleus, and nse1 mutants are hypersensitive to DNA-damaging treatments and display aberrant mitotic morphology, establishing it as a key subunit required for both DNA repair and proliferation. Co-immunoprecipitation, nuclear localization by microscopy, genetic analysis of mutants with DNA-damaging agents The Journal of biological chemistry High 11927594
2003 Fission yeast Nse1 and Nse2 were purified as co-precipitating partners of Smc5 and confirmed as non-SMC subunits of the Smc5-6 complex. Both proteins are essential and conserved from yeast to humans. Loss-of-function phenotypes mirror Smc5-6 inactivation. Epistasis with Rhp51 placed Nse1 in the homologous recombination repair pathway for DNA double-strand breaks. Mass spectrometry after Smc5 purification, co-immunoprecipitation, genetic epistasis analysis with Rhp51 The Journal of biological chemistry High 12966087
2004 In fission yeast, Nse1 is required for a coordinated DNA damage response. Cells lacking functional Nse1 (or Smc6) initiate a normal checkpoint (Chk1 phosphorylation) but enter lethal mitosis, indicating that Nse1 is needed to maintain checkpoint arrest, likely by supporting ongoing DNA repair or proper chromosomal organization rather than checkpoint initiation itself. Genetic analysis, Chk1 phosphorylation assay, checkpoint maintenance assay in fission yeast Molecular and cellular biology Medium 14701739
2004 Fission yeast Nse1, Nse2, and Nse3 are all crucial for meiosis. The Nse1-1 mutant displays meiotic DNA segregation defects and defective homologous recombination. Epistasis with Rhp51 confirmed that all three Nse subunits function in HR-based repair, and genetic interactions suggest the Smc5+6 complex (including Nse1) is important for replication fork stability. Genetic mutant analysis, spore viability assay, meiotic segregation analysis, epistasis with Rhp51 Molecular biology of the cell High 15331764
2007 In budding yeast, Nse1 is required specifically for the Rad52-dependent (homologous recombination) pathway of postreplication repair of UV-damaged DNA. Genetic analyses suggest that the Nse1-associated E3 ligase activity (along with Mms21 SUMO ligase) within the Smc5-6 complex contributes to this Rad52-dependent PRR mode. Genetic epistasis analysis with rad52, rad6-rad18, and mms2-ubc13-rad5 mutants; UV damage sensitivity assays Molecular and cellular biology Medium 17923688
2007 The human SMC5/6 complex, including NSE1 as a subunit, localizes to ALT-associated PML bodies (APBs) and is required for telomere HR and elongation in ALT cancer cells. Depletion of SMC5/6 subunits inhibits telomere HR, causes telomere shortening and senescence in ALT cells. RNAi knockdown, immunofluorescence co-localization, telomere-length analysis, senescence assay Nature structural & molecular biology Medium 17589526
2007 The human SMC5-6 complex was fully characterized with four non-SMC components including NSE1 and MAGEG1 (Nse3 ortholog). Depletion of NSE1 (or most other non-SMC subunits) leads to degradation of all other complex components, demonstrating that NSE1 is essential for complex stability. NSE1 depletion confers sensitivity to methyl methanesulfonate. NSE1 is subject to sumoylation and ubiquitination. RNAi depletion, western blotting for complex stability, MMS sensitivity assay, mass spectrometry Molecular and cellular biology High 18086888
2008 The RING-like motif of fission yeast Nse1 is not essential for cell viability but is required for DNA repair functions of the Smc5-6 complex: RING mutant cells are hypersensitive to a broad spectrum of genotoxic stresses. Neither human nor yeast full-length Nse1 nor isolated RING domains showed detectable ubiquitin E3 ligase activity in vitro. Instead, the Nse1 RING-like domain is required for normal Nse1-Nse3-Nse4 trimer formation in vitro and for damage-induced recruitment of Nse4 and Smc5 to subnuclear foci in vivo, identifying it as a protein-protein interaction domain essential for holocomplex integrity and lesion recruitment. RING domain mutagenesis, in vitro ubiquitin E3 ligase assay (human and yeast), in vitro trimer assembly assay, immunofluorescence foci analysis after DNA damage Molecular biology of the cell High 18667531
2010 The crystal structure of the MAGE-G1 (mammalian ortholog of Nse3)–NSE1 complex was solved, revealing structural insights into the MAGE protein family and their interaction with RING E3 ubiquitin ligases. NSE1 functions as a RING domain E3 ubiquitin ligase whose activity is enhanced by MAGE proteins, providing a structural basis for understanding NSMCE1's role in the Smc5/6 complex. X-ray crystallography of MAGE-G1–NSE1 complex, biochemical ubiquitin ligase assays Molecular cell High 20864041
2011 In fission yeast, the Nse1 RING domain variant has a non-canonical role: serine mutations in conserved cysteines of the RING domain suppress the DNA damage sensitivity of Smc5/6 hypomorphs but not HR mutants, and dramatically decrease the recruitment of Smc5/6 to lesion-containing loci marked for HR-mediated repair. This demonstrates that Nse1-dependent recruitment of dysfunctional Smc5/6 complexes to lesions is itself detrimental, and that lesions can be channeled into recombination-dependent and error-free PRR in the absence of such recruitment. Site-directed mutagenesis of RING domain cysteines, genetic suppression analysis, chromatin immunoprecipitation for lesion recruitment, DNA repair pathway analysis Molecular biology of the cell High 21976700
2011 Conserved hydrophobic surface residues on the N-terminal domain of Nse3 (MAGEG1) are essential for interaction with Nse1, and these interactions are conserved in human orthologs. MAGEG1 interaction with NSE4b results in transcriptional co-activation of steroidogenic factor 1 (SF1), revealing a transcriptional regulatory function for the NSE1-containing subcomplex. Site-directed mutagenesis, protein-protein interaction assays (yeast two-hybrid, co-IP), molecular modeling, transcriptional reporter assay PloS one Medium 21364888
2017 In budding yeast, the Nse1 RING domain (zinc-coordinating residues) is required for interaction with Nse3 and other Smc5/6 subunits (Nse4, Smc5). The nse1-103 RING mutant shows chromosome loss, delayed replication completion, modest sister chromatid cohesion defect, and synthetic sickness with rrm3Δ. The temperature sensitivity is partially suppressed by deletion of MPH1 (DNA helicase), placing Nse1 in a pathway that restrains Mph1 activity during replication. RING domain mutagenesis, co-immunoprecipitation, chromosome loss assay, BrdU incorporation/replication assay, genetic epistasis with mph1Δ and rrm3Δ Current genetics Medium 29119272
2019 Overexpression of mouse Nsmce1 in hippocampal neuronal cells (HT-22) promotes cell proliferation, while knockdown inhibits it. Nsmce1 overexpression suppresses expression of Alzheimer's disease marker genes (App, Bace2, Mapt), and transcriptomics reveals dysregulation of 224 genes enriched in ubiquitin-mediated proteolysis and neurodegenerative disease pathways, suggesting a role for Nsmce1 in regulating neuronal cell proliferation and UMP pathway activity. Overexpression and RNAi knockdown in HT-22 cells, cell proliferation assay, qRT-PCR for AD markers, RNA-seq transcriptomics Functional & integrative genomics Low 31792732
2021 The crystal structure of the Xenopus laevis Nse1-Nse3-Nse4 subcomplex was solved at 1.7 Å resolution. The Nse1-Nse3 dimer adopts a closed conformation and forms three interfaces with Nse4, forcing it into a Z-shaped conformation. Mutations causing lung disease/immunodeficiency/chromosome breakage syndrome dislodge Nse4 from Nse1-Nse3. DNA binding is contributed by the N-terminal and middle regions of Nse4, informed by the structural context provided by Nse1-Nse3. X-ray crystallography at 1.7 Å, DNA binding assays, mutational analysis Journal of molecular biology High 33676928
2022 S. pombe Nse1 possesses confirmed ubiquitin E3 ligase activity in vitro using purified proteins. This activity is stimulated by Nse3 and Nse4, and Nse1 specifically utilizes Ubc13/Mms2 as its cognate E2 enzyme and directly interacts with ubiquitin. The Nse1 R188E mutation specifically abrogates E3 activity. Nse4 K181 was identified as the first known SMC5/6-associated Nse1 substrate; abolishing Nse4-K181 ubiquitination suppresses DNA damage sensitivity of other SMC5/6 mutants. Nse1 ubiquitin ligase activity is particularly important under replication stress. In vitro ubiquitin E3 ligase assay with purified proteins, E2 specificity assay, site-directed mutagenesis (R188E), mass spectrometry identification of Nse4-K181 ubiquitination, genetic suppression analysis Cells High 35011726
2024 Point mutations or truncations in the RING domain of human NSE1 result in drastically reduced Smc5/6 protein levels in human cell lines, demonstrating that the NSE1 RING domain is essential for Smc5/6 complex stability. NSE1 RING mutant human cells display cell growth defects, reduced replication fork rates, and increased genomic instability. A synthetic sick interaction between Smc5/6 and FANCM was uncovered, and Smc5/6 controls fork progression and chromosome disjunction in a FANCM-independent manner, indicating this regulation is not evolutionarily conserved from yeast. Human cell line engineering with RING domain point mutations and truncations, western blotting for complex stability, replication fork rate assay (DNA fiber), genomic instability assays, genetic interaction analysis with FANCM Cellular and molecular life sciences : CMLS High 38847937
2024 In C. elegans, nse-1 is required for meiotic recombination and DNA repair. nse-1 mutants show reduced fertility, increased male incidence, sensitivity to MMS/cisplatin/HU, increased RAD-51 foci, chromosome fragmentation, and upregulation of the CEP-1/p53-mediated apoptotic pathway (ced-13, egl-1). NSE-1 is essential for proper chromosomal localization of NSE-4 and MAGE-1, placing NSE-1 as a required factor for correct SMC5/6 subcomplex assembly on chromosomes. nse-1 mutant analysis, genotoxic sensitivity assays, RAD-51 foci immunofluorescence, chromosome fragmentation analysis, immunostaining for NSE-4 and MAGE-1 localization DNA repair Medium 38507953

Source papers

Stage 0 corpus · 42 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2003 Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature genetics 754 14702039
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2010 Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science (New York, N.Y.) 421 20360068
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
1996 Normalization and subtraction: two approaches to facilitate gene discovery. Genome research 401 8889548
2010 MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases. Molecular cell 388 20864041
2018 DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of NHEJ and PARP Inhibitor Sensitivity. Cell 379 29656893
2007 The SMC5/6 complex maintains telomere length in ALT cancer cells through SUMOylation of telomere-binding proteins. Nature structural & molecular biology 312 17589526
2018 Mapping the Genetic Landscape of Human Cells. Cell 225 30033366
2006 Human SMC5/6 complex promotes sister chromatid homologous recombination by recruiting the SMC1/3 cohesin complex to double-strand breaks. The EMBO journal 224 16810316
2005 Human MMS21/NSE2 is a SUMO ligase required for DNA repair. Molecular and cellular biology 204 16055714
2000 Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome research 161 11042152
2019 Systematic bromodomain protein screens identify homologous recombination and R-loop suppression pathways involved in genome integrity. Genes & development 110 31753913
2003 Novel essential DNA repair proteins Nse1 and Nse2 are subunits of the fission yeast Smc5-Smc6 complex. The Journal of biological chemistry 101 12966087
2004 Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3, play a crucial role in meiosis. Molecular biology of the cell 98 15331764
2020 Systematic mapping of genetic interactions for de novo fatty acid synthesis identifies C12orf49 as a regulator of lipid metabolism. Nature metabolism 92 32694731
2017 Cell cycle-dependent phosphorylation regulates RECQL4 pathway choice and ubiquitination in DNA double-strand break repair. Nature communications 89 29229926
2002 Identification of a novel non-structural maintenance of chromosomes (SMC) component of the SMC5-SMC6 complex involved in DNA repair. The Journal of biological chemistry 89 11927594
2004 Coordination of DNA damage responses via the Smc5/Smc6 complex. Molecular and cellular biology 83 14701739
2007 Identification of the proteins, including MAGEG1, that make up the human SMC5-6 protein complex. Molecular and cellular biology 79 18086888
2016 Destabilized SMC5/6 complex leads to chromosome breakage syndrome with severe lung disease. The Journal of clinical investigation 64 27427983
2023 Cross-linking mass spectrometry discovers, evaluates, and corroborates structures and protein-protein interactions in the human cell. Proceedings of the National Academy of Sciences of the United States of America 60 37071682
2020 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRASG13D. Nature communications 60 31980649
2017 Mapping the interactome of HPV E6 and E7 oncoproteins with the ubiquitin-proteasome system. The FEBS journal 56 28786561
2008 Nse1 RING-like domain supports functions of the Smc5-Smc6 holocomplex in genome stability. Molecular biology of the cell 54 18667531
2018 Characterizing ZC3H18, a Multi-domain Protein at the Interface of RNA Production and Destruction Decisions. Cell reports 47 29298432
2011 Interactions between the Nse3 and Nse4 components of the SMC5-6 complex identify evolutionarily conserved interactions between MAGE and EID Families. PloS one 46 21364888
2007 Requirement of Nse1, a subunit of the Smc5-Smc6 complex, for Rad52-dependent postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae. Molecular and cellular biology 26 17923688
2011 Nse1-dependent recruitment of Smc5/6 to lesion-containing loci contributes to the repair defects of mutant complexes. Molecular biology of the cell 19 21976700
2021 Structure Basis for Shaping the Nse4 Protein by the Nse1 and Nse3 Dimer within the Smc5/6 Complex. Journal of molecular biology 14 33676928
2022 Role of Nse1 Subunit of SMC5/6 Complex as a Ubiquitin Ligase. Cells 12 35011726
2017 Interaction of the Saccharomyces cerevisiae RING-domain protein Nse1 with Nse3 and the Smc5/6 complex is required for chromosome replication and stability. Current genetics 9 29119272
2019 A transcriptomic analysis of Nsmce1 overexpression in mouse hippocampal neuronal cell by RNA sequencing. Functional & integrative genomics 7 31792732
2024 Crucial role of the NSE1 RING domain in Smc5/6 stability and FANCM-independent fork progression. Cellular and molecular life sciences : CMLS 5 38847937
2015 Nse1 and Nse4, subunits of the Smc5-Smc6 complex, are involved in Dictyostelium development upon starvation. Development, growth & differentiation 5 26036668
2024 SMC-5/6 complex subunit NSE-1 plays a crucial role in meiosis and DNA repair in Caenorhabditis elegans. DNA repair 3 38507953