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UBE2D3

Ubiquitin-conjugating enzyme E2 D3 · UniProt P61077

Length
147 aa
Mass
16.7 kDa
Annotated
2026-06-10
25 papers in source corpus 22 papers cited in narrative 22 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

UBE2D3 (UbcH5c) is a promiscuous E2 ubiquitin-conjugating enzyme that partners with diverse RING and U-box E3 ligases to ubiquitinate substrates across chromatin regulation, innate immunity, DNA damage signalling, cell-cycle control, and protein quality control (PMID:21772249, PMID:28469175, PMID:38866770, PMID:37059365). Its catalytic transfer activity depends on an active-site cysteine, Cys85, which can be covalently modified by small molecules to inactivate the enzyme (PMID:28696694, PMID:38181532). In chromatin and DNA-damage contexts it cooperates with the Ring1b/Bmi1 RING heterodimer—interacting exclusively with Ring1b—to monoubiquitinate histone H2A at K119 (PMID:21772249), and works with RNF168 downstream of ATM to drive DDR-induced chromatin ubiquitination, 53BP1 recruitment, and KAP1-S824 phosphorylation while simultaneously limiting RNF168 accumulation, defining a negative feedback circuit that promotes telomeric NHEJ (PMID:38866770); it is also selectively required for DNA-PK activation at one-ended replication-associated double-strand breaks (PMID:37244033). In innate immunity UBE2D3 acts with the E3 ligase Riplet to polyubiquitinate RIG-I, driving MAVS aggregation and antiviral signalling (PMID:28469175), and its activity supports NF-κB activation through ubiquitination of pathway components such as IκBα, RIP1, and NEMO (PMID:35272681, PMID:38181532). It directs substrate degradation in cell-cycle and p53 control, mediating ATRA-induced cyclin D1 turnover (PMID:17420285), targeting hTERT for proteasomal degradation (PMID:23741361, PMID:27105523), and enabling MDM2-driven p53 degradation through a UbcH5c-binding surface contributed by MDMX (PMID:33277368). Direct ubiquitinomic profiling identified the ribosomal proteins RPS10 and RPS20 as in vivo catalytic substrates linking UBE2D3 to ribosome-associated and autophagic protein quality control (PMID:37059365). Aurora B-mediated phosphorylation of a conserved amniote-specific Ser138 destabilizes UBE2D3 and modulates its interaction with the E3 ligase CBL, with this regulation being essential for early embryonic development (PMID:32145025).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2007 Medium

    Establishing that UBE2D3 controls a specific cell-cycle regulator addressed whether this E2 has dedicated substrate-degradation roles beyond generic ubiquitin transfer.

    Evidence Co-IP and shRNA knockdown linking UBE2D3 to ATRA-induced cyclin D1 degradation in APL cells

    PMID:17420285

    Open questions at the time
    • Cognate E3 ligase for cyclin D1 turnover not identified
    • Direct ubiquitination of cyclin D1 by UBE2D3 not reconstituted
  2. 2010 High

    Defining the structural basis of E4B U-box engagement clarified how an E3 module allosterically activates UBE2D3 for polyubiquitin chain elongation.

    Evidence Crystallography, NMR, and ITC of the E4B U-box bound to UbcH5c/Ubc4

    PMID:20696396

    Open questions at the time
    • In vivo substrates of the E4B-UBE2D3 pair not defined
    • Chain linkage type not established in this study
  3. 2011 High

    The Bmi1/Ring1b–UbcH5c structure explained how E2 selectivity and nucleosome contacts achieve site-specific H2A monoubiquitination on chromatin.

    Evidence X-ray crystallography with DNA-binding mutagenesis and H2A ubiquitination assays

    PMID:21772249

    Open questions at the time
    • Cellular consequences of H2A-K119 ubiquitination not addressed here
    • Regulation of complex assembly in vivo unknown
  4. 2013 Medium

    Identifying hTERT as a UBE2D3 interactor connected this E2 to telomerase control and radiosensitivity.

    Evidence Y2H, Co-IP, and knockdown with telomerase and cell-cycle assays

    PMID:23741361

    Open questions at the time
    • E3 ligase mediating hTERT ubiquitination not identified
    • Direct versus indirect regulation of hTERT not resolved
  5. 2016 Medium

    Demonstrating proteasome-dependent hTERT turnover upon UBE2D3 overexpression confirmed a causal degradation role rather than mere association.

    Evidence Overexpression with MG132 rescue, ubiquitination detection, and xenografts in esophageal cancer cells

    PMID:27105523

    Open questions at the time
    • Cognate E3 ligase still unidentified
    • Ubiquitin chain linkage on hTERT not characterized
  6. 2017 High

    Reconstituting RIG-I activation placed UBE2D3 at the heart of antiviral innate immune signalling.

    Evidence Chromatographic purification, reconstitution, and MAVS aggregation assays with Riplet

    PMID:28469175

    Open questions at the time
    • Ubiquitin chain architecture on RIG-I not fully defined
    • Regulation of Riplet-UBE2D3 pairing unknown
  7. 2017 Medium

    Solving the apo UbcH5c structure and identifying a covalent Cys85 inhibitor established the active site as a druggable handle for NF-κB suppression.

    Evidence X-ray crystallography of recombinant UbcH5c, plus α-santonin compound 6d binding by BIAcore, in-gel fluorescence, and NF-κB reporter assays

    PMID:28540177 PMID:28696694

    Open questions at the time
    • Selectivity of Cys85 inhibitors over other E2s not fully established
    • Functional structure determined without bound E3 in apo study
  8. 2020 High

    Genetic dissection of the MDM2/MDMX axis showed UBE2D3 binding is the limiting step that allows MDM2 to degrade p53.

    Evidence In vivo mouse p53 models, Co-IP, and MDMX-to-MDM2 domain-swap mutagenesis

    PMID:33277368

    Open questions at the time
    • Structural detail of the MDMX C-terminus–UbcH5c interface not resolved
    • Chain type built on p53 not addressed
  9. 2020 High

    Identifying Aurora B phosphorylation of an amniote-specific Ser138 revealed post-translational control of UBE2D3 stability and E3 partner selection with developmental consequences.

    Evidence Mouse S138A knock-in genetics, proximity ligation, and ESC differentiation assays

    PMID:32145025

    Open questions at the time
    • Mechanism by which phosphorylation destabilizes the fold not structurally defined
    • Full set of CBL-dependent substrates affected unknown
  10. 2021 Medium

    A cluster of disease-context studies extended UBE2D3 substrate scope to SHP-2/STAT3 signalling, p62 autophagy regulation, and COP1-mediated c-Jun degradation.

    Evidence Co-IP, ubiquitination assays, and knockdown across glioma, cardiac I/R, and Erk-inactivation models

    PMID:33918729 PMID:34195079 PMID:34391873

    Open questions at the time
    • c-Jun finding rests on single-method siRNA with western readout (Low confidence)
    • Direct ubiquitination versus indirect effects not always separated
    • Chain linkages on these substrates undefined
  11. 2022 Medium

    A second direct-binding inhibitor (DHPO) reinforced UBE2D3 as a tractable NF-κB target via blockade of IκBα ubiquitination.

    Evidence SPR and CETSA binding plus IκBα ubiquitination and NF-κB assays in pancreatic cancer models

    PMID:35272681

    Open questions at the time
    • Binding site on UBE2D3 not mapped in this study
    • Off-target E2 inhibition not excluded
  12. 2023 High

    Quantitative ubiquitinomics provided the first direct in vivo substrate identification, linking UBE2D3 catalysis to ribosome-associated protein quality control.

    Evidence SILAC diGly proteomics and TULIP2 with catalytic-mutant validation identifying RPS10/RPS20

    PMID:37059365

    Open questions at the time
    • E3 ligases pairing with UBE2D3 on RPS10/RPS20 not defined
    • Downstream fate of ubiquitinated ribosomal proteins not fully traced
  13. 2023 Medium

    An E2 siRNA screen pinpointed UBE2D3 as selectively required for DNA-PK activation at replication-associated one-ended breaks, distinguishing it from two-ended DSB responses.

    Evidence siRNA screen and knockdown with CPT versus neocarzinostatin, DNA-PK activation and chromosomal aberration assays

    PMID:37244033

    Open questions at the time
    • Direct ubiquitination substrate driving DNA-PK activation not identified
    • Cognate E3 ligase in this pathway unknown
  14. 2024 High

    Functional and structural work placed UBE2D3 as a multi-level regulator of ATM/RNF168 signalling and telomeric NHEJ, including a negative feedback loop constraining RNF168.

    Evidence UBE2D3 knockout with 53BP1, RNF168, KAP1, and PP2A assays; cryo-EM of the RNF168/UbcH5c–H1.0 chromatosome complex (preprint)

    PMID:38866770 PMID:bio_10.1101_2024.07.22.604500

    Open questions at the time
    • Mechanism by which UBE2D3 limits RNF168 accumulation not fully defined
    • Cryo-EM structure is a preprint
  15. 2025 High

    Two studies extended UBE2D3 into immune evasion via TAP2 ubiquitination and into meiotic cell-cycle control via Cyclin B1 turnover, demonstrating dosage-sensitive physiological roles.

    Evidence KLHL13-dependent K63 ubiquitination at TAP2-K245 with CD8+ T-cell and tumor assays; loss/gain-of-function in mouse oocytes with checkpoint and aneuploidy readouts

    PMID:39921465 PMID:41315272

    Open questions at the time
    • Whether UBE2D3 directly ubiquitinates Cyclin B1 versus acting through an E3 not resolved
    • Regulation of UBE2D3 expression in aged oocytes not mechanistically explained

Open questions

Synthesis pass · forward-looking unresolved questions
  • How E3 ligase pairing, chain-linkage choice, and post-translational state combine to dictate UBE2D3 substrate selectivity across its many pathways remains unresolved.
  • No unifying model linking E3 partner to linkage specificity
  • Cognate E3 ligases for several substrates (cyclin D1, hTERT, Cyclin B1) undefined
  • Tissue-specific regulation of UBE2D3 abundance poorly understood

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 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0000228 nuclear chromosome 2
Pathway
R-HSA-1640170 Cell Cycle 3 R-HSA-168256 Immune System 3 R-HSA-73894 DNA Repair 2 R-HSA-392499 Metabolism of proteins 1 R-HSA-4839726 Chromatin organization 1
Partners
BMI1CBLE4BKLHL13MDMXRING1BRIPLETRNF168

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2011 Crystal structure of the Bmi1/Ring1b RING-RING heterodimer in complex with UbcH5c revealed that UbcH5c interacts exclusively with Ring1b (not Bmi1) in a manner typical of E2-E3 interactions; the Bmi1/Ring1b dimer also contacts nucleosomal DNA via a basic surface patch unique to this heterodimer, enabling specific monoubiquitination of histone H2A at K119. X-ray crystallography, mutagenesis of DNA-binding surface residues, H2A ubiquitination activity assays, computational modelling of nucleosome interface The EMBO journal High 21772249
2010 The E4B U box domain (monomer) binds UbcH5c and Ubc4; structural and calorimetric/NMR binding assays indicate allosteric regulation of UbcH5c by the E4B U box, defining the molecular basis of E4B–UbcH5c assembly in polyubiquitin chain elongation. X-ray crystallography, NMR spectroscopy (scalar coupling measurements), isothermal titration calorimetry, NMR-based binding assays Structure High 20696396
2017 UBE2D3 (Ube2D3) was identified by chromatographic purification as an activator of RIG-I; together with the E3 ligase Riplet, UBE2D3 promotes covalent conjugation of polyubiquitin chains to RIG-I, which in turn induces MAVS prion-like aggregation on mitochondria to trigger innate immune signalling. Chromatographic purification, biochemical reconstitution, cell-based ubiquitination assays, MAVS aggregation assays, gene knockdown Nature communications High 28469175
2007 UBE2D3 is physically associated with cyclin D1 and mediates ATRA-induced cyclin D1 degradation; shRNA knockdown of UBE2D3 blocks ATRA-induced cyclin D1 degradation and cell-cycle arrest in APL NB4 cells. shRNA screen, co-immunoprecipitation, RNA interference knockdown, cell-cycle analysis Blood Medium 17420285
2020 MDMX interacts with UbcH5c (but MDM2 does not), and this interaction is essential for MDMX to enable MDM2 E3 ligase activity toward p53 degradation in vivo; grafting MDMX C-terminal residues onto MDM2 restored UbcH5c binding and enhanced MDM2-mediated p53 degradation in the absence of MDMX. In vivo mouse models (inducible p53 allele with MDM2/MDMX deletions), co-immunoprecipitation, domain-swap mutagenesis, mouse embryonic fibroblast assays Cancer research High 33277368
2013 UBE2D3 interacts with hTERT (identified by yeast two-hybrid and validated biochemically); UBE2D3 knockdown causes accumulation of hTERT and cyclin D1, increases hTERT activity, and accelerates G1-S transition, indicating UBE2D3 regulates radiosensitivity by controlling hTERT and cyclin D1 levels. Yeast two-hybrid screen, co-immunoprecipitation validation, shRNA knockdown, cell-cycle analysis, telomerase activity assay PloS one Medium 23741361
2016 UBE2D3 overexpression in EC109 esophageal cancer cells increases ubiquitinated hTERT species (detected after proteasome inhibition with MG132), decreases hTERT protein levels, and reduces telomerase activity, demonstrating UBE2D3 targets hTERT for proteasomal degradation via ubiquitination. UBE2D3 overexpression, proteasome inhibitor (MG132) treatment, detection of ubiquitinated hTERT by immunoprecipitation/western blot, telomerase activity assay, in vivo xenograft Oncotarget Medium 27105523
2017 Crystal structure of recombinant human UbcH5c was solved (space group P2₁2₁2₁, one molecule in asymmetric unit), providing structural basis for inhibitor design. X-ray crystallography of recombinant UbcH5c Acta pharmaceutica Sinica. B Medium 28540177
2017 The α-santonin-derived compound 6d covalently modifies the active-site Cys85 of UbcH5c, inactivating the enzyme and suppressing NF-κB activation; confirmed by BIAcore, in-gel fluorescence, and immunoprecipitation assays. BIAcore binding assay, in-gel fluorescence imaging, immunoprecipitation, NF-κB luciferase reporter assay, western blotting Journal of medicinal chemistry Medium 28696694
2021 UBE2D3 interacts with SHP-2 and promotes its ubiquitination, which activates the STAT3 signalling pathway and promotes glioma cell proliferation and glycolysis; UBE2D3 knockdown suppressed STAT3 phosphorylation, proliferation, and glycolysis both in vitro and in vivo. Co-immunoprecipitation, ubiquitination assays, siRNA knockdown, xenograft experiments, flow cytometry, metabolic flux assays Frontiers in oncology Medium 34195079
2021 UBE2D3 promotes ubiquitination of p62/SQSTM1, thereby impairing autophagic flux in myocardial ischemia-reperfusion injury; UBE2D3 also negatively regulates mTOR independently of the mTOR-beclin1 pathway. siRNA knockdown in vitro and in vivo rat I/R model, proteasome inhibitor (MG132) treatment, western blotting for p62 ubiquitination, autophagic flux assays Cellular signalling Medium 34391873
2021 PP1 and PP2A phosphatases and UBE2D3 were identified as required for COP1-mediated c-Jun degradation upon Erk1/2 inactivation; the C-terminus of c-Jun (last four amino acids) is also required for its degradation in this pathway. Pharmacological inhibitors (PP1/PP2A), siRNA gene knockdown of UBE2D3, c-Jun C-terminal deletion/tag mutagenesis, western blotting for c-Jun levels International journal of molecular sciences Low 33918729
2020 A conserved serine at position 138 (S138) in the C-terminal α-helical region of UBE2D3, present only in amniotes, is phosphorylated by Aurora B kinase; phosphorylation of S138 disrupts UBE2D3 structure and reduces its protein level in mouse ESCs. S138A substitution increases UBE2D3 levels, is an early embryonic lethal gain-of-function mutation in mice, reduces PDGFRα and FGFR1 levels, and increases UBE2D3 interaction with E3 ligase CBL. Protein sequence comparison, mouse genetics (S138A knock-in), proximity ligation assay, ESC differentiation assays, western blotting Molecular biology and evolution High 32145025
2023 UBE2D3 depletion by quantitative diGly ubiquitinomics revealed that RPS10 and RPS20 (ribosomal proteins critical for ribosome-associated protein quality control) are direct in vivo ubiquitination substrates of UBE2D3; catalytic activity of UBE2D3 is required for RPS10 ubiquitination in vivo. UBE2D3 also acts at multiple levels in autophagic protein quality control. SILAC-based diGly proteomics, label-free quantitative ubiquitinomics (UBE2D3 depletion), TULIP2 (Targets of Ubiquitin Ligases Identified by Proteomics) methodology, catalytic mutant UBE2D3 Molecular & cellular proteomics High 37059365
2023 UbcH5c (UBE2D3) is required for DNA-PK activation specifically in response to one-ended DSBs caused by replication fork collapse (CPT-induced), but not two-ended DSBs (neocarzinostatin-induced); this activation is independent of DNA end resection, and UbcH5c loss reduced DNA-PK-dependent chromosomal aberrations and attenuated cell-cycle checkpoint activation after CPT. siRNA library screen against E2 enzymes, siRNA knockdown of UbcH5c, camptothecin and neocarzinostatin treatment, DNA-PK activation assay, chromosomal aberration analysis, checkpoint assays Biochemical and biophysical research communications Medium 37244033
2024 UBE2D3 promotes NHEJ at telomeres by acting as a multi-level regulator: it contributes to DDR-induced chromatin ubiquitination and 53BP1 recruitment mediated by RNF168 upon ATM activation, while also limiting RNF168 accumulation and facilitating ATM-mediated phosphorylation of KAP1-S824. UBE2D3 deficiency leads to RNF168 hyperaccumulation, aberrant PP2A phosphatase activity, and defective KAP1-S824 phosphorylation, revealing a negative regulatory circuit. UBE2D3 knockout/depletion, telomeric NHEJ assays, 53BP1 recruitment assays, RNF168 accumulation monitoring, KAP1 phosphorylation assays, PP2A activity assays Nature communications High 38866770
2022 The small-molecule DHPO directly binds UbcH5c (confirmed by SPR and CETSA) and inhibits UbcH5c-mediated IκBα ubiquitination and degradation, thereby blocking NF-κB activation in pancreatic cancer cells. Surface plasmon resonance (SPR), cellular thermal shift assay (CETSA), western blot for IκBα ubiquitination, NF-κB reporter assay, in vitro and in vivo pancreatic cancer models Molecular cancer Medium 35272681
2023 Arteannuin B (ATB) covalently binds the catalytic Cys85 of UBE2D3, inhibiting its function and preventing ubiquitination of RIP1 and NEMO, thereby blocking NF-κB activation; confirmed by CETSA, DARTS, MST, LC-MS/MS identification of the binding site, and UBE2D3 siRNA knockdown. CETSA, DARTS, microscale thermophoresis (MST), LC-MS/MS mass spectrometry, molecular docking, siRNA knockdown, western blotting for RIP1/NEMO ubiquitination Phytomedicine Medium 38181532
2025 UBE2D3 binds the E3 ligase KLHL13 to mediate K63-linked polyubiquitination at K245 of TAP2, causing steric hindrance that blocks the TAP2 transporter; this impairs antigen presentation and enables pancreatic cancer cells to evade CD8+ T-cell surveillance in response to IFN-γ. Co-immunoprecipitation, ubiquitination site mapping (K245), genetic knockout/knockdown of UBE2D3, antigen presentation assays, CD8+ T-cell killing assays, mouse tumor models Nature communications High 41315272
2025 UBE2D3 is the most highly expressed E2 enzyme in mouse oocytes and is essential for meiotic division; depletion causes metaphase I arrest and Cyclin B1 accumulation, while overexpression reduces Cyclin B1 levels, causes kinetochore-microtubule mis-attachments, spindle assembly checkpoint dysfunction, and aneuploidy. Elevated UBE2D3 in aged oocytes contributes to age-related meiotic defects reversible by UBE2D3 knockdown or Cyclin B1 overexpression. UBE2D3 knockdown and overexpression in mouse oocytes, meiotic progression assays, Cyclin B1 level measurement, kinetochore-microtubule attachment analysis, spindle assembly checkpoint assays, aneuploidy scoring FASEB journal Medium 39921465
2007 Xenopus ube2d3.2 (ortholog of UBE2D3) interacts with xMLK2 (identified by yeast two-hybrid) and limits xMLK2 accumulation; ectopic ube2d3.2 expression inhibits pronephric tubule formation, phenocopying loss of xMLK2, implicating ube2d3.2 as an endogenous regulator of xMLK2 and JNK activity. Yeast two-hybrid screen, ectopic expression in Xenopus embryos, xMLK2 protein level assay, pronephros morphology analysis Differentiation Low 18021256
2024 Cryo-EM structure of the RNF168/UbcH5c–Ub/H1.0–K63-Ub₃ chromatosome complex revealed the recruitment orientation between the RNF168 UDM1 domain and K63-linked ubiquitin chain on H1.0, providing structural basis for how K63-polyubiquitinated H1.0 stimulates RNF168-mediated H2A ubiquitination. Cryo-EM structural analysis, biochemical reconstitution with synthetic ubiquitylated H1.0, RNF168 ubiquitylation activity assays on chromatosomes bioRxivpreprint Medium bio_10.1101_2024.07.22.604500

Source papers

Stage 0 corpus · 25 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2011 Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. The EMBO journal 134 21772249
2017 Ube2D3 and Ube2N are essential for RIG-I-mediated MAVS aggregation in antiviral innate immunity. Nature communications 81 28469175
2022 Targeting E2 ubiquitin-conjugating enzyme UbcH5c by small molecule inhibitor suppresses pancreatic cancer growth and metastasis. Molecular cancer 43 35272681
2010 Molecular basis for the association of human E4B U box ubiquitin ligase with E2-conjugating enzymes UbcH5c and Ubc4. Structure (London, England : 1993) 41 20696396
2007 RNAi screen identifies UBE2D3 as a mediator of all-trans retinoic acid-induced cell growth arrest in human acute promyelocytic NB4 cells. Blood 41 17420285
2017 Discovery of Potent Small-Molecule Inhibitors of Ubiquitin-Conjugating Enzyme UbcH5c from α-Santonin Derivatives. Journal of medicinal chemistry 38 28696694
2020 MDMX Recruits UbcH5c to Facilitate MDM2 E3 Ligase Activity and Subsequent p53 Degradation In Vivo. Cancer research 36 33277368
2013 Inhibition of UBE2D3 expression attenuates radiosensitivity of MCF-7 human breast cancer cells by increasing hTERT expression and activity. PloS one 26 23741361
2016 Downregulation of Ubiquitin-conjugating Enzyme UBE2D3 Promotes Telomere Maintenance and Radioresistance of Eca-109 Human Esophageal Carcinoma Cells. Journal of Cancer 25 27326259
2023 Arteannuin B, a sesquiterpene lactone from Artemisia annua, attenuates inflammatory response by inhibiting the ubiquitin-conjugating enzyme UBE2D3-mediated NF-κB activation. Phytomedicine : international journal of phytotherapy and phytopharmacology 19 38181532
2016 UBE2D3 gene overexpression increases radiosensitivity of EC109 esophageal cancer cells in vitro and in vivo. Oncotarget 18 27105523
2021 UBE2D3 Activates SHP-2 Ubiquitination to Promote Glycolysis and Proliferation of Glioma via Regulating STAT3 Signaling Pathway. Frontiers in oncology 15 34195079
2020 The E2 ubiquitin-conjugating enzyme UbcH5c: an emerging target in cancer and immune disorders. Drug discovery today 15 32947046
2021 UBE2D3 contributes to myocardial ischemia-reperfusion injury by regulating autophagy in dependence of p62/SQSTM1. Cellular signalling 13 34391873
2023 Ubiquitinome Profiling Reveals in Vivo UBE2D3 Targets and Implicates UBE2D3 in Protein Quality Control. Molecular & cellular proteomics : MCP 12 37059365
2025 Eupalinolide B inhibits periodontitis development by targeting ubiquitin conjugating enzyme UBE2D3. MedComm 9 39811801
2017 Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c. Acta pharmaceutica Sinica. B 9 28540177
2025 UBE2D3 functions in mouse oocyte meiotic maturation. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 5 39921465
2024 UBE2D3 facilitates NHEJ by orchestrating ATM signalling through multi-level control of RNF168. Nature communications 5 38866770
2021 Erk1/2 Inactivation-Induced c-Jun Degradation Is Regulated by Protein Phosphatases, UBE2d3, and the C-Terminus of c-Jun. International journal of molecular sciences 4 33918729
2023 UbcH5c-dependent activation of DNA-dependent protein kinase in response to replication-mediated DNA double-strand breaks. Biochemical and biophysical research communications 3 37244033
2020 Evolution of an Amniote-Specific Mechanism for Modulating Ubiquitin Signaling via Phosphoregulation of the E2 Enzyme UBE2D3. Molecular biology and evolution 3 32145025
2007 A ubiquitin-conjugating enzyme, ube2d3.2, regulates xMLK2 and pronephros formation in Xenopus. Differentiation; research in biological diversity 2 18021256
2024 UBE2D3 regulated by WTAP-mediated m6A modification inhibits temozolomide chemosensitivity in glioblastoma. Naunyn-Schmiedeberg's archives of pharmacology 1 39085511
2025 IFN-γ-driven UBE2D3 upregulation impairs antigen presentation pathways and anti-tumor immunity in pancreatic cancer. Nature communications 0 41315272

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