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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 E1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UbcH7]-L-cysteine
[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin carrier protein UbcH7]-S-ubiquitinyl-L-cysteine
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[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ube2r]-L-cysteine
[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin-carrier-protein Ube2r]-S-ubiquitinyl-L-cysteine
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enzyme is capable of forming a thiolester bond with ubiquitin
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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 E2]-L-cysteine
[ubiquitin-activating protein BA1]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
transfer of ubiquitin from activating protein UBA1 can take place to different ubiquitin-carrier enzymes E2, with little discrimination for the type of E2 protein
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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 UBA2]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein E2]-L-cysteine
[ubiquitin-activating protein UBA2]-L-cysteine + [ubiquitin carrier protein E2]-S-ubiquitinyl-L-cysteine
transfer of activated ubiquitin from E1 enzyme UBA2 is carried out to different ubiquitin-carrier enzymes E2, with little discrimination for the type of E2 protein
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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
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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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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
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
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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
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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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additional information
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HECT-E3 ligase ETC-1 ubiquitylates securin IFY-1 and cyclin B1 in the presence of the E2 enzyme UBC-18
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additional information
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HECT-E3 ligase ETC-1 ubiquitylates securin IFY-1 and cyclin B1 in the presence of the E2 enzyme UBC-18
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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
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
-
-
-
additional information
?
-
the enzyme interacts with E3 ligase of type RING
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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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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 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)
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-
-
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)
-
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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
?
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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
?
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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
?
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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
?
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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
?
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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 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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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
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the enzyme belongs to the E2 gene family, phylogenetic analysis of VvUBC family, 43 VvUBC members can be classified into five groups, expression pattern of VvUBCs in different genotypes, detailed overview. Chromosome localization and gene duplication analysis of VvUBCs
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
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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
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knockdown of enzyme expression in decreases tombusvirus accumulation and reduces symptom severity
malfunction
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knockdown of enzyme expression in decreases tombusvirus accumulation and reduces symptom severity
malfunction
ablation of UBC6e causes upregulation of active ERAD enhancers and so increases clearance not only of terminally misfolded substrates, but also of wild-type glycoproteins that fold comparatively slowly in vitro and in vivo. The absence of UBC6e increases the levels of ERAD enhancers with a corresponding increase in the rate of clearance of misfolded and/or incompletely folded substrates. UBC6e-/- MEFs show accelerated mannose trimming and premature substrate release from CNX, initiated by ER mannosidase-dependent eviction of substrate from the CNX cycle. Finally, by deletion of UBC6e, accelerated degradation is observed in tissue culture and in vivo, not only for canonical ERAD substrates, but also for folding intermediates of proteins that fold slowly, such as tyrosinase. The UBC6e loss-of-function mutation thus produces a gain-of-function with respect to ERAD activity, overview. Increased degradation of tyrosinase in UBC6e-/- cells and reduced skin tyrosinase levels in UBC6e-/- mice
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)
malfunction
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knockdown of enzyme expression in decreases tombusvirus accumulation and reduces symptom severity
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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 enzyme UbeC6 is involved in the endoplasmic reticulum (ER) associated degradation (ERAD)
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
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
metabolism
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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
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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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ubiquitination is involved in myriad cell and disease pathways. The ubiquitin-conjugating E2 is the central player in the ubiquitin-transfer pathway
physiological function
isoform UBC1 can partially complement the function of the yeast UBC4 and UBC5 genes. UBC1 overexpressing Vigna radiata plants display highly sensitive responses to abscisic acid and osmotic stress during germination, enhanced abscisc acid- or salt-induced stomatal closing, and increased drought stress tolerance. The expression levels of a number of key abscisic acid signaling genes are increased in overexpressing plants. Protein UBC1 interacts with a C3HC4-type RING E3 ligase named VBP1, i.e. VrUBC1 Binding Partner 1
physiological function
lack of isoform Ubc2 expression leads to a slightly enhanced resistance level against Pto DC3000 pathogen inoculation
physiological function
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silencing of isoform Ubc2 expression by 77% does not affect the level of resistance against avirulent Pto DC3000 strain inoculation. Silencing leads to upregulation of diesease-related genes RAR1 and SGT1 whereas the expression level of HSP90 only slightly increases
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
HECT-E3 ligase ETC-1 ubiquitylates securin IFY-1 and cyclin B1 in the presence of the E2 enzyme UBC-18, which functions in pharyngeal development. UBC-18 plays a distinct role together with ETC-1 in regulating the cytoplasmic level of IFY-1 during meiosis
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
residues within helix alpha2 of Ubc7 that interact with donor ubiquitin are essential for polyubiquitin conjugation by Ubc7 and its cognate E3 enzymes. Mutagenesis of these residues inhibits the in vitro activity of Ubc7 by preventing the conjugation of donor ubiquitin to the acceptor. Ubiquitin chain formation by mutant Ubc7 is restored selectively by the E3 enzyme Hrd1 RING domain but not by the E3 enzyme Doa10 RING domain. alpha2 Helix mutations selectively impair the in vivo degradation of Doa10 substrates but have no apparent effect on the degradation of Hrd1 substrates
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
Ubc11 gene encodes one of the two E2 enzymes required for progression through mitosis in fission yeast
physiological function
Ubc13 null mutant lines in which the two Ubc13 genes are disrupted display altered root development, including shorter primary root, fewer lateral roots and only a few short root hairs in comparison with the wild type and single mutant plants. The double mutant plants are insensitive to auxin treatments. Instead, the Ubc13 mutant has a reduced auxin response. Both the enzymatic activity and protein level of an AXR3/IAA17-GUS reporter are greatly increased in the Ubc13 mutant, whereas the induction of many auxin-responsive genes is suppressed
physiological function
Ube2J1-/- mice have reduced viability and fail to thrive early after birth. Male Ube2J1-/- mice are sterile due to a defect in late spermatogenesis. Removal of the cytoplasm is incomplete in Ube2J1-/- elongating spermatids, compromising the release of mature elongate spermatids into the lumen of the seminiferous tubule
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
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the enzyme is correlated with the cryogenic autolysis of Volvariella volvacea
physiological function
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the enzyme is critical for tombvirus replication and is involved in promoting the subversion of Vps23p and Vps4p ESCRT proteins for viral replicase complex assembly
physiological function
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the enzyme is critical for tombvirus replication and is involved in promoting the subversion of Vps23p and Vps4p ESCRT proteins for viral replicase complex assembly
physiological function
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the enzyme plays an important role in the innate immunity of Solanum peruvianum against Clavibacter michiganensis subsp. michiganensis
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
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involvement of ubiquitin-conjugating enzyme (UBC) in ripening process and response to cold and heat stress of Vitis vinifera
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
UBC6e is an E2 ubiquitin conjugating enzyme that localizes to the ER via its tail-anchor. Functional UBC6e requires its precise location in the endoplasmic reticulum (ER) to form a supramolecular complex with Derlin2. This complex targets ERAD enhancers for degradation, a function that depends on UBC6e's enzymatic activity. UBC6e-/- cells upregulate ERAD enhancers selectively, but UBC6e downregulates EDEM1, EDEM3, OS-9 and SEL1L (ERAD enhancers) in the absence of ER stress. Homeostasis of SEL1L, EDEM1 and OS-9 requires enzymatic activity of UBC6e. UBC6e's function depends strictly on its E2 enzymatic activity but not its phosphorylation status. The exact ER membrane localization of UBC6e and the supramolecular complexes in which UBC6e participates determine its activity, and directly control the levels of components essential for ERAD activity. Only the Derlin2-complexed UBC6e controls the levels of ERAD enhancers
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 (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. An ordered Cdc34 CTDprox extension is involved in Ub discharge, CTDprox/Ub contacts are important for Cdc34 action in cells. Cdc34 CTDprox locks Ub(t) in the closed conformation. The Cdc34 CTDprox extension is involved in Ub discharge
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
physiological function
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the enzyme is critical for tombvirus replication and is involved in promoting the subversion of Vps23p and Vps4p ESCRT proteins for viral replicase complex assembly
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physiological function
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the enzyme is correlated with the cryogenic autolysis of Volvariella volvacea
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physiological function
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Ubc11 gene encodes one of the two E2 enzymes required for progression through mitosis in fission yeast
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physiological function
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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. An ordered Cdc34 CTDprox extension is involved in Ub discharge, CTDprox/Ub contacts are important for Cdc34 action in cells. Cdc34 CTDprox locks Ub(t) in the closed conformation. The Cdc34 CTDprox extension is involved in Ub discharge
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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
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
additional information
E2 structure-function analysis, overview
additional information
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
additional information
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
additional information
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
additional information
E2 structure-function analysis, overview
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. 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
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. 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
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 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
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
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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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
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homodimer
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2 * 18400, SDS-PAGE
?
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x * 30000, SDS-PAGE
dimer
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2 * 18000, single band on SDS-PAGE, indicating a dimeric form. Gel filtration results in an estimated molecular weight of 42 kDa
dimer
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E2 enzymes spontaneously dimerize in solution, in vitro, in absence of charged ubiquitin
additional information
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
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D1 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D2 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D3 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the UBC domain organization
additional information
UBE2D4 shows the 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
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
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
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
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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
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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
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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
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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
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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
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2L6 shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2N shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2NL shows the UBC domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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UBE2Q1 shows the Ext-UBC + insert domain organization
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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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UBC6e exists in at least two different configurations: as an apparent monomer and as part of a complex
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isoformUbc2 interacts with disease-related protein SGT1
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