Affinage

ENY2

Transcription and mRNA export factor ENY2 · UniProt Q9NPA8

Length
101 aa
Mass
11.5 kDa
Annotated
2026-06-09
50 papers in source corpus 23 papers cited in narrative 23 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

ENY2 (Sus1) is an evolutionarily conserved nuclear protein that functions as a small shared subunit coupling histone modification, transcription elongation, and mRNA nuclear export by partitioning between distinct multiprotein complexes (PMID:14718168, PMID:18923079). It is a component of both the SAGA histone-modifying co-activator and the nuclear pore-associated Sac3-Thp1 (TREX-2/THSC) mRNA export complex, and its loss impairs mRNA export (PMID:14718168, PMID:18667528). Within SAGA, ENY2 supports H2B deubiquitylation: its incorporation depends on Ubp8 and Sgf11, and in human cells it acts together with ATXN7L3 as a non-enzymatic subunit required for the activity of multiple H2B deubiquitinases — USP22 within SAGA, and USP27X and USP51 acting independently of it (PMID:16855026, PMID:27132940). Structurally, ENY2 adopts an articulated helical hairpin that wraps around extended alpha-helices in Sac3 and in Sgf11 through a hydrophobic-stripe mechanism; because a single ENY2 molecule cannot engage both partners at once, it forms mutually exclusive SAGA and TREX-2 subcomplexes, and engineered mutations that selectively dissociate it from either partner disrupt TREX-2 targeting to nuclear pores and cause mRNA export defects (PMID:19328066, PMID:20007317, PMID:19269973). ENY2 also associates with elongating Ser5/Ser2-phosphorylated RNA Pol II and with export factors, links transcription to mRNP biogenesis and genome integrity through suppression of R-loops, and mediates the tethering of active genes to the nuclear periphery (PMID:18923079, PMID:18667528, PMID:18003937). In Drosophila, ENY2 is stably part of the THO complex where it drives recruitment to nascent mRNA and 3' end processing, and is recruited to Su(Hw)- and dCTCF-dependent chromatin insulators where it is required for barrier activity that blocks the spreading of H3K27me3/Polycomb (PMID:17643381, PMID:20048002, PMID:25147918). ENY2 additionally modulates telomere length through its effect on H2BK123 ubiquitination (PMID:29116388).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2004 High

    Established ENY2/Sus1 as a physical bridge shared between a histone-modifying co-activator and the mRNA export machinery, raising the question of how one protein couples transcription to export.

    Evidence Biochemical co-purification with SAGA and the Sac3-Thp1 complex, ChIP, and mRNA export assays in yeast

    PMID:14718168

    Open questions at the time
    • Did not resolve whether the two associations are simultaneous or mutually exclusive
    • No structural basis for partner binding
    • Molecular function within each complex unclear
  2. 2006 High

    Defined the SAGA-side role of Sus1 in H2B deubiquitylation and showed its incorporation depends on Ubp8 and Sgf11, situating it in a dissociable DUB subcomplex.

    Evidence Deletion analysis, co-IP, ChIP at GAL1, histone modification assays, and high-salt subcomplex dissociation in yeast

    PMID:16855026

    Open questions at the time
    • Catalytic contribution of Sus1 itself versus a purely structural role not separated
    • Did not address the export complex function
  3. 2008 High

    Connected Sus1 to transcription elongation and to the THSC/TREX-2 export pathway, defining a route linking elongation, mRNP biogenesis, and genome integrity.

    Evidence Co-IP with elongating Pol II and export factors, ChIP at coding regions, and R-loop/genetic epistasis assays in yeast

    PMID:18667528 PMID:18923079

    Open questions at the time
    • Mechanism by which Sus1 promotes elongation not defined
    • Direct versus indirect association with Pol II CTD unresolved
  4. 2009 High

    Provided the structural and mutational basis for ENY2's mutually exclusive partitioning, explaining how a single protein serves two complexes.

    Evidence X-ray crystallography of Sus1 with Sac3-CID/Cdc31 and with Sgf11, plus structure-guided and allele-specific mutagenesis with in vivo export and NPC-association assays in yeast

    PMID:19269973 PMID:19328066 PMID:20007317

    Open questions at the time
    • Regulation governing complex choice in vivo not established
    • Stoichiometric switching dynamics unknown
  5. 2010 High

    Showed in metazoans that ENY2 is a stable THO subunit driving recruitment to nascent mRNA and 3' end processing, distinguishing this role from SAGA.

    Evidence Reciprocal co-IP, ChIP, RNA-IP, and RNAi with 3'-end processing readout in Drosophila

    PMID:20048002

    Open questions at the time
    • How ENY2 mediates THO loading onto nascent RNA molecularly is unclear
    • Conservation of the 3'-processing role to yeast/human untested here
  6. 2014 Medium

    Extended ENY2's chromatin-boundary function to dCTCF insulators, linking it to prevention of Polycomb/H3K27me3 spreading.

    Evidence RNAi, ChIP for H3K27me3 and Pc spreading, and transgenic insulator assays in Drosophila

    PMID:17643381 PMID:25147918

    Open questions at the time
    • Whether barrier activity uses SAGA DUB or a separate ENY2 function not resolved
    • Single-lab insulator system
  7. 2016 High

    Defined ENY2 as a non-enzymatic activator shared across multiple H2B deubiquitinases beyond SAGA, generalizing its DUB-supporting role in human cells.

    Evidence siRNA knockdown with H2Bub1 measurement and co-IP identifying USP22/USP27X/USP51 complexes in human cells

    PMID:27132940

    Open questions at the time
    • Structural basis for ENY2 activation of USP27X/USP51 not determined
    • Biological substrates/contexts of the non-SAGA DUBs not mapped
  8. 2017 Medium

    Linked ENY2-dependent H2B ubiquitination control to telomere length regulation.

    Evidence Telomere Southern blots, H2BK123ub1 assays, co-IP, and genetic epistasis with telomere factors in yeast

    PMID:29116388

    Open questions at the time
    • Causal chain from H2Bub1 to telomere length is correlative
    • Single lab
  9. 2013 Medium

    Clarified that the human TREX-2 role of ENY2 is mRNA-specific and not required for nuclear protein export, narrowing its functional scope.

    Evidence siRNA knockdown with quantitative nuclear protein export assays in human cells (negative result)

    PMID:24291146

    Open questions at the time
    • Does not address mRNA export contribution in human cells
    • Single-pathway readout
  10. 2022 Medium

    Attributed a physiological lifespan/growth phenotype specifically to the TREX-2 export function of Sus1 rather than the SAGA DUB module.

    Evidence Lifespan epistasis, poly(A)+ RNA imaging, and Mex67/Dbp5 dosage suppression in yeast

    PMID:35771153

    Open questions at the time
    • Mechanistic link between export defect and aging not detailed
    • Single lab
  11. 2024 Medium

    Connected ENY2/TREX-2 to histone mRNP biology via a direct Paip2 interaction at histone locus bodies.

    Evidence Y2H, in vitro binding, co-IP, HLB immunofluorescence, and RNAi mRNP-binding assays in Drosophila

    PMID:39707855 PMID:41912850

    Open questions at the time
    • Functional consequence for histone mRNA export quantitatively limited
    • HLB recruitment mechanism incompletely defined
  12. 2026 Medium

    Proposed a cancer-relevant role in which ENY2 loss perturbs nucleolar/NPM1 dynamics to stabilize p53 and restrain tumor growth.

    Evidence Co-IP, ubiquitination assays, polysome profiling, RNA-seq, and in vivo tumor assays in cancer cells

    PMID:41642454

    Open questions at the time
    • Mechanistic link between TREX-2/SAGA functions and NPM1 release not fully resolved
    • Single lab, requires independent confirmation

Open questions

Synthesis pass · forward-looking unresolved questions
  • How ENY2's partitioning between SAGA, TREX-2, THO, and chromatin-boundary complexes is regulated in vivo, and how these functions are coordinated within a single cell, remains unresolved.
  • No mechanism governing complex-choice switching
  • Quantitative partitioning across complexes unmeasured
  • Integration of telomere, insulator, and export roles unclear

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 2 GO:0003723 RNA binding 1
Localization
GO:0005635 nuclear envelope 2 GO:0005634 nucleus 1 GO:0005829 cytosol 1
Pathway
R-HSA-4839726 Chromatin organization 3 R-HSA-8953854 Metabolism of RNA 3 R-HSA-74160 Gene expression (Transcription) 2 R-HSA-9609507 Protein localization 2
Partners
ATXN7L3CDC31DCTCFSAC3SGF11SU(HW)THP1UBP8
Complex memberships
SAGASAGA DUB moduleTHOTREX-2 (THSC)

Evidence

Reading pass · 23 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2004 Sus1 (ENY2) is a component of both the SAGA histone acetyltransferase complex and the nuclear pore-associated Sac3-Thp1 mRNA export complex; it localizes to the nucleus with concentration at nuclear pores, associates with the promoter of a SAGA-dependent gene during transcription activation (ChIP), and its deletion impairs mRNA export. Biochemical co-purification, chromatin immunoprecipitation (ChIP), DNA macroarray, fluorescence microscopy Cell High 14718168
2006 Sus1 (ENY2) participates in SAGA-dependent histone H2B deubiquitylation and maintenance of normal H3 methylation levels; its binding to SAGA depends on Ubp8 and Sgf11, and a stable Sus1-Sgf11-Ubp8 subcomplex can be dissociated from SAGA under high-salt conditions. In vivo recruitment of Sus1 to the GAL1 promoter requires Ubp8, and vice versa. Deletion analysis, co-immunoprecipitation, ChIP, histone modification assays, salt dissociation of subcomplexes Molecular biology of the cell High 16855026
2009 Crystal structure of Sus1 bound to the Sac3 CID domain and Cdc31 revealed that Sus1 adopts an articulated helical hairpin fold that wraps around an extended alpha-helix in Sac3. Two Sus1 chains and one Cdc31 are present per Sac3 CID. Engineered mutations disrupting individual chain binding showed Sus1 and Cdc31 function synergistically to promote NPC association of TREX-2 and mRNA nuclear export. X-ray crystallography, structure-guided mutagenesis, in vivo NPC association assays, mRNA export assays Molecular cell High 19328066
2009 Crystal structure of Sus1 bound to the N-terminal region of Sgf11 showed Sus1 wraps around a Sgf11 alpha-helix using a hydrophobic stripe mechanism similar to but narrower than the Sus1-Sac3 interface. A single Sus1 molecule cannot bind Sgf11 and Sac3 simultaneously, indicating Sus1 forms separate subcomplexes within SAGA and TREX-2. X-ray crystallography, in vitro mutagenesis disrupting the Sgf11-Sus1 interface The Journal of biological chemistry High 20007317
2009 Mutagenesis of Sus1 identified alleles (sus1-10, sus1-12) that dissociate Sus1 from TREX-2 while leaving SAGA interaction largely intact, and an allele (sus1-11) that impairs binding to both complexes. In vitro binding confirmed reduced affinity toward Sac3 and Sgf11 respectively. All three mutants were impaired in targeting TREX-2/Sac3 to nuclear pore complexes and showed mRNA export defects in vivo. Site-directed mutagenesis, in vitro binding assays, genetic interaction analysis, nuclear mRNA export assays The Journal of biological chemistry High 19269973
2008 Sus1 is required for transcription elongation and is associated with the elongating form of RNA Polymerase II phosphorylated on Ser5 and Ser2 of the CTD. Sus1 copurifies with mRNA export factors Yra1 and Mex67. ChIP shows Sus1 present at coding regions in a manner stimulated by Kin28-dependent CTD phosphorylation. Sgf73 is necessary for association of Sus1 with both SAGA and TREX-2. Co-immunoprecipitation, ChIP (coding regions and UAS), co-purification with export factors Genes & development High 18923079
2008 Thp1, Sac3, Sus1, and Cdc31 form a functional unit (THSC complex) with a role in mRNP biogenesis and genome integrity that is independent of SAGA. R-loop formation is consistent with genome instability in THSC mutants, analogous to THO/TREX mutants, defining a pathway connecting transcription elongation with mRNA export. Genetic epistasis, R-loop-forming constructs (ribozyme-containing transcription units), RNase H suppression, activation-induced cytidine deaminase assays Molecular biology of the cell Medium 18667528
2007 Drosophila E(y)2/Sus1 is recruited to Su(Hw) insulators via direct binding to the zinc-finger domain of Su(Hw). Partial inactivation of E(y)2 (e(y)2^u1 mutation) impairs barrier activity but not enhancer-blocking activity of Su(Hw) insulators. Combining su(Hw)^- and e(y)2^u1 is lethal, demonstrating functional interaction in vivo. In vivo transgenic insulator assays, genetic interaction (lethality in double mutant), protein-protein interaction studies Molecular cell Medium 17643381
2010 Drosophila ENY2 is stably associated with the THO complex (involved in mRNP biogenesis), functioning independently of SAGA and AMEX. ENY2 and THO are recruited to the transcribed region of hsp70 by loading onto nascent mRNA (not via direct association with elongating RNA Pol II). ENY2 plays an important role in THO recruitment to nascent mRNA. Knockdown of either ENY2 or THO (but not SAGA or AMEX) affects 3' end processing of the transcript. Co-immunoprecipitation, ChIP, RNA immunoprecipitation, RNAi knockdown, nascent mRNA loading assays Genes & development High 20048002
2007 Sus1, Sac3, and Thp1 are required for the persistent tethering of mRNA foci (containing improperly processed mRNP) to cognate genes, and for the prolonged post-transcriptional association of activated GAL genes with the nuclear periphery after transcriptional shutoff. Fluorescence microscopy, genetic deletion analysis, live-cell imaging of mRNA foci RNA (New York, N.Y.) Medium 18003937
2016 In human cells, depletion of the non-enzymatic SAGA DUBm components ATXN7L3 or ENY2 results in increased global H2Bub1 levels (in contrast to USP22 depletion which reduces H2Bub1). ENY2 and ATXN7L3 are shared subunits that coordinate activities of multiple H2B deubiquitinases including USP22 (SAGA), USP27X and USP51 (which function independently of SAGA); USP27X and USP51 require ATXN7L3 and ENY2 for their deubiquitinase activity. siRNA knockdown, histone modification assays (H2Bub1 levels), co-immunoprecipitation, identification of novel DUB complexes Molecular cell High 27132940
2014 Drosophila ENY2 is recruited to the zinc-finger domain of dCTCF and is required for the barrier activity of dCTCF-dependent insulators. ENY2 RNAi in BG3 cells leads to spreading of H3K27 trimethylation and Pc protein at several dCTCF boundaries. RNAi knockdown, ChIP (H3K27me3 and Pc spreading), transgenic insulator assays, protein-protein interaction Epigenetics Medium 25147918
2013 In human TREX-2, ENY2 is NOT involved in nuclear protein export (negative result), in contrast to PCID2 and centrin 2. siRNA knockdown of ENY2 did not affect the rate of nuclear protein export. siRNA knockdown, nuclear protein export assays, immunofluorescence Experimental cell research Medium 24291146
2022 Sus1 function in lifespan control operates through the TREX-2 complex (mRNA export) rather than the SAGA DUB module. Sus1 is required for proper association of mRNA export factors Mex67 and Dbp5 with the nuclear rim; increased dosage of Mex67 and Dbp5 rescues growth defects, shortened lifespan, and nuclear poly(A)+ RNA accumulation in sus1Δ cells. Genetic epistasis (lifespan assays in double mutants), fluorescence microscopy (poly(A)+ RNA accumulation), dosage suppression Aging Medium 35771153
2017 Sus1 deletion leads to elongated telomeres in yeast. Sus1 physically and genetically interacts with telomere maintenance factors. The elevated H2BK123ub1 levels in sus1Δ mutants correlate with telomere elongation, suggesting Sus1's role as a H2B deubiquitination modulator negatively regulates telomere length. Telomere length assays (Southern blot), co-immunoprecipitation, histone modification assays (H2BK123ub1), genetic epistasis with telomere mutants Current genetics Medium 29116388
2010 Sus1 has genetic interactions with P-body components (PAT1, LSM1, LSM6, DHH1); SUS1 deletion is synthetic lethal with LSM1 and PAT1. Sus1 overexpression leads to its accumulation in cytoplasmic granules that co-localize with P-bodies and stress granules. Novel physical interactions between Sus1 and P-body/stress granule factors were identified. Genetic interaction (synthetic lethality), co-immunoprecipitation, fluorescence microscopy (co-localization with P-body markers) BMC cell biology Medium 20230609
2014 Histone chaperone Asf1 co-purifies with Sus1 (TREX-2) and SAGA subunits; reciprocally, Sus1 and Thp1 interact with Asf1. Sus1 and Thp1 affect levels of Asf1-dependent histone H3K56 acetylation and histone H3/H4 incorporation onto chromatin, revealing a functional link between Asf1 and TREX-2 in histone metabolism near the nuclear pore. Tandem affinity purification coupled to mass spectrometry (TAP-MS), reciprocal co-immunoprecipitation, histone modification assays Nucleus (Austin, Tex.) Medium 24824343
2016 Drosophila ENY2 forms mutually exclusive complexes with insulator proteins (Su(Hw)/dCTCF) and with Sgf11 (SAGA component), suggesting competitive partitioning of ENY2 between the SAGA complex and insulator complexes. Co-immunoprecipitation, competition binding assays Doklady. Biochemistry and biophysics Low 27417714
2018 Drosophila ENY2 interacts with the ORC complex, specifically with ORC4 and ORC6 subunits directly. Co-immunoprecipitation, direct protein interaction assays Doklady. Biochemistry and biophysics Low 30008099
2020 Drosophila ENY2 interacts with RNA helicase MLE; this interaction was confirmed by independent methods and shown to be evolutionarily conserved and important for MLE function in both sexes. Co-immunoprecipitation, independent binding confirmation assays, genetic analysis Doklady. Biochemistry and biophysics Low 32130612
2024 Drosophila Paip2 directly binds ENY2 in vitro and associates with the ENY2-containing TREX-2 complex in vivo. Both Paip2 and ENY2 localize to histone locus bodies (HLBs). Paip2 knockdown by RNAi reduces binding of TREX-2 subunits to histone mRNPs, indicating Paip2 participates in TREX-2 binding to histone mRNPs. Yeast two-hybrid, in vitro direct binding assay, co-immunoprecipitation, immunofluorescence (HLB localization), RNAi knockdown with mRNP binding assay Molekuliarnaia biologiia Medium 39707855
2026 ENY2 is present at the histone locus body (HLB) in Drosophila and associates with histone gene chromatin as part of SAGA, THO, and TREX-2 complexes. ENY2 and subunits of all three complexes interact with FLASH (a structural HLB component). TREX-2 interacts with histone mRNA and participates in its nuclear export. Immunofluorescence (polytene chromosomes), ChIP, co-immunoprecipitation with FLASH and mRNP particles Doklady. Biochemistry and biophysics Low 41912850
2026 ENY2 depletion in cancer cells facilitates release of NPM1 into the nucleoplasm, impeding ribosomal subunit export and inducing nucleolar stress. Released NPM1 interacts with MDM2 within the nucleus to stabilize p53 protein levels, inhibiting tumor growth. In p53-mutant cells, ENY2 knockdown enhances RISC binding/silencing efficacy toward target mRNAs (p53-independent pathway). Co-IP, molecular docking, western blotting, ubiquitination assays, immunofluorescence, RNA sequencing, polysome profiling, in vivo/in vitro tumor growth assays Cellular oncology (Dordrecht, Netherlands) Medium 41642454

Source papers

Stage 0 corpus · 50 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery. Cell 300 14718168
2008 The THP1-SAC3-SUS1-CDC31 complex works in transcription elongation-mRNA export preventing RNA-mediated genome instability. Molecular biology of the cell 123 18667528
2016 ATXN7L3 and ENY2 Coordinate Activity of Multiple H2B Deubiquitinases Important for Cellular Proliferation and Tumor Growth. Molecular cell 122 27132940
2009 Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. Molecular cell 119 19328066
2006 The mRNA export factor Sus1 is involved in Spt/Ada/Gcn5 acetyltransferase-mediated H2B deubiquitinylation through its interaction with Ubp8 and Sgf11. Molecular biology of the cell 110 16855026
2008 Sus1 is recruited to coding regions and functions during transcription elongation in association with SAGA and TREX2. Genes & development 86 18923079
2007 Evolutionarily conserved E(y)2/Sus1 protein is essential for the barrier activity of Su(Hw)-dependent insulators in Drosophila. Molecular cell 74 17643381
2014 Novel three-component Rieske non-heme iron oxygenase system catalyzing the N-dealkylation of chloroacetanilide herbicides in sphingomonads DC-6 and DC-2. Applied and environmental microbiology 73 24928877
2010 Multifunctional factor ENY2 is associated with the THO complex and promotes its recruitment onto nascent mRNA. Genes & development 61 20048002
2007 Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active genes to the nuclear rim as well as to non-nascent mRNP. RNA (New York, N.Y.) 52 18003937
1994 Structural features of the maize sus1 gene and protein. Plant physiology 47 7846165
2011 Key features of the two-intron Saccharomyces cerevisiae gene SUS1 contribute to its alternative splicing. Nucleic acids research 41 21749978
2009 The cap binding complex influences H2B ubiquitination by facilitating splicing of the SUS1 pre-mRNA. RNA (New York, N.Y.) 37 19561118
2009 Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1. The Journal of biological chemistry 33 20007317
2011 SUS1 introns are required for efficient mRNA nuclear export in yeast. Nucleic acids research 27 21749979
2009 A tale of coupling, Sus1 function in transcription and mRNA export. RNA biology 24 19246994
2010 ENY2: couple, triple...more? Cell cycle (Georgetown, Tex.) 21 20090412
2009 Transcription at the proximity of the nuclear pore: a role for the THP1-SAC3-SUS1-CDC31 (THSC) complex. RNA biology 19 19229139
2009 Mutational uncoupling of the role of Sus1 in nuclear pore complex targeting of an mRNA export complex and histone H2B deubiquitination. The Journal of biological chemistry 19 19269973
2018 The SAGA/TREX-2 subunit Sus1 binds widely to transcribed genes and affects mRNA turnover globally. Epigenetics & chromatin 16 29598828
2014 Highly conserved ENY2/Sus1 protein binds to Drosophila CTCF and is required for barrier activity. Epigenetics 16 25147918
2010 A novel link between Sus1 and the cytoplasmic mRNA decay machinery suggests a broad role in mRNA metabolism. BMC cell biology 14 20230609
2013 Human TREX2 components PCID2 and centrin 2, but not ENY2, have distinct functions in protein export and co-localize to the centrosome. Experimental cell research 13 24291146
2010 E(y)2/Sus1 is required for blocking PRE silencing by the Wari insulator in Drosophila melanogaster. Chromosoma 13 20082086
2019 Comparative genome analysis reveals the evolution of chloroacetanilide herbicide mineralization in Sphingomonas wittichii DC-6. Archives of microbiology 12 30997539
2022 Integrated multi-omics analysis identifies ENY2 as a predictor of recurrence and a regulator of telomere maintenance in hepatocellular carcinoma. Frontiers in oncology 10 35992857
2017 The evolutionarily conserved factor Sus1/ENY2 plays a role in telomere length maintenance. Current genetics 10 29116388
2014 Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1. Nucleus (Austin, Tex.) 10 24824343
1990 A molecular dynamics simulation of the (dG)6 . (dC)6 minihelix including counterions and water. Biopolymers 10 2369613
2022 Sus1 maintains a normal lifespan through regulation of TREX-2 complex-mediated mRNA export. Aging 8 35771153
2020 An insight into structural plasticity and conformational transitions of transcriptional co-activator Sus1. PloS one 8 32134955
2017 Protein arginine methylation of Npl3 promotes splicing of the SUS1 intron harboring non-consensus 5' splice site and branch site. Biochimica et biophysica acta. Gene regulatory mechanisms 6 28392442
2015 An intronic RNA structure modulates expression of the mRNA biogenesis factor Sus1. RNA (New York, N.Y.) 6 26546116
1991 DC6, a novel type of Dictyostelium discoideum gene regulated by secreted factors but not by cAMP. Differentiation; research in biological diversity 6 1717330
2023 An integrative analysis of enhancer of yellow 2 homolog (ENY2) as a molecular biomarker in pan-cancer. Functional & integrative genomics 4 36862319
2018 An exon three-way junction structure modulates splicing and degradation of the SUS1 yeast pre-mRNA. Biochimica et biophysica acta. Gene regulatory mechanisms 4 29966763
2012 Suppression of the nuclear factor Eny2 increases insulin secretion in poorly functioning INS-1E insulinoma cells. Experimental diabetes research 4 22649445
2009 Getting to the gate: crystallization of a Sac3(CID):Sus1:Cdc31 complex. Molecular cell 4 19328059
2020 Multifunctional ENY2 Protein Interacts with RNA Helicase MLE. Doklady. Biochemistry and biophysics 3 32130612
2018 Role of the mRNA export factor Sus1 in oxidative stress tolerance in Candida albicans. Biochemical and biophysical research communications 3 29326041
2007 A hexanucleotide sequence (dC1-dC6 tract) restricts the dC-specific cleavage of single-stranded DNA by endonuclease IV of bacteriophage T4. Nucleic acids research 3 17940096
2018 Zinc Finger Protein CG9890 - New Component of ENY2-Containing Complexes of Drosophila. Acta naturae 2 30713769
2024 [Drosophila melanogaster Paip2 Binds ENY2 and Interacts with the TREX-2 Complex in Histone mRNP Particles]. Molekuliarnaia biologiia 1 39707855
2018 Identification of the ORC Complex Subunits That Can Interact with the ENY2 Protein of Drosophila melanogaster. Doklady. Biochemistry and biophysics 1 30008099
2016 CTCF and Sgfl1 proteins form alternative complexes with ENY2 proteins. Doklady. Biochemistry and biophysics 1 27417714
2009 [Conservative E(y)2/Sus1 protein interacts with the Su(Hw)-dependent insulators in Drosophila]. Genetika 1 19382683
2009 [Conservative E(y)2/Sus1 protein is the member of SAGA complex and new nuclear pore-associated complex in Drosophila]. Genetika 1 19947544
2026 ENY2 transcription and export complex 2 subunit deficiency induces nucleolar stress to inhibit tumor progression through NPM1/MDM2/p53-dependent and -independent responses. Cellular oncology (Dordrecht, Netherlands) 0 41642454
2026 ENY2 Protein Is Present at the Histone Locus Body HLB As Part of Complexes with Different Functions in Transcription and mRNA Export. Doklady. Biochemistry and biophysics 0 41912850
2025 Characterization of stem cell landscape and identification of stemness-related gene ENY2 in colorectal cancer by intergrated transcriptomic analysis. Global medical genetics 0 40735504

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