Affinage

UBE3C

Ubiquitin-protein ligase E3C · UniProt Q15386

Length
1083 aa
Mass
123.9 kDa
Annotated
2026-06-10
36 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

UBE3C is a HECT-domain E3 ubiquitin ligase that functions as a processivity factor for the 26S proteasome, ubiquitinating partially proteolyzed and misfolded substrates to ensure their complete degradation (PMID:24158444). It cycles dynamically on and off the proteasome, with stable association driven by the presence of ubiquitinated substrate and stabilized cooperatively by USP14 binding (PMID:28396413); structural placement of its catalytic HECT domain above the RPN11 deubiquitinase active site at the 19S regulatory particle positions UBE3C to couple ubiquitination with substrate processing at the proteasome entry channel [PMID:bio_10.1101_2025.07.31.667872]. Its catalytic HECT domain adopts an open, L-shaped bilobed fold whose C-terminal residues and N-lobe loops are required for E2-E3 transthiolation and activity, with Lys903 as the major autoubiquitination site (PMID:32039437). UBE3C responds acutely to protein misfolding, being recruited to the proteasome and ubiquitinating the ubiquitin receptors RPN10 and RPN13 upon unfolding stress (PMID:31375563), and it clears low-level misfolded oligomers through a proteasomal route distinct from NRF1-dependent proteasome upregulation (PMID:39636856); it also contributes to ER-associated degradation of misfolded CFTR (ΔF508) and ABCB1 (PMID:38067172). Beyond canonical degradation, UBE3C assembles atypical branched ubiquitin chains to regulate autophagy: K29/K48-branched chains on VPS34 (reversed by TRABID) drive its proteasomal degradation and suppress autophagosome formation (PMID:33637724), and K33-branched chains on ATG4B Lys119 inhibit ATG4B activity and LC3 interaction non-degradatively (PMID:38146933). UBE3C further targets specific substrates across diverse contexts — cyclin B1 during estrogen/ERα-stimulated mitosis (PMID:26389696), progesterone receptor under P38α-restrained control important for uterine receptivity (PMID:35914132), AXIN1 to activate Wnt/β-catenin signaling (PMID:32930707), IRF3 via K48 chains to resolve antiviral responses (PMID:39120972), picornaviral 2C protein via K33/K48 chains to restrict viral replication (PMID:39212385), and mLST8 (non-degradatively, recruited by the SLAP adaptor) to limit mTORC2-AKT signaling (PMID:41398047). P38α-mediated phosphorylation at Ser741 restrains UBE3C ligase activity (PMID:35914132).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2013 High

    Established UBE3C's core cellular role as a proteasome-associated processivity factor, answering why some substrates escape complete degradation.

    Evidence Forward genetic screen, siRNA knockdown, active-site and proteasome-binding mutagenesis, and substrate lysine-less mutants with polyubiquitination assays

    PMID:24158444

    Open questions at the time
    • Did not define which proteasome subunit anchors UBE3C
    • Chain linkage type used at the proteasome not resolved
  2. 2017 High

    Showed UBE3C association with the proteasome is substrate-driven and cooperative with USP14, explaining how its recruitment is gated.

    Evidence Biochemical fractionation and purified proteasome binding assays with recombinant USP14, plus inhibitor and cell-based blockade experiments

    PMID:28396413

    Open questions at the time
    • Molecular basis of the USP14–UBE3C cooperativity not structurally defined
    • Whether deubiquitination and ubiquitination are spatially coordinated unresolved at the time
  3. 2019 High

    Demonstrated UBE3C is an immediate responder to soluble misfolded protein, ubiquitinating proteasomal ubiquitin receptors RPN10/RPN13 as part of the response.

    Evidence Global K-GG ubiquitin proteomics with an inducible FKBP destabilizing-domain misfolding system and quantitative MS

    PMID:31375563

    Open questions at the time
    • Functional consequence of RPN10/RPN13 ubiquitination for proteasome function not fully defined
    • Distinction between monomer/oligomer and aggregate substrates not yet established
  4. 2020 High

    Provided the structural framework for UBE3C catalysis, defining the HECT fold, autoubiquitination site, and residues required for transthiolation.

    Evidence 2.7 Å X-ray crystallography of the HECT domain with in vitro ubiquitination, site-directed mutagenesis, and deletion analysis

    PMID:32039437

    Open questions at the time
    • Structure of full-length protein and substrate-bound complexes not solved
    • Structural basis of branched-chain specificity not addressed
  5. 2021 High

    Revealed UBE3C builds atypical K29/K48-branched chains on VPS34 to suppress autophagy and that proteotoxic stress redistributes UBE3C between phagophores and proteasomes, linking proteostasis to autophagy regulation.

    Evidence Co-IP, ubiquitin chain-linkage MS, in vitro ubiquitination, knockdown, live-cell imaging, and in vivo liver metabolic studies

    PMID:33637724

    Open questions at the time
    • Signals controlling UBE3C subcellular redistribution not fully defined
    • How TRABID is targeted to VPS34 chains unclear
  6. 2021 Medium

    Identified UBE3C as an ERα-stimulated mitotic ligase for cyclin B1 and as a Wnt-pathway regulator via AXIN1 degradation, extending its substrate repertoire to cell-cycle and signaling control.

    Evidence Co-IP from mitotic MCF-7 cells, in vitro E3 assays, immunofluorescence co-localization, knockdown, and xenograft models

    PMID:26389696 PMID:32930707

    Open questions at the time
    • Ubiquitin linkage types on cyclin B1 and AXIN1 not mapped
    • Findings each from a single lab without reciprocal validation
  7. 2022 High

    Established physiological regulation of UBE3C by P38α phosphorylation at Ser741 and its in vivo importance, controlling progesterone receptor stability for uterine receptivity.

    Evidence Conditional knockout mice, Co-IP, ubiquitination assays, phosphorylation-site mutagenesis, and genetic rescue

    PMID:35914132

    Open questions at the time
    • Whether Ser741 phosphorylation regulates UBE3C activity toward other substrates not tested
    • Mechanism by which phosphorylation restrains catalysis not structurally defined
  8. 2024 High

    Showed UBE3C can act non-degradatively, assembling K33-branched chains on ATG4B to inhibit its enzymatic activity, broadening the functional output of its ligase activity.

    Evidence MS site identification, Co-IP, in vitro ubiquitination, K119R mutagenesis rescue, and autophagy flux assays

    PMID:38146933

    Open questions at the time
    • Deubiquitinase removing K33 chains during starvation not identified
    • Signal decreasing the ATG4B–UBE3C interaction unknown
  9. 2024 High

    Distinguished a UBE3C-dependent proteasomal route for clearing low-level misfolded oligomers from an NRF1-dependent pathway engaged at higher aggregate burden, and excluded autophagy in this turnover.

    Evidence Inducible agDD-GFP aggregate system, targeted knockdowns, cryo-electron tomography, and quantitative degradation assays

    PMID:39636856

    Open questions at the time
    • How the cell switches between UBE3C- and NRF1-dependent responses not defined
    • Whether RPN13 ubiquitination plays any role in oligomer clearance contradicted prior model
  10. 2024 Medium

    Placed UBE3C in antiviral and ERAD contexts, mediating IRF3 K48 degradation to resolve interferon responses, restricting picornaviruses via 2C ubiquitination, and assisting degradation of misfolded CFTR.

    Evidence Co-IP, ubiquitination assays, site mutagenesis (2C K268R), recombinant virus and surface biotinylation experiments, knockdown

    PMID:38067172 PMID:39120972 PMID:39212385

    Open questions at the time
    • IRF3 substrate handoff from BAP1 not reconstituted in vitro
    • CFTR effect appears largely independent of direct CFTR ubiquitination, mechanism unclear
    • Each result from a single lab
  11. 2025 Medium

    Identified adaptor-mediated and developmental roles — SLAP-recruited non-degradative mLST8 ubiquitination limiting mTORC2-AKT, and UBE3C control of cortical neural fate via the Cbll1–m6A axis.

    Evidence Co-IP, K86R/K215R mutagenesis, mTORC2 integrity assays, xenografts; brain organoid genetics, proteomic substrate profiling, and METTL3-inhibitor rescue (preprint)

    PMID:41398047 PMID:bio_10.1101_2025.04.09.646620

    Open questions at the time
    • Disease-variant link to cortical phenotype remains in preprint and unreplicated
    • How SLAP redirects UBE3C specificity not structurally defined
  12. 2025 Medium

    Provided structural placement of UBE3C/Hul5 on the 19S regulatory particle above RPN11, proposing coupled ubiquitination and deubiquitination at the proteasome substrate entry channel.

    Evidence PhIX-MS crosslinking, cryo-EM, and AlphaFold modeling (preprint)

    PMID:bio_10.1101_2025.07.31.667872

    Open questions at the time
    • Preprint, single study not independently replicated
    • Functional coupling between UBE3C and RPN11 not demonstrated biochemically
  13. 2025 Low

    Extended the substrate list to oncogenic and tumor-suppressor proteins (p53, TP73, BRAF V600E, AHNAK) and MYC, implicating UBE3C in cancer phenotypes.

    Evidence Co-IP, ubiquitination assays, knockdown/CRISPR, MYC-GFP CRISPR screen with paralog specificity, and pharmacological rescues

    PMID:37173692 PMID:40553397 PMID:40602747 PMID:40696164 PMID:41965876

    Open questions at the time
    • Ubiquitination sites and chain linkages not mapped for these substrates
    • Direct vs indirect regulation of MYC not established
    • Each from a single lab without reciprocal validation

Open questions

Synthesis pass · forward-looking unresolved questions
  • How UBE3C achieves substrate and chain-linkage specificity — selecting among degradative K48 and non-degradative branched K29/K33 chains across its many substrates — and how adaptors, phosphorylation, and proteasome positioning collectively dictate outcome remain unresolved.
  • No unifying structural model of substrate-bound UBE3C
  • Determinants of branched vs linear chain assembly unknown
  • Rules governing degradative vs non-degradative outcomes undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016874 ligase activity 8 GO:0140096 catalytic activity, acting on a protein 4
Localization
GO:0005634 nucleus 2 GO:0005829 cytosol 2
Pathway
R-HSA-392499 Metabolism of proteins 4 R-HSA-168256 Immune System 2 R-HSA-9612973 Autophagy 2
Partners
ATG4BAXIN1ESR1IRF3MLST8SLAUSP14VPS34

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2013 UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates; knockdown causes slower and incomplete degradation of destabilizing domain-GFP reporters, and this processivity function requires UBE3C catalytic activity, its ability to bind the proteasome, and lysine residues on the substrate. Forward genetic screen, siRNA knockdown, active-site mutagenesis, proteasome-binding mutants, substrate lysine-less mutants, polyubiquitination assays The Journal of biological chemistry High 24158444
2017 UBE3C (and USP14) dynamically cycle on and off the 26S proteasome, and the presence of ubiquitinated substrate proteins promotes their stable association; ubiquitin conjugates on the proteasome also enhance USP14 binding, which in turn further stabilizes UBE3C binding. Biochemical fractionation, purified proteasome binding assays with recombinant USP14, inhibitor treatments (IU-1, ubiquitin aldehyde), cell-based ubiquitination blockade experiments Proceedings of the National Academy of Sciences of the United States of America High 28396413
2019 Acute protein misfolding (unfolding of AgDD) rapidly recruits UBE3C to the 26S proteasome and triggers ubiquitylation of the proteasomal ubiquitin receptors RPN10 and RPN13; this is an immediate cellular response to misfolded monomers/oligomers rather than insoluble aggregates. Global diglycine-capture (K-GG) ubiquitin proteomics, engineered FKBP-based destabilizing domain system, quantitative MS The Journal of biological chemistry High 31375563
2020 Crystal structure of the UBE3C HECT domain (aa 693–1083) at 2.7 Å reveals an open, L-shaped bilobed conformation; Lys903 is the major autoubiquitination site; deletion of the last three C-terminal residues abolishes activity; mutations of Gln961 and Ser1049 substantially reduce autoubiquitination; the N-terminal region (aa 693–743) and a loop (aa 758–762) in the N-lobe affect stability and activity; these regions are involved in E2-E3 transthiolation. X-ray crystallography (2.7 Å), in vitro ubiquitination assays, site-directed mutagenesis, deletion analysis The Biochemical journal High 32039437
2021 UBE3C assembles K29/K48-branched ubiquitin chains on VPS34, promoting VPS34 binding to proteasomes and its degradation, thereby suppressing autophagosome formation and maturation; TRABID deubiquitinase reverses this modification. Under ER/proteotoxic stress, UBE3C is redistributed from phagophores to proteasomes, attenuating VPS34 ubiquitination and elevating autophagy. Co-immunoprecipitation, ubiquitin chain-linkage mass spectrometry, in vitro ubiquitination assays, siRNA knockdown, live-cell imaging, subcellular fractionation, in vivo liver metabolic studies Nature communications High 33637724
2021 UBE3C interacts with ERα during mitosis in an estrogen-dependent manner; estrogen stimulates UBE3C E3 ligase activity in the presence of ERα in vitro; UBE3C ubiquitinates cyclin B1 (CCNB1) and promotes its degradation during mitosis; ERα, UBE3C, and CCNB1 co-localize in prophase nuclei and metaphase spindles; UBE3C depletion attenuates estrogen-dependent cell proliferation. Co-immunoprecipitation from mitotic MCF-7 cells, in vitro E3 ubiquitin ligase assay, siRNA knockdown, immunofluorescence co-localization Molecular endocrinology (Baltimore, Md.) Medium 26389696
2021 UBE3C promotes ubiquitination and proteasomal degradation of AXIN1, thereby increasing β-catenin nuclear accumulation and activating Wnt/β-catenin signaling in gastric cancer cells; knockdown increases AXIN1 and reduces nuclear β-catenin. Co-immunoprecipitation, ubiquitination assay, siRNA knockdown and overexpression, xenograft mouse model, western blot Carcinogenesis Medium 32930707
2022 Ube3c targets progesterone receptor (PR) for polyubiquitination and proteasomal degradation; P38α kinase phosphorylates Ube3c at serine 741, restraining its polyubiquitination activity toward PR; uterine-selective P38α deletion leads to excessive Ube3c-mediated PR degradation, defective uterine receptivity, and female infertility. Conditional knockout mouse model, Co-immunoprecipitation, ubiquitination assay, phosphorylation site mutagenesis, genetic rescue experiments Proceedings of the National Academy of Sciences of the United States of America High 35914132
2024 UBE3C assembles K33-branched ubiquitin chains on ATG4B at Lys119 without causing ATG4B degradation; this ubiquitination inhibits ATG4B activity and its interaction with LC3, suppressing autophagy flux; under starvation, the ATG4B–UBE3C interaction decreases with concomitant removal of K33-branched chains, allowing starvation-induced autophagy. Mass spectrometry identification, Co-immunoprecipitation, in vitro ubiquitination assay, site-directed mutagenesis (K119R ATG4B), autophagy flux assays, overexpression/knockout cell studies Autophagy High 38146933
2024 UBE3C sequentially follows BAP1 to control IRF3 stability during viral infection: in the early innate immune phase, BAP1 removes K48-linked ubiquitination from IRF3 in the nucleus; in the late phase, IFN-β-induced UBE3C mediates K48-linked ubiquitination of IRF3, promoting its proteasomal degradation to resolve the antiviral response. Co-immunoprecipitation, ubiquitination assay, siRNA knockdown, overexpression, temporal analysis of viral infection stages Cell reports Medium 39120972
2024 UBE3C facilitates ERAD of misfolded CFTR (ΔF508) and ΔY490-ABCB1 independently of RNF185/RNF5; UBE3C knockdown has limited impact on CFTR ubiquitination itself but stabilizes mature ΔF508-CFTR and increases its plasma membrane expression, as well as stabilizing a class VI CFTR mutant (T70-CFTR). siRNA knockdown, cell surface biotinylation, western blot, functional channel assays, combined RNF5/185 ablation with UBE3C knockdown Cells Medium 38067172
2024 UBE3C binds the 2C protein of EV-A71 (via its C-terminal domain) and promotes K33/K48-linked ubiquitination of 2C at Lys268, leading to its degradation and restriction of viral replication; the K268R mutant 2C resists UBE3C-mediated degradation; UBE3C also ubiquitinates 2C from CVB3 and CVA16. Co-immunoprecipitation, in vitro ubiquitination assay, site-directed mutagenesis (2C K268R), recombinant virus experiments, siRNA knockdown and overexpression, viral titer measurement Journal of virology Medium 39212385
2024 Acute lower-level misfolded protein aggregates (oligomers) are degraded via a UBE3C-dependent proteasomal pathway that is independent of RPN13 ubiquitylation by UBE3C; higher aggregate burden activates NRF1-dependent proteasome upregulation instead; no evidence for autophagy involvement in aggregate turnover. Inducible agDD-GFP aggregate system, targeted gene knockdown, cryo-electron tomography, quantitative protein degradation assays Proceedings of the National Academy of Sciences of the United States of America High 39636856
2025 UBE3C interacts with BRAF V600E via the kinase domain and promotes its ubiquitination; BRAF V600E stability is modulated by UBE3C expression and also depends on HSP90 activity; UBE3C knockout increases BRAF V600E levels in multiple myeloma cells. Tandem affinity purification, Co-immunoprecipitation, ubiquitination assay, HSP90 inhibitor treatment, CRISPR/siRNA knockdown Life sciences Low 40602747
2025 UBE3C catalyzes p53 ubiquitination, promoting its proteasomal degradation in pancreatic ductal adenocarcinoma cells; UBE3C knockdown increases p53 levels and promotes apoptosis, effects reversed by the p53 inhibitor pifithrin-α. Co-immunoprecipitation, ubiquitination assay, siRNA knockdown and overexpression, pharmacological p53 inhibitor rescue, cell proliferation and apoptosis assays Molecular biology reports Low 40553397
2025 The SLAP adaptor protein interacts with mLST8 and recruits UBE3C to mediate non-degradative ubiquitination of mLST8 at Lys86 and Lys215, reducing mTORC2 complex integrity and suppressing mTORC2-AKT signaling in colorectal cancer cells. Co-immunoprecipitation, ubiquitination assay with mutagenesis (K86R/K215R), Co-IP of SLAP-UBE3C interaction, mTORC2 integrity assays, xenograft mouse model Cell death and differentiation Medium 41398047
2025 UBE3C regulates cellular composition of the murine cerebral cortex and human brain organoids; its loss favors neurogenesis and suppresses glial fate; disease-associated UBE3C mutations alter autoubiquitination activity and disrupt cortical lamination; proteomic profiling identifies Cbll1 (a m6A methyltransferase component) as a UBE3C substrate; the UBE3C–Cbll1 axis drives m6A mRNA methylation in neural progenitors; hyperactivation of m6A writers in UBE3C-deficient progenitors impairs cell cycle exit, reversible by the METTL3 inhibitor STM2457. Genetic complementation in mouse and human brain organoids, proteomic substrate profiling, autoubiquitination assays, disease-variant mutagenesis, METTL3 inhibitor rescue in vivo bioRxivpreprint Medium bio_10.1101_2025.04.09.646620
2025 PhIX-MS crosslinking coupled with cryo-EM places UBE3C/Hul5 along the 19S regulatory particle (RP) of the proteasome with its catalytic HECT domain positioned above the RPN11 deubiquitinase active site, enabling coupled ubiquitination and deubiquitination activities at the proteasome entry channel. Photo-induced in situ crosslinking mass spectrometry (PhIX-MS), cryo-electron microscopy, AlphaFold structural modeling bioRxivpreprint Medium bio_10.1101_2025.07.31.667872
2025 CRISPR loss-of-function screen in multiple myeloma cells shows UBE3C knockout markedly increases endogenous MYC protein levels, suggesting UBE3C negatively regulates MYC; paralogs UBE3A and UBE3B showed no measurable effect, indicating specificity. Genome-wide CRISPR-Cas9 loss-of-function screen, endogenous MYC-GFP reporter, FACS sorting, next-generation sequencing, functional validation of individual knockouts Scientific reports Low 41965876
2023 UBE3C mediates ubiquitination-dependent proteasomal degradation of TP73, contributing to radioresistance in breast cancer cells; FOSB transcriptionally activates UBE3C, and LINC00963 recruits FOSB to the UBE3C promoter. Co-immunoprecipitation, immunofluorescence, siRNA knockdown and overexpression, in vitro/in vivo functional assays, rescue experiments Journal of translational medicine Low 37173692
2025 UBE3C promotes ubiquitination and degradation of AHNAK protein in osteosarcoma cells, suppressing ferroptosis; METTL5-mediated m6A modification of UBE3C mRNA enhances its stability via YTHDF1 binding. Co-immunoprecipitation, ubiquitination assay, siRNA knockdown, ferroptosis assays, m6A methylation analysis Journal of molecular histology Low 40696164

Source papers

Stage 0 corpus · 36 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2021 VPS34 K29/K48 branched ubiquitination governed by UBE3C and TRABID regulates autophagy, proteostasis and liver metabolism. Nature communications 73 33637724
2013 The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates. The Journal of biological chemistry 69 24158444
2017 Ubiquitinated proteins promote the association of proteasomes with the deubiquitinating enzyme Usp14 and the ubiquitin ligase Ube3c. Proceedings of the National Academy of Sciences of the United States of America 63 28396413
2022 Circular RNA circPOLR2A promotes clear cell renal cell carcinoma progression by facilitating the UBE3C-induced ubiquitination of PEBP1 and, thereby, activating the ERK signaling pathway. Molecular cancer 61 35840930
2016 MiR-30a-5p/UBE3C axis regulates breast cancer cell proliferation and migration. Biochemical and biophysical research communications 48 27003255
2017 MiR-542-3p inhibits metastasis and epithelial-mesenchymal transition of hepatocellular carcinoma by targeting UBE3C. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 43 28666208
2014 Clinical significance of the ubiquitin ligase UBE3C in hepatocellular carcinoma revealed by exome sequencing. Hepatology (Baltimore, Md.) 40 24425307
2015 UBE3C promotes growth and metastasis of renal cell carcinoma via activating Wnt/β-catenin pathway. PloS one 36 25658088
2021 UBE3C promotes proliferation and inhibits apoptosis by activating the β-catenin signaling via degradation of AXIN1 in gastric cancer. Carcinogenesis 19 32930707
2020 Crystal structure of HECT domain of UBE3C E3 ligase and its ubiquitination activity. The Biochemical journal 19 32039437
2024 UBE3C tunes autophagy via ATG4B ubiquitination. Autophagy 18 38146933
2022 P38α MAPK is a gatekeeper of uterine progesterone responsiveness at peri-implantation via Ube3c-mediated PGR degradation. Proceedings of the National Academy of Sciences of the United States of America 18 35914132
2019 Acute unfolding of a single protein immediately stimulates recruitment of ubiquitin protein ligase E3C (UBE3C) to 26S proteasomes. The Journal of biological chemistry 16 31375563
2010 Association analysis of UBE3C polymorphisms in Korean aspirin-intolerant asthmatic patients. Annals of allergy, asthma & immunology : official publication of the American College of Allergy, Asthma, & Immunology 16 20934631
2023 LINC00963-FOSB-mediated transcription activation of UBE3C enhances radioresistance of breast cancer cells by inducing ubiquitination-dependent protein degradation of TP73. Journal of translational medicine 15 37173692
2016 Ubiquitin ligase UBE3C promotes melanoma progression by increasing epithelial-mesenchymal transition in melanoma cells. Oncotarget 15 26894856
2011 UBE3C genetic variations as potent markers of nasal polyps in Korean asthma patients. Journal of human genetics 12 21881582
2021 Oncogenic UBE3C promotes breast cancer progression by activating Wnt/β-catenin signaling. Cancer cell international 11 33407510
2023 Novel gene-intergenic fusion involving ubiquitin E3 ligase UBE3C causes distal hereditary motor neuropathy. Brain : a journal of neurology 10 36380488
2022 Biallelic variants in HECT E3 paralogs, HECTD4 and UBE3C, encoding ubiquitin ligases cause neurodevelopmental disorders that overlap with Angelman syndrome. Genetics in medicine : official journal of the American College of Medical Genetics 10 36401616
2015 Liganded ERα Stimulates the E3 Ubiquitin Ligase Activity of UBE3C to Facilitate Cell Proliferation. Molecular endocrinology (Baltimore, Md.) 10 26389696
2024 Recurrent UBE3C-LRP5 translocations in head and neck cancer with therapeutic implications. NPJ precision oncology 8 38438481
2024 The deubiquitinase BAP1 and E3 ligase UBE3C sequentially target IRF3 to activate and resolve the antiviral innate immune response. Cell reports 6 39120972
2023 UBE3C Facilitates the ER-Associated and Peripheral Degradation of Misfolded CFTR. Cells 6 38067172
2016 Effect of UBE3C polymorphisms on intramuscular fat content and fatty acid composition in Duroc pigs. Genetics and molecular research : GMR 5 27706631
2024 Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways. Proceedings of the National Academy of Sciences of the United States of America 4 39636856
2025 METTL5-mediated m6A modification of UBE3C promotes osteosarcoma progression by suppressing ferroptosis via inducing AHNAK ubiquitination. Journal of molecular histology 3 40696164
2020 Association of UBE3C Variants with Reduced Kidney Function in Patients with Diabetic Kidney Disease. Journal of personalized medicine 3 33171965
2025 Exosomal miR-137-3p targets UBE3C to activate STAT3, promoting migration and differentiation into endometrial epithelial cell of human umbilical cord mesenchymal stem cells under hypoxia. World journal of stem cells 2 40308888
2024 UBE3C restricts EV-A71 replication by ubiquitination-dependent degradation of 2C. Journal of virology 2 39212385
2025 Melatonin mitigates ovarian aging through regulation of the YTHDF2/m 6A/UBE3C axis. Acta biochimica et biophysica Sinica 1 40495659
2025 Identification of UBE3C as an E3 ubiquitin ligase for mutant BRAF. Life sciences 1 40602747
2026 Endogenous protein tagging coupled with a CRISPR screening approach identifies UBE3C as a potential MYC oncogene regulator. Scientific reports 0 41965876
2025 UBE3C promotes pancreatic ductal adenocarcinoma progression by catalysing p53 ubiquitination. Molecular biology reports 0 40553397
2025 SLAP controls mTORC2 integrity via UBE3C-mediated non-degradative mLST8 ubiquitination to suppress colorectal tumorigenesis. Cell death and differentiation 0 41398047
2024 Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways. bioRxiv : the preprint server for biology 0 39282280

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