Affinage

UBE2G2

Ubiquitin-conjugating enzyme E2 G2 · UniProt P60604

Length
165 aa
Mass
18.6 kDa
Annotated
2026-04-28
35 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

UBE2G2 is an E2 ubiquitin-conjugating enzyme that functions as a central catalytic component of ER-associated degradation (ERAD), assembling Lys-48-linked polyubiquitin chains on substrates destined for proteasomal destruction. It builds polyubiquitin chains at its active-site cysteine through a proximity mechanism in which gp78 oligomers bring multiple UBE2G2 molecules together, and its catalytic activity is allosterically enhanced ~50-fold when the G2BR domains of partner proteins gp78 or AUP1 bind its backside surface, promoting a closed E2~Ub conformation that stimulates ubiquitin transfer (PMID:19223579, PMID:28434917, PMID:34879065). UBE2G2 partners with E3 ligases gp78, HRD1, and TRIM38 to target diverse ERAD substrates including type 2 iodothyronine deiodinase, InsP3 receptors, CYP3A4, HERP, proinsulin, and LGALS3BP (PMID:12933904, PMID:24496447, PMID:25451919, PMID:38787820, PMID:39807310). Beyond ERAD, the AUP1–UBE2G2 complex retains STING at the ER membrane to restrain spontaneous type I interferon signaling (PMID:40237449), and a cytosolic pool of UBE2G2 regulates actin organization, cell shape, and motility independently of its ER-membrane function (PMID:41989348).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1999 Medium

    A 13-residue loop insertion unique to mammalian UBC7/UBE2G2 was shown to modulate E1 interaction and E3/substrate specificity, establishing that structural elements distal to the active-site cysteine govern enzymatic selectivity.

    Evidence Loop deletion/grafting mutagenesis with E1 charging and E3-dependent ubiquitination assays in vitro

    PMID:10329663

    Open questions at the time
    • Single-lab study without independent replication
    • No structural visualization of loop–E1 interface
    • Physiological substrates affected by loop specificity not identified
  2. 2003 Medium

    UBE2G2 was identified as the E2 enzyme mediating ERAD of specific ER-resident substrates—type 2 iodothyronine deiodinase (D2) and InsP3 receptors—establishing its role as a key ERAD E2 in mammalian cells.

    Evidence GST pulldown, co-IP, dominant-negative UBE2G2 expression with pulse-chase and ubiquitination assays in HEK-293 and SH-SY5Y cells

    PMID:12869571 PMID:12933904

    Open questions at the time
    • Dominant-negative approach does not exclude indirect effects
    • The cognate E3 ligase for InsP3R ubiquitination was not identified
    • In vitro reconstitution of D2 ubiquitination with purified components not performed
  3. 2006 High

    The crystal structure of UBE2G2 revealed a canonical E2 fold with loop regions predicted to confer RING-domain binding specificity, providing the first atomic framework for understanding its E3 partnerships.

    Evidence X-ray crystallography at 2.56 Å with structural superimposition onto known E2–RING complexes

    PMID:16582478

    Open questions at the time
    • No co-crystal with a cognate RING domain
    • Catalytic loop dynamics not captured in the crystal
  4. 2009 High

    The mechanism by which UBE2G2 builds Lys-48-linked polyubiquitin chains was elucidated: gp78 oligomers bring multiple UBE2G2 molecules into proximity, enabling trans-thiolester ubiquitin transfer between neighboring E2s to assemble chains at the active-site cysteine.

    Evidence In vitro ubiquitination reconstitution with gp78 oligomerization mutants, co-IP, and identification of a novel Ube2g2 surface

    PMID:19223579

    Open questions at the time
    • Whether this proximity mechanism operates identically with other E3 partners (e.g., HRD1) was not tested
    • Structural resolution of the gp78 oligomer–UBE2G2 assembly not achieved
  5. 2010 High

    NMR studies revealed that catalytic loops flanking the active-site cysteine are intrinsically dynamic and that UBE2G2 preferentially engages the distal ubiquitin of Lys-48-linked chains, explaining how it processively elongates polyubiquitin regardless of chain length.

    Evidence Solution NMR with 15N relaxation, residual dipolar coupling, chemical shift perturbation, and paramagnetic relaxation enhancement

    PMID:20014027 PMID:21098018

    Open questions at the time
    • Ubiquitin-binding affinity measured was weak (~90 µM); in vivo relevance not confirmed
    • No direct visualization of a ternary UBE2G2–Ub–diUb complex
  6. 2010 High

    AUP1 was identified as a second G2BR-containing partner that recruits UBE2G2 to lipid droplets and the ER membrane, broadening the understanding of how UBE2G2 is spatially directed beyond gp78.

    Evidence Co-IP, pulldown, G2BR domain deletion/mutagenesis, confocal microscopy, and subcellular fractionation

    PMID:21127063

    Open questions at the time
    • Whether AUP1–UBE2G2 carries out ubiquitination at lipid droplets or only at the ER was not resolved
    • Substrate specificity conferred by AUP1 versus gp78 not compared
  7. 2014 High

    Substrate scope of UBE2G2–gp78 was extended to HERP (degraded after ER stress) and CYP3A4 (targeted via phosphodegron recognition), demonstrating that gp78 uses distinct substrate-recognition motifs to channel clients to UBE2G2-dependent ubiquitination.

    Evidence In vitro ubiquitination, domain mutagenesis, phosphopeptide mapping, LC-MS/MS, and cell-based degradation assays

    PMID:24496447 PMID:25451919

    Open questions at the time
    • Whether phosphodegron-dependent recruitment is general for other gp78 substrates was untested
    • Contribution of UBE2G2 versus other E2s to endogenous CYP3A4 turnover not fully delineated
  8. 2017 High

    The allosteric activation mechanism was resolved: G2BR binding to the UBE2G2 backside increases RING affinity ~50-fold and RING binding then shifts the E2~Ub conjugate toward a closed catalytically active conformation (~82%), establishing a two-step allosteric cascade that licenses ubiquitin transfer.

    Evidence NMR conformational dynamics, single-turnover diubiquitin formation assays, and mutagenesis of the ubiquitin hydrophobic patch

    PMID:28434917 PMID:28884161

    Open questions at the time
    • Structural basis of the allosteric coupling between backside and RING-binding surfaces not resolved at atomic detail in a single complex
    • Whether the two-step cascade applies to non-gp78 G2BR-containing partners not tested
  9. 2019 High

    A co-crystal structure of the fission yeast E2BR–Ubc7 complex revealed an inhibitory mode in which backside helix binding sterically impedes E1 charging, showing that the backside regulatory mechanism is conserved but functionally divergent across species.

    Evidence X-ray crystallography at 1.7 Å with in vitro E1-charging assay in S. pombe

    PMID:31397327

    Open questions at the time
    • Whether the inhibitory E1-blocking mode occurs with any mammalian G2BR partner is unknown
    • In vivo relevance of this inhibition in fission yeast ERAD was not tested
  10. 2021 High

    The co-crystal structure of AUP1-G2BR bound to UBE2G2 confirmed nanomolar-affinity backside binding and showed that AUP1 both allosterically activates UBE2G2 and protects it from degradation, unifying recruitment, activation, and stabilization as linked functions of G2BR interaction.

    Evidence Co-crystal structure, in vitro ubiquitination, mutagenesis, ERAD degradation assays, and UBE2G2 protein stability measurements in cells

    PMID:34879065

    Open questions at the time
    • Whether AUP1 and gp78 compete or cooperate in vivo for UBE2G2 binding remains unclear
    • Structural basis for the allosteric transmission from AUP1-G2BR to the active site not fully modeled
  11. 2024 Medium

    UBE2G2 was shown to function with the E3 ligase TRIM38 to ubiquitinate LGALS3BP at K104 and target it for proteasomal degradation, and separately to mediate proinsulin ERAD in β-cells, expanding its substrate repertoire beyond classical ERAD clients.

    Evidence Co-IP, ubiquitination assay with K104 mutagenesis, siRNA knockdown screen, proinsulin degradation and antigen presentation assays

    PMID:38787820 PMID:39807310

    Open questions at the time
    • TRIM38–UBE2G2 interaction has not been structurally characterized
    • Whether TRIM38 employs a G2BR-like mechanism is unknown
    • Proinsulin study based on knockdown without rescue
  12. 2025 Medium

    The AUP1–UBE2G2 complex was found to retain STING at the ER membrane and prevent its spontaneous activation, establishing UBE2G2 as a regulator of innate immune signaling beyond protein quality control; concurrently, a nanobody targeting the UBE2G2 backside demonstrated that backside occupation differentially modulates activity with distinct E3s (HRD1 > CHIP >> TRC8).

    Evidence Co-IP, genetic KO with innate immune signaling assays; nanobody-binding and in vitro ubiquitination with multiple E3s

    PMID:40234692 PMID:40237449

    Open questions at the time
    • Mechanism by which AUP1–UBE2G2 retains STING (direct ubiquitination versus scaffolding) not resolved
    • Nanobody studies are in vitro only; in vivo E3-selectivity consequences unknown
    • Whether STING retention requires UBE2G2 catalytic activity is not established
  13. 2025 Medium

    A cytosolic pool of UBE2G2 was shown to control actin organization, cell shape, and motility independently of its ERAD function, revealing a non-canonical role; separately, UBE2G2 expression was found to be regulated post-transcriptionally by the m6A reader YTHDF3.

    Evidence Dominant-negative/inactive UBE2G2 expression with actin/vinculin imaging and wound closure assays; RIP-qPCR, MeRIP-qPCR, and ACSL4 ubiquitination assays

    PMID:41125048 PMID:41989348

    Open questions at the time
    • Cytosolic substrates mediating the actin phenotype are unidentified
    • Whether the m6A–YTHDF3 regulatory axis operates in non-benzene-exposed physiological contexts is unknown
    • ACSL4 as a direct UBE2G2 substrate awaits in vitro reconstitution

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: (1) how UBE2G2 is selectively allocated among its multiple E3 partners in vivo, (2) the identity of the cytosolic substrates through which UBE2G2 controls actin dynamics, (3) whether STING retention by AUP1–UBE2G2 is ubiquitination-dependent, and (4) a high-resolution structure of a complete E2~Ub–E3–substrate ERAD complex containing UBE2G2.
  • No complete structural model of UBE2G2 within an ERAD retrotranslocon complex
  • In vivo E3 partner selectivity mechanism uncharacterized
  • Cytosolic function substrates unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140096 catalytic activity, acting on a protein 7 GO:0016874 ligase activity 3
Localization
GO:0005783 endoplasmic reticulum 3 GO:0005811 lipid droplet 1 GO:0005829 cytosol 1
Pathway
R-HSA-392499 Metabolism of proteins 9 R-HSA-168256 Immune System 1
Partners
ACSL4AMFRAUP1LGALS3BPSTING1TMEM259TRIM38
Complex memberships
AUP1-UBE2G2 complexgp78/AMFR-UBE2G2 ERAD complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2009 Ube2g2 can assemble Lys-48-linked polyubiquitin chains on its own catalytic cysteine (active site-linked polyubiquitin chains) via a gp78 oligomer that simultaneously associates with multiple Ube2g2 molecules, bringing them into close proximity to allow ubiquitin transfer between neighboring Ube2g2s. In vitro ubiquitination assay, co-IP/pulldown, identification of gp78 oligomerization sites and a novel Ube2g2 surface distinct from the RING-binding site Proceedings of the National Academy of Sciences of the United States of America High 19223579
2010 AUP1 localizes to lipid droplets and binds Ube2g2 via its G2BR (G2 binding region) domain, recruiting the ubiquitination machinery to lipid droplets; deletion or mutation of the G2BR abolishes Ube2g2 binding without affecting AUP1 LD localization. Co-IP, pulldown, domain deletion/mutagenesis, confocal microscopy, subcellular fractionation The Journal of biological chemistry High 21127063
2006 Crystal structure of human UBE2G2/UBC7 at 2.56 Å resolution reveals a single domain with antiparallel β-sheet, five α-helices, and two 3(10)-helices; structural comparison with UbcH7 in a RING-containing ternary complex suggests that two loop regions of UBE2G2 interact with the RING domain and may confer binding specificity. X-ray crystallography, structural superimposition Acta crystallographica. Section F, Structural biology and crystallization communications High 16582478
2010 Solution NMR structure of Ube2g2 demonstrates that catalytically important loops flanking the active site cysteine (residues 95-107 and 130-135) are highly dynamic, suggesting that partner proteins (E3, acceptor ubiquitin, or thiolester-linked ubiquitin) are required to stabilize a catalytically relevant conformation; His94 may act as a general base activated by Asp98/Asp99. NMR spectroscopy, 15N spin relaxation, residual dipolar coupling analysis Proteins High 20014027
2010 Ube2g2 binds ubiquitin with ~90 µM affinity in two orientations; it preferentially interacts with the distal subunit (containing the free Lys-48) of Lys-48-linked diubiquitin (~3-fold higher affinity than proximal subunit), positioning the terminal ubiquitin for chain elongation regardless of chain length. NMR chemical shift perturbation, paramagnetic relaxation enhancement, RosettaDock modeling The Journal of biological chemistry Medium 21098018
2014 Ube2g2 and gp78 mediate polyubiquitylation and proteasomal degradation of HERP after ER stress; this requires a physical interaction between the CUE domain of gp78 and the ubiquitin-like (UBL) domain of HERP. In vitro ubiquitylation assay, co-IP, domain deletion/mutagenesis, cell-based degradation assays Journal of cell science High 24496447
2014 CYP3A4 ubiquitination is mediated by the UBC7-gp78 E2-E3 complex; Ser/Thr phosphorylation of CYP3A4 by PKA/PKC generates phosphodegrons (acidic Asp/Glu/Ser(P)/Thr(P) clusters) that are recognized by gp78 for substrate recruitment and ubiquitination. Site-directed mutagenesis, chemical cross-linking, peptide mapping, LC-MS/MS, in vitro ubiquitination The Journal of biological chemistry High 25451919
2016 The CUE domain of Cue1 (the yeast Ube2g2/Ubc7 activator) aligns growing Lys-48-linked ubiquitin chains with Ubc7 for rapid elongation by binding to a ubiquitin moiety adjacent to the acceptor ubiquitin; disrupting this mechanism delays ERAD substrate turnover. NMR-based analysis, in vitro ubiquitination reactions, mutagenesis Molecular cell High 27264873
2017 Binding of the gp78 G2BR domain to Ube2g2 increases RING affinity for Ube2g2 ~50-fold through allosteric redistribution of conformational populations; RING binding then promotes closed conformation of the Ube2g2~Ub conjugate (from ~60% to ~82% closed) to stimulate ubiquitin transfer. NMR conformational dynamics, single-turnover diubiquitin formation assay, mutagenesis Structure (London, England : 1993) High 28434917
2017 gp78-RING binding stabilizes the closed (catalytically active) conformation of the Ube2g2~Ub conjugate, with the hydrophobic patch of the thiolester-linked ubiquitin being required for the closed state; the rate-limiting step for a single ubiquitin ligation event is organization of the active site into a catalytically viable conformation. NMR spectroscopy, single-turnover diubiquitin formation assay, hydrophobic patch mutagenesis ACS omega Medium 28884161
2021 The 27-aa G2BR domain of AUP1 binds with nanomolar affinity to the backside of UBE2G2 via salt bridges, hydrogen bonds, and hydrophobic interactions; this interaction allosterically activates UBE2G2 for ubiquitination, recruits UBE2G2 to the ER membrane, and prevents rapid degradation of UBE2G2 itself. Crystal/co-crystal structure, in vitro ubiquitination assay, mutagenesis, cell-based ERAD assays, protein stability measurements PLoS biology High 34879065
2019 Crystal structure of the S. pombe U7BR (E2BR) in complex with Ubc7 at 1.7 Å shows the E2BR binds the backside of the E2 as an α-helix; the S. pombe E2BR sterically impedes E1 binding and inhibits E1-mediated charging of Ubc7, a biochemical outcome distinct from the S. cerevisiae E2BR. X-ray crystallography, in vitro E1-charging assay Acta crystallographica. Section F, Structural biology communications High 31397327
2003 Mammalian UBC7 (UBE2G2) directly associates with the C-terminal region (amino acids 169-234) of type 2 iodothyronine deiodinase (D2), mediating its ERAD; truncated D2 containing residues 169-234 acts as a dominant negative to stabilize D2, and dominant-negative UBC7 stabilizes D2 half-life in cells. GST pulldown, co-IP, dominant-negative overexpression, pulse-chase half-life assay in HEK-293 cells Molecular endocrinology (Baltimore, Md.) Medium 12933904
2003 MmUbc7 (UBE2G2) mediates ubiquitination and proteasomal down-regulation of inositol 1,4,5-trisphosphate receptors (InsP3Rs) in response to muscarinic agonist stimulation; dominant-negative MmUbc7 blocks InsP3R ubiquitination whereas dominant-negative MmUbc6 does not; Zn2+ chelation blocks InsP3R ubiquitination, implicating a RING finger E3. Stable expression of dominant-negative E2s, ubiquitination assay, receptor down-regulation assay in SH-SY5Y cells and rat brain slices The Journal of biological chemistry Medium 12869571
2024 UBE2G2 directly binds LGALS3BP and, together with the E3 ligase TRIM38, forms a complex that mediates K104 ubiquitination and proteasomal degradation of LGALS3BP, thereby inhibiting PI3K/AKT signaling and vasculogenic mimicry in uveal melanoma. Co-IP, ubiquitination assay, site-directed mutagenesis (K104 site), KD/OE with phenotypic readouts (VM, metastasis, signaling) Acta pharmaceutica Sinica. B Medium 39807310
2025 The AUP1-UBE2G2 complex interacts with STING and retains it in the ER membrane to prevent its translocation to the Golgi and spontaneous activation; deficiency of either AUP1 or UBE2G2 leads to spontaneous STING activation and enhanced type I interferon expression. Co-IP, genetic knockdown/knockout, innate immune signaling assays, virus infection experiments in vitro and in vivo mBio Medium 40237449
2025 A nanobody binding the backside of UBE2G2 differentially inhibits E3-mediated ubiquitination in the order HRD1 > CHIP >> TRC8, and the natural G2BR segment of gp78 (which normally enhances UBE2G2 activity) shows similar inhibitory effects on the same E3s when added in trans; this demonstrates that occupation of the backside site of UBE2G2 modulates its interactions with different E3s in a partner-specific manner. Nanobody-binding assay, in vitro ubiquitination assay with multiple E3s, comparison with G2BR peptide Communications biology Medium 40234692
2024 UBE2G2 is required for ERAD-mediated degradation of proinsulin in pancreatic β-cells; knockdown of UBE2G2 impairs proinsulin degradation and reduces HLA class I presentation of the PPIB10-18 autoantigen, identifying UBE2G2 as the relevant E2 in this ERAD pathway. siRNA knockdown screen of E2 enzymes, proinsulin degradation assay, antigen presentation assay PloS one Medium 38787820
1999 The 13-amino acid loop insertion in mammalian UBC7 (UBE2G2) distal to the active site cysteine influences E1 interaction and E3/substrate specificity; deletion of the loop increased E1-Ub thiolester affinity and permitted partial E3-dependent conjugation, whereas grafting the loop onto E214k redirected it to accept NEDD8 instead of ubiquitin. Loop deletion/insertion mutagenesis, E1 charging assay, E3-dependent ubiquitination assay The Journal of biological chemistry Medium 10329663
2026 Beyond ERAD, UBE2G2 influences cell shape and motility: inactive UBE2G2 causes cell elongation with reorganization of actin stress fibers to cortical ventral fibers, redistribution of vinculin, loss of lamellipodia, and polarized filopodia, resulting in reduced wound closure; sequestration of wild-type UBE2G2 to the membrane by AUP1 mimics the elongated phenotype, indicating the cytosolic pool of UBE2G2 is responsible. Dominant-negative/inactive mutant expression, actin/vinculin imaging, wound closure assay, AUP1 co-expression experiments, live-cell tracking FASEB journal Medium 41989348
2025 YTHDF3 (an m6A reader) binds UBE2G2 mRNA in an m6A-dependent manner and stabilizes it; benzene exposure reduces YTHDF3, decreasing UBE2G2 expression and thereby impairing UBE2G2-mediated ubiquitination of ACSL4, leading to ACSL4 stabilization, lipid peroxidation, and ferroptosis. RIP-qPCR, MeRIP-qPCR, UBE2G2 overexpression/knockdown, ubiquitination assay for ACSL4, ferroptosis readouts Ecotoxicology and environmental safety Medium 41125048

Source papers

Stage 0 corpus · 35 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2010 Ancient ubiquitous protein 1 (AUP1) localizes to lipid droplets and binds the E2 ubiquitin conjugase G2 (Ube2g2) via its G2 binding region. The Journal of biological chemistry 103 21127063
2009 Mechanistic insights into active site-associated polyubiquitination by the ubiquitin-conjugating enzyme Ube2g2. Proceedings of the National Academy of Sciences of the United States of America 83 19223579
1997 Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution. Biochemistry 63 9048545
2003 Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+. The Journal of biological chemistry 46 12869571
2003 Endoplasmic reticulum-associated degradation of the human type 2 iodothyronine deiodinase (D2) is mediated via an association between mammalian UBC7 and the carboxyl region of D2. Molecular endocrinology (Baltimore, Md.) 46 12933904
2014 Ube2g2-gp78-mediated HERP polyubiquitylation is involved in ER stress recovery. Journal of cell science 37 24496447
2016 The CUE Domain of Cue1 Aligns Growing Ubiquitin Chains with Ubc7 for Rapid Elongation. Molecular cell 35 27264873
2009 Degradation of sterol regulatory element-binding protein precursor requires the endoplasmic reticulum-associated degradation components Ubc7 and Hrd1 in fission yeast. The Journal of biological chemistry 30 19520858
2000 courtless, the Drosophila UBC7 homolog, is involved in male courtship behavior and spermatogenesis. Genetics 30 10880487
2010 Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2. Proteins 29 20014027
2017 Conformational Dynamics and Allostery in E2:E3 Interactions Drive Ubiquitination: gp78 and Ube2g2. Structure (London, England : 1993) 26 28434917
2014 Human liver cytochrome P450 3A4 ubiquitination: molecular recognition by UBC7-gp78 autocrine motility factor receptor and UbcH5a-CHIP-Hsc70-Hsp40 E2-E3 ubiquitin ligase complexes. The Journal of biological chemistry 26 25451919
1998 Identification, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the Saccharomyces cerevisiae ubc7 gene. Genomics 26 9693041
1996 The Arabidopsis thaliana UBC7/13/14 genes encode a family of multiubiquitin chain-forming E2 enzymes. The Journal of biological chemistry 24 8647807
2020 Arabidopsis Ubiquitin-Conjugating Enzymes UBC7, UBC13, and UBC14 Are Required in Plant Responses to Multiple Stress Conditions. Plants (Basel, Switzerland) 21 32521733
1996 Molecular cloning of UBE2G, encoding a human skeletal muscle-specific ubiquitin-conjugating enzyme homologous to UBC7 of C. elegans. Cytogenetics and cell genetics 21 8893823
2006 Structure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7). Acta crystallographica. Section F, Structural biology and crystallization communications 20 16582478
2010 Mechanism of polyubiquitin chain recognition by the human ubiquitin conjugating enzyme Ube2g2. The Journal of biological chemistry 16 21098018
2021 A structurally conserved site in AUP1 binds the E2 enzyme UBE2G2 and is essential for ER-associated degradation. PLoS biology 14 34879065
2018 Ubc7/Ube2g2 ortholog in Entamoeba histolytica: connection with the plasma membrane and phagocytosis. Parasitology research 10 29594345
1999 Identification of rabbit reticulocyte E217K as a UBC7 homologue and functional characterization of its core domain loop. The Journal of biological chemistry 9 10329663
2018 Design, synthesis, and anticancer activity evaluation of irreversible allosteric inhibitors of the ubiquitin-conjugating enzyme Ube2g2. MedChemComm 7 30542531
2024 UBE2G2 inhibits vasculogenic mimicry and metastasis of uveal melanoma by promoting ubiquitination of LGALS3BP. Acta pharmaceutica Sinica. B 5 39807310
2017 Conformational Dynamics Modulate Activation of the Ubiquitin Conjugating Enzyme Ube2g2. ACS omega 5 28884161
2005 Expression, purification, and structural analysis of (HIS)UBE2G2 (human ubiquitin-conjugating enzyme). Protein expression and purification 5 16214370
2024 Proinsulin degradation and presentation of a proinsulin B-chain autoantigen involves ER-associated protein degradation (ERAD)-enzyme UBE2G2. PloS one 4 38787820
1996 Bacterial expression of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Ubc7. Protein expression and purification 4 9172777
2024 Endoplasmic reticulum and inner nuclear membrane ubiquitin-conjugating enzymes Ubc6 and Ubc7 confer resistance to hygromycin B in Saccharomyces cerevisiae. microPublication biology 2 39139584
2019 Assays for dissecting the in vitro enzymatic activity of yeast Ubc7. Methods in enzymology 2 30910030
2025 A nanobody that binds to the backside of the ubiquitin conjugating enzyme Ube2G2 differentially affects interactions with its partner E3 Ligases. Communications biology 1 40234692
2025 RNA m6A reader YTHDF3/ UBE2G2 m6A methylation/ ACSL4 ubiquitination axis facilitated cell ferroptosis to mediate benzene hematotoxicity and the protective effect of melatonin. Ecotoxicology and environmental safety 1 41125048
2022 The Protective Effect of UBE2G2 Knockdown Against Atherosclerosis in Apolipoprotein E-Deficient Mice and Its Association with miR-204-5p. Molecular biotechnology 1 35394254
2019 Crystal structure of the Schizosaccharomyces pombe U7BR E2-binding region in complex with Ubc7. Acta crystallographica. Section F, Structural biology communications 1 31397327
2026 A Novel Role of the Ubiquitin Conjugating Enzyme, UBE2G2, in Regulation of Cell Shape and Movement. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 0 41989348
2025 AUP1 and UBE2G2 complex targets STING signaling and regulates virus-induced innate immunity. mBio 0 40237449