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S-SUMOyl-[E1 SUMO-activating enzyme]-L-cysteine + [Ubc9]-L-cysteine
[E1 SUMO-activating enzyme]-L-cysteine + S-SUMOyl-[Ubc9]-L-cysteine
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isoform Ubc9 is involved as E2 enzyme both in the ubiquitin and the ubiquitin-like SUMO pathway. Ubiquitin-like proteins SUMO-1, -2, and -3 interact with the same N-terminal region of the E2 conjugating enzyme Ubc9 with similar affinities
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
S-ubiquitinyl-[Uba1]-L-cysteine + [Ubc5a]-L-cysteine
[Uba1]-L-cysteine + S-ubiquitinyl-[Ubc5a]-L-cysteine
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the E1 enzyme Uba1, the E2 enzyme UbcH5a, and the E3 enzyme TRIP12 are responsible for ubiquitylation of ubiquitin mutant G76V
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[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein Ubc4]-L-cysteine
[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin carrier protein Ubc4]-S-ubiquitinyl-L-cysteine
binding of Ubc4 to the E1ubiquitin covalent intermediate leads to productive catalysis of ubiquitin transfer to Ubc4 in the form of a thioester linkage. No significant ubiquitination of Ubc4 through formation of lysyl isopeptide bonds is observed
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[ubiquitin-activating protein Uba1a]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-L-cysteine
[ubiquitin-activating protein Uba1a]-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-S-ubiquitinyl-L-cysteine
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[ubiquitin-activating protein Uba1]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-L-cysteine
[ubiquitin-activating protein Uba1]-L-cysteine + [ubiquitin-carrier-protein Ubc2b]-S-ubiquitinyl-L-cysteine
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[ubiquitin-activating protein Uba3]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ubc12]-L-cysteine
[ubiquitin-activating protein Uba3]-L-cysteine + [ubiquitin-carrier-protein Ubc12]-S-ubiquitinyl-L-cysteine
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[ubiquitin-activating protein Uba6]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UbcH5B]-L-cysteine
[ubiquitin-activating protein Uba]-L-cysteine + [ubiquitin carrier protein UbcH5B]-S-ubiquitinyl-L-cysteine
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recombinant E1 enzyme Uba6 can activate ubiquitin and transfer it onto the ubiquitin-conjugating enzyme UbcH5B. Ubiquitin activated by Uba6 can be used for ubiquitylation of p53 and supports the autoubiquitylation of the E3 ubiquitin ligases HectH9 and E6-AP
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[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein E2]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
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purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
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[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UB2R2]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein UB2R2]-S-ubiquitinyl-L-cysteine
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purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
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[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UBE2NL]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein UBE2NL]-S-ubiquitinyl-L-cysteine
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purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
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[ubiquitin-activating protein UBE1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UBE2W]-L-cysteine
[ubiquitin-activating protein UBE1]-L-cysteine + [ubiquitin carrier protein UBE2W]-S-ubiquitinyl-L-cysteine
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purified E1 enzyme UBE1 can activate and conjugate ubiquitin to ubiquitin-conjugating enzyme E2s. Transfer is restricted to distinct E2 isoforms UB2R2, UBE2W and UBE2NL
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additional information
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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erythrocyte spectrin has a chimeric E2/E3 ubiquitin-conjugating/ligating activity, which is capable of ubiquitinating itself
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
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the enzyme ubiquitinates the N terminus of substrates
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
K48- and K63-linked ubiquitination
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
acceptor ubiquitin residue Arg54 participated in Ube2R1-catalyzed Lys 48 polyubiquitin chain formation. Significance of the Asp143 Ube2R1/2-Arg54 acceptor ubiquitin ion pair
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
acceptor ubiquitin residue Arg54 participates in Ube2R1-catalyzed Lys48 polyubiquitin chain formation. Significance of the Asp143 Ube2R1/2-Arg54 acceptor ubiquitin ion pair
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 backside interaction was of Ub non-covalently bound to Ube2D3 via the hydrophobic patch centered on I44, a Ub surface used in many different protein-protein interactions. Although weak in affinity, the interaction promotes an increase in processivity of polyUb chain building by Ube2D3
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
E2 loading reaction assay using ubiquitin D, i.e. FAT10, UniProt ID O15205. UBE2Z is specific for E1-like ubiquitin-activating enzyme UBA6. UBE2Z N-terminal extension and loop LB are essential for selectivity toward UBA6. UBA6 charges UBE2Z with FAT10 less efficiently than with ubiquitin. The C-terminal CYCI peptide in rFAT10 limits transfer Rates onto UBE2Z
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
the E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
ubiquitin K48- and K63-linked ubiquitination
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additional information
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polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
a thiol ester-linked ubiquitin to the E2 active site is an intermediate in any polyubiquination reactions
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additional information
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functional survey of 11 representative human E2 paralogs reveals similar Km values for binding to human Uba1 ternary complex with an average Km of 121 nM and kcat for ubiquitin transfer of 4.0 per s, suggesting that they possess a conserved binding site and transition state geometry and that they compete for charging through differences in intracellular concentration. This binding motif is localized to three basic residues within Helix 1 of the E2 core domain
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additional information
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functional survey of 11 representative human E2 paralogs reveals similar Km values for binding to human Uba1 ternary complex with an average Km of 121 nM and kcat for ubiquitin transfer of 4.0 per s, suggesting that they possess a conserved binding site and transition state geometry and that they compete for charging through differences in intracellular concentration. This binding motif is localized to three basic residues within Helix 1 of the E2 core domain
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additional information
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kinetics for Uba1a-catalyzed transthiolation of Ubc2b are used as a reporter assay for determining the Km and kcat values for the three cosubstrates of the ubiquitin-activating enzyme. The E2 transthiolation assays are more sensitive to the potential presence of trace catalytically active fragments than the single turnover end point assays used for quantitating ternary complex stoichiometry
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additional information
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during transfer of ubiquitin to the final substrate or E3 ligase, reaction of EC 2.3.2.27, enzyme is restricted to monoubiquitinylation. UbcM2 shows enhanced polyubiquitin synthesizing activity in reaction mixtures containing ubiquitin mutant K48R. In contrast, reaction mixtures containing ubiquitin mutant K6R show a mild suppression of UbcM2 activity
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additional information
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human liver endoplasmic reticulum-anchored cytochrome P450 enzyme CYP3A4 is degraded via ubiquitylation by E2 ubiquitin-conjugating enzyme UBC7/E3 ubiquitin-ligase gp78, reaction of EC 2.3.2.27. CYP3A4 Asp/Glu/Ser(P)/Thr(P) surface clusters are important for its intermolecular electrostatic interactions with each of these E2-E3 subcomponents. By imparting additional negative charge to these Asp/Glu clusters, such Ser/Thr phosphorylation would generate P450 phosphodegrons for molecular recognition by the E2-E3 complexes, thereby controlling the timing of CYP3A4 ubiquitination and endoplasmic reticulum-associated degradation
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additional information
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the enzyme is nonreactive with free lysine
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additional information
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determination of the E1 catalyzed E2-25K-Ub thioester conjugation reaction
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additional information
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diubiquitin synthesis by enzyme UBE2R2 with 32P-labeled K48R donor ubiquitin and acceptor ubiquitin, which contains an additional Asp residue at its C-terminus (referred to as D77 ubiquitin, which cannot be thioesterified to Ube2R2), analysis of activities of wild-type Ube2R2 and mutants, D143K, D143R, D143A, and D91K, with wild-type ubiquitin and mutant ubiquitins, R54D, R54A, I44A, I44D, and D58R. The mutations reduce the activity, the combination of D143K enzyme with D58R ubiquitin is inactive, the mutation of Arg54 to an Asp residue in acceptor ubiquitin leads to a 52fold reduction in Ube2R2 activity compared with wild-type ubiquitin results. The Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
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additional information
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diubiquitin synthesis by enzyme UBE2R2 with 32P-labeled K48R donor ubiquitin and acceptor ubiquitin, which contains an additional Asp residue at its C-terminus (referred to as D77 ubiquitin, which cannot be thioesterified to Ube2R2), analysis of activities of wild-type Ube2R2 and mutants, D143K, D143R, D143A, and D91K, with wild-type ubiquitin and mutant ubiquitins, R54D, R54A, I44A, I44D, and D58R. The mutations reduce the activity, the combination of D143K enzyme with D58R ubiquitin is inactive, the mutation of Arg54 to an Asp residue in acceptor ubiquitin leads to a 52fold reduction in Ube2R2 activity compared with wild-type ubiquitin results. The Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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enzyme UBE2V1 and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. The enzyme interacts with ubiquitin, and with E3 ligases of types RING, and HECT (in combination with Ube2N). Whereas K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligase of type RING
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
-
the enzyme interacts with E3 ligases of types HECT, and RBR, but not with E3 RING, and not with ubiquitin. UBE2L3 is a cysteine-only reactive E2
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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-
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additional information
?
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the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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-
-
additional information
?
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the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
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-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types HECT, RBR, and RING, but not with ubiquitin. UBE2N builds K63 Ub-chains, inetracts with UBE2V1 and UBE2V2 for K63 chain formation. K63-specific Ube2N uses a tightly bound E2-like subunit (either Ube2V1 or Ube2V2) to position the K63 side chain of the incoming (acceptor) Ub. A substrate that is modified by Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K. K63-linked polyUb is built directly onto the active site cysteine of Ube2N
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING and HECT. UBE2G1 is a K48 chain-building enzyme even in the absence of an E3
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, and RBR. Ube2L6 is a bispecific E2 active with ISG15 and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR, but not with ubiquitin. Ube2E1 provides an example of E2 regulation by autoubiquitylation. Modification occurs on a lysine near the active site and on lysines in the unstructured N-terminal extension of Ube2E1
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. It is K48 chain-building enzyme even in the absence of an E3. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Its shows hydroxyl specificity (serine/threonine)
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R1 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. The highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2R2 is a K48 Ub chain-building enzyme. Ube2R1 is the cognate E2 of SCF E3 ligases. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2S is a K11 Ub chain-building enzyme. highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with E3 ligases of types RING, HECT, and RBR. Ube2T monoubiquitylates its substrate FANCD2 on a specific lysine with its RING E3 FANCL in the Fanconi Anemia DNA repair pathway
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with the C-terminal extension. Ube2Z is a bispecific E2 active with FAT10 (ubiquitin D) and ubiquitin (Ub)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin and E3 ligases, of types RING, HECT, RBR. The preference of Ube2E3 to generate monoubiquitylated products arises from specific interactions involving K48 on Ub and backside residues of the E2
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Backside binding by Ub increases the intrinsic lysine reactivity of Ube2D2-Ub, indicating an allosteric effect
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, and E3 ligases of types RING, HECT, and RBR. Neither HECTs nor RBRs enhance the intrinsic lysine reactivity of Ube2D3. In the open conformation, Ube2D3-Ub is highly reactive towards free cysteine, but shows greatly reduced reactivity towards free lysine when compared with free Ube2D3-Ub
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
-
-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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additional information
?
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the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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additional information
?
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the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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additional information
?
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the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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additional information
?
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the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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-
-
additional information
?
-
the enzyme interacts with ubiquitin, E3 ligases of types RING, HECT, and RBR, with Cue1, and with itself. UBE2G2 is a K48 chain-building enzyme dependent on E3. Chain building directly on E2 active sites has been reported in limited cases (e.g. Ube2G2, and Ube2D in collaboration with the bacterial effector SspH2)
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additional information
?
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the Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
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additional information
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the Ube2R1/2 acidic loop participates in Lys48-specific polyubiquitin chain formation by binding to Skp1-cullin-Fbox (SCF), kinetics
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Acquired Immunodeficiency Syndrome
Identification of New Lead Molecules Against UBE2NL Enzyme for Cancer Therapy.
Acquired Immunodeficiency Syndrome
The E2-25K ubiquitin-associated (UBA) domain aids in polyubiquitin chain synthesis and linkage specificity.
Adenocarcinoma
cDNA cloning, characterization, and chromosome mapping of UBE2E3 (alias UbcH9), encoding an N-terminally extended human ubiquitin-conjugating enzyme.
Adenocarcinoma
Comparative functional genomics analysis of NNK tobacco-carcinogen induced lung adenocarcinoma development in Gprc5a-knockout mice.
Adenocarcinoma
Expression of UbcH10 in pancreatic ductal adenocarcinoma and its correlation with prognosis.
Adenocarcinoma
Identification of potential crucial genes associated with the pathogenesis and prognosis of pancreatic adenocarcinoma.
Adenocarcinoma
Inhibitors of the Cdc34 acidic loop: A computational investigation integrating molecular dynamics, virtual screening and docking approaches.
Adenocarcinoma
Silencing ubiquitin-conjugating enzyme 2C inhibits proliferation and epithelial-mesenchymal transition in pancreatic ductal adenocarcinoma.
Adenocarcinoma
The expression of ubiquitin-conjugating enzyme E2C and KAI1 in ovarian carcinoma and their clinical significance.
Adenocarcinoma
UbcH10 expression provides a useful tool for the prognosis and treatment of non-small cell lung cancer.
Adenocarcinoma
UBE2C induces EMT through Wnt/??catenin and PI3K/Akt signaling pathways by regulating phosphorylation levels of Aurora-A.
Adenocarcinoma
UBE2C mRNA expression controlled by miR-300 and HuR determines its oncogenic role in gastric cancer.
Adenocarcinoma
Uev1A-Ubc13 promotes colorectal cancer metastasis through regulating CXCL1 expression via NF-?B activation.
Adenocarcinoma of Lung
Circulating miR-1246 Targeting UBE2C, TNNI3, TRAIP, UCHL1 Genes and Key Pathways as a Potential Biomarker for Lung Adenocarcinoma: Integrated Biological Network Analysis.
Adenocarcinoma of Lung
Elevated TOP2A and UBE2C expressions correlate with poor prognosis in patients with surgically resected lung adenocarcinoma: a study based on immunohistochemical analysis and bioinformatics.
Adenocarcinoma of Lung
Expression of UBE2C in lung adenocarcinoma based on database analysis and its clinical significance.
Adenocarcinoma of Lung
High EGFR_1 Inside-Out Activated Inflammation-Induced Motility through SLC2A1-CCNB2-HMMR-KIF11-NUSAP1-PRC1-UBE2C.
Adenocarcinoma of Lung
Role of SUMO/Ubc9 in DNA damage repair and tumorigenesis.
Adenocarcinoma of Lung
Targeting Ubc9 for cancer therapy.
Adenocarcinoma of Lung
UBE2D1 RNA Expression Was an Independent Unfavorable Prognostic Indicator in Lung Adenocarcinoma, but Not in Lung Squamous Cell Carcinoma.
Adenocarcinoma of Lung
UBE2S promotes the proliferation and survival of human lung adenocarcinoma cells.
Adenocarcinoma of Lung
UBE2T promotes autophagy via the p53/AMPK/mTOR signaling pathway in lung adenocarcinoma.
Adenocarcinoma of Lung
UBE2V2 Positively Correlates With PD-L1 Expression and Confers Poor Patient Survival in Lung Adenocarcinoma.
Adenocarcinoma of Lung
Ubiquitin Conjugating Enzyme E2 H (UBE2H) Is Linked to Poor Outcomes and Metastasis in Lung Adenocarcinoma.
Adenocarcinoma of Lung
Ubiquitin-conjugating enzyme E2T (UBE2T) and denticleless protein homolog (DTL) are linked to poor outcome in breast and lung cancers.
Adenoma
UbcH10 overexpression may represent a marker of anaplastic thyroid carcinomas.
African Swine Fever
African swine fever virus encodes for an E2-ubiquitin conjugating enzyme that is mono- and di-ubiquitinated and required for viral replication cycle.
Albuminuria
Chronic kidney disease: novel insights from genome-wide association studies.
Alzheimer Disease
Deficiency in the Ubiquitin Conjugating Enzyme UBE2A in Alzheimer's Disease (AD) is Linked to Deficits in a Natural Circular miRNA-7 Sponge (circRNA; ciRS-7).
Alzheimer Disease
High ubiquitin conjugating enzyme E2 T mRNA expression and its prognostic significance in lung adenocarcinoma: A study based on the TCGA database.
Alzheimer Disease
Predictive Potential of Circulating Ube2h mRNA as an E2 Ubiquitin-Conjugating Enzyme for Diagnosis or Treatment of Alzheimer's Disease.
Alzheimer Disease
Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2).
Alzheimer Disease
Sumoylation of amyloid precursor protein negatively regulates Abeta aggregate levels.
Anemia
Hereditary poikilocytic anemia associated with the co-inheritance of two alpha spectrin abnormalities.
Anemia
RAD6B is a major mediator of triple negative breast cancer cisplatin resistance: Regulation of translesion synthesis/Fanconi anemia crosstalk and BRCA1 independence.
Anemia
Red blood cell membrane disorders.
Anemia
Three Novel Spectrin Variants in Jaundiced Neonates.
Anemia, Diamond-Blackfan
Inherited bone marrow failure syndromes.
Anemia, Hemolytic
Combination of two mutant alpha spectrin alleles underlies a severe spherocytic hemolytic anemia.
Anemia, Hemolytic
Hereditary poikilocytic anemia associated with the co-inheritance of two alpha spectrin abnormalities.
Arthritis
Discovery of Potent Small-Molecule Inhibitors of Ubiquitin-Conjugating Enzyme UbcH5c from ?-Santonin Derivatives.
Arthritis, Experimental
SUMO-Conjugating Enzyme UBC9 Promotes Proliferation and Migration of Fibroblast-like Synoviocytes in Rheumatoid Arthritis.
Arthritis, Rheumatoid
SUMO-Conjugating Enzyme UBC9 Promotes Proliferation and Migration of Fibroblast-like Synoviocytes in Rheumatoid Arthritis.
Arthritis, Rheumatoid
The autoimmune disease risk allele of UBE2L3 in African American patients with systemic lupus erythematosus: a recessive effect upon subphenotypes.
Asthma
Identification of critical genes associated with the development of asthma by co-expression modules construction.
Astrocytoma
Analysis of UbcH10 expression represents a useful tool for the diagnosis and therapy of astrocytic tumors.
Astrocytoma
Expression of ubiquitin-conjugating enzyme E2C/UbcH10 in astrocytic tumors.
Atherosclerosis
Analysis of Differentially Expressed Genes and Molecular Pathways in Familial Hypercholesterolemia Involved in Atherosclerosis: A Systematic and Bioinformatics Approach.
Atrial Fibrillation
Identification of Co-expressed Genes Between Atrial Fibrillation and Stroke.
Autoimmune Diseases
Effect of UBE2L3 genotype on regulation of the linear ubiquitin chain assembly complex in systemic lupus erythematosus.
Autoimmune Diseases
Emerging roles of Lys63-linked polyubiquitylation in immune responses.
Autoimmune Diseases
New developments in genetics of myositis.
Autoimmune Diseases
Structural analysis of recombinant human ubiquitin-conjugating enzyme UbcH5c.
Autoimmune Diseases
The autoimmune disease risk allele of UBE2L3 in African American patients with systemic lupus erythematosus: a recessive effect upon subphenotypes.
Autoimmune Diseases
UBE2L3 Polymorphism Amplifies NF-?B Activation and Promotes Plasma Cell Development, Linking Linear Ubiquitination to Multiple Autoimmune Diseases.
Autoimmune Diseases
Variants on the UBE2L3-YDJC autoimmune disease risk haplotype increase UBE2L3 gene expression by modulating CTCF and YY1 binding.
Azoospermia
A functional variant in the UBE2B gene promoter is associated with idiopathic azoospermia.
Bacterial Infections
Legionella pneumophila inhibits immune signalling via MavC-mediated transglutaminase-induced ubiquitination of UBE2N.
Bacterial Infections
The Atypical Ubiquitin E2 Conjugase UBE2L3 Is an Indirect Caspase-1 Target and Controls IL-1? Secretion by Inflammasomes.
Bile Duct Diseases
The diagnostic and prognostic value of UBE2T in intrahepatic cholangiocarcinoma.
Biliary Tract Diseases
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Blast Crisis
De novo UBE2A mutations are recurrently acquired during chronic myeloid leukemia progression and interfere with myeloid differentiation pathways.
Brain Injuries, Traumatic
Downregulation of UBE2Q1 is associated with neuronal apoptosis in rat brain cortex following traumatic brain injury.
Breast Diseases
UbcH10 is overexpressed in malignant breast carcinomas.
Breast Neoplasms
A High-Throughput Screening Strategy for Development of RNF8-Ubc13 Protein-Protein Interaction Inhibitors.
Breast Neoplasms
Additive effect of the AZGP1, PIP, S100A8 and UBE2C molecular biomarkers improves outcome prediction in breast carcinoma.
Breast Neoplasms
AluY-mediated germline deletion, duplication and somatic stem cell reversion in UBE2T defines a new subtype of Fanconi anemia.
Breast Neoplasms
Clinicopathological relevance of UbcH10 in breast cancer.
Breast Neoplasms
Combination of multiple mRNA markers (PTTG1, Survivin, UbcH10 and TK1) in the diagnosis of Taiwanese patients with breast cancer by membrane array.
Breast Neoplasms
Derlin-1 exhibits oncogenic activities and indicates an unfavorable prognosis in breast cancer.
Breast Neoplasms
Design, synthesis and in vitro anticancer evaluation of 4,6-diamino-1,3,5-triazine-2-carbohydrazides and -carboxamides.
Breast Neoplasms
Downregulation of Ubiquitin-conjugating Enzyme UBE2D3 Promotes Telomere Maintenance and Radioresistance of Eca-109 Human Esophageal Carcinoma Cells.
Breast Neoplasms
Erratum to: UBE2S is associated with malignant characteristics of breast cancer cells.
Breast Neoplasms
Essential role of T-cell factor/beta-catenin in regulation of Rad6B: a potential mechanism for Rad6B overexpression in breast cancer cells.
Breast Neoplasms
Exceptionally high UBE2C expression is a unique phenomenon in basal-like type breast cancer and is regulated by BRCA1.
Breast Neoplasms
Exosomes Mediated Transfer of Circ_UBE2D2 Enhances the Resistance of Breast Cancer to Tamoxifen by Binding to MiR-200a-3p.
Breast Neoplasms
Expression of the novel human gene, UBE2Q1, in breast tumors.
Breast Neoplasms
Expression of UBE2Q2, a putative member of the ubiquitin-conjugating enzyme family in pediatric acute lymphoblastic leukemia.
Breast Neoplasms
Free ISG15 triggers an antitumor immune response against breast cancer: a new perspective.
Breast Neoplasms
Genomic Correlates of DNA Damage in Breast Cancer Subtypes.
Breast Neoplasms
Incorporating prior biological knowledge for network-based differential gene expression analysis using differentially weighted graphical LASSO.
Breast Neoplasms
Increased proteasome activity, ubiquitin-conjugating enzymes, and eEF1A translation factor detected in breast cancer tissue.
Breast Neoplasms
Inhibition of UBE2D3 expression attenuates radiosensitivity of MCF-7 human breast cancer cells by increasing hTERT expression and activity.
Breast Neoplasms
Inhibition of ubiquitin conjugating enzyme UBE2C reduces proliferation and sensitizes breast cancer cells to radiation, doxorubicin, tamoxifen and letrozole.
Breast Neoplasms
ISG15 as a novel tumor biomarker for drug sensitivity.
Breast Neoplasms
ISG15 disrupts cytoskeletal architecture and promotes motility in human breast cancer cells.
Breast Neoplasms
Knockdown of UbcH10 Enhances the Chemosensitivity of Dual Drug Resistant Breast Cancer Cells to Epirubicin and Docetaxel.
Breast Neoplasms
Lysine 394 is a novel Rad6B-induced ubiquitination site on beta-catenin.
Breast Neoplasms
Mapping of Genomic Vulnerabilities in the Post-Translational Ubiquitination, SUMOylation and Neddylation Machinery in Breast Cancer.
Breast Neoplasms
MicroRNA-196a post-transcriptionally upregulates the UBE2C proto-oncogene and promotes cell proliferation in breast cancer.
Breast Neoplasms
Midline2 is overexpressed and a prognostic indicator in human breast cancer and promotes breast cancer cell proliferation in vitro and in vivo.
Breast Neoplasms
Mutation screening of the RNF8, UBC13 and MMS2 genes in Northern Finnish breast cancer families.
Breast Neoplasms
Overexpression of the novel human gene, UBE2Q2, in breast cancer.
Breast Neoplasms
Prognostic significance of UBE2C mRNA expression in high-risk early breast cancer. A Hellenic Cooperative Oncology Group (HeCOG) Study.
Breast Neoplasms
Prognostic value of ubiquitin E2 UBE2W and its correlation with tumor-infiltrating immune cells in breast cancer.
Breast Neoplasms
RAD6B is a major mediator of triple negative breast cancer cisplatin resistance: Regulation of translesion synthesis/Fanconi anemia crosstalk and BRCA1 independence.
Breast Neoplasms
Rad6B is a positive regulator of beta-catenin stabilization.
Breast Neoplasms
Regulatory network reconstruction of five essential microRNAs for survival analysis in breast cancer by integrating miRNA and mRNA expression datasets.
Breast Neoplasms
RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis.
Breast Neoplasms
Slug-induced elevation of D1 cyclin in breast cancer cells through the inhibition of its ubiquitination.
Breast Neoplasms
The clinicopathological significance of UBE2C in breast cancer: a study based on immunohistochemistry, microarray and RNA-sequencing data.
Breast Neoplasms
The clinicopathological significance of ubiquitin-conjugating enzyme E2C, leucine-rich repeated-containing G protein-coupled receptor, WW domain-containing oxidoreductase, and vasculogenic mimicry in invasive breast carcinoma.
Breast Neoplasms
UbcH10 expression in human lymphomas.
Breast Neoplasms
UbcH10 is overexpressed in malignant breast carcinomas.
Breast Neoplasms
UBE2C Overexpression Aggravates Patient Outcome by Promoting Estrogen-Dependent/Independent Cell Proliferation in Early Hormone Receptor-Positive and HER2-Negative Breast Cancer.
Breast Neoplasms
UBE2D3 gene overexpression increases radiosensitivity of EC109 esophageal cancer cells in vitro and in vivo.
Breast Neoplasms
UBE2Q1 in a Human Breast Carcinoma Cell Line: Overexpression and Interaction with p53.
Breast Neoplasms
UBE2S is associated with malignant characteristics of breast cancer cells.
Breast Neoplasms
UBE2T promotes proliferation, invasion and glycolysis of breast cancer cells by regualting the PI3K/AKT signaling pathway.
Breast Neoplasms
Ubiquitin-conjugating enzyme complex Uev1A-Ubc13 promotes breast cancer metastasis through nuclear factor-[cyrillic small letter ka]B mediated matrix metalloproteinase-1 gene regulation.
Breast Neoplasms
Ubiquitin-conjugating enzyme E2T (UBE2T) and denticleless protein homolog (DTL) are linked to poor outcome in breast and lung cancers.
Breast Neoplasms
Ubiquitin-Conjugating Enzyme E2T is an Independent Prognostic Factor and Promotes Gastric Cancer Progression.
Breast Neoplasms
Ubiquitin-conjugating enzyme Ubc13 controls breast cancer metastasis through a TAK1-p38 MAP kinase cascade.
Breast Neoplasms
Ubiquitin-Conjugating Enzyme UBE2C Is Highly Expressed in Breast Microcalcification Lesions.
Breast Neoplasms
Ubiquitination and downregulation of BRCA1 by ubiquitin-conjugating enzyme E2T overexpression in human breast cancer cells.
Breast Neoplasms
Uev1A promotes breast cancer cell migration by up-regulating CT45A expression via the AKT pathway.
Breast Neoplasms
Uev1A promotes breast cancer cell survival and chemoresistance through the AKT-FOXO1-BIM pathway.
Breast Neoplasms
Validation of UBE2C protein as a prognostic marker in node-positive breast cancer.
Calcinosis
Ubiquitin-Conjugating Enzyme UBE2C Is Highly Expressed in Breast Microcalcification Lesions.
Carcinogenesis
A monoclonal antibody against a potential cancer biomarker, human ubiquitin-conjugating enzyme E2.
Carcinogenesis
Age-specific gene expression signatures for breast tumors and cross-species conserved potential cancer progression markers in young women.
Carcinogenesis
Association of clinicopathological features with UbcH10 expression in colorectal cancer.
Carcinogenesis
Bioinformatic analysis identifies potentially key differentially expressed genes in oncogenesis and progression of clear cell renal cell carcinoma.
Carcinogenesis
Combined elevation of AURKB and UBE2C predicts severe outcomes and therapy resistance in glioma.
Carcinogenesis
Depletion of UBE2C reduces ovarian cancer malignancy and reverses cisplatin resistance via downregulating CDK1.
Carcinogenesis
Elevated expression of UBE2T exhibits oncogenic properties in human prostate cancer.
Carcinogenesis
Epstein-Barr Virus Latent Membrane Protein-1 Induces the Expression of SUMO-1 and SUMO-2/3 in LMP1-positive Lymphomas and Cells.
Carcinogenesis
Expression of ubiquitin-conjugating enzyme E2C/UbcH10 in astrocytic tumors.
Carcinogenesis
Expression of ubiquitin-conjugating enzyme E2T in colorectal cancers and clinical implications.
Carcinogenesis
Hepatitis C Virus Downregulates Ubiquitin-Conjugating Enzyme E2S Expression To Prevent Proteasomal Degradation of NS5A, Leading to Host Cells More Sensitive to DNA Damage.
Carcinogenesis
High expression of UBE2T predicts poor prognosis and survival in multiple myeloma.
Carcinogenesis
Homology modeling and virtual screening of ubiquitin conjugation enzyme E2A for designing a novel selective antagonist against cancer.
Carcinogenesis
Hypomethylated Ubiquitin-Conjugating Enzyme2 Q1 (UBE2Q1) Gene Promoter in the Serum Is a Promising Biomarker for Hepatitis B Virus-Associated Hepatocellular Carcinoma.
Carcinogenesis
Identification of Biomarkers Based on Bioinformatics Analysis: The Expression of Ubiquitin-Conjugating Enzyme E2T (UBE2T) in the Carcinogenesis and Progression of Hepatocellular Carcinoma.
Carcinogenesis
Molecular subtyping and functional validation of TTK, TPX2, UBE2C, and LRP8 in sensitivity of TNBC to paclitaxel.
Carcinogenesis
Overexpression of ubiquitin-conjugating enzyme E2 L3 in hepatocellular carcinoma potentiates apoptosis evasion by inhibiting the GSK3?/p65 pathway.
Carcinogenesis
Role of ubiquitin-conjugating enzyme E2T in the carcinogenesis and progression of pancreatic cancer.
Carcinogenesis
SENP1 is a crucial promotor for hepatocellular carcinoma through deSUMOylation of UBE2T.
Carcinogenesis
Silencing ubiquitin-conjugating enzyme 2C inhibits proliferation and epithelial-mesenchymal transition in pancreatic ductal adenocarcinoma.
Carcinogenesis
Systematic identification of CDC34 that functions to stabilize EGFR and promote lung carcinogenesis.
Carcinogenesis
The clinical significance of UBE2C gene in progression of renal cell carcinoma.
Carcinogenesis
The sumoylation pathway is dysregulated in multiple myeloma and is associated with adverse patient outcome.
Carcinogenesis
UbcH10 and Its Emerging Role in Systemic Carcinogenesis.
Carcinogenesis
UbcH10 Expression in Benign, Hyperplastic, and Malignant Endometrial Curetted Materials: A Tissue Microarray Study.
Carcinogenesis
UbcH10 expression may be a useful tool in the prognosis of ovarian carcinomas.
Carcinogenesis
UbcH10 expression provides a useful tool for the prognosis and treatment of non-small cell lung cancer.
Carcinogenesis
UbcH10 is the cancer-related E2 ubiquitin-conjugating enzyme.
Carcinogenesis
UbcH10 overexpression increases carcinogenesis and blocks ALLN susceptibility in colorectal cancer.
Carcinogenesis
UBE2C is a Potential Biomarker for Tumorigenesis and Prognosis in Tongue Squamous Cell Carcinoma.
Carcinogenesis
UBE2C Is a Potential Biomarker of Intestinal-Type Gastric Cancer With Chromosomal Instability.
Carcinogenesis
UBE2C is overexpressed in ESCC tissues and its abrogation attenuates the malignant phenotype of ESCC cell lines.
Carcinogenesis
UBE2C promotes the progression of head and neck squamous cell carcinoma.
Carcinogenesis
UBE2C, Directly Targeted by miR-548e-5p, Increases the Cellular Growth and Invasive Abilities of Cancer Cells Interacting with the EMT Marker Protein Zinc Finger E-box Binding Homeobox 1/2 in NSCLC.
Carcinogenesis
Ube2s expression is elevated in hepatocellular carcinoma and predicts poor prognosis of the patients.
Carcinogenesis
UBE2T promotes nasopharyngeal carcinoma cell proliferation, invasion, and metastasis by activating the AKT/GSK3?/?-catenin pathway.
Carcinogenesis
UBE2T promotes proliferation via G2/M checkpoint in hepatocellular carcinoma.
Carcinogenesis
Ubiquitin-conjugating enzyme complex Uev1A-Ubc13 promotes breast cancer metastasis through nuclear factor-[cyrillic small letter ka]B mediated matrix metalloproteinase-1 gene regulation.
Carcinogenesis
Ubiquitin-Conjugating Enzyme E2T is an Independent Prognostic Factor and Promotes Gastric Cancer Progression.
Carcinogenesis
Ubiquitin-conjugating enzyme E2T knockdown suppresses hepatocellular tumorigenesis via inducing cell cycle arrest and apoptosis.
Carcinogenesis
Ubiquitin-conjugating enzyme UBE2C: molecular biology, role in tumorigenesis, and potential as a biomarker.
Carcinogenesis
Ubiquitin-conjugating enzyme UBE2Q2 suppresses cell proliferation and is down-regulated in recurrent head and neck cancer.
Carcinogenesis
Ubiquitination and downregulation of BRCA1 by ubiquitin-conjugating enzyme E2T overexpression in human breast cancer cells.
Carcinogenesis
Uev1A promotes breast cancer cell migration by up-regulating CT45A expression via the AKT pathway.
Carcinogenesis
Up-regulation of miR-455-5p by the TGF-?-SMAD signalling axis promotes the proliferation of oral squamous cancer cells by targeting UBE2B.
Carcinoma
Alterations of ubiquitylation and sumoylation in conventional renal cell carcinomas after the Chernobyl accident: a comparison with Spanish cases.
Carcinoma
Comparative proteomic profiling of triple-negative breast cancer reveals that up-regulation of RhoGDI-2 is associated to the inhibition of caspase 3 and caspase 9.
Carcinoma
Downregulation of Ubiquitin-conjugating Enzyme UBE2D3 Promotes Telomere Maintenance and Radioresistance of Eca-109 Human Esophageal Carcinoma Cells.
Carcinoma
Elevated expression of UBE2T in lung cancer tumors and cell lines.
Carcinoma
Expression of UBE2Q2, a putative member of the ubiquitin-conjugating enzyme family in pediatric acute lymphoblastic leukemia.
Carcinoma
Gene expression patterns in the histopathological classification of epithelial ovarian cancer.
Carcinoma
High UBCH10 protein expression as a marker of poor prognosis in esophageal squamous cell carcinoma.
Carcinoma
Induction of cell proliferation, clonogenicity and cell accumulation in S phase as a consequence of human UBE2Q1 overexpression.
Carcinoma
Inhibiting ubiquitin conjugating enzyme E2 N by microRNA-590-3p reduced cell growth of cervical carcinoma.
Carcinoma
LncRNA MALAT1 Regulating Lung Carcinoma Progression via the miR-491-5p/UBE2C Axis.
Carcinoma
Multicenter validation of cyclin D1, MCM7, TRIM29, and UBE2C as prognostic protein markers in non-muscle-invasive bladder cancer.
Carcinoma
Overexpression of the novel human gene, UBE2Q2, in breast cancer.
Carcinoma
Overexpression of UBE2C in esophageal squamous cell carcinoma tissues and molecular analysis.
Carcinoma
Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin.
Carcinoma
Precision cancer therapy: profiting from tumor specific defects in the DNA damage tolerance system.
Carcinoma
Preventive effect of oral hangeshashinto (TJ-14) on the development of reflux-induced esophageal cancer.
Carcinoma
Role of SUMO/Ubc9 in DNA damage repair and tumorigenesis.
Carcinoma
Targeting Ubc9 for cancer therapy.
Carcinoma
The expression of ubiquitin-conjugating enzyme E2C and KAI1 in ovarian carcinoma and their clinical significance.
Carcinoma
UbcH10 expression can predict prognosis and sensitivity to the antineoplastic treatment for colorectal cancer patients.
Carcinoma
UbcH10 Expression in Benign, Hyperplastic, and Malignant Endometrial Curetted Materials: A Tissue Microarray Study.
Carcinoma
UbcH10 expression may be a useful tool in the prognosis of ovarian carcinomas.
Carcinoma
UbcH10 expression provides a useful tool for the prognosis and treatment of non-small cell lung cancer.
Carcinoma
UbcH10 is overexpressed in malignant breast carcinomas.
Carcinoma
UbcH10 overexpression in human lung carcinomas and its correlation with EGFR and p53 mutational status.
Carcinoma
UbcH10 overexpression may represent a marker of anaplastic thyroid carcinomas.
Carcinoma
UBE2C Drives Human Cervical Cancer Progression and Is Positively Modulated by mTOR.
Carcinoma
UBE2C is a marker of unfavorable prognosis in bladder cancer after radical cystectomy.
Carcinoma
UBE2C is a Potential Biomarker for Tumorigenesis and Prognosis in Tongue Squamous Cell Carcinoma.
Carcinoma
UBE2C is involved in the functions of ECRG4 on esophageal squamous cell carcinoma.
Carcinoma
UBE2C promotes rectal carcinoma via miR-381.
Carcinoma
UBE2C promotes the progression of head and neck squamous cell carcinoma.
Carcinoma
UBE2D1 RNA Expression Was an Independent Unfavorable Prognostic Indicator in Lung Adenocarcinoma, but Not in Lung Squamous Cell Carcinoma.
Carcinoma
UBE2QL1 is Disrupted by a Constitutional Translocation Associated with Renal Tumour Predisposition and is a Novel Candidate Renal Tumour Suppressor Gene.
Carcinoma
UBE2T Contributes to the Prognosis of Esophageal Squamous Cell Carcinoma.
Carcinoma
UBE2T promotes proliferation and regulates PI3K/Akt signaling in renal cell carcinoma.
Carcinoma
Ubiquitin-conjugating enzyme UBE2Q2 suppresses cell proliferation and is down-regulated in recurrent head and neck cancer.
Carcinoma
Up-regulation of interferon-stimulated gene 15 and its conjugation machinery, UbE1L and UbcH8 expression by tumor necrosis factor-? through p38 MAPK and JNK signaling pathways in human lung carcinoma.
Carcinoma, Ductal
Age-specific gene expression signatures for breast tumors and cross-species conserved potential cancer progression markers in young women.
Carcinoma, Hepatocellular
Enhanced expression of mRNAs of antisecretory factor-1, gp96, DAD1 and CDC34 in human hepatocellular carcinomas.
Carcinoma, Hepatocellular
Gain of UBE2D1 facilitates hepatocellular carcinoma progression and is associated with DNA damage caused by continuous IL-6.
Carcinoma, Hepatocellular
Identification of Biomarkers Based on Bioinformatics Analysis: The Expression of Ubiquitin-Conjugating Enzyme E2T (UBE2T) in the Carcinogenesis and Progression of Hepatocellular Carcinoma.
Carcinoma, Hepatocellular
Identification of the potential therapeutic target gene UBE2C in human hepatocellular carcinoma: An investigation based on GEO and TCGA databases.
Carcinoma, Hepatocellular
Inhibitors of the Cdc34 acidic loop: A computational investigation integrating molecular dynamics, virtual screening and docking approaches.
Carcinoma, Hepatocellular
MicroRNA miR-147b promotes tumor growth via targeting UBE2N in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Prognostic value of ubiquitin-conjugating enzyme E2 S overexpression in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Proteome analysis reveals ubiquitin-conjugating enzymes to be a new family of interferon-alpha-regulated genes.
Carcinoma, Hepatocellular
SENP1 is a crucial promotor for hepatocellular carcinoma through deSUMOylation of UBE2T.
Carcinoma, Hepatocellular
The interplay of UBE2T and Mule in regulating Wnt/?-catenin activation to promote hepatocellular carcinoma progression.
Carcinoma, Hepatocellular
UBE2C functions as a potential oncogene by enhancing cell proliferation, migration, invasion, and drug resistance in hepatocellular carcinoma cells.
Carcinoma, Hepatocellular
UBE2I promotes metastasis and correlates with poor prognosis in hepatocellular carcinoma.
Carcinoma, Hepatocellular
UBE2J2 promotes hepatocellular carcinoma cell epithelial-mesenchymal transition and invasion
Carcinoma, Hepatocellular
UBE2L3, a susceptibility gene that plays oncogenic role in hepatitis B-related hepatocellular carcinoma.
Carcinoma, Hepatocellular
UBE2S enhances the ubiquitination of p53 and exerts oncogenic activities in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Ube2s expression is elevated in hepatocellular carcinoma and predicts poor prognosis of the patients.
Carcinoma, Hepatocellular
UBE2S interacting with TRIM28 in the nucleus accelerates cell cycle by ubiquitination of p27 to promote hepatocellular carcinoma development.
Carcinoma, Hepatocellular
UBE2T promotes hepatocellular carcinoma cell growth via ubiquitination of p53.
Carcinoma, Hepatocellular
UBE2T promotes proliferation via G2/M checkpoint in hepatocellular carcinoma.
Carcinoma, Hepatocellular
UBE2T: A new molecular regulator of cancer stemness in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Upregulation of UBE2Q1 via gene copy number gain in hepatocellular carcinoma promotes cancer progression through ?-catenin-EGFR-PI3K-Akt-mTOR signaling pathway.
Carcinoma, Hepatocellular
Upregulation of ubiquitin-conjugating enzyme E2T (UBE2T) predicts poor prognosis and promotes hepatocellular carcinoma progression.
Carcinoma, Hepatocellular
[UbcH10 expression in hepatocellular carcinoma and its clinicopathological significance].
Carcinoma, Intraductal, Noninfiltrating
Age-specific gene expression signatures for breast tumors and cross-species conserved potential cancer progression markers in young women.
Carcinoma, Non-Small-Cell Lung
KIAA0101 and UbcH10 interact to regulate non-small cell lung cancer cell proliferation by disrupting the function of the spindle assembly checkpoint.
Carcinoma, Non-Small-Cell Lung
The Relationship Between UBE2C and AGGF1 Overexpression and Tumor Angiogenesis in Non-Small Cell Lung Cancer.
Carcinoma, Non-Small-Cell Lung
UbcH10 expression provides a useful tool for the prognosis and treatment of non-small cell lung cancer.
Carcinoma, Non-Small-Cell Lung
UBE2C, Directly Targeted by miR-548e-5p, Increases the Cellular Growth and Invasive Abilities of Cancer Cells Interacting with the EMT Marker Protein Zinc Finger E-box Binding Homeobox 1/2 in NSCLC.
Carcinoma, Non-Small-Cell Lung
Ube2S regulates Wnt/?-catenin signaling and promotes the progression of non-small cell lung cancer.
Carcinoma, Non-Small-Cell Lung
UBE2T promotes radiation resistance in non-small cell lung cancer via inducing epithelial-mesenchymal transition and the ubiquitination-mediated FOXO1 degradation.
Carcinoma, Non-Small-Cell Lung
UBE2T silencing inhibited non-small cell lung cancer cell proliferation and invasion by suppressing the wnt/?-catenin signaling pathway.
Carcinoma, Non-Small-Cell Lung
Ubiquitin-conjugating enzyme E2C regulates apoptosis-dependent tumor progression of non-small cell lung cancer via ERK pathway.
Carcinoma, Ovarian Epithelial
Correlations among ERCC1, XPB, UBE2I, EGF, TAL2 and ILF3 revealed by gene signatures of histological subtypes of patients with epithelial ovarian cancer.
Carcinoma, Ovarian Epithelial
Gene expression patterns in the histopathological classification of epithelial ovarian cancer.
Carcinoma, Ovarian Epithelial
Increased Expression of UBE2T Predicting Poor Survival of Epithelial Ovarian Cancer: Based on Comprehensive Analysis of UBE2s, Clinical Samples, and the GEO Database.
Carcinoma, Ovarian Epithelial
The expression of ubiquitin-conjugating enzyme E2C and KAI1 in ovarian carcinoma and their clinical significance.
Carcinoma, Renal Cell
Alterations of ubiquitylation and sumoylation in conventional renal cell carcinomas after the Chernobyl accident: a comparison with Spanish cases.
Carcinoma, Renal Cell
Precision cancer therapy: profiting from tumor specific defects in the DNA damage tolerance system.
Carcinoma, Renal Cell
UBE2QL1 is Disrupted by a Constitutional Translocation Associated with Renal Tumour Predisposition and is a Novel Candidate Renal Tumour Suppressor Gene.
Carcinoma, Renal Cell
UBE2T promotes proliferation and regulates PI3K/Akt signaling in renal cell carcinoma.
Carcinoma, Small Cell
Elevated expression of UBE2T in lung cancer tumors and cell lines.
Carcinoma, Squamous Cell
Expression of UBE2Q2, a putative member of the ubiquitin-conjugating enzyme family in pediatric acute lymphoblastic leukemia.
Carcinoma, Squamous Cell
UbcH10 expression provides a useful tool for the prognosis and treatment of non-small cell lung cancer.
Carcinoma, Squamous Cell
UBE2C Drives Human Cervical Cancer Progression and Is Positively Modulated by mTOR.
Carcinoma, Squamous Cell
UBE2C is a Potential Biomarker for Tumorigenesis and Prognosis in Tongue Squamous Cell Carcinoma.
Carcinoma, Squamous Cell
UBE2C promotes the progression of head and neck squamous cell carcinoma.
Carcinoma, Squamous Cell
UBE2D1 RNA Expression Was an Independent Unfavorable Prognostic Indicator in Lung Adenocarcinoma, but Not in Lung Squamous Cell Carcinoma.
Carcinoma, Squamous Cell
UBE2D3 gene overexpression increases radiosensitivity of EC109 esophageal cancer cells in vitro and in vivo.
Carcinoma, Squamous Cell
Ubiquitin-conjugating enzyme UBE2Q2 suppresses cell proliferation and is down-regulated in recurrent head and neck cancer.
Cataract
Whole exome sequencing reveals putatively novel associations in retinopathies and drusen formation.
Cerebral Infarction
E2-25K SUMOylation inhibits proteasome for cell death during cerebral ischemia/reperfusion.
Chikungunya Fever
Ubiquitin-Conjugating Enzyme E2 L3 is Downregulated by the Chikungunya Virus nsP2 Protease.
Cholangiocarcinoma
The diagnostic and prognostic value of UBE2T in intrahepatic cholangiocarcinoma.
Cholangiocarcinoma
Ubiquitin-conjugating enzyme E2T regulates cell proliferation and migration in cholangiocarcinoma.
Classical Swine Fever
[Ubiquitin-proteasome pathway and virus infection]
Colitis
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Colitis, Ulcerative
Cutting Edge: Hypoxia-Induced Ubc9 Promoter Hypermethylation Regulates IL-17 Expression in Ulcerative Colitis.
Colitis, Ulcerative
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Colonic Neoplasms
Bioinformatics Analysis of Prognostic miRNA Signature and Potential Critical Genes in Colon Cancer.
Colonic Neoplasms
Detection of aberrations of ubiquitin-conjugating enzyme E2C gene (UBE2C) in advanced colon cancer with liver metastases by DNA microarray and two-color FISH.
Colonic Neoplasms
IMP-1 Displays Cross-Talk with K-Ras and Modulates Colon Cancer Cell Survival through the Novel Proapoptotic Protein CYFIP2.
Colonic Neoplasms
Increased proteasome activity, ubiquitin-conjugating enzymes, and eEF1A translation factor detected in breast cancer tissue.
Colonic Neoplasms
Overexpression of UbcH10 alternates the cell cycle profile and accelerate the tumor proliferation in colon cancer.
Colonic Neoplasms
Uev1A-Ubc13 promotes colorectal cancer metastasis through regulating CXCL1 expression via NF-?B activation.
Colorectal Neoplasms
Association of clinicopathological features with UbcH10 expression in colorectal cancer.
Colorectal Neoplasms
Bortezomib stabilizes mitotic cyclins and prevents cell cycle progression via inhibition of UBE2C in colorectal carcinoma.
Colorectal Neoplasms
Comprehensive analysis of differentially expressed genes reveals the promotive effects of UBE2T on colorectal cancer cell proliferation.
Colorectal Neoplasms
Expression of ubiquitin-conjugating enzyme E2T in colorectal cancers and clinical implications.
Colorectal Neoplasms
Expression Status of UBE2Q2 in Colorectal Primary Tumors and Cell Lines.
Colorectal Neoplasms
Frameshift mutations of ubiquitination-related genes HERC2, HERC3, TRIP12, UBE2Q1 and UBE4B in gastric and colorectal carcinomas with microsatellite instability.
Colorectal Neoplasms
Induction of cell proliferation, clonogenicity and cell accumulation in S phase as a consequence of human UBE2Q1 overexpression.
Colorectal Neoplasms
Inhibition of Ubiquitin-conjugating Enzyme E2 May Activate the Degradation of Hypoxia-inducible Factors and, thus, Overcome Cellular Resistance to Radiation in Colorectal Cancer.
Colorectal Neoplasms
Promoter Methylation Status of Two Novel Human Genes, UBE2Q1 and UBE2Q2, in Colorectal Cancer: a New Finding in Iranian Patients.
Colorectal Neoplasms
RNA INTERFERENCE-MEDIATED SILENCING OF UBCH10 GENE INHIBITS COLORECTAL CANCER CELL GROWTH IN VITRO AND IN VIVO.
Colorectal Neoplasms
RNA interference-mediated silencing of UBCH10 gene inhibits colorectal cancer cell growth in vitro and in vivo.
Colorectal Neoplasms
Spatial UBE2N protein expression indicates genomic instability in colorectal cancers.
Colorectal Neoplasms
UbcH10 expression can predict prognosis and sensitivity to the antineoplastic treatment for colorectal cancer patients.
Colorectal Neoplasms
UbcH10 overexpression in human lung carcinomas and its correlation with EGFR and p53 mutational status.
Colorectal Neoplasms
UbcH10 overexpression increases carcinogenesis and blocks ALLN susceptibility in colorectal cancer.
Colorectal Neoplasms
UbcH10 overexpression is less pronounced in older colorectal cancer patients.
Colorectal Neoplasms
UBE2Q1 expression in human colorectal tumors and cell lines.
Colorectal Neoplasms
Ube2s stabilizes ?-Catenin through K11-linked polyubiquitination to promote mesendoderm specification and colorectal cancer development.
Colorectal Neoplasms
Ubiquitin-conjugating enzyme E2T(UBE2T) promotes colorectal cancer progression by facilitating ubiquitination and degradation of p53.
Colorectal Neoplasms
Uev1A-Ubc13 promotes colorectal cancer metastasis through regulating CXCL1 expression via NF-?B activation.
Congenital Bone Marrow Failure Syndromes
Inherited bone marrow failure syndromes.
Coronary Artery Disease
Evaluating the association of common UBE2Z variants with coronary artery disease in an Iranian population.
COVID-19
An integrative analysis identifying transcriptional features and key genes involved in COVID-19.
Crohn Disease
Analysis of SNPs with an effect on gene expression identifies UBE2L3 and BCL3 as potential new risk genes for Crohn's disease.
Crohn Disease
Genome-Wide Association Study of Ulcerative Colitis in Koreans Suggests Extensive Overlapping of Genetic Susceptibility With Caucasians.
Crohn Disease
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Dehydration
Cowpea and abiotic stresses: identification of reference genes for transcriptional profiling by qPCR.
Dehydration
Selection of Reference Genes for qRT-PCR Analysis in Medicinal Plant Glycyrrhiza under Abiotic Stresses and Hormonal Treatments.
Diabetes Mellitus
Association between UBE2E2 variant rs7612463 and type 2 diabetes mellitus in a Chinese Han population.
Diabetes Mellitus
Lack of association between UBE2E2 gene polymorphism (rs7612463) and type 2 diabetes mellitus in a Saudi population.
Diabetes Mellitus
Signals regulating accelerated muscle protein catabolism in uremia.
Diabetes Mellitus
The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan.
Diabetes Mellitus, Type 2
A genome-wide association study in the Japanese population identifies susceptibility loci for type 2 diabetes at UBE2E2 and C2CD4A-C2CD4B.
Diabetes Mellitus, Type 2
Association between the UBE2Z rs46522 and TCF7L2 rs7903146 polymorphisms with type 2 diabetes in south western Iran.
Diabetes Mellitus, Type 2
Association between UBE2E2 variant rs7612463 and type 2 diabetes mellitus in a Chinese Han population.
Diabetes Mellitus, Type 2
Genetic risk score constructed using 14 susceptibility alleles for type 2 diabetes is associated with the early onset of diabetes and may predict the future requirement of insulin injections among Japanese individuals.
Diabetes Mellitus, Type 2
Impact of KCNQ1, CDKN2A/2B, CDKAL1, HHEX, MTNR1B, SLC30A8, TCF7L2, and UBE2E2 on risk of developing type 2 diabetes in Thai population.
Diabetes Mellitus, Type 2
Lack of association between UBE2E2 gene polymorphism (rs7612463) and type 2 diabetes mellitus in a Saudi population.
Diabetes Mellitus, Type 2
Rs46522 in the Ubiquitin-Conjugating Enzyme E2Z Gene Is Associated with the Risk of Coronary Artery Disease in Individuals of Chinese Han Population with Type 2 Diabetes.
Diabetes Mellitus, Type 2
The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan.
Diabetes Mellitus, Type 2
Type 2 Diabetes Risk Allele UBE2E2 Is Associated With Decreased Glucose-Stimulated Insulin Release in Elderly Chinese Han Individuals.
Diabetes, Gestational
Putative association between UBE2E2 polymorphisms and the risk of gestational diabetes mellitus.
e2 ubiquitin-conjugating enzyme deficiency
A novel UBE2A mutation in a Chinese family with X-linked intellectual disability.
e2 ubiquitin-conjugating enzyme deficiency
Adjunctive use of the ketogenic diet in a young adult with UBE2A deficiency syndrome and super-refractory status epilepticus.
e2 ubiquitin-conjugating enzyme deficiency
An essential role for UBE2A/HR6A in learning and memory and mGLUR-dependent long-term depression.
e2 ubiquitin-conjugating enzyme deficiency
Delineation of Clinical Manifestations of the Inherited Xq24 Microdeletion Segregating with sXCI in Mothers: Two Novel Cases with Distinct Phenotypes Ranging from UBE2A Deficiency Syndrome to Recurrent Pregnancy Loss.
e2 ubiquitin-conjugating enzyme deficiency
Phosphorylation of the E3 ubiquitin protein ligase ITCH diminishes binding to its cognate E2 ubiquitin ligase.
e2 ubiquitin-conjugating enzyme deficiency
RAD6B Plays a Critical Role in Neuronal DNA Damage Response to Resist Neurodegeneration.
e2 ubiquitin-conjugating enzyme deficiency
Refinement of the clinical and mutational spectrum of UBE2A deficiency syndrome.
e2 ubiquitin-conjugating enzyme deficiency
The Fanconi anaemia components UBE2T and FANCM are functionally linked to nucleotide excision repair.
e2 ubiquitin-conjugating enzyme deficiency
The ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntington's disease protein, huntingtin.
e2 ubiquitin-conjugating enzyme deficiency
Ubc13 maintains the suppressive function of regulatory T cells and prevents their conversion into effector-like T cells.
e2 ubiquitin-conjugating enzyme deficiency
UbcH10 overexpression increases carcinogenesis and blocks ALLN susceptibility in colorectal cancer.
e2 ubiquitin-conjugating enzyme deficiency
UBE2A deficiency in two siblings: A novel splicing variant inherited from a maternal germline mosaicism.
e2 ubiquitin-conjugating enzyme deficiency
UBE2A deficiency syndrome: a report of two unrelated cases with large Xq24 deletions encompassing UBE2A gene.
e2 ubiquitin-conjugating enzyme deficiency
UBE2A deficiency syndrome: Mild to severe intellectual disability accompanied by seizures, absent speech, urogenital, and skin anomalies in male patients.
Elliptocytosis, Hereditary
A novel mobile element inserted in the alpha spectrin gene: spectrin dayton. A truncated alpha spectrin associated with hereditary elliptocytosis.
Elliptocytosis, Hereditary
Clinical expression of alpha spectrin mutants in hereditary elliptocytosis.
Elliptocytosis, Hereditary
Four different mutations in codon 28 of alpha spectrin are associated with structurally and functionally abnormal spectrin alpha I/74 in hereditary elliptocytosis.
Elliptocytosis, Hereditary
Genetic basis of the polymorphisms of the alphaI domain of spectrin.
Elliptocytosis, Hereditary
SP alpha I/65 hereditary elliptocytosis in Calabria (southern Italy).
Elliptocytosis, Hereditary
Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway.
Elliptocytosis, Hereditary
Structural and functional heterogeneity of alpha spectrin mutations involving the spectrin heterodimer self-association site: relationships to hematologic expression of homozygous hereditary elliptocytosis and hereditary pyropoikilocytosis.
Elliptocytosis, Hereditary
Unique alpha-spectrin mutant in a kindred with common hereditary elliptocytosis.
Endometrial Neoplasms
Combining Bioinformatics and Experiments to Identify and Verify Key Genes with Prognostic Values in Endometrial Carcinoma.
Endometrial Neoplasms
UbcH10 Expression in Benign, Hyperplastic, and Malignant Endometrial Curetted Materials: A Tissue Microarray Study.
Endometrial Neoplasms
UBE2C Is Upregulated by Estrogen and Promotes Epithelial-Mesenchymal Transition via p53 in Endometrial Cancer.
Endometrial Neoplasms
UBE2S mediates tumor progression via SOX6/?-Catenin signaling in endometrial cancer.
Endometrial Neoplasms
Zfx-induced upregulation of UBE2J1 facilitates endometrial cancer progression via PI3K/AKT pathway.
Epilepsy
An essential role for UBE2A/HR6A in learning and memory and mGLUR-dependent long-term depression.
Epilepsy, Generalized
Adjunctive use of the ketogenic diet in a young adult with UBE2A deficiency syndrome and super-refractory status epilepticus.
Escherichia coli Infections
High ubiquitin conjugating enzyme E2 T mRNA expression and its prognostic significance in lung adenocarcinoma: A study based on the TCGA database.
Esophageal Neoplasms
Overexpression of UBE2C in esophageal squamous cell carcinoma tissues and molecular analysis.
Esophageal Neoplasms
UBE2D3 gene overexpression increases radiosensitivity of EC109 esophageal cancer cells in vitro and in vivo.
Esophageal Neoplasms
UBE2D3 is a positive prognostic factor and is negatively correlated with hTERT expression in esophageal cancer.
Esophageal Neoplasms
UBE2L6/UBCH8 and ISG15 attenuate autophagy in esophageal cancer cells.
Esophageal Neoplasms
[Screening and identification of anoikis-resistant gene UBCH7 in esophageal cancer cells].
Esophageal Squamous Cell Carcinoma
High UBCH10 protein expression as a marker of poor prognosis in esophageal squamous cell carcinoma.
Esophageal Squamous Cell Carcinoma
Overexpression of UBE2C in esophageal squamous cell carcinoma tissues and molecular analysis.
Esophageal Squamous Cell Carcinoma
Preventive effect of oral hangeshashinto (TJ-14) on the development of reflux-induced esophageal cancer.
Esophageal Squamous Cell Carcinoma
UBE2C is involved in the functions of ECRG4 on esophageal squamous cell carcinoma.
Esophageal Squamous Cell Carcinoma
UBE2T Contributes to the Prognosis of Esophageal Squamous Cell Carcinoma.
Esotropia
Novel deletion at Xq24 including the UBE2A gene in a patient with X-linked mental retardation.
Fanconi Anemia
Allosteric Targeting of the Fanconi Anemia Ubiquitin-Conjugating Enzyme Ube2T by Fragment Screening.
Fanconi Anemia
AluY-mediated germline deletion, duplication and somatic stem cell reversion in UBE2T defines a new subtype of Fanconi anemia.
Fanconi Anemia
Deficiency of the Fanconi anemia E2 ubiqitin conjugase UBE2T only partially abrogates Alu-mediated recombination in a new model of homology dependent recombination.
Fanconi Anemia
Deficiency of UBE2T, the E2 Ubiquitin Ligase Necessary for FANCD2 and FANCI Ubiquitination, Causes FA-T Subtype of Fanconi Anemia.
Fanconi Anemia
High expression of UBE2T predicts poor prognosis and survival in multiple myeloma.
Fanconi Anemia
Homozygous missense variant in UBE2T is associated with mild Fanconi anemia phenotype.
Fanconi Anemia
Human alpha spectrin II and the FANCA, FANCC, and FANCG proteins bind to DNA containing psoralen interstrand cross-links.
Fanconi Anemia
Human alpha spectrin II and the Fanconi anemia proteins FANCA and FANCC interact to form a nuclear complex.
Fanconi Anemia
Hypoxia disrupts the Fanconi anemia pathway and sensitizes cells to chemotherapy through regulation of UBE2T.
Fanconi Anemia
Inherited bone marrow failure syndromes.
Fanconi Anemia
Knockdown of mu-calpain in Fanconi anemia, FA-A, cells by siRNA restores alphaII spectrin levels and corrects chromosomal instability and defective DNA interstrand cross-link repair.
Fanconi Anemia
Mind the metal: a fragment library-derived zinc impurity binds the E2 ubiquitin-conjugating enzyme Ube2T and induces structural rearrangements.
Fanconi Anemia
Mutations in the gene encoding the E2 conjugating enzyme UBE2T cause Fanconi anemia.
Fanconi Anemia
The Fanconi anaemia components UBE2T and FANCM are functionally linked to nucleotide excision repair.
Fanconi Anemia
The SH3 domain of alphaII spectrin is a target for the Fanconi anemia protein, FANCG.
Fanconi Anemia
Transcriptional Silencing of ALDH2 Confers a Dependency on Fanconi Anemia Proteins in Acute Myeloid Leukemia.
Fanconi Anemia
UBE2T Contributes to the Prognosis of Esophageal Squamous Cell Carcinoma.
Fanconi Anemia
UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative autoregulation.
Fanconi Anemia
UBE2T silencing suppresses proliferation and induces cell cycle arrest and apoptosis in bladder cancer cells.
Fanconi Anemia
UBE2T, the Fanconi anemia core complex, and FANCD2 are recruited independently to chromatin: a basis for the regulation of FANCD2 monoubiquitination.
Fanconi Anemia
UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2.
Fatty Liver
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Fractures, Spontaneous
Identification of potential target genes and related regulatory transcription factors in spontaneous hairline fracture induced by hypervitaminosis A.
Gallbladder Neoplasms
Erratum: Identification of UBE2T as an independent prognostic biomarker for gallbladder cancer.
Gallbladder Neoplasms
Identification of UBE2T as an independent prognostic biomarker for gallbladder cancer.
Gastroesophageal Reflux
Preventive effect of oral hangeshashinto (TJ-14) on the development of reflux-induced esophageal cancer.
Glioblastoma
Analysis of UbcH10 expression represents a useful tool for the diagnosis and therapy of astrocytic tumors.
Glioblastoma
High expression of UBE2C is associated with the aggressive progression and poor outcome of malignant glioma.
Glioblastoma
Molecular and Clinical Characterization of UBE2S in Glioma as a Biomarker for Poor Prognosis and Resistance to Chemo-Radiotherapy.
Glioblastoma
Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin.
Glioblastoma
SUMOylation Regulator-Related Molecules Can Be Used as Prognostic Biomarkers for Glioblastoma.
Glioblastoma
UBE2S, a novel substrate of Akt1, associates with Ku70 and regulates DNA repair and glioblastoma multiforme resistance to chemotherapy.
Glioblastoma
UBE2T promotes glioblastoma invasion and migration via stabilizing GRP78 and regulating EMT.
Glioma
Combined elevation of AURKB and UBE2C predicts severe outcomes and therapy resistance in glioma.
Glioma
Forkhead Box M1 positively regulates UBE2C and protects glioma cells from autophagic death.
Glioma
High expression of UBE2C is associated with the aggressive progression and poor outcome of malignant glioma.
Glioma
Knockdown of ubiquitin-conjugating enzyme E2C/UbcH10 expression by RNA interference inhibits glioma cell proliferation and enhances cell apoptosis in vitro.
Glioma
Molecular and Clinical Characterization of UBE2S in Glioma as a Biomarker for Poor Prognosis and Resistance to Chemo-Radiotherapy.
Glioma
SUMOylation of PUM2 promotes the vasculogenic mimicry of glioma cells via regulating CEBPD.
Glioma
UBE2D3 Activates SHP-2 Ubiquitination to Promote Glycolysis and Proliferation of Glioma via Regulating STAT3 Signaling Pathway.
Glioma
UBE2T promotes glioblastoma invasion and migration via stabilizing GRP78 and regulating EMT.
Glioma
Ubiquitin-conjugating enzyme UBE2C: molecular biology, role in tumorigenesis, and potential as a biomarker.
Goiter
UbcH10 overexpression may represent a marker of anaplastic thyroid carcinomas.
Graves Disease
The haplotype of UBE2L3 gene is associated with Hashimoto's thyroiditis in a Chinese Han population.
Head and Neck Neoplasms
Ubiquitin-conjugating enzyme UBE2Q2 suppresses cell proliferation and is down-regulated in recurrent head and neck cancer.
Heart Defects, Congenital
Novel deletion at Xq24 including the UBE2A gene in a patient with X-linked mental retardation.
Hematologic Neoplasms
Ubiquitin-conjugating enzyme UBE2C: molecular biology, role in tumorigenesis, and potential as a biomarker.
Hematuria
UBE2C cell-free RNA in urine can discriminate between bladder cancer and hematuria.
Hemochromatosis
UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is closely related to SFT, a stimulator of iron transport, and is up-regulated in hereditary hemochromatosis.
Hemosiderosis
Transplantation studies in mice with congenital hemolytic anemia.
Hepatitis
Gain of UBE2D1 facilitates hepatocellular carcinoma progression and is associated with DNA damage caused by continuous IL-6.
Hepatitis
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Hepatitis
UBE2L3, a susceptibility gene that plays oncogenic role in hepatitis B-related hepatocellular carcinoma.
Hepatitis B
Aberrant methylation of UBE2Q1 promoter is associated with poor prognosis of acute-on-chronic hepatitis B pre-liver failure.
Hepatitis B
Hypomethylated Ubiquitin-Conjugating Enzyme2 Q1 (UBE2Q1) Gene Promoter in the Serum Is a Promising Biomarker for Hepatitis B Virus-Associated Hepatocellular Carcinoma.
Hepatitis B, Chronic
Aberrant methylation of UBE2Q1 promoter is associated with poor prognosis of acute-on-chronic hepatitis B pre-liver failure.
Hepatitis B, Chronic
Hypomethylated Ubiquitin-Conjugating Enzyme2 Q1 (UBE2Q1) Gene Promoter in the Serum Is a Promising Biomarker for Hepatitis B Virus-Associated Hepatocellular Carcinoma.
Hepatitis B, Chronic
UBE2L3, a susceptibility gene that plays oncogenic role in hepatitis B-related hepatocellular carcinoma.
Hepatoblastoma
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Herpes Simplex
Functional characterization of residues required for the herpes simplex virus 1 E3 ubiquitin ligase ICP0 to interact with the cellular E2 ubiquitin-conjugating enzyme UBE2D1 (UbcH5a).
Herpes Simplex
Herpes simplex virus 1 mutant in which the ICP0 HUL-1 E3 ubiquitin ligase site is disrupted stabilizes cdc34 but degrades D-type cyclins and exhibits diminished neurotoxicity.
Herpes Simplex
Herpes simplex virus type 1 regulatory protein ICP0 does not protect cyclins D1 and D3 from degradation during infection.
Herpes Simplex
The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a.
Herpes Simplex
The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity.
Hirsutism
Novel deletion at Xq24 including the UBE2A gene in a patient with X-linked mental retardation.
Hirsutism
UBE2A deficiency in two siblings: A novel splicing variant inherited from a maternal germline mosaicism.
Hirsutism
UBE2A deficiency syndrome: Mild to severe intellectual disability accompanied by seizures, absent speech, urogenital, and skin anomalies in male patients.
Hodgkin Disease
UbcH10 expression in human lymphomas.
Huntington Disease
The ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntington's disease protein, huntingtin.
Huntington Disease
Ubiquitin-conjugating enzyme E2-25K increases aggregate formation and cell death in polyglutamine diseases.
Hypersensitivity
A critical role for the ubiquitin-conjugating enzyme Ubc13 in initiating homologous recombination.
Hypersensitivity
Arabidopsis UBC13 differentially regulates two programmed cell death pathways in responses to pathogen and low-temperature stress.
Hypersensitivity
Neddylation promotes ubiquitylation and release of Ku from DNA-damage sites.
Hypersensitivity
Nucleotide excision repair-induced H2A ubiquitination is dependent on MDC1 and RNF8 and reveals a universal DNA damage response.
Hypersensitivity
RAD6B overexpression confers chemoresistance: RAD6 expression during cell cycle and its redistribution to chromatin during DNA damage-induced response.
Hypersensitivity
UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40.
Hypertelorism
Novel deletion at Xq24 including the UBE2A gene in a patient with X-linked mental retardation.
Hypertriglyceridemia
Association of genetic variants with dyslipidemia.
Hypervitaminosis A
Identification of potential target genes and related regulatory transcription factors in spontaneous hairline fracture induced by hypervitaminosis A.
Immune System Diseases
The E2 ubiquitin-conjugating enzyme UbcH5c: an emerging target in cancer and immune disorders.
Immune System Diseases
UBE2N Promotes Melanoma Growth via MEK/FRA1/SOX10 Signaling.
Infarction, Middle Cerebral Artery
E2-25K SUMOylation inhibits proteasome for cell death during cerebral ischemia/reperfusion.
Infections
A functional variant in UBE2L3 contributes to HBV infection and maintains cccDNA stability by inducing degradation of APOBEC3A protein.
Infections
Antitumor effects of hsa?miR661?3p on non?small cell lung cancer in vivo and in vitro.
Infections
Consecutive Inhibition of ISG15 Expression and ISGylation by Cytomegalovirus Regulators.
Infections
E2 ubiquitin-conjugating enzyme UBE2L6 promotes Senecavirus A proliferation by stabilizing the viral RNA polymerase.
Infections
Echinococcus multilocularis infection induces UBE2N suppression via exosomal emu-miR-4989.
Infections
Evaluation of a SUMO E2 Conjugating Enzyme Involved in Resistance to Clavibacter michiganensis Subsp. michiganensis in Solanum peruvianum, Through a Tomato Mottle Virus VIGS Assay.
Infections
Herpes simplex virus type 1 regulatory protein ICP0 does not protect cyclins D1 and D3 from degradation during infection.
Infections
High ubiquitin conjugating enzyme E2 T mRNA expression and its prognostic significance in lung adenocarcinoma: A study based on the TCGA database.
Infections
Host genetic variants influencing the clinical course of hepatitis B virus infection.
Infections
ICP0 enables and monitors the function of D cyclins in herpes simplex virus 1 infected cells.
Infections
ISG15 in Host Defense Against Candida albicans Infection in a Mouse Model of Fungal Keratitis.
Infections
Large-Scale Arrayed Analysis of Protein Degradation Reveals Cellular Targets for HIV-1 Vpu.
Infections
Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination.
Infections
Leishmania donovani targets tumor necrosis factor receptor-associated factor (TRAF) 3 for impairing TLR4-mediated host response.
Infections
New loci associated with chronic hepatitis B virus infection in Han Chinese.
Infections
Proteasome inhibition attenuates coxsackievirus-induced myocardial damage in mice.
Infections
Structural basis for the recognition of Ubc13 by the Shigella flexneri effector OspI.
Infections
The deubiquitinase OTUB1 augments NF-?B-dependent immune responses in dendritic cells in infection and inflammation by stabilizing UBC13.
Infections
The stability of HSV-1 ICP0 early after infection is defined by the RING finger and the UL13 protein kinase.
Infections
UBE2L3, a susceptibility gene that plays oncogenic role in hepatitis B-related hepatocellular carcinoma.
Infections
Ubiquitin-Conjugating Enzyme E2 L3 is Downregulated by the Chikungunya Virus nsP2 Protease.
Infections
Ubiquitin-conjugating enzyme UBE2J1 negatively modulates interferon pathway and promotes RNA virus infection.
Infections
[Screening and identification of anoikis-resistant gene UBCH7 in esophageal cancer cells].
Infertility
Function of RAD6B and RNF8 in spermatogenesis.
Infertility
Genetic association of UBE2B variants with susceptibility to male infertility in a Northeast Chinese population.
Infertility
Loss of the E2 SUMO-conjugating enzyme Ube2i in oocytes during ovarian folliculogenesis causes infertility in mice.
Infertility
UBE2B mRNA alterations are associated with severe oligozoospermia in infertile men.
Infertility, Female
Loss of the E2 SUMO-conjugating enzyme Ube2i in oocytes during ovarian folliculogenesis causes infertility in mice.
Infertility, Male
Genetic association of UBE2B variants with susceptibility to male infertility in a Northeast Chinese population.
Infertility, Male
Novel variants in UBE2B gene and idiopathic male infertility.
Infertility, Male
Spermatid nuclear and sperm periaxonemal anomalies in the mouse Ube2b null mutant.
Infertility, Male
UBE2W down-regulation promotes cell apoptosis and correlates with hypospermatogenesis.
Infertility, Male
[UBE2B gene and male infertility: an update].
Inflammatory Bowel Diseases
Expression Quantitative Trait Loci Analysis Identifies Associations Between Genotype and Gene Expression in Human Intestine.
Inflammatory Bowel Diseases
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Inflammatory Bowel Diseases
SUMOylation pathway alteration coupled with downregulation of SUMO E2 enzyme at mucosal epithelium modulates inflammation in inflammatory bowel disease.
Influenza in Birds
SUMO1 modification of the non-structural protein 1 of influenza A virus.
Influenza, Human
Reliable reference genes for the quantification of mRNA in human T-cells and PBMCs stimulated with live influenza virus.
Insulin Resistance
Adipose-specific knockout of ubiquitin-conjugating enzyme E2L6 (Ube2l6) reduces diet-induced obesity, insulin resistance, and hepatic steatosis.
Insulin Resistance
Ubc13 haploinsufficiency protects against age-related insulin resistance and high-fat diet-induced obesity.
Insulin Resistance
[Identification and bioinformatics analysis of differentially expressed microRNAs in mice liver tissues with a high fat diet-induced insulin resistance].
Intellectual Disability
A novel 47.2 Mb duplication on chromosomal bands Xq21.1-25 associated with mental retardation.
Intellectual Disability
A novel missense mutation in the UBE2A gene causes intellectual disability in the large X-linked family.
Intellectual Disability
A novel splice site mutation in the UBE2A gene leads to aberrant mRNA splicing in a Chinese patient with X-linked intellectual disability type Nascimento.
Intellectual Disability
A novel UBE2A mutation causes X-linked intellectual disability type Nascimento.
Intellectual Disability
A novel UBE2A mutation in a Chinese family with X-linked intellectual disability.
Intellectual Disability
Adjunctive use of the ketogenic diet in a young adult with UBE2A deficiency syndrome and super-refractory status epilepticus.
Intellectual Disability
An essential role for UBE2A/HR6A in learning and memory and mGLUR-dependent long-term depression.
Intellectual Disability
KCMF1 (potassium channel modulatory factor 1) Links RAD6 to UBR4 (ubiquitin N-recognin domain-containing E3 ligase 4) and Lysosome-Mediated Degradation.
Intellectual Disability
Mechanistic insights revealed by a UBE2A mutation linked to intellectual disability.
Intellectual Disability
Mutations in the intellectual disability gene Ube2a cause neuronal dysfunction and impair parkin-dependent mitophagy.
Intellectual Disability
Novel deletion at Xq24 including the UBE2A gene in a patient with X-linked mental retardation.
Intellectual Disability
Refinement of the clinical and mutational spectrum of UBE2A deficiency syndrome.
Intellectual Disability
The Role of the Reanalysis of Genetic Test Results in the Diagnosis of Dysmorphic Syndrome Caused by Inherited xq24 Deletion including the UBE2A and CXorf56 Genes.
Intellectual Disability
UBE2A deficiency in two siblings: A novel splicing variant inherited from a maternal germline mosaicism.
Intellectual Disability
UBE2A deficiency syndrome: a report of two unrelated cases with large Xq24 deletions encompassing UBE2A gene.
Intellectual Disability
UBE2A deficiency syndrome: Mild to severe intellectual disability accompanied by seizures, absent speech, urogenital, and skin anomalies in male patients.
Intellectual Disability
X-linked intellectual disability type Nascimento is a clinically distinct, probably underdiagnosed entity.
Iron Deficiencies
A lysine-63-linked ubiquitin chain-forming conjugase, UBC13, promotes the developmental responses to iron deficiency in Arabidopsis roots.
Jaundice, Neonatal
Three Novel Spectrin Variants in Jaundiced Neonates.
Keratitis
ISG15 in Host Defense Against Candida albicans Infection in a Mouse Model of Fungal Keratitis.
Learning Disabilities
Whole exome sequencing reveals putatively novel associations in retinopathies and drusen formation.
Leukemia
Differential regulation of PML-RAR? stability by the ubiquitin ligases SIAH1/SIAH2 and TRIAD1.
Leukemia
Exome sequencing reveals novel and recurrent mutations with clinical impact in blastic plasmacytoid dendritic cell neoplasm.
Leukemia
Expression and localization of the CDC34 ubiquitin-conjugating enzyme in pediatric acute lymphoblastic leukemia.
Leukemia
Honokiol induces proteasomal degradation of AML1-ETO oncoprotein via increasing ubiquitin conjugase UbcH8 expression in leukemia.
Leukemia
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Leukemia
Inhibiting ubiquitination causes an accumulation of SUMOylated newly synthesized nuclear proteins at PML bodies.
Leukemia
Inhibition of UBE2L6 attenuates ISGylation and impedes ATRA-induced differentiation of leukemic cells.
Leukemia
Mechanism for ubiquitylation of the leukemia fusion proteins AML1-ETO and PML-RARalpha.
Leukemia
Physical and functional interactions between ZIP kinase and UbcH5.
Leukemia
The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a.
Leukemia, Erythroblastic, Acute
Biosynthesis of spectrin and its assembly into the cytoskeletal system of Friend erythroleukemia cells.
Leukemia, Myelogenous, Chronic, BCR-ABL Positive
De novo UBE2A mutations are recurrently acquired during chronic myeloid leukemia progression and interfere with myeloid differentiation pathways.
Leukemia, Myeloid, Acute
De novo UBE2A mutations are recurrently acquired during chronic myeloid leukemia progression and interfere with myeloid differentiation pathways.
Leukemia, Myeloid, Acute
Inhibition of UBE2L6 attenuates ISGylation and impedes ATRA-induced differentiation of leukemic cells.
Leukemia, Myeloid, Chronic, Atypical, BCR-ABL Negative
De novo UBE2A mutations are recurrently acquired during chronic myeloid leukemia progression and interfere with myeloid differentiation pathways.
Leukemia, Promyelocytic, Acute
Differential regulation of PML-RAR? stability by the ubiquitin ligases SIAH1/SIAH2 and TRIAD1.
Leukemia, Promyelocytic, Acute
Inhibition of UBE2L6 attenuates ISGylation and impedes ATRA-induced differentiation of leukemic cells.
Leukemia, T-Cell
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Leukemia, T-Cell
The human T-cell leukemia virus type 1 Tax oncoprotein requires the ubiquitin-conjugating enzyme Ubc13 for NF-kappaB activation.
Lipodystrophy
Lamin A tail modification by SUMO1 is disrupted by familial partial lipodystrophy-causing mutations.
Lipodystrophy, Familial Partial
Lamin A tail modification by SUMO1 is disrupted by familial partial lipodystrophy-causing mutations.
Liver Cirrhosis
Hypomethylated Ubiquitin-Conjugating Enzyme2 Q1 (UBE2Q1) Gene Promoter in the Serum Is a Promising Biomarker for Hepatitis B Virus-Associated Hepatocellular Carcinoma.
Liver Cirrhosis
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Liver Diseases
Aberrant methylation of UBE2Q1 promoter is associated with poor prognosis of acute-on-chronic hepatitis B pre-liver failure.
Liver Diseases
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Liver Diseases
Targeted deep sequencing of plasma circulating cell-free DNA reveals Vimentin and Fibulin 1 as potential epigenetic biomarkers for hepatocellular carcinoma.
Liver Neoplasms
Computational analysis for identification of early diagnostic biomarkers and prognostic biomarkers of liver cancer based on GEO and TCGA databases and studies on pathways and biological functions affecting the survival time of liver cancer.
Liver Neoplasms
Identification of the potential therapeutic target gene UBE2C in human hepatocellular carcinoma: An investigation based on GEO and TCGA databases.
Liver Neoplasms
Upregulated expression of ubiquitin-conjugating enzyme E2Q1 (UBE2Q1) is associated with enhanced cell proliferation and poor prognosis in human hapatocellular carcinoma.
Lung Neoplasms
Combinatory effect of BRCA1 and HERC2 expression on outcome in advanced non-small-cell lung cancer.
Lung Neoplasms
Deregulation of UBE2C-mediated autophagy repression aggravates NSCLC progression.
Lung Neoplasms
Effects of ubiquitin-conjugating enzyme 2C on invasion, proliferation and cell cycling of lung cancer cells.
Lung Neoplasms
Elevated expression of UBE2T in lung cancer tumors and cell lines.
Lung Neoplasms
KIAA0101 and UbcH10 interact to regulate non-small cell lung cancer cell proliferation by disrupting the function of the spindle assembly checkpoint.
Lung Neoplasms
Knockdown of UBE2T Inhibits Osteosarcoma Cell Proliferation, Migration, and Invasion by Suppressing the PI3K/Akt Signaling Pathway.
Lung Neoplasms
Lung Cancer and DNA Repair Genes: Multilevel Association Analysis from the International Lung Cancer Consortium.
Lung Neoplasms
miRNAs deregulation in serum of mice is associated with lung cancer related pathway deregulation induced by PM2.5.
Lung Neoplasms
Targeting CDC34 E2 ubiquitin conjugating enzyme for lung cancer therapy.
Lung Neoplasms
The miR 495-UBE2C-ABCG2/ERCC1 axis reverses cisplatin resistance by downregulating drug resistance genes in cisplatin-resistant non-small cell lung cancer cells.
Lung Neoplasms
The Relationship Between UBE2C and AGGF1 Overexpression and Tumor Angiogenesis in Non-Small Cell Lung Cancer.
Lung Neoplasms
UbcH10 expression provides a useful tool for the prognosis and treatment of non-small cell lung cancer.
Lung Neoplasms
UbcH10 overexpression in human lung carcinomas and its correlation with EGFR and p53 mutational status.
Lung Neoplasms
UBE2C, Directly Targeted by miR-548e-5p, Increases the Cellular Growth and Invasive Abilities of Cancer Cells Interacting with the EMT Marker Protein Zinc Finger E-box Binding Homeobox 1/2 in NSCLC.
Lung Neoplasms
Ube2S regulates Wnt/?-catenin signaling and promotes the progression of non-small cell lung cancer.
Lung Neoplasms
UBE2T promotes autophagy via the p53/AMPK/mTOR signaling pathway in lung adenocarcinoma.
Lung Neoplasms
UBE2T promotes radiation resistance in non-small cell lung cancer via inducing epithelial-mesenchymal transition and the ubiquitination-mediated FOXO1 degradation.
Lung Neoplasms
UBE2T silencing inhibited non-small cell lung cancer cell proliferation and invasion by suppressing the wnt/?-catenin signaling pathway.
Lung Neoplasms
Ubiquitin conjugating enzyme E2 L3 promoted tumor growth of NSCLC through accelerating p27kip1 ubiquitination and degradation.
Lung Neoplasms
Ubiquitin-conjugating enzyme E2C regulates apoptosis-dependent tumor progression of non-small cell lung cancer via ERK pathway.
Lung Neoplasms
Ubiquitin-conjugating enzyme E2T (UBE2T) and denticleless protein homolog (DTL) are linked to poor outcome in breast and lung cancers.
Lung Neoplasms
Ubiquitin-Conjugating Enzyme E2T is an Independent Prognostic Factor and Promotes Gastric Cancer Progression.
Lupus Erythematosus, Systemic
A functional haplotype of UBE2L3 confers risk for systemic lupus erythematosus.
Lupus Erythematosus, Systemic
Effect of UBE2L3 genotype on regulation of the linear ubiquitin chain assembly complex in systemic lupus erythematosus.
Lupus Erythematosus, Systemic
The autoimmune disease risk allele of UBE2L3 in African American patients with systemic lupus erythematosus: a recessive effect upon subphenotypes.
Lupus Erythematosus, Systemic
UBE2L3 Polymorphism Amplifies NF-?B Activation and Promotes Plasma Cell Development, Linking Linear Ubiquitination to Multiple Autoimmune Diseases.
Lupus Erythematosus, Systemic
Variants in TNFSF4, TNFAIP3, TNIP1, BLK, SLC15A4 and UBE2L3 interact to confer risk of systemic lupus erythematosus in Chinese population.
Lymphatic Metastasis
Association of clinicopathological features with UbcH10 expression in colorectal cancer.
Lymphatic Metastasis
Expression of UbcH10 in pancreatic ductal adenocarcinoma and its correlation with prognosis.
Lymphatic Metastasis
Overexpression of UBE2C correlates with poor prognosis in gastric cancer patients.
Lymphatic Metastasis
Silencing ubiquitin-conjugating enzyme 2C inhibits proliferation and epithelial-mesenchymal transition in pancreatic ductal adenocarcinoma.
Lymphatic Metastasis
The clinicopathological significance of UBE2C in breast cancer: a study based on immunohistochemistry, microarray and RNA-sequencing data.
Lymphatic Metastasis
The clinicopathological significance of ubiquitin-conjugating enzyme E2C, leucine-rich repeated-containing G protein-coupled receptor, WW domain-containing oxidoreductase, and vasculogenic mimicry in invasive breast carcinoma.
Lymphatic Metastasis
The expression of ubiquitin-conjugating enzyme E2C and KAI1 in ovarian carcinoma and their clinical significance.
Lymphatic Metastasis
The Relationship Between UBE2C and AGGF1 Overexpression and Tumor Angiogenesis in Non-Small Cell Lung Cancer.
Lymphatic Metastasis
UBE2C is a Potential Biomarker for Tumorigenesis and Prognosis in Tongue Squamous Cell Carcinoma.
Lymphatic Metastasis
Ube2S regulates Wnt/?-catenin signaling and promotes the progression of non-small cell lung cancer.
Lymphatic Metastasis
UBE2T promotes radiation resistance in non-small cell lung cancer via inducing epithelial-mesenchymal transition and the ubiquitination-mediated FOXO1 degradation.
Lymphoma
Furosine Induced Apoptosis by the Regulation of STAT1/STAT2 and UBA7/UBE2L6 Genes in HepG2 Cells.
Lymphoma
UbcH10 expression in human lymphomas.
Lymphoma, B-Cell
Identification of collaborative activities with oxidative phosphorylation in bipolar disorder.
Lymphoma, Non-Hodgkin
UbcH10 expression in human lymphomas.
Malaria
Identification of an Atg8-Atg3 protein-protein interaction inhibitor from the medicines for Malaria Venture Malaria Box active in blood and liver stage Plasmodium falciparum parasites.
Malaria
Red blood cell membrane disorders.
Malaria, Cerebral
Self-reactivities to the non-erythroid alpha spectrin correlate with cerebral malaria in Gabonese children.
Medulloblastoma
Analysis of transcripts from 17p13.3 in medulloblastoma suggests ROX/MNT as a potential tumour suppressor gene.
Medulloblastoma
Zfx facilitates tumorigenesis caused by activation of the Hedgehog pathway.
Medulloblastoma
Zfx-induced upregulation of UBE2J1 facilitates endometrial cancer progression via PI3K/AKT pathway.
Medulloblastoma
[WGCNA screening of prognostic markers in medulloblastoma].
Melanoma
Alternative Splicing of RAD6B and Not RAD6A is Selectively Increased in Melanoma: Identification and Functional Characterization.
Melanoma
Comprehensive Investigation into the Role of Ubiquitin-Conjugating Enzyme E2S in Melanoma Development.
Melanoma
Differential UBE2C and HOXA1 expression in melanocytic nevi and melanoma.
Melanoma
RAD6B Loss Disrupts Expression of Melanoma Phenotype in Part by Inhibiting WNT/?-Catenin Signaling.
Melanoma
Role of SUMO/Ubc9 in DNA damage repair and tumorigenesis.
Melanoma
Targeting Ubc9 for cancer therapy.
Melanoma
UBE2C overexpression in melanoma and its essential role in G2/M transition.
Melanoma
UBE2N plays a pivotal role in maintaining melanoma malignancy.
Melanoma
UBE2N Promotes Melanoma Growth via MEK/FRA1/SOX10 Signaling.
Meningioma
A study of UbcH10 expression and its association with recurrence of meningiomas.
Meningioma
RIZ1 negatively regulates ubiquitin-conjugating enzyme E2C/UbcH10 via targeting c-Myc in meningioma.
Mental Retardation, X-Linked
Delineation of Clinical Manifestations of the Inherited Xq24 Microdeletion Segregating with sXCI in Mothers: Two Novel Cases with Distinct Phenotypes Ranging from UBE2A Deficiency Syndrome to Recurrent Pregnancy Loss.
Mental Retardation, X-Linked
Novel deletion at Xq24 including the UBE2A gene in a patient with X-linked mental retardation.
Mental Retardation, X-Linked
Novel missense mutations in the ubiquitination-related gene UBE2A cause a recognizable X-linked mental retardation syndrome.
Mental Retardation, X-Linked
UBE2A, which encodes a ubiquitin-conjugating enzyme, is mutated in a novel X-linked mental retardation syndrome.
Metabolic Diseases
Ubc13 haploinsufficiency protects against age-related insulin resistance and high-fat diet-induced obesity.
Metabolic Syndrome
Association analysis of genetic variants with metabolic syndrome components in the Moroccan population.
Mouth Neoplasms
Cancer Stem Cell based molecular predictors of tumor recurrence in Oral squamous cell carcinoma.
Mouth Neoplasms
UBE2C promotes the progression of head and neck squamous cell carcinoma.
Mouth Neoplasms
UBE2S associated with OSCC proliferation by promotion of P21 degradation via the ubiquitin-proteasome system.
Mouth Neoplasms
Up-regulation of miR-455-5p by the TGF-?-SMAD signalling axis promotes the proliferation of oral squamous cancer cells by targeting UBE2B.
Multiple Myeloma
Amplification and overexpression of E2 ubiquitin conjugase UBE2T promotes homologous recombination in multiple myeloma.
Multiple Myeloma
Blockade of ubiquitin-conjugating enzyme CDC34 enhances anti-myeloma activity of Bortezomib/Proteasome inhibitor PS-341.
Multiple Myeloma
High expression of UBE2T predicts poor prognosis and survival in multiple myeloma.
Multiple Myeloma
hsa-miR-631 resensitizes bortezomib-resistant multiple myeloma cell lines by inhibiting UbcH10.
Muscle Hypotonia
The Role of the Reanalysis of Genetic Test Results in the Diagnosis of Dysmorphic Syndrome Caused by Inherited xq24 Deletion including the UBE2A and CXorf56 Genes.
Muscular Atrophy
Effects of ornithine alpha-ketoglutarate on protein metabolism in Yoshida sarcoma-bearing rats.
Muscular Atrophy
UBE2D2 is not involved in MuRF1-dependent muscle wasting during hindlimb suspension.
Muscular Atrophy
UBE2L3, a Partner of MuRF1/TRIM63, Is Involved in the Degradation of Myofibrillar Actin and Myosin.
Myocardial Infarction
The rs46522 Polymorphism of the Ubiquitin-Conjugating Enzyme E2Z Gene Is Associated with Abnormal Metabolic Parameters in Patients with Myocardial Infarction: The Genetics of Atherosclerosis Disease Mexican Study.
Nasopharyngeal Carcinoma
Epigenetic downregulation of the ISG15-conjugating enzyme UbcH8 impairs lipolysis and correlates with poor prognosis in nasopharyngeal carcinoma.
Nasopharyngeal Carcinoma
High expression of ubiquitin-conjugating enzyme 2C (UBE2C) correlates with nasopharyngeal carcinoma progression.
Nasopharyngeal Carcinoma
UBE2T promotes nasopharyngeal carcinoma cell proliferation, invasion, and metastasis by activating the AKT/GSK3?/?-catenin pathway.
Nasopharyngeal Carcinoma
Ubiquitin-conjugating enzyme E2 B regulates the ubiquitination of O6-methylguanine-DNA methyltransferase and BCNU sensitivity in human nasopharyngeal carcinoma cells.
Neoplasm Metastasis
A novel Ubc9 -dependent pathway regulates SIRT1- ER-? Axis and BRCA1-associated TNBC lung metastasis.
Neoplasm Metastasis
Association of clinicopathological features with UbcH10 expression in colorectal cancer.
Neoplasm Metastasis
Characterization of KRAS Rearrangements in Metastatic Prostate Cancer.
Neoplasm Metastasis
Comprehensive Investigation into the Role of Ubiquitin-Conjugating Enzyme E2S in Melanoma Development.
Neoplasm Metastasis
Deregulation of UBE2C-mediated autophagy repression aggravates NSCLC progression.
Neoplasm Metastasis
Detection of aberrations of ubiquitin-conjugating enzyme E2C gene (UBE2C) in advanced colon cancer with liver metastases by DNA microarray and two-color FISH.
Neoplasm Metastasis
Downregulated genes by silencing MYC pathway identified with RNA-SEQ analysis as potential prognostic biomarkers in gastric adenocarcinoma.
Neoplasm Metastasis
Elevated expression of UBE2T exhibits oncogenic properties in human prostate cancer.
Neoplasm Metastasis
Expression of UbcH10 in pancreatic ductal adenocarcinoma and its correlation with prognosis.
Neoplasm Metastasis
Genetic and epigenetic analysis of non-small cell lung cancer with NotI-microarrays.
Neoplasm Metastasis
Hypomethylated Ubiquitin-Conjugating Enzyme2 Q1 (UBE2Q1) Gene Promoter in the Serum Is a Promising Biomarker for Hepatitis B Virus-Associated Hepatocellular Carcinoma.
Neoplasm Metastasis
Oncogenic Activities Of UBE2S Mediated By VHL/HIF-1?/STAT3 Signal Via The Ubiquitin-Proteasome System In PDAC.
Neoplasm Metastasis
Prognostic value of ubiquitin E2 UBE2W and its correlation with tumor-infiltrating immune cells in breast cancer.
Neoplasm Metastasis
Prognostic value of ubiquitin-conjugating enzyme E2 S overexpression in hepatocellular carcinoma.
Neoplasm Metastasis
RAD6B Loss Disrupts Expression of Melanoma Phenotype in Part by Inhibiting WNT/?-Catenin Signaling.
Neoplasm Metastasis
RIZ1 negatively regulates ubiquitin-conjugating enzyme E2C/UbcH10 via targeting c-Myc in meningioma.
Neoplasm Metastasis
Silencing ubiquitin-conjugating enzyme 2C inhibits proliferation and epithelial-mesenchymal transition in pancreatic ductal adenocarcinoma.
Neoplasm Metastasis
Slug-induced elevation of D1 cyclin in breast cancer cells through the inhibition of its ubiquitination.
Neoplasm Metastasis
The clinicopathological significance of UBE2C in breast cancer: a study based on immunohistochemistry, microarray and RNA-sequencing data.
Neoplasm Metastasis
The clinicopathological significance of ubiquitin-conjugating enzyme E2C, leucine-rich repeated-containing G protein-coupled receptor, WW domain-containing oxidoreductase, and vasculogenic mimicry in invasive breast carcinoma.
Neoplasm Metastasis
The expression of ubiquitin-conjugating enzyme E2C and KAI1 in ovarian carcinoma and their clinical significance.
Neoplasm Metastasis
The interplay of UBE2T and Mule in regulating Wnt/?-catenin activation to promote hepatocellular carcinoma progression.
Neoplasm Metastasis
The Relationship Between UBE2C and AGGF1 Overexpression and Tumor Angiogenesis in Non-Small Cell Lung Cancer.
Neoplasm Metastasis
UBE2C is a Potential Biomarker for Tumorigenesis and Prognosis in Tongue Squamous Cell Carcinoma.
Neoplasm Metastasis
UBE2C, Directly Targeted by miR-548e-5p, Increases the Cellular Growth and Invasive Abilities of Cancer Cells Interacting with the EMT Marker Protein Zinc Finger E-box Binding Homeobox 1/2 in NSCLC.
Neoplasm Metastasis
UBE2I promotes metastasis and correlates with poor prognosis in hepatocellular carcinoma.
Neoplasm Metastasis
UBE2L3, a susceptibility gene that plays oncogenic role in hepatitis B-related hepatocellular carcinoma.
Neoplasm Metastasis
UBE2S interacting with TRIM28 in the nucleus accelerates cell cycle by ubiquitination of p27 to promote hepatocellular carcinoma development.
Neoplasm Metastasis
UBE2S promotes the progression and Olaparib resistance of ovarian cancer through Wnt/?-catenin signaling pathway.
Neoplasm Metastasis
Ube2S regulates Wnt/?-catenin signaling and promotes the progression of non-small cell lung cancer.
Neoplasm Metastasis
UBE2T promotes nasopharyngeal carcinoma cell proliferation, invasion, and metastasis by activating the AKT/GSK3?/?-catenin pathway.
Neoplasm Metastasis
UBE2T promotes radiation resistance in non-small cell lung cancer via inducing epithelial-mesenchymal transition and the ubiquitination-mediated FOXO1 degradation.
Neoplasm Metastasis
Ube2v1-mediated ubiquitination and degradation of Sirt1 promotes metastasis of colorectal cancer by epigenetically suppressing autophagy.
Neoplasm Metastasis
Ubiquitin Conjugating Enzyme E2 H (UBE2H) Is Linked to Poor Outcomes and Metastasis in Lung Adenocarcinoma.
Neoplasm Metastasis
Ubiquitin-conjugating enzyme complex Uev1A-Ubc13 promotes breast cancer metastasis through nuclear factor-[cyrillic small letter ka]B mediated matrix metalloproteinase-1 gene regulation.
Neoplasm Metastasis
Ubiquitin-conjugating enzyme E2T(UBE2T) promotes colorectal cancer progression by facilitating ubiquitination and degradation of p53.
Neoplasm Metastasis
Ubiquitin-conjugating enzyme Ubc13 controls breast cancer metastasis through a TAK1-p38 MAP kinase cascade.
Neoplasm Metastasis
Uev1A promotes breast cancer cell migration by up-regulating CT45A expression via the AKT pathway.
Neoplasm Metastasis
Uev1A promotes breast cancer cell survival and chemoresistance through the AKT-FOXO1-BIM pathway.
Neoplasm Metastasis
Uev1A-Ubc13 promotes colorectal cancer metastasis through regulating CXCL1 expression via NF-?B activation.
Neoplasm Metastasis
Upregulation of UBE2Q1 via gene copy number gain in hepatocellular carcinoma promotes cancer progression through ?-catenin-EGFR-PI3K-Akt-mTOR signaling pathway.
Neoplasms
A Complex Regulatory Network Coordinating Cell Cycles During Caenorhabditis elegans Development Is Revealed by a Genome-Wide RNAi Screen.
Neoplasms
A Comprehensive Bioinformatics Analysis of UBE2C in Cancers.
Neoplasms
A conditional transposon-based insertional mutagenesis screen for genes associated with mouse hepatocellular carcinoma.
Neoplasms
A molecular 'signature' of primary breast cancer cultures; patterns resembling tumor tissue.
Neoplasms
A molecular basis for stabilization of the von Hippel-Lindau (VHL) tumor suppressor protein by components of the VHL ubiquitin ligase.
Neoplasms
A monoclonal antibody against a potential cancer biomarker, human ubiquitin-conjugating enzyme E2.
Neoplasms
A study of UbcH10 expression and its association with recurrence of meningiomas.
Neoplasms
All-trans retinoic acid treatment of Wilms tumor cells reverses expression of genes associated with high risk and relapse in vivo.
Neoplasms
Allosteric Targeting of the Fanconi Anemia Ubiquitin-Conjugating Enzyme Ube2T by Fragment Screening.
Neoplasms
AluY-mediated germline deletion, duplication and somatic stem cell reversion in UBE2T defines a new subtype of Fanconi anemia.
Neoplasms
Analysis of transcripts from 17p13.3 in medulloblastoma suggests ROX/MNT as a potential tumour suppressor gene.
Neoplasms
Analysis of UbcH10 expression represents a useful tool for the diagnosis and therapy of astrocytic tumors.
Neoplasms
Antitumor effects of hsa?miR661?3p on non?small cell lung cancer in vivo and in vitro.
Neoplasms
Association of clinicopathological features with UbcH10 expression in colorectal cancer.
Neoplasms
Association of survival and disease progression with chromosomal instability: a genomic exploration of colorectal cancer.
Neoplasms
Autophagy regulates UBC9 levels during viral-mediated tumorigenesis.
Neoplasms
Cancer Stem Cell based molecular predictors of tumor recurrence in Oral squamous cell carcinoma.
Neoplasms
CCI-779 Inhibits Cell-Cycle G2-M Progression and Invasion of Castration-Resistant Prostate Cancer via Attenuation of UBE2C Transcription and mRNA Stability.
Neoplasms
Cell division cycle 34 is highly expressed in hepatitis C virus-positive hepatocellular carcinoma with favorable phenotypes.
Neoplasms
Changes in the transcriptome of bovine ovarian cortex during follicle activation in vitro.
Neoplasms
Chromenopyrimidinone Controls Stemness and Malignancy by suppressing CD133 Expression in Hepatocellular Carcinoma.
Neoplasms
Clinical implications of gene dosage and gene expression patterns in diploid breast carcinoma.
Neoplasms
Clinicopathological relevance of UbcH10 in breast cancer.
Neoplasms
Combinatory effect of BRCA1 and HERC2 expression on outcome in advanced non-small-cell lung cancer.
Neoplasms
Combined elevation of AURKB and UBE2C predicts severe outcomes and therapy resistance in glioma.
Neoplasms
Comprehensive Investigation into the Role of Ubiquitin-Conjugating Enzyme E2S in Melanoma Development.
Neoplasms
Constitutional trisomy 8p11.21-q11.21 mosaicism: a germline alteration predisposing to myeloid leukaemia.
Neoplasms
Depletion of UBE2C reduces ovarian cancer malignancy and reverses cisplatin resistance via downregulating CDK1.
Neoplasms
Deregulation of Rb-E2F1 axis causes chromosomal instability by engaging the transactivation function of Cdc20-anaphase-promoting complex/cyclosome.
Neoplasms
Deregulation of UBE2C-mediated autophagy repression aggravates NSCLC progression.
Neoplasms
Detection of aberrations of ubiquitin-conjugating enzyme E2C gene (UBE2C) in advanced colon cancer with liver metastases by DNA microarray and two-color FISH.
Neoplasms
Dietary flavonoids, luteolin and quercetin, inhibit invasion of cervical cancer by reduction of UBE2S through epithelial-mesenchymal transition signaling.
Neoplasms
Differentially expressed genes in hormone refractory prostate cancer: association with chromosomal regions involved with genetic aberrations.
Neoplasms
DNA methylation patterns in luminal breast cancers differ from non-luminal subtypes and can identify relapse risk independent of other clinical variables.
Neoplasms
Downregulation of UBE2E2 in rat liver cells after hepatocarcinogen treatment facilitates cell proliferation and slowing down of DNA damage response in GST-P-expressing preneoplastic lesions.
Neoplasms
Elevated expression of UBE2T exhibits oncogenic properties in human prostate cancer.
Neoplasms
Elevated expression of UBE2T in lung cancer tumors and cell lines.
Neoplasms
Elevated TOP2A and UBE2C expressions correlate with poor prognosis in patients with surgically resected lung adenocarcinoma: a study based on immunohistochemical analysis and bioinformatics.
Neoplasms
Emerging roles of Lys63-linked polyubiquitylation in immune responses.
Neoplasms
Epigallocatechin gallate inhibits HeLa cells by modulation of epigenetics and signaling pathways.
Neoplasms
Essential cytoplasmic translocation of a cytokine receptor-assembled signaling complex.
Neoplasms
Estrogen-regulated gene expression predicts response to endocrine therapy in patients with ovarian cancer.
Neoplasms
Exome sequencing reveals novel mutation targets in diffuse large B-cell lymphomas derived from Chinese patients.
Neoplasms
Expression and clinical significance of UBE2V1 in cervical cancer.
Neoplasms
Expression and effect of inhibition of the ubiquitin-conjugating enzyme E2C on esophageal adenocarcinoma.
Neoplasms
Expression of the novel human gene, UBE2Q1, in breast tumors.
Neoplasms
Expression of UbcH10 in pancreatic ductal adenocarcinoma and its correlation with prognosis.
Neoplasms
Expression of UBE2C in lung adenocarcinoma based on database analysis and its clinical significance.
Neoplasms
Expression of UBE2Q2, a putative member of the ubiquitin-conjugating enzyme family in pediatric acute lymphoblastic leukemia.
Neoplasms
Expression of ubiquitin-conjugating enzyme E2C/UbcH10 in astrocytic tumors.
Neoplasms
Expression of ubiquitin-conjugating enzyme E2T in colorectal cancers and clinical implications.
Neoplasms
Expression Status of UBE2Q2 in Colorectal Primary Tumors and Cell Lines.
Neoplasms
FOXP3 Activates SUMO-Conjugating UBC9 Gene in MCF7 Breast Cancer Cells.
Neoplasms
Gain of UBE2D1 facilitates hepatocellular carcinoma progression and is associated with DNA damage caused by continuous IL-6.
Neoplasms
Gene expression patterns in the histopathological classification of epithelial ovarian cancer.
Neoplasms
Gene expression profiling of mouse p53-deficient epidermal carcinoma defines molecular determinants of human cancer malignancy.
Neoplasms
Genetic and epigenetic analysis of non-small cell lung cancer with NotI-microarrays.
Neoplasms
Genomic Integration of High-Risk HPV Alters Gene Expression in Oropharyngeal Squamous Cell Carcinoma.
Neoplasms
Genomic profiling of circulating plasma RNA for the analysis of cancer.
Neoplasms
Global analysis of gene expression signature and diagnostic/prognostic biomarker identification of hepatocellular carcinoma.
Neoplasms
HIF-1alpha and EPAS ubiquitination mediated by the VHL tumour suppressor involves flexibility in the ubiquitination mechanism, similar to other RING E3 ligases.
Neoplasms
High Expression of UBE2B as a Poor Prognosis Factor in Patients With Rectal Cancer Following Chemoradiotherapy.
Neoplasms
High expression of UBE2C is associated with the aggressive progression and poor outcome of malignant glioma.
Neoplasms
High ubiquitin conjugating enzyme E2 T mRNA expression and its prognostic significance in lung adenocarcinoma: A study based on the TCGA database.
Neoplasms
Homology modeling and virtual screening of ubiquitin conjugation enzyme E2A for designing a novel selective antagonist against cancer.
Neoplasms
HP1? Sensitizes Cervical Cancer Cells to Cisplatin through the Suppression of UBE2L3.
Neoplasms
Hypomethylated Ubiquitin-Conjugating Enzyme2 Q1 (UBE2Q1) Gene Promoter in the Serum Is a Promising Biomarker for Hepatitis B Virus-Associated Hepatocellular Carcinoma.
Neoplasms
Hypoxia disrupts the Fanconi anemia pathway and sensitizes cells to chemotherapy through regulation of UBE2T.
Neoplasms
Identification of a novel microRNA-mRNA regulatory biomodule in human prostate cancer.
Neoplasms
Identification of a potential tumor suppressor gene, UBL3, in non-small cell lung cancer.
Neoplasms
Identification of biomarkers correlated with diagnosis and prognosis of endometrial cancer using bioinformatics analysis.
Neoplasms
Identification of collaborative activities with oxidative phosphorylation in bipolar disorder.
Neoplasms
Identification of epigenetically downregulated Tmem70 and Ube2e2 in rat liver after 28-day treatment with hepatocarcinogenic thioacetamide showing gene product downregulation in hepatocellular preneoplastic and neoplastic lesions produced by tumor promotion.
Neoplasms
Identification of genes associated with tumorigenesis of meibomian cell carcinoma by microarray analysis.
Neoplasms
Identification of hub genes involved in the occurrence and development of hepatocellular carcinoma via bioinformatics analysis.
Neoplasms
Identification of New Lead Molecules Against UBE2NL Enzyme for Cancer Therapy.
Neoplasms
Identification of Novel Prognostic Biomarkers in Head and Neck Squamous Cell Carcinoma using Bioinformatics Analysis.
Neoplasms
Identification of overexpressed genes in hepatocellular carcinoma, with special reference to ubiquitin-conjugating enzyme E2C gene expression.
Neoplasms
Identification of small molecule inhibitors against UBE2C by using docking studies.
Neoplasms
Identification of the potential therapeutic target gene UBE2C in human hepatocellular carcinoma: An investigation based on GEO and TCGA databases.
Neoplasms
Identification of UBE2T as an independent prognostic biomarker for gallbladder cancer.
Neoplasms
Inactivation of the ubiquitin conjugating enzyme UBE2Q2 causes a prophase arrest and enhanced apoptosis in response to microtubule inhibiting agents.
Neoplasms
Increased Expression of UBE2T Predicting Poor Survival of Epithelial Ovarian Cancer: Based on Comprehensive Analysis of UBE2s, Clinical Samples, and the GEO Database.
Neoplasms
Induction of cell proliferation, clonogenicity and cell accumulation in S phase as a consequence of human UBE2Q1 overexpression.
Neoplasms
Inhibition of UBE2N-dependent CDK6 protein degradation by miR-934 promotes human bladder cancer cell growth.
Neoplasms
Integrated clinicopathological features and gene microarray analysis of pancreatic neuroendocrine tumors.
Neoplasms
Interleukin-1 and TRAF6-dependent activation of TAK1 in the absence of TAB2 and TAB3.
Neoplasms
Involvement of ubiquitin-conjugating enzyme E2C in proliferation and invasion of prostate carcinoma cells.
Neoplasms
ISG15 as a novel tumor biomarker for drug sensitivity.
Neoplasms
ISGylation governs the oncogenic function of Ki-Ras in breast cancer.
Neoplasms
Ixazomib inhibits myeloma cell proliferation by targeting UBE2K.
Neoplasms
KIAA0101 and UbcH10 interact to regulate non-small cell lung cancer cell proliferation by disrupting the function of the spindle assembly checkpoint.
Neoplasms
Knockdown of UbcH10 Enhances the Chemosensitivity of Dual Drug Resistant Breast Cancer Cells to Epirubicin and Docetaxel.
Neoplasms
Knockdown of UBE2T Inhibits Osteosarcoma Cell Proliferation, Migration, and Invasion by Suppressing the PI3K/Akt Signaling Pathway.
Neoplasms
Lentivirus-mediated RNA interference targeting UbcH10 reduces cell growth and invasion of human osteosarcoma cells via inhibition of Ki-67 and matrix metalloproteinases.
Neoplasms
LncRNA MALAT1 Regulating Lung Carcinoma Progression via the miR-491-5p/UBE2C Axis.
Neoplasms
Mapping of Genomic Vulnerabilities in the Post-Translational Ubiquitination, SUMOylation and Neddylation Machinery in Breast Cancer.
Neoplasms
MicroRNA miR-147b promotes tumor growth via targeting UBE2N in hepatocellular carcinoma.
Neoplasms
MicroRNA-mediated regulation of Ubc9 expression in cancer cells.
Neoplasms
Midline2 is overexpressed and a prognostic indicator in human breast cancer and promotes breast cancer cell proliferation in vitro and in vivo.
Neoplasms
miR-205 acts as a tumour radiosensitizer by targeting ZEB1 and Ubc13.
Neoplasms
MiR-525-5p Repressed Metastasis and Anoikis Resistance in Cervical Cancer via Blocking UBE2C/ZEB1/2 Signal Axis.
Neoplasms
miR-671-5p Inhibits Tumor Proliferation by Blocking Cell Cycle in Osteosarcoma.
Neoplasms
miRNA?101?3p.1 as an independent diagnostic biomarker aggravates chronic obstructive pulmonary disease via activation of the EGFR/PI3K/AKT signaling pathway.
Neoplasms
Molecular and Clinical Characterization of UBE2S in Glioma as a Biomarker for Poor Prognosis and Resistance to Chemo-Radiotherapy.
Neoplasms
Molecular characterization of central neurocytomas: Potential markers for tumor typing and progression.
Neoplasms
Niclosamide Induces Cell Cycle Arrest in G1 Phase in Head and Neck Squamous Cell Carcinoma Through Let-7d/CDC34 Axis.
Neoplasms
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Neoplasms
Oncogenic Activities Of UBE2S Mediated By VHL/HIF-1?/STAT3 Signal Via The Ubiquitin-Proteasome System In PDAC.
Neoplasms
Over-accumulation of nuclear IGF-1 receptor in tumor cells requires elevated expression of the receptor and the SUMO-conjugating enzyme Ubc9.
Neoplasms
Overexpression of the E2 ubiquitin-conjugating enzyme UbcH10 causes chromosome missegregation and tumor formation.
Neoplasms
Overexpression of the novel human gene, UBE2Q2, in breast cancer.
Neoplasms
Overexpression of UbcH10 alternates the cell cycle profile and accelerate the tumor proliferation in colon cancer.
Neoplasms
Overexpression of ubiquitin-conjugating enzyme E2 L3 in hepatocellular carcinoma potentiates apoptosis evasion by inhibiting the GSK3?/p65 pathway.
Neoplasms
Overexpression, genomic amplification and therapeutic potential of inhibiting the UbcH10 ubiquitin conjugase in human carcinomas of diverse anatomic origin.
Neoplasms
Phospho-MED1-enhanced UBE2C locus looping drives castration-resistant prostate cancer growth.
Neoplasms
Precision cancer therapy: profiting from tumor specific defects in the DNA damage tolerance system.
Neoplasms
Prognostic significance of UBE2C mRNA expression in high-risk early breast cancer. A Hellenic Cooperative Oncology Group (HeCOG) Study.
Neoplasms
Prognostic value of ubiquitin E2 UBE2W and its correlation with tumor-infiltrating immune cells in breast cancer.
Neoplasms
Prognostic value of ubiquitin-conjugating enzyme E2 S overexpression in hepatocellular carcinoma.
Neoplasms
Promoter Methylation Status of Two Novel Human Genes, UBE2Q1 and UBE2Q2, in Colorectal Cancer: a New Finding in Iranian Patients.
Neoplasms
Provirus integration into a gene encoding a ubiquitin-conjugating enzyme results in a placental defect and embryonic lethality.
Neoplasms
Quantitative SWATH-Based Proteomic Profiling for Identification of Mechanism-Driven Diagnostic Biomarkers Conferring in the Progression of Metastatic Prostate Cancer.
Neoplasms
Rad6B is a positive regulator of beta-catenin stabilization.
Neoplasms
RAD6B Loss Disrupts Expression of Melanoma Phenotype in Part by Inhibiting WNT/?-Catenin Signaling.
Neoplasms
Renal medullary carcinomas depend upon SMARCB1 loss and are sensitive to proteasome inhibition.
Neoplasms
RNA INTERFERENCE-MEDIATED SILENCING OF UBCH10 GENE INHIBITS COLORECTAL CANCER CELL GROWTH IN VITRO AND IN VIVO.
Neoplasms
RNA interference-mediated silencing of UBCH10 gene inhibits colorectal cancer cell growth in vitro and in vivo.
Neoplasms
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Neoplasms
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity that is Essential for DNA Double-Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment.
Neoplasms
Role of SUMO/Ubc9 in DNA damage repair and tumorigenesis.
Neoplasms
Role of ubiquitin-conjugating enzyme E2T in the carcinogenesis and progression of pancreatic cancer.
Neoplasms
SENP1 is a crucial promotor for hepatocellular carcinoma through deSUMOylation of UBE2T.
Neoplasms
Silencing ubiquitin-conjugating enzyme 2C inhibits proliferation and epithelial-mesenchymal transition in pancreatic ductal adenocarcinoma.
Neoplasms
Spindle assembly checkpoint protein Cdc20 transcriptionally activates expression of ubiquitin carrier protein UbcH10.
Neoplasms
Surmounting cancer drug resistance: New insights from the perspective of N6-methyladenosine RNA modification.
Neoplasms
Synthesis and in vitro anticancer evaluation of some 4,6-diamino-1,3,5-triazine-2-carbohydrazides as Rad6 ubiquitin conjugating enzyme inhibitors.
Neoplasms
Systematic identification of CDC34 that functions to stabilize EGFR and promote lung carcinogenesis.
Neoplasms
Targeting the ubiquitin-conjugating enzyme E2D4 for cancer drug discovery-a structure-based approach.
Neoplasms
Targeting Ubc9 for cancer therapy.
Neoplasms
The Catalytically Inactive Mutation of the Ubiquitin-Conjugating Enzyme CDC34 Affects its Stability and Cell Proliferation.
Neoplasms
The clinical significance of UBE2C gene in progression of renal cell carcinoma.
Neoplasms
The clinicopathological significance of UBE2C in breast cancer: a study based on immunohistochemistry, microarray and RNA-sequencing data.
Neoplasms
The clinicopathological significance of ubiquitin-conjugating enzyme E2C, leucine-rich repeated-containing G protein-coupled receptor, WW domain-containing oxidoreductase, and vasculogenic mimicry in invasive breast carcinoma.
Neoplasms
The diagnostic and prognostic value of UBE2T in intrahepatic cholangiocarcinoma.
Neoplasms
The E2 ubiquitin-conjugating enzyme UbcH5c: an emerging target in cancer and immune disorders.
Neoplasms
The expression of ubiquitin-conjugating enzyme E2C and KAI1 in ovarian carcinoma and their clinical significance.
Neoplasms
The human T-cell leukemia virus type 1 Tax oncoprotein requires the ubiquitin-conjugating enzyme Ubc13 for NF-kappaB activation.
Neoplasms
The interplay of UBE2T and Mule in regulating Wnt/?-catenin activation to promote hepatocellular carcinoma progression.
Neoplasms
The PTTG1-Binding Factor (PBF/PTTG1IP) Regulates p53 Activity in Thyroid Cells.
Neoplasms
The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2.
Neoplasms
The Relationship Between UBE2C and AGGF1 Overexpression and Tumor Angiogenesis in Non-Small Cell Lung Cancer.
Neoplasms
The ubiquitinase ZFP91 promotes tumor cell survival and confers chemoresistance through FOXA1 destabilization.
Neoplasms
Tissue Effects in a Randomized Controlled Trial of Short-term Finasteride in Early Prostate Cancer.
Neoplasms
Transcript Levels of Androgen Receptor Variant 7 and Ubiquitin-Conjugating Enzyme 2C in Hormone Sensitive Prostate Cancer and Castration-Resistant Prostate Cancer.
Neoplasms
Transcriptional patterns, biomarkers and pathways characterizing nasopharyngeal carcinoma of Southern China.
Neoplasms
Transcriptional Silencing of ALDH2 Confers a Dependency on Fanconi Anemia Proteins in Acute Myeloid Leukemia.
Neoplasms
Transcriptomic analysis of aggressive meningiomas identifies PTTG1 and LEPR as prognostic biomarkers independent of WHO grade.
Neoplasms
Tumor suppressor candidate TSSC5 is regulated by UbcH6 and a novel ubiquitin ligase RING105.
Neoplasms
Two-step differential expression analysis reveals a new set of genes involved in thyroid oncocytic tumors.
Neoplasms
Ubc13: the Lys63 ubiquitin chain building machine.
Neoplasms
UbcH10 a Major Actor in Cancerogenesis and a Potential Tool for Diagnosis and Therapy.
Neoplasms
UbcH10 Expression in Benign, Hyperplastic, and Malignant Endometrial Curetted Materials: A Tissue Microarray Study.
Neoplasms
UbcH10 expression in human lymphomas.
Neoplasms
UbcH10 expression may be a useful tool in the prognosis of ovarian carcinomas.
Neoplasms
UbcH10 expression on thyroid fine-needle aspirates.
Neoplasms
UbcH10 is the cancer-related E2 ubiquitin-conjugating enzyme.
Neoplasms
UbcH10 overexpression in human lung carcinomas and its correlation with EGFR and p53 mutational status.
Neoplasms
UbcH10 overexpression increases carcinogenesis and blocks ALLN susceptibility in colorectal cancer.
Neoplasms
UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is closely related to SFT, a stimulator of iron transport, and is up-regulated in hereditary hemochromatosis.
Neoplasms
UbcH7 regulates 53BP1 stability and DSB repair.
Neoplasms
UBE2C cell-free RNA in urine can discriminate between bladder cancer and hematuria.
Neoplasms
UBE2C functions as a potential oncogene by enhancing cell proliferation, migration, invasion, and drug resistance in hepatocellular carcinoma cells.
Neoplasms
UBE2C is a marker of unfavorable prognosis in bladder cancer after radical cystectomy.
Neoplasms
UBE2C is a Potential Biomarker for Tumorigenesis and Prognosis in Tongue Squamous Cell Carcinoma.
Neoplasms
UBE2C Is a Potential Biomarker of Intestinal-Type Gastric Cancer With Chromosomal Instability.
Neoplasms
UBE2C Is a Transcriptional Target of the Cell Cycle Regulator FOXM1.
Neoplasms
UBE2C is involved in the functions of ECRG4 on esophageal squamous cell carcinoma.
Neoplasms
UBE2C is overexpressed in ESCC tissues and its abrogation attenuates the malignant phenotype of ESCC cell lines.
Neoplasms
UBE2C Overexpression Aggravates Patient Outcome by Promoting Estrogen-Dependent/Independent Cell Proliferation in Early Hormone Receptor-Positive and HER2-Negative Breast Cancer.
Neoplasms
UBE2C overexpression in melanoma and its essential role in G2/M transition.
Neoplasms
UBE2C promotes rectal carcinoma via miR-381.
Neoplasms
UBE2C promotes the progression of head and neck squamous cell carcinoma.
Neoplasms
UBE2C, Directly Targeted by miR-548e-5p, Increases the Cellular Growth and Invasive Abilities of Cancer Cells Interacting with the EMT Marker Protein Zinc Finger E-box Binding Homeobox 1/2 in NSCLC.
Neoplasms
UBE2D3 Activates SHP-2 Ubiquitination to Promote Glycolysis and Proliferation of Glioma via Regulating STAT3 Signaling Pathway.
Neoplasms
UBE2D3 is a positive prognostic factor and is negatively correlated with hTERT expression in esophageal cancer.
Neoplasms
UBE2I promotes metastasis and correlates with poor prognosis in hepatocellular carcinoma.
Neoplasms
UBE2L3, a susceptibility gene that plays oncogenic role in hepatitis B-related hepatocellular carcinoma.
Neoplasms
UBE2N plays a pivotal role in maintaining melanoma malignancy.
Neoplasms
UBE2N Promotes Melanoma Growth via MEK/FRA1/SOX10 Signaling.
Neoplasms
UBE2N Regulates Paclitaxel Sensitivity of Ovarian Cancer via Fos/P53 Axis.
Neoplasms
UBE2Q1, as a Down Regulated Gene in Pediatric Acute Lymphoblastic Leukemia.
Neoplasms
UBE2QL1 is Disrupted by a Constitutional Translocation Associated with Renal Tumour Predisposition and is a Novel Candidate Renal Tumour Suppressor Gene.
Neoplasms
UBE2S enhances the ubiquitination of p53 and exerts oncogenic activities in hepatocellular carcinoma.
Neoplasms
UBE2S exerts oncogenic activities in urinary bladder cancer by ubiquitinating TSC1.
Neoplasms
Ube2s expression is elevated in hepatocellular carcinoma and predicts poor prognosis of the patients.
Neoplasms
UBE2S interacting with TRIM28 in the nucleus accelerates cell cycle by ubiquitination of p27 to promote hepatocellular carcinoma development.
Neoplasms
UBE2S mediates tumor progression via SOX6/?-Catenin signaling in endometrial cancer.
Neoplasms
UBE2S promotes the proliferation and survival of human lung adenocarcinoma cells.
Neoplasms
Ube2S regulates Wnt/?-catenin signaling and promotes the progression of non-small cell lung cancer.
Neoplasms
Ube2s stabilizes ?-Catenin through K11-linked polyubiquitination to promote mesendoderm specification and colorectal cancer development.
Neoplasms
UBE2T Contributes to the Prognosis of Esophageal Squamous Cell Carcinoma.
Neoplasms
UBE2T knockdown inhibits gastric cancer progression.
Neoplasms
UBE2T promotes autophagy via the p53/AMPK/mTOR signaling pathway in lung adenocarcinoma.
Neoplasms
UBE2T promotes glioblastoma invasion and migration via stabilizing GRP78 and regulating EMT.
Neoplasms
UBE2T promotes hepatocellular carcinoma cell growth via ubiquitination of p53.
Neoplasms
UBE2T promotes proliferation and regulates PI3K/Akt signaling in renal cell carcinoma.
Neoplasms
UBE2T promotes proliferation, invasion and glycolysis of breast cancer cells by regualting the PI3K/AKT signaling pathway.
Neoplasms
UBE2T promotes radiation resistance in non-small cell lung cancer via inducing epithelial-mesenchymal transition and the ubiquitination-mediated FOXO1 degradation.
Neoplasms
UBE2T silencing inhibited non-small cell lung cancer cell proliferation and invasion by suppressing the wnt/?-catenin signaling pathway.
Neoplasms
UBE2T silencing suppresses proliferation and induces cell cycle arrest and apoptosis in bladder cancer cells.
Neoplasms
UBE2T-regulated H2AX monoubiquitination induces hepatocellular carcinoma radioresistance by facilitating CHK1 activation.
Neoplasms
UBE2T: A new molecular regulator of cancer stemness in hepatocellular carcinoma.
Neoplasms
Ube2v1-mediated ubiquitination and degradation of Sirt1 promotes metastasis of colorectal cancer by epigenetically suppressing autophagy.
Neoplasms
UBE2V2 Positively Correlates With PD-L1 Expression and Confers Poor Patient Survival in Lung Adenocarcinoma.
Neoplasms
Ubiquitin conjugating enzyme E2 L3 promoted tumor growth of NSCLC through accelerating p27kip1 ubiquitination and degradation.
Neoplasms
Ubiquitin-conjugating enzyme complex Uev1A-Ubc13 promotes breast cancer metastasis through nuclear factor-[cyrillic small letter ka]B mediated matrix metalloproteinase-1 gene regulation.
Neoplasms
Ubiquitin-conjugating enzyme E2C regulates apoptosis-dependent tumor progression of non-small cell lung cancer via ERK pathway.
Neoplasms
Ubiquitin-conjugating enzyme E2C: a potential cancer biomarker.
Neoplasms
Ubiquitin-conjugating enzyme E2T (UBE2T) and denticleless protein homolog (DTL) are linked to poor outcome in breast and lung cancers.
Neoplasms
Ubiquitin-Conjugating Enzyme E2T is an Independent Prognostic Factor and Promotes Gastric Cancer Progression.
Neoplasms
Ubiquitin-conjugating enzyme E2T knockdown suppresses hepatocellular tumorigenesis via inducing cell cycle arrest and apoptosis.
Neoplasms
Ubiquitin-conjugating enzyme E2T regulates cell proliferation and migration in cholangiocarcinoma.
Neoplasms
Ubiquitin-conjugating enzyme E2T(UBE2T) promotes colorectal cancer progression by facilitating ubiquitination and degradation of p53.
Neoplasms
Ubiquitin-conjugating enzyme Ubc13 controls breast cancer metastasis through a TAK1-p38 MAP kinase cascade.
Neoplasms
Ubiquitin-conjugating enzyme UbcH10 promotes gastric cancer growth and is a potential biomarker for gastric cancer.
Neoplasms
Ubiquitin-Conjugating Enzyme UBE2C Is Highly Expressed in Breast Microcalcification Lesions.
Neoplasms
Ubiquitin-conjugating enzyme UBE2C: molecular biology, role in tumorigenesis, and potential as a biomarker.
Neoplasms
Ubiquitin-conjugating enzyme UBE2Q2 suppresses cell proliferation and is down-regulated in recurrent head and neck cancer.
Neoplasms
Uev1A facilitates osteosarcoma differentiation by promoting Smurf1-mediated Smad1 ubiquitination and degradation.
Neoplasms
Uev1A promotes breast cancer cell survival and chemoresistance through the AKT-FOXO1-BIM pathway.
Neoplasms
Uev1A-Ubc13 promotes colorectal cancer metastasis through regulating CXCL1 expression via NF-?B activation.
Neoplasms
Up-regulation of interferon-stimulated gene 15 and its conjugation machinery, UbE1L and UbcH8 expression by tumor necrosis factor-? through p38 MAPK and JNK signaling pathways in human lung carcinoma.
Neoplasms
Up-regulation of miR-455-5p by the TGF-?-SMAD signalling axis promotes the proliferation of oral squamous cancer cells by targeting UBE2B.
Neoplasms
Upregulation of UBE2Q1 via gene copy number gain in hepatocellular carcinoma promotes cancer progression through ?-catenin-EGFR-PI3K-Akt-mTOR signaling pathway.
Neoplasms
Upregulation of ubiquitin-conjugating enzyme E2T (UBE2T) predicts poor prognosis and promotes hepatocellular carcinoma progression.
Neoplasms
Upregulation of ubiquitin-conjugating enzyme E2Z is associated with human hepatocellular carcinoma.
Neoplasms
Validation of UBE2C protein as a prognostic marker in node-positive breast cancer.
Neoplasms
WITHDRAWN: Production of a novel UBE2S anti-body and significance of its expression in some tumors.
Neoplasms
Zfx-induced upregulation of UBE2J1 facilitates endometrial cancer progression via PI3K/AKT pathway.
Neuroblastoma
A small-molecule inhibitor of UBE2N induces neuroblastoma cell death via activation of p53 and JNK pathways.
Neurodegenerative Diseases
Ataxin-3 deubiquitination is coupled to Parkin ubiquitination via E2 ubiquitin-conjugating enzyme.
Neurodegenerative Diseases
D: -Serine exposure resulted in gene expression changes implicated in neurodegenerative disorders and neuronal dysfunction in male Fischer 344 rats.
Neurodegenerative Diseases
Expression profiling of the ubiquitin conjugating enzyme UbcM2 in murine brain reveals modest age-dependent decreases in specific neurons.
Neurodegenerative Diseases
Reduction of HIP2 expression causes motor function impairment and increased vulnerability to dopaminergic degeneration in Parkinson's disease models.
Neurodegenerative Diseases
The ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntington's disease protein, huntingtin.
Neurofibrosarcoma
Precision cancer therapy: profiting from tumor specific defects in the DNA damage tolerance system.
Nevus
Differential UBE2C and HOXA1 expression in melanocytic nevi and melanoma.
Nevus, Pigmented
Differential UBE2C and HOXA1 expression in melanocytic nevi and melanoma.
Obesity
Adipose-specific knockout of ubiquitin-conjugating enzyme E2L6 (Ube2l6) reduces diet-induced obesity, insulin resistance, and hepatic steatosis.
Obesity
GWA-based pleiotropic analysis identified potential SNPs and genes related to type 2 diabetes and obesity.
Obesity
Identification of a loss-of-function mutation in Ube2l6 associated with obesity resistance.
Obesity
Ubc13 haploinsufficiency protects against age-related insulin resistance and high-fat diet-induced obesity.
Obesity, Morbid
The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan.
Oligospermia
UBE2B mRNA alterations are associated with severe oligozoospermia in infertile men.
Oligospermia
UBE2W down-regulation promotes cell apoptosis and correlates with hypospermatogenesis.
Osteoarthritis
MicroRNA-101a-3p could be involved in the pathogenesis of temporomandibular joint osteoarthritis by mediating UBE2D1 and FZD4.
Osteoporosis
Gene co-expression network analysis identifies BRCC3 as a key regulator in osteogenic differentiation of osteoblasts through a ?-catenin signaling dependent pathway.
Osteosarcoma
Downregulation of UBE2T can enhance the radiosensitivity of osteosarcoma in vitro and in vivo.
Osteosarcoma
Knockdown of UBE2T Inhibits Osteosarcoma Cell Proliferation, Migration, and Invasion by Suppressing the PI3K/Akt Signaling Pathway.
Osteosarcoma
Lentivirus-mediated RNA interference targeting UbcH10 reduces cell growth and invasion of human osteosarcoma cells via inhibition of Ki-67 and matrix metalloproteinases.
Osteosarcoma
Screening and Interaction Analysis of Key Genes in miR-542-3p Over- Expressed Osteosarcoma Cells by Bioinformatics.
Osteosarcoma
Uev1A facilitates osteosarcoma differentiation by promoting Smurf1-mediated Smad1 ubiquitination and degradation.
Ovarian Neoplasms
Depletion of UBE2C reduces ovarian cancer malignancy and reverses cisplatin resistance via downregulating CDK1.
Ovarian Neoplasms
Estrogen-regulated gene expression predicts response to endocrine therapy in patients with ovarian cancer.
Ovarian Neoplasms
Functional transcriptomic annotation and protein-protein interaction analysis identify EZH2 and UBE2C as key upregulated proteins in ovarian cancer.
Ovarian Neoplasms
Gene expression patterns in the histopathological classification of epithelial ovarian cancer.
Ovarian Neoplasms
Increased Expression of UBE2T Predicting Poor Survival of Epithelial Ovarian Cancer: Based on Comprehensive Analysis of UBE2s, Clinical Samples, and the GEO Database.
Ovarian Neoplasms
Integrated bioinformatic analysis identifies UBE2Q1 as a potential prognostic marker for high grade serous ovarian cancer.
Ovarian Neoplasms
Rad6 upregulation promotes stem cell-like characteristics and platinum resistance in ovarian cancer.
Ovarian Neoplasms
The inhibition of UBC13 expression and blockage of the DNMT1-CHFR-Aurora A pathway contribute to paclitaxel resistance in ovarian cancer.
Ovarian Neoplasms
The lncRNA 'UCA1' modulates the response to chemotherapy of ovarian cancer through direct binding to miR-27a-5p and control of UBE2N levels.
Ovarian Neoplasms
UBE2N Regulates Paclitaxel Sensitivity of Ovarian Cancer via Fos/P53 Axis.
Ovarian Neoplasms
UBE2S promotes the progression and Olaparib resistance of ovarian cancer through Wnt/?-catenin signaling pathway.
Pancreatic Neoplasms
Oncogenic Activities Of UBE2S Mediated By VHL/HIF-1?/STAT3 Signal Via The Ubiquitin-Proteasome System In PDAC.
Pancreatic Neoplasms
Role of ubiquitin-conjugating enzyme E2T in the carcinogenesis and progression of pancreatic cancer.
Pancreatic Neoplasms
Silencing ubiquitin-conjugating enzyme 2C inhibits proliferation and epithelial-mesenchymal transition in pancreatic ductal adenocarcinoma.
Papilloma
Promoter analysis of the human ubiquitin-conjugating enzyme gene family UBE2L1-4, including UBE2L3 which encodes UbcH7.
Parkinson Disease
Reduction of HIP2 expression causes motor function impairment and increased vulnerability to dopaminergic degeneration in Parkinson's disease models.
Parkinson Disease
Thyroarytenoid Muscle Gene Expression in a Rat Model of Early-Onset Parkinson's Disease.
Parkinson Disease
Ubiquitin enzymes, ubiquitin and proteasome activity in blood mononuclear cells of MCI, Alzheimer and Parkinson patients.
Persistent Infection
The use of endogenous and exogenous reference RNAs for qualitative and quantitative detection of PRRSV in porcine semen.
Pituitary Neoplasms
Combination of multiple mRNA markers (PTTG1, Survivin, UbcH10 and TK1) in the diagnosis of Taiwanese patients with breast cancer by membrane array.
Pleural Effusion
A novel Ubc9 -dependent pathway regulates SIRT1- ER-? Axis and BRCA1-associated TNBC lung metastasis.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Expression and localization of the CDC34 ubiquitin-conjugating enzyme in pediatric acute lymphoblastic leukemia.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Expression of UBE2Q2, a putative member of the ubiquitin-conjugating enzyme family in pediatric acute lymphoblastic leukemia.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
Induction of cell proliferation, clonogenicity and cell accumulation in S phase as a consequence of human UBE2Q1 overexpression.
Precursor Cell Lymphoblastic Leukemia-Lymphoma
UBE2Q1, as a Down Regulated Gene in Pediatric Acute Lymphoblastic Leukemia.
Prostatic Hyperplasia
Identification of key genes and pathways in benign prostatic hyperplasia.
Prostatic Neoplasms
A Hierarchical Machine Learning Model to Discover Gleason Grade-Specific Biomarkers in Prostate Cancer.
Prostatic Neoplasms
A novel prostate cancer therapeutic strategy using icaritin-activated arylhydrocarbon-receptor to co-target androgen receptor and its splice variants.
Prostatic Neoplasms
Anticancer effect of icaritin on prostate cancer via regulating miR-381-3p and its target gene UBE2C.
Prostatic Neoplasms
CCI-779 Inhibits Cell-Cycle G2-M Progression and Invasion of Castration-Resistant Prostate Cancer via Attenuation of UBE2C Transcription and mRNA Stability.
Prostatic Neoplasms
Characterization of KRAS Rearrangements in Metastatic Prostate Cancer.
Prostatic Neoplasms
Distinct transcriptional programs mediated by the ligand-dependent full-length androgen receptor and its splice variants in castration-resistant prostate cancer.
Prostatic Neoplasms
Elevated expression of UBE2T exhibits oncogenic properties in human prostate cancer.
Prostatic Neoplasms
Identification of potential diagnostic markers of prostate cancer and prostatic intraepithelial neoplasia using cDNA microarray.
Prostatic Neoplasms
Identification of UBE2C as hub gene in driving prostate cancer by integrated bioinformatics analysis.
Prostatic Neoplasms
Involvement of ubiquitin-conjugating enzyme E2C in proliferation and invasion of prostate carcinoma cells.
Prostatic Neoplasms
Knockdown of UBE2T Inhibits Osteosarcoma Cell Proliferation, Migration, and Invasion by Suppressing the PI3K/Akt Signaling Pathway.
Prostatic Neoplasms
KRAS oncogene rearrangements and gene fusions: unexpected rare encounters in late-stage prostate cancers.
Prostatic Neoplasms
Long non-coding RNA LINC01116 acts as an oncogene in prostate cancer cells through regulation of miR-744-5p/UBE2L3 axis.
Prostatic Neoplasms
MED1 mediates androgen receptor splice variant induced gene expression in the absence of ligand.
Prostatic Neoplasms
miR-499a inhibits the proliferation and apoptosis of prostate cancer via targeting UBE2V2.
Prostatic Neoplasms
Phospho-MED1-enhanced UBE2C locus looping drives castration-resistant prostate cancer growth.
Prostatic Neoplasms
Suppression of prostate tumor cell survival by antisense oligonucleotide-mediated inhibition of AR-V7 mRNA synthesis.
Psoriasis
hsa-miR-4516 Mediated Downregulation of STAT3/CDK6/UBE2N Plays a Role in PUVA Induced Apoptosis in Keratinocytes.
Pulmonary Disease, Chronic Obstructive
Screening and Identification of Differentially Expressed Genes Expressed among Left and Right Colon Adenocarcinoma.
Rectal Neoplasms
High Expression of UBE2B as a Poor Prognosis Factor in Patients With Rectal Cancer Following Chemoradiotherapy.
Reperfusion Injury
UBE2D3 contributes to myocardial ischemia-reperfusion injury by regulating autophagy in dependence of p62/SQSTM1.
Retinal Degeneration
[Generation of mouse UBE2W antibody and analysis of UBE2W expression in mouse tissues]
Retinoblastoma
ARI-1, an RBR family ubiquitin-ligase, functions with UBC-18 to regulate pharyngeal development in C. elegans.
Retinoblastoma
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Retinoblastoma
Implicating SCF complexes in organogenesis in Caenorhabditis elegans.
Retinoschisis
Whole exome sequencing reveals putatively novel associations in retinopathies and drusen formation.
Rhinitis, Allergic
miR-338-3p inhibits autophagy in a rat model of allergic rhinitis after PM2.5 exposure through AKT/mTOR signaling by targeting UBE2Q1.
RNA Virus Infections
Ubiquitin-conjugating enzyme UBE2J1 negatively modulates interferon pathway and promotes RNA virus infection.
Sarcoma
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Sarcoma, Yoshida
Effects of ornithine alpha-ketoglutarate on protein metabolism in Yoshida sarcoma-bearing rats.
Scleroderma, Diffuse
Association of UBE2L3 polymorphisms with diffuse cutaneous systemic sclerosis in a Japanese population.
Scleroderma, Systemic
Association of UBE2L3 polymorphisms with diffuse cutaneous systemic sclerosis in a Japanese population.
Seizures
A novel UBE2A mutation in a Chinese family with X-linked intellectual disability.
Seizures
Novel deletion at Xq24 including the UBE2A gene in a patient with X-linked mental retardation.
Seizures
Refinement of the clinical and mutational spectrum of UBE2A deficiency syndrome.
Seizures
UBE2A deficiency syndrome: Mild to severe intellectual disability accompanied by seizures, absent speech, urogenital, and skin anomalies in male patients.
Seizures
X-linked intellectual disability type Nascimento is a clinically distinct, probably underdiagnosed entity.
Sepsis
Screening of Key Genes of Sepsis and Septic Shock Using Bioinformatics Analysis.
Shock, Septic
Screening of Key Genes of Sepsis and Septic Shock Using Bioinformatics Analysis.
Sickle Cell Trait
Preliminary characterization of a structural defect in homozygous sickled cell alpha spectrin demonstrated by a rabbit autoantibody.
Skin Abnormalities
A novel UBE2A mutation in a Chinese family with X-linked intellectual disability.
Skin Abnormalities
UBE2A deficiency syndrome: Mild to severe intellectual disability accompanied by seizures, absent speech, urogenital, and skin anomalies in male patients.
Spinocerebellar Ataxias
A key lysine residue in the AXH domain of ataxin-1 is essential for its ubiquitylation.
Spinocerebellar Ataxias
The ubiquitin-conjugating enzyme UbcH6 regulates the transcriptional repression activity of the SCA1 gene product ataxin-1.
Spinocerebellar Ataxias
UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1.
Squamous Cell Carcinoma of Head and Neck
Expression of UBE2Q2, a putative member of the ubiquitin-conjugating enzyme family in pediatric acute lymphoblastic leukemia.
Squamous Cell Carcinoma of Head and Neck
Robust rank aggregation and cibersort algorithm applied to the identification of key genes in head and neck squamous cell cancer.
Squamous Cell Carcinoma of Head and Neck
UBE2C promotes the progression of head and neck squamous cell carcinoma.
Squamous Cell Carcinoma of Head and Neck
Ubiquitin-conjugating enzyme UBE2Q2 suppresses cell proliferation and is down-regulated in recurrent head and neck cancer.
Starvation
Heat Stress Affects Pi-related Genes Expression and Inorganic Phosphate Deposition/Accumulation in Barley.
Starvation
Identification of transcription factors that bind to the 5'-UTR of the barley PHO2 gene.
Starvation
Regulation of Phosphate Homeostasis by MicroRNA in Arabidopsis.
Starvation
The ATG12-Conjugating Enzyme ATG10 Is Essential for Autophagic Vesicle Formation in Arabidopsis thaliana.
Starvation
Uev1A promotes breast cancer cell survival and chemoresistance through the AKT-FOXO1-BIM pathway.
Status Epilepticus
Adjunctive use of the ketogenic diet in a young adult with UBE2A deficiency syndrome and super-refractory status epilepticus.
Stomach Neoplasms
A novel UBE2T inhibitor suppresses Wnt/?-catenin signaling hyperactivation and gastric cancer progression by blocking RACK1 ubiquitination.
Stomach Neoplasms
Correction: A novel UBE2T inhibitor suppresses Wnt/?-catenin signaling hyperactivation and gastric cancer progression by blocking RACK1 ubiquitination.
Stomach Neoplasms
Identification of Potential Biomarkers Involved in Gastric Cancer Through Integrated Analysis of Non-Coding RNA Associated Competing Endogenous RNAs Network.
Stomach Neoplasms
Inhibition of microRNA-17/20a suppresses cell proliferation in gastric cancer by modulating UBE2C expression.
Stomach Neoplasms
Overexpression of UBE2C correlates with poor prognosis in gastric cancer patients.
Stomach Neoplasms
UBE2C induces EMT through Wnt/??catenin and PI3K/Akt signaling pathways by regulating phosphorylation levels of Aurora-A.
Stomach Neoplasms
UBE2C Is a Potential Biomarker of Intestinal-Type Gastric Cancer With Chromosomal Instability.
Stomach Neoplasms
UBE2C mRNA expression controlled by miR-300 and HuR determines its oncogenic role in gastric cancer.
Stomach Neoplasms
UBE2T knockdown inhibits gastric cancer progression.
Stomach Neoplasms
Ubiquitin-Conjugating Enzyme E2T is an Independent Prognostic Factor and Promotes Gastric Cancer Progression.
Stomach Neoplasms
Ubiquitin-conjugating enzyme UbcH10 promotes gastric cancer growth and is a potential biomarker for gastric cancer.
Stroke
Identification of Co-expressed Genes Between Atrial Fibrillation and Stroke.
Thyroid Carcinoma, Anaplastic
Array-CGH identifies cyclin D1 and UBCH10 amplicons in anaplastic thyroid carcinoma.
Thyroid Carcinoma, Anaplastic
The UbcH10 gene is a novel therapeutic target in anaplastic thyroid carcinoma.
Thyroid Carcinoma, Anaplastic
UbcH10 overexpression may represent a marker of anaplastic thyroid carcinomas.
Thyroid Diseases
The haplotype of UBE2L3 gene is associated with Hashimoto's thyroiditis in a Chinese Han population.
Thyroid Neoplasms
Integrated Bioinformatics Analysis of Hub Genes and Pathways in Anaplastic Thyroid Carcinomas.
Thyroid Neoplasms
UbcH10 expression may be a useful tool in the prognosis of ovarian carcinomas.
Thyroid Neoplasms
UbcH10 expression on thyroid fine-needle aspirates.
Thyroid Neoplasms
UbcH10 is overexpressed in malignant breast carcinomas.
Thyroid Neoplasms
UbcH10 overexpression may represent a marker of anaplastic thyroid carcinomas.
Thyroiditis
The haplotype of UBE2L3 gene is associated with Hashimoto's thyroiditis in a Chinese Han population.
Triple Negative Breast Neoplasms
Mapping of Genomic Vulnerabilities in the Post-Translational Ubiquitination, SUMOylation and Neddylation Machinery in Breast Cancer.
Triple Negative Breast Neoplasms
RAD6B is a major mediator of triple negative breast cancer cisplatin resistance: Regulation of translesion synthesis/Fanconi anemia crosstalk and BRCA1 independence.
Triple Negative Breast Neoplasms
Targeting ubiquitin conjugating enzyme UbcH5b by a triterpenoid PC3-15 from Schisandra plants sensitizes triple-negative breast cancer cells to lapatinib.
Tuberous Sclerosis
The GID ubiquitin ligase complex is a regulator of AMPK activity and organismal lifespan.
Urinary Bladder Neoplasms
A potential panel of five mRNAs in urinary extracellular vesicles for the detection of bladder cancer.
Urinary Bladder Neoplasms
Knockdown of UBE2T Inhibits Osteosarcoma Cell Proliferation, Migration, and Invasion by Suppressing the PI3K/Akt Signaling Pathway.
Urinary Bladder Neoplasms
Multicenter validation of cyclin D1, MCM7, TRIM29, and UBE2C as prognostic protein markers in non-muscle-invasive bladder cancer.
Urinary Bladder Neoplasms
UBE2C cell-free RNA in urine can discriminate between bladder cancer and hematuria.
Urinary Bladder Neoplasms
UBE2C is a marker of unfavorable prognosis in bladder cancer after radical cystectomy.
Urinary Bladder Neoplasms
UBE2S exerts oncogenic activities in urinary bladder cancer by ubiquitinating TSC1.
Urinary Bladder Neoplasms
UBE2T silencing suppresses proliferation and induces cell cycle arrest and apoptosis in bladder cancer cells.
Urinary Bladder Neoplasms
[Analysis and verification of the interaction network of differentially expressed genes in invasive bladder cancer.]
Uterine Cervical Neoplasms
Dietary flavonoids, luteolin and quercetin, inhibit invasion of cervical cancer by reduction of UBE2S through epithelial-mesenchymal transition signaling.
Uterine Cervical Neoplasms
Epigallocatechin gallate inhibits HeLa cells by modulation of epigenetics and signaling pathways.
Uterine Cervical Neoplasms
Expression and clinical significance of UBE2V1 in cervical cancer.
Uterine Cervical Neoplasms
Gene expression profiling of mouse p53-deficient epidermal carcinoma defines molecular determinants of human cancer malignancy.
Uterine Cervical Neoplasms
HP1? Sensitizes Cervical Cancer Cells to Cisplatin through the Suppression of UBE2L3.
Uterine Cervical Neoplasms
HPV-mediated nuclear export of HP1? drives cervical tumorigenesis by downregulation of p53.
Uterine Cervical Neoplasms
Identification of small molecule inhibitors against UBE2C by using docking studies.
Uterine Cervical Neoplasms
UBE2C Drives Human Cervical Cancer Progression and Is Positively Modulated by mTOR.
Uterine Cervical Neoplasms
UHRF1 epigenetically down-regulates UbcH8 to inhibit apoptosis in cervical cancer cells.
Uterine Cervical Neoplasms
Vorinostat targets UBE2C to reverse epithelial-mesenchymal transition and control cervical cancer growth through the ubiquitination pathway.
Virus Diseases
Herpes simplex virus type 1 regulatory protein ICP0 does not protect cyclins D1 and D3 from degradation during infection.
Virus Diseases
Ubc13: the Lys63 ubiquitin chain building machine.
Virus Diseases
Ube2D3 and Ube2N are essential for RIG-I-mediated MAVS aggregation in antiviral innate immunity.
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evolution
enzyme UBE2L3 belongs to the E2 family. Humans have around 35 ubiquitin E2 family members, all sharing a core ubiquitin conjugation (UBC) domain that spans roughly 150 residues. E2s are classified by their UBC domain extensions, class I E2s have only the core domain, classes II and III have N- or C-terminal extensions respectively, and class IV are extended at both ends
evolution
enzyme UBE2T belongs to the E2 family. Humans have around 35 ubiquitin E2 family members, all sharing a core ubiquitin conjugation (UBC) domain that spans roughly 150 residues. E2s are classified by their UBC domain extensions, class I E2s have only the core domain, classes II and III have N- or C-terminal extensions respectively, and class IV are extended at both ends
evolution
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Common functional and structural features that define unifying themes among E2s, overview. Highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule. This leads to a division of labor among E2s in which one E2 initiates or primes chain synthesis and a second E2 builds and extends the polyUb chain
evolution
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Common functional and structural features that define unifying themes among E2s, overview. Highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule. This leads to a division of labor among E2s in which one E2 initiates or primes chain synthesis and a second E2 builds and extends the polyUb chain
evolution
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Common functional and structural features that define unifying themes among E2s, overview. Highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule. This leads to a division of labor among E2s in which one E2 initiates or primes chain synthesis and a second E2 builds and extends the polyUb chain. Either Ube2C or a Ube2D family member transfers the first Ub onto human APC/C substrates and Ube2S then builds the K11-linked polyUb chains that are a hallmark of APC/C-mediated proteasomal degradation
evolution
UBE2Z is a 354-residue-long atypical ubiquitin conjugating enzyme comprising about 100-residue long N- and C-terminal extensions on top of the conserved core UBC domain, classifying it as a class IV E2 enzyme
evolution
ubiquitin-conjugating enzyme E2T (UBE2T) is a member of the E2 family that mediates the ubiquitin-proteasome system and regulates gene expression
malfunction
-
knockdown of E2 enzymes delays ubiquitylation and degradation of mitochondrial substrates like p62 and the adaptor protein p62/SQSTM1. Depletion of UBE2R1 enhances the translocation of Parkin to, and clustering of, mitochondria
malfunction
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 backside binding by accessory elements of the RING E3 Rad18 inhibits the intrinsic chain-forming activity of Ube2B, thus promoting monoubiquitylation of PCNA and histone 2B
malfunction
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 Disruption of specific interactions involving K48 on Ub and backside residues of the E2 by mutation of either Ub or E2 backside residues results in the rapid generation of K63-linked Ub chains by Ube2E3
malfunction
in UBE2G2 knockout cells, sterol-stimulated degradation of squalene monooxygenase (SQLE) is partly attenuated, but that of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) is abolished
malfunction
in UBE2J1 knockout cells, sterol-stimulated degradation of squalene monooxygenase (SQLE) and of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) are unaffected
malfunction
in UBE2J2 knockout cells, sterol-stimulated degradation of squalene monooxygenase (SQLE), but not that of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), is largely attenuated. RNAi-mediated silencing of UBE2J2 expression in HepG2 cells also attenuates sterol-stimulated degradation of SQLE in a proteasome-dependent manner
malfunction
knocking down ubiquitin-conjugating enzyme E2 D1 (Ube2D1) impairs March-I ubiquitination, increased March-I expression, and enhanced March-I-dependent down-regulation of MHC-II proteins
malfunction
mutation in UBE2T are involved in the Fanconi anaemia pathway. UBE2T is the E2 enzyme in the Fanconi anaemia pathway, the Fanconi anaemia ubiquitin signalling module. Analysis of E2 function in the Fanconi anaemia syndrome (FA) disease, patient phenotypes, detailed overview
malfunction
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 mutations designed to disrupt canonical E2/RING interactions that would involve the APC/C RING domain subunit (Apc11) do not affect activity
malfunction
overexpression/knockdown of UBE2B enhances/reduces BCNU-mediated O6-methylguanine-DNA methyltransferase (MGMT) ubiquitination. UBE2B knockdown significantly increases 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU)cytotoxicity in NPC cells. Therefore, loss of UBE2B seems to disrupt ubiquitin-mediated degradation of alkylated MGMT. UBE2B knockdown reduces MGMT activity, suggesting that loss of UBE2B leads to the accumulation of deactivated MGMT and suppresses MGMT protein turnover in BCNU-treated cells
malfunction
UBE2J2 depletion increases TRC8 expression levels in the presence of US2, and in this way, enhances US2-mediated HLA-I downregulation
malfunction
UBE2T downregulation induces gastric cancer cell cycle arrest
malfunction
without this enzyme, the clearance of ruptured lysosomes is compromised not only upon lysosomal damage but also under normal conditions, revealing its adaptive and constitutive functions. Depletion of the E2 enzyme UBE2QL1 successfully inhibits damage-induced lysosomal ubiquitination. UBE2QL1 depletion affection is greater for K48-linked ubiquitination (K48-Ub) than K63-linked ubiquitination (K63-Ub)
metabolism
March-I is ubiquitinated and degraded in the endocytic pathway involving enzyme UBE2D2
metabolism
misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). During infection with human cytomegalovirus (HCMV), the viral US2 protein targets HLA class I molecules (HLA-I) for degradation via ERAD to avoid elimination by the immune system. US2-mediated degradation of HLA-I serves as a paradigm of ERAD and has facilitated the identification of TRC8 (also known as RNF139) as an E3 ubiquitin ligase. Identification of multiple E2 enzymes that are involved in the US2-mediated HLA-I downregulation process, of which UBE2G2 is crucial for the degradation of various immunoreceptors. UBE2G2 affects US2-mediated degradation of HLA-I
metabolism
misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). During infection with human cytomegalovirus (HCMV), the viral US2 protein targets HLA class I molecules (HLA-I) for degradation via ERAD to avoid elimination by the immune system. US2-mediated degradation of HLA-I serves as a paradigm of ERAD and has facilitated the identification of TRC8 (also known as RNF139) as an E3 ubiquitin ligase. Identification of multiple E2 enzymes that are involved in the US2-mediated HLA-I downregulation process. UBE2D3 affects US2-mediated degradation of HLA-I
metabolism
misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). During infection with human cytomegalovirus (HCMV), the viral US2 protein targets HLA class I molecules (HLA-I) for degradation via ERAD to avoid elimination by the immune system. US2-mediated degradation of HLA-I serves as a paradigm of ERAD and has facilitated the identification of TRC8 (also known as RNF139) as an E3 ubiquitin ligase. Identification of multiple E2 enzymes that are involved in the US2-mediated HLA-I downregulation process. UBE2J2 counteracts US2-mediated HLA-I downregulation, UBE2J2 counteracts US2-induced ERAD by downregulating TRC8 expression
metabolism
the enzyme is involved in lysophagy induced by lysosomal membrane rupture, pathway overview
metabolism
the enzyme is involved in the ubiquitin pathway. The E1 mediates ubiquitin activation in an energy-consuming step. The ubiquitin thioester is then transferred onto a catalytic cysteine of the E2 enzyme. RING-type E3s form a non-covalent complex with the E2-Ub thioester intermediate or, alternatively, ubiquitin is transferred to catalytic sites of HECT and RBR-type E3 ligases. The E3 enzymes ultimately catalyze ubiquitination of a substrate lysine. Ubiquitin signals can also be extended to form polyubiquitin chains
metabolism
the ubiquitin-like modifier-activating enzyme 1 (Uba1, EC 6.2.1.45) is a multidomain enzyme that serves as the gatekeeper of the ubiquitin (Ub) conjugation cascade by activating Ub in a two-step process involving adenylation and thioester bond formation followed by transfer of Ub to E2s in a process termed E1-E2 thioester transfer or transthiolation. Cdc34 is one of tens of E2s that must function with Uba1 despite significant differences at their predicted UFD-interacting surfaces. Molecular recognition of Cdc34 by Uba1, overview
metabolism
Ube2T is the E2 ubiquitin-conjugating enzyme of the Fanconi anemia DNA repair pathway
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. E2 enzyme Ube2W (EC 2.3.2.25) can transfer Ub to the alpha-amino group of small lysine-less peptides but not to free lysine, whereas Ube2D3, for example, can transfer Ub to lysine but not to the alpha-amino group
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Either Ube2C or a Ube2D family member transfers the first Ub onto human APC/C substrates and Ube2S then builds the K11-linked polyUb chains that are a hallmark of APC/C-mediated proteasomal degradation. The APC/C appears to repurpose its RING subunit to bind and track the growing Ub chain during Ube2S-mediated catalysis, presumably inhibiting incorrect chain building by the promiscuous Ube2D E2s. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Enzyme UBE2J1 is involved in the ERAD pathway. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. UBE2G2 is an E2 involved in the ERAD pathway. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Ube2R1 and its yeast counterpart Cdc34 are dedicated E2s for the large multi-subunit SCF (Skp/Cullin/F-Box) E3s that target proteins to the proteasome for degradation. Both of these enzymes also have an acidic C-terminal extension that interacts with a basic canyon on the cullin subunit of an SCF complex, helping to position the E2 near the RING subunit while allowing for rapid association and turnover in chain building. A disulfide bond formed between the Ub E1 Uba1 and the E2 Ube2R1 upon oxidative stress is associated with increased Ube2R1 substrate stability and delayed cell cycle progression. E2 regulation mechanisms, overview
metabolism
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. Ube2W (EC 2.3.2.25) appears to monoubiquitylate the RING E3 ligases TRIM5alpha and TRIM21, a prerequisite for their K63 polyubiquitylation by Ube2N/Ube2V2. E2 regulation mechanisms, overview
physiological function
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Some E2s possess N and/or C-terminal extensions that mediate E2-specific processes: class I, enzyme consists of the catalytic domain, without extensions, Class II, enzyme has a N-terminal extension, class III, enzyme has a C-terminal extension, class IV, enzyme has both, N- and C-terminal extensions, showing differences in function, subcellular localization, stabilization of the interaction with E1 enzymes, or modulation of the activity of the interacting E3
physiological function
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the family of ubiquitin-conjugating enzymes is characterized by the presence of a highly conserved ubiquitin-conjugating (UBC) domain
physiological function
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ubiquitin-conjugating enzyme UbcM2 is a regulator of transcription factor nuclear factor E2-related factor Nrf2. Nrf2 induces the expression of antioxidant gene products that neutralize reactive oxygen species and restore redox homeostasis Recombinant Nrf2 and UbcM2 form a complex upon alkylation of a non-catalytic cysteine in UbcM2, Cys-136. UbcM2 and Nrf2 form a nuclear complex utilizing the DNA binding Neh1 domain of Nrf2. UbcM2 can enhance the transcriptional activity of endogenous Nrf2 and Cys-136 and the active-site cysteine, Cys-145, jointly contribute to this regulation
physiological function
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E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2, UBE2D3, UBE2D4, UBE2E1, UBE2E2, UBE2E3 and UBE2N interact non-hierarchically and exclusively with deubiquitylating enzyme OTUB1, i.e. Otubain-1
physiological function
isoform TRIP12 catalyzes in vitro ubiquitination of ubiquitin fusion degradation substrates in conjunction with E1, E2, and E4 enzymes. Knockdown of TRIP12 stabilizes artificial ubiquitin fusion degradation substrates and physiological substrate, mutant ubiquitin UBB+1. TRIP12 knockdown reduces UBB+1-induced cell death in human neuroblastoma cells. Complementation of TRIP12 knockdown cells with the TRIP12 HECT domain mostly restores efficient degradation of ubiquitin fusion degradation substrates. The TRIP12 HECT domain directs ubiquitination of ubiquitin fusion degradation substrates in vitro and can be specifically cross-linked to the ubiquitin moiety of the substrates in vivo. A mutant ubiquitin that cannot be conjugated to other proteins is a substrate of the TRIP12 HECT domain both in vivo and in vitro
physiological function
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reduction of Ubc9 protein levels by small interfering RNA attenuates hormonal activation of a mineralocorticoid receptor reporter construct as well as an endogenous target gene by mineralocorticoid receptor. A sumoylation-inactive mutant Ubc9 (C93S) similarly interacts with mineralocorticoid receptor and potentiates aldosterone-dependent mineralocorticoid receptor transactivation. An mineralocorticoid receptor mutant in which four lysine residues within sumoylation motifs are mutated into arginine (K89R/K399R/K494R/K953R) fails to be sumoylated, but Ubc9 similarly enhances transactivation by the mutant mineralocorticoid receptor. Coexpression of Ubc9 and steroid receptor coactivator SRC-1 synergistically enhances mineralocorticoid receptor-mediated transactivation in transient transfection assays
physiological function
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the cognate E2 coenzymes of E3 enzyme Parkin regulate the activation, translocation and enzymatic functions of Parkin during mitochondrial quality control. UBE2D family members and UBE2L3 redundantly charge the RING-HECT hybrid ligase Parkin with ubiquitin, resulting in its initial activation and translocation to mitochondria. UBE2N primarily mediates the proper clustering of mitochondria, a prerequisite for degradation. Depletion of UBE2R1 results in enhanced Parkin translocation and clustering upon mitochondrial uncoupling
physiological function
USE1 modifies itself with HLA-F adjacent transcript 10, i.e. FAT10, in cis, mainly at Lys323. Mutation of Lys323 to an arginine does not abolish auto-FAT10ylation of USE1, but every other lysine can instead be modified with FAT10. FAT10ylation of USE1 accelerates its proteasomal degradation. The USE1FAT10 conjugate continues to be an active E2 enzyme
physiological function
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E2 enzymes regulate activation and mitochondrial translocation of Parkin. UBE2L3 is able to charge Parkin with ubiquitin and are essential for its initial activation
physiological function
study on energy landscapes during the initial phases of the ubiquitination reaction, on Ube2g2 in the free form and in complex with E3 enzyme gp78 domains RING and G2BR. Ube2g2 goes through a sequence of allosteric binding to gp78, transfer of Ub, and release from gp78 during the ubiquitination reaction. Ube2g2 dynamics is significantly modulated along this pathway, and the population distribution in the dynamic energy landscape drives the sequence of allosteric binding, catalysis and release
physiological function
although damaged lysosomes with ruptured membranes can be repaired, these dangerous organelles are also selectively eliminated by autophagic degradation termed lysophagy. This process is initiated by ubiquitination of lysosomal proteins. The E2 enzyme UBE2QL1 catalyzes ubiquitination of damaged lysosomes. UBE2QL1-mediated ubiquitination of lysosomal proteins is crucial for lysophagy following various types of lysosomal damage. L-leucyl-L-leucine methyl ester (LLOMe) treatment induces both ubiquitin K48- and K63-linked ubiquitination through damage of lysosomal membranes. UBE2QL1 has a constitutive housekeeping role in lysosomal homeostasis. UBE2QL1-dependent ubiquitination recruits VCP and SQSTM1 and induces autophagosome formation. Identification of lysosomal membrane proteins, including LIMP2, NPC1, LAMP1, and LAMP2, as potential targets of ubiquitination. UBE2QL1 itself might recognize membrane pores of damaged lysosomes or it might be recruited by an E3 enzyme
physiological function
enzyme UBE2T promotes cell proliferation and inhibits cell cycle arrest. In addition, UBE2T modulates cell mobility by inducing epithelial-mesenchymal transition. UBE2T plays an important role in the tumorigenesis of gastric cancer, it promotes tumor cell growth and metastasis. UBE2T has been reported to be recruited independently to regulate FANCD2 monoubiquitination and participates in the Fanconi anemia pathway together with FANCD2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D1 is a promiscuous lysine- and cysteine-reactive E2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D3 is a promiscuous lysine- and cysteine-reactive E2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D4 is a promiscuous lysine- and cysteine-reactive E2
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2E1 is a monoubiquitylating E2 of its N-terminal extension
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2E1 is a monoubiquitylating E2 of its N-terminal extension. The E2 Ube2E3 regulates the activity of Nrf2, a transcription factor that induces expression of anti-oxidant genes to neutralize reactive oxygen species and restore redox homeostasis. Alkylation of non-catalytic C136 of Ube2E3 (to mimic its oxidation) results in constitutive binding of the E2 to Nrf2, increasing its half-life and thus its transcriptional activity. The regulation also depends on the catalytic activity of Ube2E3. Intriguingly, Ube2E3's C136 replaces the proline in a conserved HPN triad, which has been reported to be required for E2 activity
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2E2 is a monoubiquitylating E2 by of its N-terminal extension
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme UBE2N is collaborating with proteins of the Ube2V family to build K63 Ub-chain. Ube2W (EC 2.3.2.25) appears to monoubiquitylate the RING E3 ligases TRIM5alpha and TRIM21, a prerequisite for their K63 polyubiquitylation by Ube2N/Ube2V2, Ube2N/Ube2V2 form a E2/E3 pair
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzymes UBE2V1, UBE2V2, and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzymes UBE2V1, UBE2V2, and homologues are catalytically inactive E2-like proteins interacting with Ube2N for K63 chain formation. PCNA is monoubiquitylated by the E2/E3 pair Ube2N/Ube2V2 and the RING E3 Rad5, together builds a K63-linked chain at the same site, to create a signal that promotes template-switching and engagement of the homologous recombination machinery
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2A functions in DNA damage repair. PCNA is monoubiquitylated by the Ube2A/B (Rad6) E2s and the RING E3 Rad18 during postreplicative DNA damage repair
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2C functions in chain-initiation of APC/C
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2G2 acts in K48 chain-building in dependence of an E3. It is an E2 involved in the ERAD pathway
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2J2 attaches Ub to the major histocompatibility complex via hydroxyl groups (serine/threonine) in collaboration with a viral RING E3 ligase. Ube2J2 ubiquitylation products are sensitive to treatment with strong base, which hydrolyzes oxyesters but not amide bonds
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2L3 plays in cell cycle regulation. Ube2L3 (UbcH7), the E2 used in many structural studies with RING-type E3s, is not reactive towards lysine and only exhibits reactivity towards cysteine. The implication is that Ube2L3, although it binds to many RING domains, is only functional as an E2 with HECT-type E3s. RBRs, such as Parkin and HHARI, have RING domains, but also contain a conserved cysteine residue that forms an obligatory E3-Ub intermediate. Thus, RBRs are functional hybrids that exploit elements found in both RING and HECT E3s
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2R1 is the cognate E2 of SCF E3 ligases
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2S is the dedicated E2 for the multi-subunit APC/C E3 that regulates cell cycle progression. On its own, Ube2S-Ub populates closed states to a considerable extent and can catalyze formation of free polyUb chains in the absence of an E3. Two non-RING subunits, Apc2 and Apc4, contribute to Ube2S activation in a mechanism that may involve the C-terminal helix of the Ube2S UBC domain
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2T, the E2 involved in the Fanconi Anemia DNA repair pathway and specific for E3 ligase FANCL, transfers Ub to a lysine near its active site and two lysines located in its C-terminal extension. Ubiquitylated Ube2T has been observed in vitro and in cells, and its production is enhanced by the E3, FANCL. Unlike Ubc7 autoubiquitylation, (multi)-monoubiquitylated Ube2T does not signal for its degradation, but has decreased Ub transfer activity in vitro
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2W (EC 2.3.2.25) can serve as the template for chain building by Ube2N and Ube2K
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Enzyme Ube2D2 is a promiscuous lysine- and cysteine-reactive E2. OTUB1 DUB activity is enhanced by interaction with free E2s. Binding of Ube2D2 stabilizes the disordered OTUB1 N-terminus in an alpha-helical conformation, which completes the binding site for K48-linked diUb. The E2-mediated conformational change decreases the Km of OTUB1 for diUb by over 35fold, thereby enhancing the rate of OTUB1-dependent polyUb degradation. The E2 acting as an effector protein to stimulate enzyme (DUB) activity
physiological function
A1L167, O00762, O14933, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q5JXB2, Q5VVX9, Q712K3, Q7Z7E8, Q8N2K1, Q8WVN8, Q969T4, Q96LR5, Q9H832, Q9NPD8, Q9Y385 humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g., SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. UBE2B functions in DNA damage repair. The chain-building activity of other E2s is enhanced by Ub backside binding as well. The interaction is critical for the E3-independent ability of Ube2B to build K11-linked polyUb chains. PCNA is monoubiquitylated by the Ube2A/B (Rad6) E2s and the RING E3 Rad18 during postreplicative DNA damage repair
physiological function
MARCH6, an E3 ubiquitin ligase, specifically promotes cholesterol-stimulated ubiquitylation and subsequent proteasomal degradation of squalene monooxygenase (SQLE), but not of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR). The sterol-dependent degradation machinery makes use of distinct E2 ubiquitin conjugating enzymes
physiological function
the E2 ubiquitin-conjugating enzyme UBE2G2 is broadly involved in regulating the downregulation of immunoreceptors targeted by HCMV US2. The E2 ubiquitin conjugating enzyme UBE2G2 to be essential for US2-mediated HLA-I downregulation
physiological function
the E2 ubiquitin-conjugating enzyme UBE2J2 is broadly involved in regulating the downregulation of immunoreceptors targeted by HCMV US2
physiological function
UBE2J2 is a new regulator of cellular cholesterol homeostasis in mammalian cells. MARCH6, an E3 ubiquitin ligase, specifically promotes cholesterol-stimulated ubiquitylation and subsequent proteasomal degradation of squalene monooxygenase (SQLE), but not of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR). The sterol-dependent degradation machinery makes use of distinct E2 ubiquitin conjugating enzymes. The ability of UBE2J2 to support SQLE degradation critically depends on its enzymatic activity. UBE2J2 as an important partner of MARCH6 in cholesterol-stimulated degradation of SQLE, thereby contributing to the complex regulation of cellular cholesterol homeostasis
physiological function
Ube2T is the E2 ubiquitin-conjugating enzyme of the Fanconi anemia DNA repair pathway. Together with FANCL (the E3 ligase), Ube2T catalyzes the monoubiquitination of the heterodimeric FANCI/FANCD2 complex, which is the key signaling event to activate the FA pathway for DNA repair
physiological function
UBE2Z is a selective E2 enzyme, functioning in ubiquitination only with E1-like ubiquitin-activating enzyme UBA6
physiological function
ubiquitin (Ub) signaling requires the sequential interactions and activities of three enzymes, E1, E2, and E3. Cdc34 is an E2 that plays a key role in regulating cell cycle progression and requires unique structural elements to function, molecular mechanisms by which Cdc34 function in cells, overview
physiological function
ubiquitin signalling is a fundamental eukaryotic regulatory system, controlling diverse cellular functions. A cascade of E1, E2, and E3 enzymes is required for assembly of distinct signals, whereas an array of deubiquitinases and ubiquitin-binding modules edit, remove, and translate the signals. In the centre of this cascade sits the E2-conjugating enzyme, relaying activated ubiquitin from the E1 activating enzyme to the substrate, usually via an E3 ubiquitin ligase. Function of UBE2L3 with HOIL-1L-interacting protein (HOIP) in cancer. HOIL-1L is the haem-oxidized IRP2 ubiquitin ligase-1. Functional association of UBE2L3 with Parkinson's disease (PD). Parkin E3 ligase activity is auto-inhibited by the N-terminal UBL domain, which obscures the catalytic interaction between Parkin and the ubiquitin-loaded E2. Parkin apparently employs different E2 enzymes to generate distinct ubiquitin chain signals that mediate efficient mitophagy. The apparent redundant functions of UBE2L3 with other E2s may explain the current lack of any genetic association of UBE2L3 gene alterations with PD
physiological function
ubiquitin signalling is a fundamental eukaryotic regulatory system, controlling diverse cellular functions. A cascade of E1, E2, and E3 enzymes is required for assembly of distinct signals, whereas an array of deubiquitinases and ubiquitin-binding modules edit, remove, and translate the signals. In the centre of this cascade sits the E2-conjugating enzyme, relaying activated ubiquitin from the E1 activating enzyme to the substrate, usually via an E3 ubiquitin ligase. UBE2T has potential oncogenic and tumour suppressor function in carcinogenesis
physiological function
ubiquitin-conjugating enzyme E2 B (UBE2B) is a regulator of O6-methylguanine-DNA methyltransferase (MGMT) ubiquitination mediated by 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU)in nasopharyngeal carcinoma (NPC) cells. BCNU enhances the interaction between MGMT, RAD18, and ubiquitinated UBE2B. The E3 ubiquitin ligase RAD18, a partner of UBE2B, is also involved in BCNU-mediated MGMT ubiquitination. UBE2B modulates sensitivity to BCNU in NPC cells by regulating MGMT ubiquitination. UBE2B and RAD18 facilitate and accelerate MGMT ubiquitination in vitro, and BCNU and O6-benzylguanine promote UBE2B/RAD18-induced MGMT ubiquitination
physiological function
ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I, which contributes to March-I turnover. March-I is a membrane-bound E3 ubiquitin ligase belonging to the membrane-associated RING-CH (March) family. March-I ubiquitinates and downregulates the expression of major histocompatibility complex (MHC) class II and cluster of differentiation 86 (CD86) in antigen-presenting cells. Molecular mechanism regulating March-I ubiquitination, overview. March-I is not ubiquinated on a lysine residue. March-I E3 ligase activity is not required for its ubiquitination and does not regulate March-I protein expression. March-I does not undergo autoubiquitination. Ube2D1 together with another E3 ubiquitin ligase regulates March-I expression. March-I is oligo-ubiquitinated and undergoes proteolytic degradation
physiological function
ubiquitination process consists of three main steps: the first step is activation: ubiquitin is activated by an E1 ubiquitin-activating enzyme, which is dependent on ATP. The second step is conjugation: E2 ubiquitin-conjugating enzymes catalyze the transfer of ubiquitin from E1 to the active site cysteine of the E2 via a trans(thio)esterification reaction. The third step is ligation: E3 ubiquitin ligases catalyze the final step of the ubiquitination cascade. Most commonly, they create an isopeptide bond between a lysine of the target protein and the C-terminal glycine of ubiquitin. E2 ubiquitin-conjugating enzymes RAD6A and RAD6B are interacting with E3 ubiquitin ligase RNF168 and RAD18 in response to DNA damage, recombinant coexpression and interaction analysis, overview. Following the localization of E3 enzymes to DNA damage sites, the E2 enzymes are recruited to these sites, where they catalyze protein ubiquitination. DNA damage-induced foci of E2 ubiquitin-conjugating enzyme require E3 ubiquitin ligase for its formation in mammalian cells. RNF168 or RAD18 recruit RAD6A and RAD6B to DNA damage sites, the interaction is specific, no other E3 ligases intecat with Rad6A/Rad6B
physiological function
ubiquitination process consists of three main steps: the first step is activation: ubiquitin is activated by an E1 ubiquitin-activating enzyme, which is dependent on ATP. The second step is conjugation: E2 ubiquitin-conjugating enzymes catalyze the transfer of ubiquitin from E1 to the active site cysteine of the E2 via a trans(thio)esterification reaction. The third step is ligation: E3 ubiquitin ligases catalyze the final step of the ubiquitination cascade. Most commonly, they create an isopeptide bond between a lysine of the target protein and the C-terminal glycine of ubiquitin. E2 ubiquitin-conjugating enzymes RAD6A and RAD6B are interacting with E3 ubiquitin ligase RNF168 and RAD18 in response to DNA damage, recombinant coexpression and interaction analysis, overview. Following the localization of E3 enzymes to DNA damage sites, the E2 enzymes are recruited to these sites, where they catalyze protein ubiquitination. DNA damage-induced foci of E2 ubiquitin-conjugating enzyme require E3 ubiquitin ligase for its formation in mammalian cells. RNF168 or RAD18 recruit RAD6A and RAD6B to DNA damage sites, the interaction is specific, no other E3 ligases interact with Rad6A/Rad6B
additional information
active site gate dynamics modulate the catalytic activity of the ubiquitination enzyme E2-25K. NMR study of purified recombinant detagged wild-type and mutant enzymes, analysis of enzyme structure and E2-25K-ubiquitin interaction, overview. Molecular dynamics simulations for E2-25K and the Q126L/D127G active site gate mutants
additional information
analyis of the molecular basis by which Cdc34 engages its E1, and the structural mechanisms, by which its unique C-terminal extension functions in Cdc34 activity. Conformational changes in Uba1 and Cdc34 and a unique binding mode are required for transthiolation. The Cdc34-Ub structure reveals contacts between the Cdc34 C-terminal extension and Ub that stabilize Cdc34-Ub in a closed conformation and are critical for Ub discharge
additional information
construction of initial Ube2R1-Rbx1 models, Rbx1 (PDB ID 2LGV) and Ube2R1 (PDB ID 4MDK) are aligned to the respective components from the Ube2G2/Rnf45 cocrystal structure (PDB ID 2LXP) and energy is minimized with Rosetta algorithms relax and fixbb. Next, an initial conformation for the acidic loop (residues 97 to 115) is built onto the top-scoring Ube2R1-Rbx1 model using the CCD algorithm with fragments derived from the Ube2R1 amino acid sequence. This model of the Ube2R1-Rbx1 complex is used to create initial models of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex using the UBQ_E2_thioester protocol, which allows the user to sequentially model the orientation of the thioesterified donor ubiquitin and the approach of an acceptor ubiquitin and to perform standard loop modeling on the acidic loop. The acceptor ubiquitin is based on an apo structure (PDB ID 1UBQ). To generate models consistent with the crystallized orientation of donor ubiquitin, a constraint was implemented between Leu129 on Ube2R1 and both Ile44 and Val70 on the donor ubiquitin. Using this procedure, 4000 theoretical models of Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 are generated yielding 286 low-scoring models. Refining the acceptor ubiquitin and acidic loop. Ube2R1 structural modeling, overview. Molecular modeling of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex results in 14 distinct clusters of the Ube2R1-acceptor ubiquitin conformation
additional information
construction of initial Ube2R1-Rbx1 models, Rbx1 (PDB ID 2LGV) and Ube2R1 (PDB ID 4MDK) are aligned to the respective components from the Ube2G2/Rnf45 cocrystal structure (PDB ID 2LXP) and energy is minimized with Rosetta algorithms relax and fixbb. Next, an initial conformation for the acidic loop (residues 97 to 115) is built onto the top-scoring Ube2R1-Rbx1 model using the CCD algorithm with fragments derived from the Ube2R1 amino acid sequence. This model of the Ube2R1-Rbx1 complex is used to create initial models of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex using the UBQ_E2_thioester protocol, which allows the user to sequentially model the orientation of the thioesterified donor ubiquitin and the approach of an acceptor ubiquitin and to perform standard loop modeling on the acidic loop. The acceptor ubiquitin is based on an apo structure (PDB ID 1UBQ). To generate models consistent with the crystallized orientation of donor ubiquitin, a constraint was implemented between Leu129 on Ube2R1 and both Ile44 and Val70 on the donor ubiquitin. Using this procedure, 4000 theoretical models of Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 are generated yielding 286 low-scoring models. Refining the acceptor ubiquitin and acidic loop. Ube2R1 structural modeling, overview. Molecular modeling of the Ube2R1-donor ubiquitin/acceptor ubiquitin-Rbx1 complex results in 14 distinct clusters of the Ube2R1-acceptor ubiquitin conformation
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview
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E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
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E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Deletion of the N-terminal extension of Ube2E family members switches their (in vitro) activity from mono- to polyubiquitylation
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
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E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
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E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
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E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
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E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
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E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
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E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. Enzyme UBE2NL has no catalytic cysteine
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
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E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. K48-specific Ube2R2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Multi-subunit E3s make use of the E2 backside surface. The APC/C engages Ube2C using both a RING subunit Apc11 and the WHB domain of a cullin subunit Apc2, the latter interaction being via the E2's backside. While use of two subunits to recruit the E2 serves to ensure specificity for Ube2C, the additional interaction also appears to direct substrate ubiquitylation by reducing the degrees of freedom available for the E2/RING assembly
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Structures of E2-Ub bound to a HECT (NEDD4L) or RBR (HOIP) E3 reveal a Ube2D2-Ub conjugate in an open conformation, poised for transthiolation to the E3 active-site cysteine
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2D3-Ub and Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although Ube2D3-Ub and Ube2N-Ub conjugates are highly dynamic, the ensembles of conformations adopted by them are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. UBE2E3 can be thought of having an intrinsic ability to build polyUb chains that is inhibited by Ub binding on its backside. The two opposite effects of backside Ub binding suggest that it can act as either a throttle or a brake for chain building
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G1 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2G2 has a short about 12 amino acid insertion proximal to the E2 active site that determines specificity. In the case of Ube2G2, binding of a non-RING region (G2BR) of its E3, gp78, to the backside of the UBC domain alters the acidic loop conformation, which is helical in the free E2 structure but is unwound in the G2BR-bound structure. The unwinding generates a series of interactions among E2, E3, and Ub that help stabilize a closed E2-Ub conformation to increase aminolysis reactivity. The requirement of an extra, allosteric interaction between Ube2G2 and gp78 ensures that the K48 chain-building E2 cannot work with any RING E3 it happens to contact. The human ERAD E3 ligase, gp78, uses the non-RING G2BR to interact with the backside of its E2, Ube2G2. G2BR binding in trans can increase the affinity of Ube2G2-Ub for the gp78 RING and can enhance both E3-dependent and E3-independent Ub transfer activity, suggesting cooperative allosteric interactions between RING and G2BR binding. The situation is different in the case of uncharged Ube2G2, which binds the E3 with lower affinity due to loss of some G2BR contacts, an effect that promotes dissociation of reacted (or inactive) E2 from the E3, allowing for exchange with active E2-Ub conjugate
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2N-Ub conjugates show an array of orientations that involve little or no contact between the E2 and ubiquitin (open states) and some conformations (closed states) that involve contacts between the Ub hydrophobic patch centered on Ub I44 and residues in the E2 crossover helix. Although the Ube2N-Ub conjugates is highly dynamic, the ensembles of conformations adopted by it are different in terms of the relative fraction of closed versus open states
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
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E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
additional information
E2 structure-function analysis, overview. Ube2S uses acidic residues in the final UBC domain helix to interact with the acceptor Ub and orient K11 towards the C-terminus of the donor Ub bound to its active site
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molecular dynamics simulations of Ubc9
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structure-function overview of the E2 fold
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structure-function overview of the E2 fold
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the catalytic cysteine is C86
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the structure of UBE2Z enzyme provides functional insight into specificity in the FAT10 protein conjugation machinery. UBE2Z is specific for E1-like ubiquitin-activating enzyme UBA6. UBE2Z N-terminal extension and loop LB are essential for selectivity toward UBA6
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dimer
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E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2A shows the UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the Ext-UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2B shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D1 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D2 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D3 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2D4 shows the UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
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UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E1 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2E3 shows the Ext-UBC domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G1 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2G2 shows the UBC + insert domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2H shows the Ext-UBC domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J1 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2J2 shows the UBC + insert-Ext domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC domain organization
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2K shows the UBC-UBA domain organization, an additional structured domain is linked to their UBC domain. Ube2K has a unique region near its active site that interacts with a tyrosine near K48 in the acceptor Ub to provide K48-linkage specificity
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2L6 shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2N shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2NL shows the UBC domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
additional information
UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2QL shows the UBC + insert domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R1 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2R2 shows the UBC + insert-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2S shows the UBC-Ext domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V1 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2V2 shows the Ext-UBC domain organization
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UBE2Z is a 354-residue-long atypical ubiquitin conjugating enzyme comprising about 100-residue long N- and C-terminal extensions on top of the conserved core UBC domain, classifying it as a class IV E2 enzyme. The UBE2Z core domain adopts the characteristic ellipsoid shape of UBC domains but also harbors two extensions termed loops LA (residues 169-173) and LB (residues 194-197) compared with the prototypical class I E2 enzyme UBE2D3. Structural organization of UBE2Z, modeling, overview
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBE2Z shows the Ext-UBC-Ext domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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UBEE2 shows the Ext-UBC domain organization
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