Affinage

UBE2E3

Ubiquitin-conjugating enzyme E2 E3 · UniProt Q969T4

Length
207 aa
Mass
22.9 kDa
Annotated
2026-06-10
43 papers in source corpus 20 papers cited in narrative 19 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

UBE2E3 (UbcM2) is a metazoan ubiquitin-conjugating (E2) enzyme that forms an E1-dependent thioester with ubiquitin through its active-site cysteine C145, supporting E3-dependent substrate ubiquitination (PMID:10343118). A defining feature of UBE2E3 is its intrinsic restriction to monoubiquitylation: backside surface residues of the enzyme acting together with K48 of ubiquitin block polyubiquitin chain synthesis, and mutation of these backside residues unlocks K63-, K6-, and K48-linked chain formation (PMID:24901938). UBE2E3 cooperates with diverse E3 ligases to ubiquitinate distinct substrates: it partners with the HECT ligases Nedd4/Nedd4-2 to ubiquitinate and downregulate the epithelial sodium channel ENaC (PMID:14993279, PMID:16337426), with the RING ligases ARA54 and RNF8 to support their autoubiquitination (PMID:11322894), and with the RING ligases PJA1 to drive ubiquitination of TDP-43, suppressing TDP-43 phosphorylation and cytoplasmic aggregation (PMID:24825905, PMID:32686212). Its E2/E3 pairing is selectively gated by its class III N-terminal extension, which prevents productive pairing with Ro52/TRIM21 (PMID:21862588), and its polyubiquitination output is constrained by the deubiquitinase OTUB1 (PMID:32049508). Beyond proteostasis, UBE2E3 controls the redox transcription factor NRF2 by promoting its nuclear localization and target-gene expression together with importin-11 (PMID:25378586), and it operates at the outer mitochondrial membrane within a Mulan-UBE2E3-GABARAP complex implicated in mitophagy (PMID:25224329). Functionally, UBE2E3 is required for cell proliferation, and its depletion induces cellular senescence with a senescence-associated secretory phenotype that is partially suppressed by co-depletion of p53, p21, or p16 (PMID:18614808, PMID:29879550). Several early reports attributing SUMO-1 conjugation to 'Ubch9' (PMID:9409737, PMID:9734360, PMID:10582246, PMID:10187858, PMID:15355988) reflect the activity of the distinct SUMO E2 UBC9/UBE2I sharing the alias, not UBE2E3.

Mechanistic history

Synthesis pass · year-by-year structured walk · 14 steps
  1. 1999 High

    Established that UBE2E3 is a genuine ubiquitin-conjugating E2, resolving its identity against the SUMO-pathway 'Ubch9' alias by directly demonstrating ubiquitin thioester formation through its catalytic cysteine.

    Evidence GST-fusion thioester assay with active-site C145S mutagenesis

    PMID:10343118

    Open questions at the time
    • Did not identify cognate E3 partners or substrates
    • Alias collision with UBC9/UBE2I leaves earlier SUMO-conjugation reports (idx 0,1,2,6) attributable to a different gene
  2. 2001 Medium

    Connected UBE2E3 to nuclear protein ubiquitination by showing it pairs with RING E3 ligases through its UBC domain and supports their autoubiquitination, defining a class of physiological E3 partners.

    Evidence Yeast two-hybrid, deletion mapping, in vitro and cell-based ubiquitination of ARA54 and RNF8

    PMID:11322894

    Open questions at the time
    • Physiological substrates beyond E3 autoubiquitination not defined
    • Chain type and processivity not characterized
  3. 2004 High

    Placed UBE2E3 in a defined physiological pathway by showing it serves as the E2 for Nedd4-2-mediated ubiquitination and downregulation of the ENaC channel via reciprocal epistasis.

    Evidence Xenopus oocyte electrophysiology, co-IP, catalytic-dead mutant, epistasis with inactive Nedd4-2, renal cell transport assay

    PMID:14993279

    Open questions at the time
    • Relative in vivo contribution versus other E2s not quantified
    • Did not establish chain linkage on ENaC
  4. 2005 Medium

    Tested the efficiency of UBE2E3 as a HECT-ligase partner, showing it works with Nedd4/Nedd4-2 but less efficiently than UbcH5b, framing UBE2E3 as a context-selective rather than dominant E2.

    Evidence In vitro ubiquitination assay comparing multiple E2 enzymes

    PMID:16337426

    Open questions at the time
    • Does not explain which substrates require UBE2E3 specifically
    • No cellular validation of efficiency differences
  5. 2008 Medium

    Linked UBE2E3 to a cellular phenotype by demonstrating it is nuclear and required for RPE cell proliferation, with depletion causing cell-cycle exit and p27Kip1 accumulation.

    Evidence siRNA knockdown with rescue, Ki-67/p27 immunofluorescence, developmental reporter mouse

    PMID:18614808

    Open questions at the time
    • Ubiquitination substrate driving proliferation not identified
    • Mechanistic link from E2 activity to cell-cycle arrest unresolved
  6. 2011 Medium

    Explained E2/E3 pairing specificity by showing the class III N-terminal extension of UBE2E3 uniquely blocks productive pairing with Ro52/TRIM21, distinguishing it from UBE2E1/UBE2E2.

    Evidence E2 panel ubiquitination assay, NMR and ELISA interface mapping

    PMID:21862588

    Open questions at the time
    • Generality of N-terminal gating across other E3s not mapped
    • Structural basis at residue level incomplete
  7. 2014 High

    Defined the intrinsic catalytic restriction of UBE2E3 to monoubiquitylation, attributing it to enzyme backside residues plus K48 of ubiquitin and showing backside mutation unlocks chain synthesis.

    Evidence Fully recombinant in vitro ubiquitylation with backside and ubiquitin K-to-R mutagenesis

    PMID:24901938

    Open questions at the time
    • Whether E3 partners can override the restriction in cells not determined
    • Physiological consequence of mono- versus poly-output on substrates untested
  8. 2014 Medium

    Expanded UBE2E3 substrate range to TDP-43 and to redox signaling, showing it ubiquitinates TDP-43 and controls NRF2 nuclear localization and target-gene activity with importin-11.

    Evidence Yeast two-hybrid, reciprocal co-IP, catalytic mutant and knockdown for TDP-43; siRNA, immunofluorescence, fractionation and target-gene readouts for NRF2

    PMID:24825905 PMID:25378586

    Open questions at the time
    • Direct E3 ligase for NRF2 regulation not defined in this work
    • Whether NRF2 effect requires UBE2E3 catalytic activity not resolved
  9. 2014 Medium

    Positioned UBE2E3 at the outer mitochondrial membrane in a mitophagy context by showing the mitochondrial E3 Mulan recruits GABARAP via a LIR motif in a UBE2E3-dependent manner.

    Evidence RING-E2 fusion yeast two-hybrid, co-IP, LIR mutagenesis

    PMID:25224329

    Open questions at the time
    • Mitophagy outcome not reconstituted or assayed functionally
    • Substrate ubiquitinated within the Mulan-UBE2E3-GABARAP complex unknown
  10. 2018 Medium

    Established UBE2E3 as a guardian against senescence, showing its loss triggers p53/p21/p16-dependent senescence with a SASP and altered organelle mass independent of overt DNA damage.

    Evidence siRNA knockdown, SA-β-gal, SASP and organelle assays, genetic epistasis with p53/p21/p16

    PMID:29879550

    Open questions at the time
    • Direct ubiquitination substrate upstream of the senescence program not identified
    • Connection between NRF2/mitochondrial roles and senescence not mechanistically bridged
  11. 2020 Medium

    Refined regulation of UBE2E3 output by showing OTUB1 inhibits its polyubiquitination but uniquely cannot suppress its autoubiquitination, distinguishing it within the UBE2E family.

    Evidence In vitro ubiquitination assay with kinetic/thermodynamic characterization of OTUB1:E2 complexes

    PMID:32049508

    Open questions at the time
    • Cellular consequence of OTUB1 regulation of UBE2E3 untested
    • Substrate context of OTUB1 inhibition unknown
  12. 2020 Medium

    Extended the TDP-43 axis in vivo by identifying PJA1 as the E3 partner for UBE2E3-mediated TDP-43 ubiquitination, with PJA1 suppressing TDP-43 aggregation in motor neurons.

    Evidence Co-IP, adenoviral overexpression in neurons, in vivo mouse facial motor neuron model

    PMID:32686212

    Open questions at the time
    • Requirement for UBE2E3 catalytic activity in the in vivo phenotype not isolated
    • Chain type on TDP-43 and proteostatic fate not defined
  13. 2021 Low

    Linked UBE2E3 to stem-cell aging, indicating its level controls BMSC senescence and osteogenic differentiation via the NRF2 pathway.

    Evidence siRNA knockdown and lentiviral overexpression with senescence and osteogenic readouts

    PMID:34820159

    Open questions at the time
    • NRF2 mechanistic link asserted but not directly demonstrated
    • No ubiquitination substrate identified in this context
  14. 2023 Low

    Suggested UBE2E3 participates in a CUL3-based ligase assembly relevant to RPE oxidative stress by detecting it in a complex with RCBTB1 and CUL3.

    Evidence Co-immunoprecipitation from iPSC-derived RPE cells

    PMID:37408192

    Open questions at the time
    • Single co-IP without reciprocal or functional validation for UBE2E3
    • Substrate and biological output of the CUL3-RCBTB1-UBE2E3 complex unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved which direct ubiquitination substrate(s) of UBE2E3 mediate its NRF2-regulatory, proliferative, and anti-senescence functions, and how its enforced monoubiquitylation output is reconciled with substrate fates across its distinct E3 partners.
  • No substrate causally linking UBE2E3 catalytic activity to senescence
  • Mechanism connecting monoubiquitylation restriction to physiological signaling outcomes undefined
  • In vivo roles beyond neuronal TDP-43 model not established

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 4 GO:0016740 transferase activity 2 GO:0140657 ATP-dependent activity 1
Localization
GO:0005634 nucleus 1 GO:0005739 mitochondrion 1
Pathway
R-HSA-392499 Metabolism of proteins 3 R-HSA-1640170 Cell Cycle 2 R-HSA-8953897 Cellular responses to stimuli 2
Complex memberships
CUL3-RCBTB1-UBE2E3 complexMulan-UBE2E3-GABARAP complex

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1997 UBE2E3 (Ubch9) cannot form a thioester with ubiquitin but can form a thioester with SUMO-1, establishing it as a SUMO conjugating enzyme rather than a ubiquitin conjugating enzyme. SUMO conjugation proceeds via a distinct E1 activity separate from the ubiquitin E1. In vitro thioester formation assay with ubiquitin and SUMO-1 FEBS letters High 9409737
1998 In the presence of the SUMO-1 E1 activating enzyme, UBE2E3 (Ubch9) directly conjugates SUMO-1 to IκBα primarily on K21 (also used for ubiquitin modification), thereby protecting IκBα from signal-induced ubiquitination and proteasomal degradation and inhibiting NF-κB activation. Notably, unlike ubiquitination, SUMO-1 modification of IκBα is inhibited by phosphorylation of S32/S36. In vitro reconstitution with purified recombinant proteins; mutagenesis of IκBα lysine and serine residues Molecular cell High 10582246 9734360
1999 The SUMO-1 E1 activating enzyme (SAE1/SAE2 heterodimer) transfers SUMO-1 thioester to UBE2E3 (Ubch9), which then conjugates SUMO-1 to IκBα in vitro without requiring an E3-equivalent activity, defining UBE2E3 as the E2 enzyme in the minimal SUMO-1 conjugation pathway. In vitro reconstitution with purified recombinant SAE1/SAE2, UBE2E3, SUMO-1, and IκBα; ATP-dependent thioester assay The Journal of biological chemistry High 10187858
1999 UBE2E3 encodes a functional E2 ubiquitin-conjugating enzyme that forms an E1-dependent thioester bond with ubiquitin through its active-site cysteine (C145); mutation of C145 to serine abolishes thioester formation, confirming the catalytic cysteine. GST-fusion protein thioester assay; active-site mutagenesis (C145S) Cytogenetics and cell genetics High 10343118
2001 UBE2E3 interacts with RING-finger proteins ARA54 and RNF8 via its UBC domain (interaction requires intact RING domain on the E3 partners), and supports E3-dependent autoubiquitination of ARA54 and RNF8 in vitro and in cells, linking UBE2E3 to nuclear protein ubiquitination. Yeast two-hybrid screen; deletion mutagenesis mapping; in vitro ubiquitination assay with Sf9-expressed proteins; transfection/ubiquitination in COS-7 cells European journal of biochemistry Medium 11322894
2004 UBE2E3 acts as the E2 enzyme in concert with the E3 ligase Nedd4-2 to ubiquitinate and downregulate ENaC. UBE2E3 and Nedd4-2 co-immunoprecipitate. A catalytically inactive UBE2E3-C145S mutant increases ENaC cell-surface expression in Xenopus oocytes, and this effect depends on intact PY motifs (Nedd4-2 binding sites) and ubiquitination sites on ENaC. No additive effect is seen when UBE2E3-CS is co-expressed with an inactive Nedd4-2 mutant, placing UBE2E3 in the same pathway as Nedd4-2. Xenopus oocyte electrophysiology; co-immunoprecipitation; catalytic inactive mutant; epistasis with Nedd4-2 mutant; renal mpkCCD cell transepithelial Na+ transport assay Molecular and cellular biology High 14993279
2004 UBE2E3 (Ubch9) promotes SUMO modification of Werner helicase (WRN) in a synergistic manner with the tumor suppressor p14 Arf. p14 Arf-driven WRN SUMOylation causes redistribution of WRN within the nucleus, an effect reversed by a SUMO-specific protease, implicating UBE2E3-mediated SUMOylation in WRN nuclear localization. Cell-based SUMO conjugation assay; co-expression; SUMO-specific protease reversal; fluorescence microscopy of WRN redistribution The Journal of biological chemistry Medium 15355988
2005 Both Nedd4 and Nedd4-2 use UBE2E3 as an E2 partner in in vitro ubiquitination assays, but UBE2E3 supports substrate ubiquitination less efficiently than UbcH5b for these HECT E3 ligases. In vitro ubiquitination assay comparing multiple E2 enzymes The international journal of biochemistry & cell biology Medium 16337426
2008 UBE2E3 localizes to the nucleus of RPE cells and is required for their proliferation; siRNA-mediated depletion causes cell-cycle exit, loss of Ki-67, accumulation of the CDK inhibitor p27Kip1, and doubling of cell area. The mouse ortholog UbcM2 is transcriptionally downregulated during RPE development in vivo. siRNA knockdown; immunofluorescence (Ki-67, p27Kip1); cell counting; rescue experiment; LacZ reporter mouse for developmental expression Investigative ophthalmology & visual science Medium 18614808
2011 The N-terminal extension of UBE2E3 prevents it from functioning together with the RING E3 ligase Ro52 (TRIM21), unlike the N-terminal extensions of UBE2E1 and UBE2E2 which allow productive interaction, demonstrating that the class III E2 N-terminal extension uniquely modulates E2/E3 pairing specificity. E2 panel screening in ubiquitination assay; NMR and ELISA mapping of E2/E3 interface The Journal of biological chemistry Medium 21862588
2014 UBE2E3 ubiquitinates TDP-43; all three UBE2E family members enhance TDP-43 ubiquitination, but catalytically inactive UBE2E3(C145S) is much less efficient. Silencing UBE2E3 reduces TDP-43 ubiquitination. UBE2E3 was identified as a TDP-43 interactor by yeast two-hybrid and confirmed by co-immunoprecipitation and co-localization in HEK293E cells. Yeast two-hybrid; co-immunoprecipitation; siRNA knockdown; overexpression with proteasome inhibitor; catalytic mutant (C145S) The Journal of biological chemistry Medium 24825905
2014 UBE2E3 (UbcM2) is intrinsically restricted to monoubiquitylation: backside residues of the enzyme (distant from the active site) and K48 of ubiquitin together prevent polyubiquitin chain synthesis. Mutation of backside residues enables K63-linked (and to a lesser extent K6- and K48-linked) chain synthesis, revealing a two-fold non-catalytic restriction mechanism. Fully recombinant in vitro ubiquitylation assay; backside mutagenesis; ubiquitin K-to-R mutant panel Biochemistry High 24901938
2014 UBE2E3 and its nuclear import receptor importin-11 (Imp-11) regulate NRF2 subcellular distribution and transcriptional activity. Knockdown of UBE2E3 reduces nuclear NRF2, decreases NRF2 target gene expression, and relocalizes NRF2 to a perinuclear cluster of mitochondria. Imp-11 restricts KEAP1 from prematurely extracting NRF2 from target gene promoters. siRNA knockdown; immunofluorescence; gene expression analysis of NRF2 target genes; subcellular fractionation Molecular biology of the cell Medium 25378586
2014 Mulan (mitochondrial E3 ubiquitin ligase) interacts specifically with UBE2E3 among multiple E2 partners; the Mulan-UBE2E3 complex recruits GABARAP via an LC3-interacting region (LIR) in Mulan's RING domain, and this interaction requires the presence of UBE2E3. This places UBE2E3 in a mitophagy regulatory complex at the outer mitochondrial membrane. Modified yeast two-hybrid screen (RING-E2 fusion); co-immunoprecipitation; LIR motif mutagenesis Cellular signalling Medium 25224329
2018 UBE2E3 loss induces cellular senescence in the absence of overt DNA damage. Cells depleted of UBE2E3 display a distinct senescence-associated secretory phenotype, increased mitochondrial and lysosomal mass, increased sensitivity to mitochondrial/lysosomal poisons, and elevated basal autophagic flux. The senescence phenotype is partially suppressed by co-depletion of p53, p21CIP1/WAF1, or p16INK4a. siRNA knockdown; SA-β-galactosidase assay; SASP marker analysis; organelle mass assays; genetic epistasis with p53/p21/p16 co-depletion Redox biology Medium 29879550
2020 PJA1 (Praja1 RING-finger E3 ubiquitin ligase) co-immunoprecipitates with both CTF TDP-43 and UBE2E3, identifying UBE2E3 as the E2 partner for PJA1-mediated ubiquitination of TDP-43. PJA1 suppresses phosphorylation and cytoplasmic aggregate formation of TDP-43 in neuronal cells and in vivo in mouse motor neurons. Co-immunoprecipitation; adenoviral overexpression in neural stem cell-derived neurons; in vivo mouse facial motor neuron model Neuropathology Medium 32686212
2020 OTUB1 inhibits the polyubiquitination activity of UBE2E3 (along with UBE2E1 and UBE2E2) at physiologically relevant concentrations. However, unlike UBE2E1 and UBE2E2, OTUB1 is unable to suppress autoubiquitination by UBE2E3, revealing a unique feature of UBE2E3 within the UBE2E family in its interaction with OTUB1. In vitro ubiquitination assay; kinetic/thermodynamic characterization of OTUB1:E2 complexes Biochemistry Medium 32049508
2021 UBE2E3 knockdown accelerates cellular senescence and inhibits osteogenic differentiation of bone marrow mesenchymal stem cells (BMSCs), while overexpression of UBE2E3 attenuates senescence and enhances osteogenic differentiation of aged BMSCs. Mechanistically, UBE2E3 regulates the NRF2 pathway to control BMSC senescence and differentiation. siRNA knockdown; lentiviral overexpression; osteogenic differentiation assay; senescence markers; NRF2 pathway readout PeerJ Low 34820159
2023 RCBTB1 co-immunoprecipitates with UBE2E3 and with CUL3 from RPE cell protein lysates, placing RCBTB1 in a complex with UBE2E3 and the CUL3 E3 ligase scaffold and suggesting UBE2E3 participates in a CUL3-RCBTB1 ubiquitin ligase complex relevant to oxidative stress response. Co-immunoprecipitation from iPSC-derived RPE cells using UBE2E3 and CUL3 antibodies Cells Low 37408192

Source papers

Stage 0 corpus · 43 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1998 SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Molecular cell 930 9734360
1997 Ubch9 conjugates SUMO but not ubiquitin. FEBS letters 314 9409737
1999 Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. The Journal of biological chemistry 304 10187858
2012 The circadian protein period 1 contributes to blood pressure control and coordinately regulates renal sodium transport genes. Hypertension (Dallas, Tex. : 1979) 123 22526258
2012 Selective histone deacetylase (HDAC) inhibition imparts beneficial effects in Huntington's disease mice: implications for the ubiquitin-proteasomal and autophagy systems. Human molecular genetics 100 22965876
1999 Control of NF-kappa B transcriptional activation by signal induced proteolysis of I kappa B alpha. Philosophical transactions of the Royal Society of London. Series B, Biological sciences 86 10582246
2001 N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8. European journal of biochemistry 85 11322894
2011 Anti-Ro52 autoantibodies from patients with Sjögren's syndrome inhibit the Ro52 E3 ligase activity by blocking the E3/E2 interface. The Journal of biological chemistry 74 21862588
2014 UBE2E ubiquitin-conjugating enzymes and ubiquitin isopeptidase Y regulate TDP-43 protein ubiquitination. The Journal of biological chemistry 72 24825905
2014 Mulan E3 ubiquitin ligase interacts with multiple E2 conjugating enzymes and participates in mitophagy by recruiting GABARAP. Cellular signalling 71 25224329
2004 p14 Arf promotes small ubiquitin-like modifier conjugation of Werners helicase. The Journal of biological chemistry 53 15355988
2021 Sex-stratified gene-by-environment genome-wide interaction study of trauma, posttraumatic-stress, and suicidality. Neurobiology of stress 40 33665242
2021 Genome-wide association studies detects candidate genes for wool traits by re-sequencing in Chinese fine-wool sheep. BMC genomics 36 33602144
2020 Praja1 RING-finger E3 ubiquitin ligase suppresses neuronal cytoplasmic TDP-43 aggregate formation. Neuropathology : official journal of the Japanese Society of Neuropathology 30 32686212
2012 Identification of cellular proteins required for replication of human immunodeficiency virus type 1. AIDS research and human retroviruses 30 22404213
2004 Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-dependent regulation of the epithelial Na+ channel. Molecular and cellular biology 30 14993279
2010 Identification of target genes and pathways associated with chicken microRNA miR-143. Animal genetics 29 20064147
2014 The ubiquitin-conjugating enzyme UBE2E3 and its import receptor importin-11 regulate the localization and activity of the antioxidant transcription factor NRF2. Molecular biology of the cell 27 25378586
2005 The ubiquitin-protein ligases Nedd4 and Nedd4-2 show similar ubiquitin-conjugating enzyme specificities. The international journal of biochemistry & cell biology 25 16337426
2014 The ubiquitin-conjugating enzyme, UbcM2, is restricted to monoubiquitylation by a two-fold mechanism that involves backside residues of E2 and Lys48 of ubiquitin. Biochemistry 22 24901938
2015 Quantitative candidate gene association studies of metabolic traits in Han Chinese type 2 diabetes patients. Genetics and molecular research : GMR 21 26634513
2008 The human ubiquitin conjugating enzyme, UBE2E3, is required for proliferation of retinal pigment epithelial cells. Investigative ophthalmology & visual science 19 18614808
2023 miR-143-3p Promotes Ovarian Granulosa Cell Senescence and Inhibits Estradiol Synthesis by Targeting UBE2E3 and LHCGR. International journal of molecular sciences 17 37628741
2018 Loss of the ubiquitin conjugating enzyme UBE2E3 induces cellular senescence. Redox biology 17 29879550
2021 UBE2E3 regulates cellular senescence and osteogenic differentiation of BMSCs during aging. PeerJ 16 34820159
2020 UBA2 activates Wnt/β-catenin signaling pathway during protection of R28 retinal precursor cells from hypoxia by extracellular vesicles derived from placental mesenchymal stem cells. Stem cell research & therapy 16 33008487
2015 Transcription regulation of nuclear receptor PXR: Role of SUMO-1 modification and NDSM in receptor function. Molecular and cellular endocrinology 15 26549688
2024 Inhibition of miR-143-3p Restores Blood-Testis Barrier Function and Ameliorates Sertoli Cell Senescence. Cells 14 38391926
2023 Disruption in networking of KCMF1 linked ubiquitin ligase impairs autophagy in CD8+ memory T cells of patients with renal cell carcinoma. Cancer letters 13 37084875
2021 Epigenomic Profiles of African-American Transthyretin Val122Ile Carriers Reveals Putatively Dysregulated Amyloid Mechanisms. Circulation. Genomic and precision medicine 12 33428857
2014 The stability of herpes simplex virus 1 ICP0 early after infection is defined by the RING finger and the UL13 protein kinase. Journal of virology 12 24574411
1999 cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme. Cytogenetics and cell genetics 10 10343118
2020 Comprehensive Analysis of Differently Expressed and Methylated Genes in Preeclampsia. Computational and mathematical methods in medicine 9 33204297
2020 Comparison of Cross-Regulation by Different OTUB1:E2 Complexes. Biochemistry 8 32049508
2019 Identification of Important Invasion-Related Genes in Non-functional Pituitary Adenomas. Journal of molecular neuroscience : MN 7 30982163
2018 iTRAQ-Based Proteomic Analysis reveals possible target-related proteins and signal networks in human osteoblasts overexpressing FGFR2. Proteome science 6 29950929
2020 Genes regulating membrane-associated E-cadherin and proliferation in adenomatous polyposis coli mutant colon cancer cells: High content siRNA screen. PloS one 5 33057364
2023 Mitochondrial Dysfunction and Impaired Antioxidant Responses in Retinal Pigment Epithelial Cells Derived from a Patient with RCBTB1-Associated Retinopathy. Cells 4 37408192
2024 miR-379-5p affects breast cancer cell behavior by targeting UBE2E3 ubiquitin conjugating enzyme. PloS one 3 39621672
2023 Identification and Characterization of Physiological Pairing of E2 Ubiquitin-Conjugating Enzymes and E3 Ubiquitin Ligases. Methods in molecular biology (Clifton, N.J.) 2 36413307
2026 Genome-Wide Association Study for Glucocorticoid-Induced Ocular Hypertension. medRxiv : the preprint server for health sciences 0 41503457
2026 Genomic and transcriptomic analyses revealed potential candidate genes for egg production traits in domesticated ducks. Poultry science 0 41764961
2025 Preliminary exploration of potential biomarkers for heart failure and bipolar disorder: an exploratory study based on bioinformatics. Frontiers in psychiatry 0 41000338

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