Affinage

UBE2L3

Ubiquitin-conjugating enzyme E2 L3 · UniProt P68036

Length
154 aa
Mass
17.9 kDa
Annotated
2026-04-28
60 papers in source corpus 30 papers cited in narrative 30 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

UBE2L3 (UbcH7) is an E2 ubiquitin-conjugating enzyme that lacks intrinsic lysine reactivity and therefore functions selectively with HECT-type and RBR-type E3 ligases, which transfer ubiquitin through an obligate thioester intermediate on their own catalytic cysteine (PMID:21532592). Structural studies reveal that UBE2L3 is recruited by RING domains of E3 ligases such as c-Cbl and HHARI, with RBR E3s employing a unique steric mechanism to maintain the E2~Ub conjugate in an open conformation that favors transthiolation to the E3 active site rather than direct substrate lysine discharge (PMID:10966114, PMID:28552575, PMID:30446597). UBE2L3 partners with diverse E3 ligases—including LUBAC (HOIL-1/HOIP), E6-AP, Itch/Ndfip1, TRIP12, AREL1, SMURF1, and parkin—to ubiquitinate substrates such as pro-IL-1β, 53BP1, p27Kip1, steroid receptors, and mitochondrial proteins, thereby regulating NF-κB signaling, DNA double-strand break repair pathway choice, cell cycle progression, inflammatory cytokine homeostasis, and mitophagy (PMID:25640675, PMID:25422456, PMID:37474493, PMID:38301893, PMID:24906799, PMID:15367689). Notably, UBE2L3 catalyzes non-canonical (K27-, K29-, K33-linked) ubiquitin chains on pro-IL-1β and p27Kip1, generating proteolytically competent or incompetent modifications depending on the E3 partner and chain type (PMID:37474493, PMID:38301893).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1996 High

    Identification of UBE2L3 as a functional E2 conjugating enzyme for the HECT E3 E6-AP established its entry point into the ubiquitin pathway and demonstrated it could support ubiquitination of p53 and NF-κB precursors.

    Evidence Biochemical interaction and in vitro ubiquitination assays

    PMID:8576257

    Open questions at the time
    • No structural basis for E2–E3 selectivity
    • Range of E3 partners unknown
  2. 1998 High

    Systematic testing against multiple HECT E3s revealed that UBE2L3 is selective for an E6-AP-like subclass of HECT ligases, establishing the principle of E2–HECT specificity classes.

    Evidence In vitro binding and ubiquitin thioester formation assays across HECT family members

    PMID:9575161

    Open questions at the time
    • Structural determinants of selectivity unresolved
    • In vivo relevance of specificity not tested
  3. 1999 High

    Crystal structures of UBE2L3 bound to E6-AP (HECT) and c-Cbl (RING) defined the two principal modes of E2 recruitment and revealed how RING E3s scaffold the E2 active site for ubiquitin transfer, while HECT E3s accept ubiquitin via transthiolation.

    Evidence X-ray crystallography of E6-AP HECT–UbcH7 and c-Cbl RING–UbcH7 complexes with functional validation

    PMID:10531381 PMID:10558980 PMID:10966114

    Open questions at the time
    • Why UBE2L3 pairs with RING E3s like c-Cbl despite lacking lysine reactivity was unexplained
    • RBR class not yet recognized
  4. 1999 Medium

    Discovery that UBE2L3 interacts with RBR-containing proteins HHARI and H7-AP1 through their RING1 domain linked the then-uncharacterized RBR family to the ubiquitin pathway.

    Evidence Yeast two-hybrid and in vitro binding assays

    PMID:10521492

    Open questions at the time
    • RBR catalytic mechanism unknown
    • Whether RBR proteins function as E3 ligases unproven at this time
  5. 2004 High

    UBE2L3 was shown to function as a transcriptional coactivator for steroid hormone receptors and to target HPV E7 for proteasomal degradation via SCF, broadening its substrate repertoire beyond canonical ubiquitin pathway roles.

    Evidence ChIP, siRNA knockdown, reporter assays for steroid receptors; in vitro ubiquitination and Skp2-knockout MEFs for E7

    PMID:15113913 PMID:15367689

    Open questions at the time
    • How UBE2L3 is recruited to chromatin mechanistically unclear
    • Whether UBE2L3 catalytic activity at promoters involves substrate ubiquitination or non-degradative modification unknown
  6. 2011 High

    The landmark discovery that UBE2L3 lacks intrinsic lysine reactivity resolved the paradox of its E3 selectivity: it functions exclusively with E3s that form a covalent thioester with ubiquitin (HECT and RBR types), and RBR E3s were reclassified as RING/HECT hybrids.

    Evidence In vitro ubiquitination assays with mutagenesis and structural comparisons

    PMID:21532592

    Open questions at the time
    • How UBE2L3 is prevented from functioning with canonical RING E3s in cells not fully addressed
    • Structural basis for open vs. closed E2~Ub conformations with RBR E3s unresolved
  7. 2014 Medium

    Functional studies established UBE2L3 in two new cellular processes: regulation of DNA double-strand break repair pathway choice (via 53BP1 ubiquitination) and Parkin-dependent mitophagy (cooperating with UBE2N and UBE2D).

    Evidence shRNA screen and knockdown with DSB repair assays; siRNA knockdown with mitophagy flux assays

    PMID:24906799 PMID:25422456

    Open questions at the time
    • Identity of E3 ligase partnering with UBE2L3 for 53BP1 ubiquitination unknown
    • Relative contribution of UBE2L3 vs. UBE2D in Parkin-mediated ubiquitination unclear
  8. 2015 High

    UBE2L3 was identified as the preferred E2 for the LUBAC complex in vivo, directly linking it to linear ubiquitin chain assembly and NF-κB activation; the autoimmune risk haplotype at the UBE2L3 locus increases its expression and enhances NF-κB-driven plasma cell development.

    Evidence Reporter assays, dominant-negative C86S, siRNA, imaging flow cytometry in primary human B cells

    PMID:25640675

    Open questions at the time
    • Whether UBE2L3 directly charges HOIP or acts through HOIL-1 within LUBAC not resolved
    • Mechanism by which expression-level variation drives autoimmune risk incompletely defined
  9. 2017 High

    Structural analysis of the HHARI RING1–UbcH7~Ub complex revealed how a Zn²⁺-loop extension unique to RBR RING1 domains acts as a steric wedge to enforce the open E2~Ub conformation, explaining why UBE2L3 delivers ubiquitin exclusively via transthiolation with RBR E3s.

    Evidence Crystal structure with biochemical assays

    PMID:28552575

    Open questions at the time
    • Generalizability to all RBR E3s not formally tested
    • Whether the open conformation is dynamically regulated in cells unknown
  10. 2018 High

    NMR studies of UbcH7~Ub with Parkin showed that conjugated ubiquitin binds at the RING1/IBR interface in the open conformation, and that E2 binding synergizes with Ubl phosphorylation to activate Parkin's RING2 catalytic cysteine.

    Evidence NMR chemical shift perturbation, mass spectrometry, in vitro ubiquitination assays

    PMID:30446597

    Open questions at the time
    • Full-length activated Parkin–UbcH7~Ub structure not available
    • How substrate selection occurs after E2~Ub docking unclear
  11. 2023 High

    Conditional Ube2l3 knockout in mice revealed its role in disposing of pro-IL-1β via TRIP12- and AREL1-catalyzed K27/K29/K33 polyubiquitin chains, establishing UBE2L3 as a gatekeeper of inflammasome-driven inflammation.

    Evidence Conditional KO mouse, RNAi screen for E3 partners, in vitro ubiquitination with chain-type specificity

    PMID:37474493

    Open questions at the time
    • Whether TRIP12 and AREL1 act redundantly or sequentially on pro-IL-1β unclear
    • Chain-type decoding mechanism downstream not identified
  12. 2024 High

    SMURF1 was identified as the E3 ligase that cooperates with UBE2L3 to conjugate K29-linked chains on p27Kip1, stabilizing rather than degrading p27 and promoting cell migration, demonstrating that UBE2L3 can generate non-degradative ubiquitin signals.

    Evidence In vitro ubiquitination screen, K29 chain-type mutagenesis, co-localization imaging, knockdown migration assays

    PMID:38301893

    Open questions at the time
    • How K29 chains on p27 are read by downstream effectors unknown
    • Whether other non-K48/K63 chain types built by UBE2L3 have distinct signaling roles untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: how UBE2L3 is directed to specific E3 partners in a context-dependent manner in vivo; the full spectrum of non-canonical ubiquitin chain types it generates and their downstream readers; and whether its roles in necroptosis and ferroptosis represent direct or indirect functions.
  • No global proteomics of UBE2L3-dependent ubiquitinome
  • Structural basis for UBE2L3 selectivity among different HECT E3 subclasses incomplete
  • In vivo relevance of UBE2L3 in necroptosis regulation based on single low-confidence study

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 7 GO:0016740 transferase activity 4
Localization
GO:0005634 nucleus 2 GO:0005829 cytosol 2 GO:0005886 plasma membrane 2
Pathway
R-HSA-392499 Metabolism of proteins 5 R-HSA-168256 Immune System 3 R-HSA-162582 Signal Transduction 2 R-HSA-1640170 Cell Cycle 2 R-HSA-5357801 Programmed Cell Death 1 R-HSA-73894 DNA Repair 1 R-HSA-9612973 Autophagy 1
Partners
CBLE6APHHARIHOIL1HOIPPRKNSMURF1TRIP12
Complex memberships
LUBAC (as cognate E2)

Evidence

Reading pass · 30 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2000 Crystal structure of c-Cbl (RING E3) bound to UbcH7 (UBE2L3) reveals that the RING domain recruits the E2 and positions it optimally for ubiquitin transfer; a conserved surface channel leads from the substrate peptide to the E2 active site, suggesting RING E3s act as scaffolds. X-ray crystallography with functional validation Cell High 10966114
1999 Crystal structure of the E6AP HECT domain bound to UbcH7 (UBE2L3) reveals determinants of E2-E3 specificity and the mechanism of ubiquitin transfer from E2 to E3 via a thioester intermediate in the catalytic cleft. X-ray crystallography Science High 10558980
2011 UBE2L3 (UBCH7) lacks intrinsic lysine reactivity (unlike many E2s that function with RING E3s), explaining its preference for HECT-type E3s. RBR E3s (parkin, HHARI) function as RING/HECT hybrids: they bind E2s via RING1 but transfer Ub through an obligate thioester at a conserved RING2 cysteine, and UBE2L3 is the cognate E2 for this class. In vitro ubiquitination assays, mutagenesis, structural comparisons Nature High 21532592
1999 The c-Cbl RING finger domain directly interacts with UbcH7 (UBE2L3), and together they synergistically promote ligand-induced ubiquitination of the EGFR; oncogenic 70Z-Cbl (lacking part of the RING finger) fails to bind UbcH7 and blocks EGFR ubiquitination. Yeast two-hybrid, in vitro binding assay, in vivo and in vitro ubiquitination assays The Journal of biological chemistry High 10531381
1996 UBE2L3 encodes an E2 ubiquitin-conjugating enzyme (UbcH7) that interacts with the HECT E3 E6-AP and efficiently substitutes for UbcH5 in E6-AP-dependent ubiquitination of p53; UbcH7 can also interact with E6-AP to participate in NF-κB maturation and c-Fos degradation. Biochemical interaction assays, in vitro ubiquitination assays The Journal of biological chemistry High 8576257
1998 UBE2L3 (UbcH7) interacts preferentially with a subset of HECT E3s (those sharing E6-AP-like specificity) but not others (e.g., RSP5), demonstrating that different HECT E3s are grouped into at least two classes based on their E2 specificity. In vitro binding and ubiquitin thioester formation assays with multiple HECT E3s The Journal of biological chemistry High 9575161
1999 UBE2L3 (UbcH7) interacts with RBR-containing proteins HHARI and H7-AP1 through their N-terminal RING finger (HHARI) and IBR domains; this interaction is specific to UbcH7/UbcH8 and not seen with UbcH5 or UbcH1, linking RBR proteins to the ubiquitin pathway via UBE2L3. Yeast two-hybrid screen, in vitro binding assays The Journal of biological chemistry Medium 10521492
2001 HHARI co-localizes with UbcH7 (UBE2L3) in mammalian cells, particularly in the perinuclear region; a minimal interaction region (residues 186-254) was defined, and the distance between RING1 and IBR domains is critical; mutation of RING1 from RING-HC to RING-H2 type abolishes UbcH7 interaction. Co-immunoprecipitation, co-localization (immunofluorescence), mutagenesis The Journal of biological chemistry Medium 11278816
2004 UbcH7 (UBE2L3) is the specific E2 for ubiquitination of HPV E7 oncoprotein; E7 interacts with the SCF complex (Cul1/Skp2) E3 ligase, and can be ubiquitinated by the Cul1-containing ligase in vitro; E7 half-life is longer in Skp2-/- MEFs. In vitro ubiquitination assay, co-immunoprecipitation, Skp2 knockout MEFs Journal of virology High 15113913
2004 UbcH7 (UBE2L3) acts as a coactivator for steroid hormone receptors (PR, GR, AR, RAR) in a hormone-dependent manner; its ubiquitin conjugation activity is required for coactivation; UbcH7 is recruited to ER- and PR-responsive promoters and cooperates with E6-AP and SRC-1 to potentiate transactivation. Transient transfection reporter assays, siRNA knockdown, chromatin immunoprecipitation (ChIP), Co-IP Molecular and cellular biology High 15367689
2006 UbcH7 (UBE2L3) physically interacts with the glucocorticoid receptor (GR) and promotes its ubiquitination and proteasome-dependent degradation; a catalytically inactive UbcH7 dominant negative (C89S) fails to repress GR transactivation and stabilizes GR protein, demonstrating that UbcH7 enzymatic activity mediates GR turnover. Co-immunoprecipitation, dominant-negative mutagenesis, reporter assays, proteasome inhibitor experiments The Journal of endocrinology Medium 17003263
2014 UbcH7 (UBE2L3) regulates steady-state and replicative stress-induced ubiquitination and proteasomal degradation of 53BP1; depletion of UbcH7 stabilizes 53BP1, inhibits DSB end resection, increases NHEJ, and reduces homologous recombination, making cells sensitive to DNA damage. shRNA screen, knockdown/depletion, ubiquitination assays, DSB repair pathway assays Proceedings of the National Academy of Sciences of the United States of America Medium 25422456
2014 UBE2N, UBE2L3, and UBE2D2/3 are required synergistically for Parkin-dependent mitophagy; UBE2L3 knockdown reduces autophagic clearance of depolarized mitochondria without interfering with PINK1 stabilization or Parkin translocation; combined knockdown reduces mitochondrial polyubiquitylation of substrates including mitofusins, TOM20, TOM70, and VDAC1. siRNA knockdown, autophagic flux assays, ubiquitination assays Journal of cell science Medium 24906799
2015 UBE2L3 is the preferred E2 conjugating enzyme for LUBAC (linear ubiquitin chain assembly complex, containing HOIL-1 and HOIP) in vivo, and is essential for LUBAC-mediated NF-κB activation; dominant-negative UBE2L3 (C86S) or UBE2L3 silencing abolishes NF-κB upregulation by LUBAC; the autoimmune risk haplotype increases UBE2L3 expression, correlating with enhanced NF-κB activation and plasma cell development. Reporter assays, dominant-negative mutant (C86S), siRNA knockdown, imaging flow cytometry for NF-κB translocation, flow cytometry for B cell subsets American journal of human genetics High 25640675
2017 Structural analysis of HHARI RING1 in complex with UbcH7~Ub shows that a Zn2+-loop II extension unique to RBR RING1 (absent in canonical RING E3s) acts as a steric wedge to disrupt closed E2~Ub conformation, favoring open conformation required for Ub transfer to the E3 active-site cysteine rather than directly to substrate. Structural biology (crystal structure), biochemical assays Structure High 28552575
2018 NMR and mass spectrometry show that UbcH7~Ub binds to parkin in the open conformation, with conjugated Ub binding at the RING1/IBR interface; recruitment of UbcH7~Ub and phosphorylation of parkin's Ubl domain act synergistically to rearrange the RING2 catalytic cysteine and enhance ubiquitin transfer activity. NMR chemical shift perturbation, mass spectrometry, in vitro ubiquitination assays The EMBO journal High 30446597
2005 HIV Nef mediates exclusion of UbcH7 (UBE2L3) from lipid rafts via a p85Cool-1/βPix–c-Cbl ternary complex, preventing ubiquitination of activated Vav by c-Cbl/UbcH7 and thereby enhancing T cell signaling to promote HIV replication. Lipid raft fractionation, siRNA knockdown of p85Cool-1/βPix, ubiquitination assays, Co-IP Immunity Medium 16356860
2009 The RBR E3 ligase Triad1 inhibits myeloid cell proliferation through differential interactions of its two RING domains with UbcH7 (UBE2L3) and Ubc13, catalyzing distinct ubiquitin chain types; deletion of either RING domain abrogates the inhibitory effect on myeloid colony formation. In vitro binding assays, myeloid clonogenic assays, domain deletion mutagenesis Leukemia Medium 19340006
2015 Ndfip1 acts as an adaptor protein that facilitates recruitment of UbcH7 (UBE2L3) to the HECT E3 Itch, enhancing Itch ligase activity and Tak1 ubiquitination; the N-terminal region of Ndfip1 binds UbcH7 while the PY motif binds Itch, and reconstitution with full-length Ndfip1 (but not interaction-dead mutants) restores defective Tak1 ubiquitination. Co-immunoprecipitation, in vitro reconstitution, Ndfip1-/- and Itch-/- mouse models, mutagenesis Journal of immunology High 25632008
2014 MAP1B light chain 1 (LC1) interacts with both CaV2.2 (N-type Ca2+ channel) and UBE2L3 via Co-IP; the LC1/UBE2L3 complex promotes ubiquitination and proteasomal degradation of CaV2.2, reducing channel surface expression and current density; MG132 prevents LC1-induced channel degradation. Co-immunoprecipitation, yeast two-hybrid, patch-clamp, proteasome inhibition Pflugers Archiv Medium 24566975
2018 UBE2L3 (UBCH7) specifically stabilizes p27Kip1 by catalyzing the conjugation of heterotypic ubiquitin chains on p27 that are proteolytically incompetent; overexpression of UBE2L3 stabilizes p27 and delays G1-to-S transition, while depletion increases p27 turnover, without affecting p21, p57, cyclin A, or cyclin E levels. Overexpression, siRNA knockdown, cell cycle analysis, in vitro ubiquitination assays FASEB journal Medium 30113882
2023 UBE2L3 promotes pro-IL-1β ubiquitylation and proteasomal disposal; deletion of Ube2l3 in mice reduces pro-IL-1β turnover in macrophages, leading to excessive mature IL-1β production, neutrophilic inflammation after inflammasome activation; RNAi screen identified TRIP12 and AREL1 (HECT E3s) as the partner E3 ligases that add destabilizing K27-, K29-, and K33-linked poly-ubiquitin chains on pro-IL-1β. Ube2l3 conditional knockout mouse, RNAi screen, in vitro ubiquitination assays, inflammasome activation assays Nature communications High 37474493
2023 UBE2L3 is critical for NF-κB activation downstream of TLR7 stimulation via interaction with LUBAC; dimethyl fumarate (DMF) directly inhibits UBE2L3 and significantly reduces TLR7-induced NF-κB activation, plasmablast/memory B cell differentiation, and autoantibody secretion in SLE. Knockdown, overexpression, reporter assays, flow cytometry, DMF pharmacological inhibition Journal of autoimmunity Medium 37001433
2024 SMURF1 acts as the E3 ligase partner of UBE2L3 (UbcH7) to ubiquitinate p27Kip1 with K29-linked chains, stabilizing p27 and promoting cell migration; SMURF1, UbcH7, and p27 co-localize at the leading edge of migrating cells; knockdown of SMURF1 or UbcH7 reduces cell migration. In vitro ubiquitination screen, K29 chain-type mutagenesis, co-localization imaging, knockdown assays, migration assays The Journal of biological chemistry High 38301893
2024 MARCHF8 (a membrane RING E3 ligase) binds to and ubiquitinates UBE2L3 and CUL1, promoting their degradation and thereby stabilizing HPV16 E7; MARCHF8 knockdown increases UBE2L3 and CUL1 levels and enhances E7 ubiquitination; overexpression of CUL1 or UBE2L3 decreases E7 levels and suppresses tumor growth in vivo. Co-immunoprecipitation, ubiquitination assays, MARCHF8 knockdown, in vivo xenograft Journal of virology Medium 38226814
2024 UBE2L3 interacts with the E3 ligase ZNF598 (confirmed by LC-MS/MS and Co-IP) and disrupts ZNF598-mediated ubiquitination of the autophagy protein LAMP-2, thereby reducing GPX4 expression and activating an autophagy-dependent ferroptosis pathway in benzene-exposed cells. Co-immunoprecipitation, LC-MS/MS, overexpression/knockdown, immunofluorescence, TEM Ecotoxicology and environmental safety Low 39059346
2025 UBE2L3 specifically binds to and ubiquitinates MLKL (necroptosis effector), promoting its degradation; UBE2L3 knockdown increases phospho-MLKL and phospho-RIP1 levels and promotes necroptosis in osteosarcoma cells and in vivo xenograft tumors. Co-immunoprecipitation, ubiquitination assays, in vivo xenograft model World journal of surgical oncology Low 39988669
2026 UBE2L3 interacts with the E3 ligase SMURF2 to control TSC2 protein ubiquitination and degradation; UBE2L3 downregulation increases TSC2, suppresses mTOR activity, and alters autophagy in TNBC cells, sensitizing tumors to anti-PD-1 therapy. In vivo CRISPR/Cas9 library screen, Co-IP, knockdown, in vivo tumor models International journal of biological sciences Medium 41943836
2009 UbcH7 (UBE2L3) overexpression delays entry into S phase while its depletion increases S phase length and decreases cell proliferation; UbcH7 depletion increases Chk1 levels and decreases phospho-PTEN, placing UbcH7 in a PTEN/Akt/Chk1 pathway that regulates S phase length. Overexpression, siRNA knockdown, FACS cell cycle analysis, protein level analysis Cell division Low 19664228
2017 TCDD (an AhR ligand) promotes AhR binding to the UBE2L3 (Ubch7) gene promoter and induces UbcH7 expression in the mouse brain; increased UbcH7 promotes ubiquitination and degradation of synphilin-1 via the UbcH7-parkin complex. ChIP, promoter assay, protein stability/half-life analysis in mouse brain Journal of biochemical and molecular toxicology Low 28621812

Source papers

Stage 0 corpus · 60 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 719 10966114
1999 Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade. Science (New York, N.Y.) 468 10558980
2011 UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 454 21532592
1999 Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. The Journal of biological chemistry 278 10531381
1998 Characterization of human hect domain family members and their interaction with UbcH5 and UbcH7. The Journal of biological chemistry 143 9575161
1996 Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5. The Journal of biological chemistry 137 8576257
1999 The ubiquitin-conjugating enzymes UbcH7 and UbcH8 interact with RING finger/IBR motif-containing domains of HHARI and H7-AP1. The Journal of biological chemistry 101 10521492
2014 The ubiquitin-conjugating enzymes UBE2N, UBE2L3 and UBE2D2/3 are essential for Parkin-dependent mitophagy. Journal of cell science 95 24906799
2015 UBE2L3 polymorphism amplifies NF-κB activation and promotes plasma cell development, linking linear ubiquitination to multiple autoimmune diseases. American journal of human genetics 84 25640675
2004 The papillomavirus E7 oncoprotein is ubiquitinated by UbcH7 and Cullin 1- and Skp2-containing E3 ligase. Journal of virology 80 15113913
2004 The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors. Molecular and cellular biology 74 15367689
2001 Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, Ubch7. The Journal of biological chemistry 69 11278816
2016 Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3. The Biochemical journal 61 27729585
2012 A functional haplotype of UBE2L3 confers risk for systemic lupus erythematosus. Genes and immunity 50 22476155
2017 Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1. Structure (London, England : 1993) 46 28552575
2018 Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation. The EMBO journal 42 30446597
2014 UbcH7 regulates 53BP1 stability and DSB repair. Proceedings of the National Academy of Sciences of the United States of America 40 25422456
2005 Nef-mediated lipid raft exclusion of UbcH7 inhibits Cbl activity in T cells to positively regulate signaling. Immunity 33 16356860
2013 Variants in TNFSF4, TNFAIP3, TNIP1, BLK, SLC15A4 and UBE2L3 interact to confer risk of systemic lupus erythematosus in Chinese population. Rheumatology international 32 24091983
2009 The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains. Leukemia 29 19340006
2022 Mechanism and Disease Association With a Ubiquitin Conjugating E2 Enzyme: UBE2L3. Frontiers in immunology 27 35265070
2011 The autoimmune disease risk allele of UBE2L3 in African American patients with systemic lupus erythematosus: a recessive effect upon subphenotypes. The Journal of rheumatology 24 22045845
2014 CaV2.2 channel cell surface expression is regulated by the light chain 1 (LC1) of the microtubule-associated protein B (MAP1B) via UBE2L3-mediated ubiquitination and degradation. Pflugers Archiv : European journal of physiology 23 24566975
2006 UbcH7 interacts with the glucocorticoid receptor and mediates receptor autoregulation. The Journal of endocrinology 22 17003263
2020 Synergistic activation of NF-κB by TNFAIP3 (A20) reduction and UBE2L3 (UBCH7) augment that synergistically elevate lupus risk. Arthritis research & therapy 21 32334614
2023 IL-1β turnover by the UBE2L3 ubiquitin conjugating enzyme and HECT E3 ligases limits inflammation. Nature communications 19 37474493
1998 Fine-mapping, genomic organization, and transcript analysis of the human ubiquitin-conjugating enzyme gene UBE2L3. Genomics 18 9693040
1996 Characterization of a human ubiquitin-conjugating enzyme gene UBE2L3. Mammalian genome : official journal of the International Mammalian Genome Society 18 8672131
2018 UBE2L3, a susceptibility gene that plays oncogenic role in hepatitis B-related hepatocellular carcinoma. Journal of viral hepatitis 15 29969176
2018 Stabilization of p27Kip1/CDKN1B by UBCH7/UBE2L3 catalyzed ubiquitinylation: a new paradigm in cell-cycle control. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 15 30113882
2015 Effect of UBE2L3 genotype on regulation of the linear ubiquitin chain assembly complex in systemic lupus erythematosus. Lancet (London, England) 15 26312912
2023 UBE2L3 regulates TLR7-induced B cell autoreactivity in Systemic Lupus Erythematosus. Journal of autoimmunity 14 37001433
2014 The MAP1B-LC1/UBE2L3 complex catalyzes degradation of cell surface CaV2.2 channels. Channels (Austin, Tex.) 14 25483588
2021 Long non-coding RNA LINC01116 acts as an oncogene in prostate cancer cells through regulation of miR-744-5p/UBE2L3 axis. Cancer cell international 13 33726770
2020 HP1γ Sensitizes Cervical Cancer Cells to Cisplatin through the Suppression of UBE2L3. International journal of molecular sciences 13 32825184
2009 Ubiquitin control of S phase: a new role for the ubiquitin conjugating enzyme, UbcH7. Cell division 13 19664228
2022 Indole-3-Carbinol, a Phytochemical Aryl Hydrocarbon Receptor-Ligand, Induces the mRNA Overexpression of UBE2L3 and Cell Proliferation Arrest. Current issues in molecular biology 12 35678668
2017 TCDD induces UbcH7 expression and synphilin-1 protein degradation in the mouse ventral midbrain. Journal of biochemical and molecular toxicology 12 28621812
2015 Ndfip1 regulates itch ligase activity and airway inflammation via UbcH7. Journal of immunology (Baltimore, Md. : 1950) 12 25632008
2008 Modelling and molecular dynamics of the interaction between the E3 ubiquitin ligase Itch and the E2 UbcH7. Biochemical pharmacology 12 18805400
2024 The membrane-associated ubiquitin ligase MARCHF8 stabilizes the human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in head and neck cancer. Journal of virology 11 38226814
2022 UBE2L3 Reduces TRIM21 Expression and IL-1β Secretion in Epidermal Keratinocytes and Improves Psoriasis-Like Skin. The Journal of investigative dermatology 11 36502938
2016 The haplotype of UBE2L3 gene is associated with Hashimoto's thyroiditis in a Chinese Han population. BMC endocrine disorders 10 27094594
2022 UBE2L3 promotes squamous cell carcinoma progression in the oral cavity and hypopharynx via activating the NF-κB signaling by increasing IκBα degradation. Cell biology international 8 35128752
2022 UBE2L3 promotes lung adenocarcinoma invasion and metastasis through the GSK-3β/Snail signaling pathway. American journal of translational research 8 35958458
2007 1H, 13C and 15N resonance assignments for the human E2 conjugating enzyme, UbcH7. Biomolecular NMR assignments 7 19636915
2021 Variants on the UBE2L3/YDJC Autoimmune Disease Risk Haplotype Increase UBE2L3 Expression by Modulating CCCTC-Binding Factor and YY1 Binding. Arthritis & rheumatology (Hoboken, N.J.) 6 34279042
2000 Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7. Biochimica et biophysica acta 5 10760570
2025 UBE2L3 Suppresses Oxidative Stress-regulated Necroptosis to Accelerate Osteosarcoma Progression. Recent patents on anti-cancer drug discovery 3 38385491
2024 The E3 ligase SMURF1 stabilizes p27 via UbcH7 catalyzed K29-linked ubiquitin chains to promote cell migration SMURF1-UbcH7 K29 ubiquitination of p27 and cell migration. The Journal of biological chemistry 3 38301893
2019 1H, 13C, 15N backbone and side-chain resonance assignment of the native form of UbcH7 (UBE2L3) through solution NMR spectroscopy. Biomolecular NMR assignments 3 31792831
2025 Single cell transcriptomics of human psoriasis and epidermal specific Ube2l3 deficient mice highlight CXCL16/CXCR6 involvement in psoriasis development. Nature communications 2 41083457
2024 Combined Genetic Association and Differed Expression Analysis of UBE2L3 Uncovers a Genetic Regulatory Role of (Immuno)proteasome in IgA Nephropathy. Kidney diseases (Basel, Switzerland) 2 38835407
2024 UBE2L3 promotes benzene-induced hematotoxicity via autophagy-dependent ferroptosis. Ecotoxicology and environmental safety 2 39059346
2012 [Screening and identification of anoikis-resistant gene UBCH7 in esophageal cancer cells]. Yi chuan = Hereditas 2 22382060
2026 In vivo CRISPR/Cas9 Screening Reveals that UBE2L3 Modulates Autophagic Flux through TSC2 Ubiquitination and Potentiates PD-1 Blockade in Triple-Negative Breast Cancer. International journal of biological sciences 0 41943836
2025 Interfering with UBE2L3 expression targets regulation of MLKL to promote necroptosis inhibition of growth in osteosarcoma. World journal of surgical oncology 0 39988669
2024 UBE2L3 expression in human gastric cancer and its clinical significance. Journal of cancer research and clinical oncology 0 38656363
2023 The membrane-associated ubiquitin ligase MARCHF8 stabilizes the human papillomavirus oncoprotein E7 by degrading CUL1 and UBE2L3 in head and neck cancer. bioRxiv : the preprint server for biology 0 37961092
2017 [Predictive value of single nucleotide polymorphisms of HLA-C and UBE2L3 in evaluating the effect of telbivudine antiviral therapy during pregnancy]. Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology 0 29056010