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[(E3-independent) E2 ubiquitin-conjugating E2 enzyme]-S-monoubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
(1b)
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [(E3-independent) E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + [(E3-independent) ubiquitin-conjugating enzyme]-S-monoubiquitinyl-L-cysteine
(1a)
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
overall reaction
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues, the latter described for this enzyme. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys11, as well as Lys48-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues, the latter described for this enzyme. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys48-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues, the latter described for this enzyme. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Polyubiquination occurs through all seven lysines of ubiquitin, with Lys11 as common as those of Lys48. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues, the latter described for this enzyme. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical polyubiquitin chains that are linked through Lys63
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues, the latter described for this enzyme. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys63. This type of poly-ubiquitination does not lead to protein degradation by the proteasome
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys11-and Lys48-, as well as Lys63-linked polyubiquitination.
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes Lys11-linked polyubiquitination. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, except Lys48-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. In vitro able to promote polyubiquitination using all 7 ubiquitin Lys residues, but may prefer Lys11-, Lys27-, Lys48-, and Lys-63-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. In vitro catalyzes Lys11-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys11- and Lys48-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys11-, as well as Lys48- and Lys63-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys11-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys48-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and Lys48-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of Lys48-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Polyubiquination occurs through all seven lysines of ubiquitin, with Lys11 as common as those of Lys48
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Polyubiquination occurs through all seven lysines of ubiquitin, with Lys11 as common as those of Lys48. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Polyubiquination occurs through all seven lysines of ubiquitin. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys11- and Lys48-, as well as Lys63-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. Polyubiquination occurs through all seven lysines of ubiquitinAccepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes Lys48-linked polyubiquitination
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
E2 enzymes autoubiquitinate both their active sites cysteine and lysine residues. E2 enzymes catalyze polyubiquitin formation with a specific lysine preference or a limited subset of lysine residues of ubiquitin. The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical Lys63-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome
O00762, P49427, P49459, P51668, P51965, P60604, P61077, P61086, P61088, P62253, P62256, P62837, P63146, P68036, Q13404, Q15819, Q16763, Q712K3, Q8WVN8, Q969T4, Q96B02, Q96LR5, Q9NPD8, Q9Y2X8
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
the enzyme forms a labile ubiquitin adduct in the presence of E1, ubiquitin, and MgATP and catalyzes the conjugation of ubiquitin to protein substrates, independent of E3
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2 N6-monoubiquitinyl-[Ubc1]-L-lysine
N6-diubiquitinyl-[Ubc1]-L-lysine + [Ube2K]-L-lysine
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2 N6-monoubiquitinyl-[Ube2K]-L-lysine
N6-diubiquitinyl-[Ube2K]-L-lysine + [Ube2K]-L-lysine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-L-lysine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[E2 enzyme CDC34]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[E2 enzyme CDC34]-L-lysine
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CDC34 mutants differ in the extent of multiubiquitination they catalyze during an autoubiquitination reaction
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[histone H2A]-L-lysine
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reaction does not require additional factors such as E3 enzyme but depends on the E1 and ATP
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2g2-L-cysteine
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short chains of polyubiquitins can be linked bonds to E2 enzyme Ube2g2
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2K-L-cysteine
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longer chains of polyubiquitins can be linked bonds to E2 enzyme Ube2K. Ubiquitin chains are assembled on the active site cysteine of Ube2K through thioester bond
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + UbcH10-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-UbcH10-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2g2-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2g2-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2K-L-cysteine
[E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2K-L-cysteine
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [cytochrome c]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[cytochrome c]-L-lysine lysine
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approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 enzyme CDC34]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[E2 enzyme CDC34]-L-lysine
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CDC34 mutants differ in the extent of multiubiquitination they catalyze during an autoubiquitination reaction
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H1]-L-lysine
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significant rates of processive multiple ubiquitination of calf thymus H1 are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine lysine
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approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H3]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H3]-L-lysine
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significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H4]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H4]-L-lysine
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significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48
[E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2 ]-N6-monoubiquitinyl-L-lysine48
polyubiquitination of AMPKalpha2
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48
[E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2]-N6-monoubiquitinyl-L-lysine48
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BAP1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BAP1]-N6-monoubiquitinyl-L-lysine
UBE2O promotes multi-monoubiquitination on BAP1. The ubiquitination of BAP1 requires both the N-terminal CR1-CR2 domain and the C-terminal UBC domain of UBE2O. The absence of either domain completely abolishes BAP1 ubiquitination
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [c-Maf]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor c-Maf]-N6-monoubiquitinyl-L-lysine
polyubiquitination of o-Maf
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[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [MLL protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [MLL protein]-N6-monoubiquitinyl-L-lysine
polyubiquitination of protein MLL
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?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [SMAD6]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [SMAD6]-N6-monoubiquitinyl-L-lysine
monoubiquitination of SMAD6
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-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [TRAF6]-L-lysine63
[E1 ubiquitin-activating enzyme]-L-cysteine + [TRAF6]-N6-monoubiquitinyl-L-lysine63
polyubiquitination of TRAF6 K63
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-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [alpha-casein]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [alpha-casein]-N6-ubiquitinyl-L-lysine
-
42% relative activity compared to cytochrome c as substrate
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [alpha-lactalbumin]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [alpha-lactalbumin]-N6-ubiquitinyl-L-lysine
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12% with human and 15% with bovine alpha-lactalbumin, relative activity compared to cytochrome c as substrate
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-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [cytochrome c]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [cytochrome c]-N6-ubiquitinyl-L-lysine
-
yeast cytochrome c, ubiquitin from human blood
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-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [histone H3]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [histone H3]-N6-ubiquitinyl-L-lysine
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-
-
-
?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [lysozyme]-L-lysine
[ubiquitin-carrier protein E2]-L-cysteine + [lysozyme]-N6-ubiquitinyl-L-lysine
-
5% relative activity compared to cytochrome c as substrate
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-
?
[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
-
substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
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?
[ubiquitin-carrier protein UbcH2]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH2]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
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substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
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?
[ubiquitin-carrier protein UbcH5A]-S-ubiquitinyl-L-cysteine + [Stam2]-L-lysine
[ubiquitin-carrier protein UbcH5A]-L-cysteine + [Stam6]-N6-ubiquitinyl-L-lysine
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substrate protein Stam2 contains a N-terminal ubiquitin-interacting motif and VHS domain, it is most strongly ubiquitinated by E2 isoform UbcH5A
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-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
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substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
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-
?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
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substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
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?
[ubiquitin-carrier protein UbcH5]-S-ubiquitinyl-L-cysteine + [Pol tau]-L-lysine
[ubiquitin-carrier protein UbcH5]-L-cysteine + [Pol tau]-N6-ubiquitinyl-L-lysine
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substrate protein Pol tau contains two C-terminal ubiquitin-associated domains. It is ubiquitinated by all E2 isoforms tested
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?
[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Eps15]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Eps15]-N6-ubiquitinyl-L-lysine
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substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
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-
?
[ubiquitin-carrier protein UbcH6]-S-ubiquitinyl-L-cysteine + [Pol k]-L-lysine
[ubiquitin-carrier protein UbcH6]-L-cysteine + [Pol k]-N6-ubiquitinyl-L-lysine
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substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
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-
?
additional information
?
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
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reaction does not require additional factors such as E3 enzyme but depends on the E1 and ATP
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
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approximate relative activities as ubiquitin acceptors are: histones H2A:H2B:cytochrome c 1:0.5:0.2
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine
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-
significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine
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-
significant rates of nonprocessive core histone monoubiquitination are catalyzed by E2 enzymes of 14 kDa, 20 kDa, and 32 kDa
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine
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-
isoform CDC34 mutant proteins expressed in Escherichia coli display E3-independent ubiquitin-conjugating activity
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?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
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-
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?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
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-
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?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N6-monoubiquitinyl-L-lysine
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-
-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
mapping of the BMAL1-interacting domain in UBE2O
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-
?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
polyubiquitination of BMAL1
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?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine
polyubiquitination of hydrocarbon receptor nuclear translocator-like protein 1 (Arntl or Bmal1). The critical Cys residue in the CR2 domain of UBE2O is responsible for BMAL1 ubiquitination
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?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
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-
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?
[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [Hippel-Lindau protein]-L-lysine
[E1 ubiquitin-activating enzyme]-L-cysteine + [Hippel-Lindau protein]-N6-monoubiquitinyl-L-lysine
the polyubiquitin chain formation on Hippel-Lindau protein (pVHL) occurrs on all three of its lysines (Lys159, Lys171 and Lys196)
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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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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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the presence of ubiquitin-binding domains (UBDs) allows the ubiquitination of host proteins independently of E3 ligases. UBDs of different types, including ubiquitin-interacting motif UIM, ubiquitin-associated domain UBM, and ubiquitin-binding zinc finger domain UBZ, can directly cooperate with ubiquitin-charged E2 enzymes to promote monoubiquitination. Ubiquitin-loaded E2 and substrates interact in cells and E2 enzymes are essential for their monoubiquitination in vivo. This modification is mechanistically and functionally distinct from E3-mediated and growth factor-dependent monoubiquitination. The ability to transfer ubiquitin to a substrate is a common feature of all tested E2 enzymes. However, E2 enzymes show substrate specificity
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additional information
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E3-independent ubiquitination by Ube2K produces unanchored but also Ube2K-linked polyubiquitins through thioester and isopeptide bonds. E3-independent assembly of polyubiquitins on the catalytic cysteine of Ube2K strongly supports the possibility of en bloc transfer for polyubiquitination. Different lengths of polyubiquitins are linked to different E2s through thioester bond. In vitro E3-independent ubiquitination by Ube2K simultaneously produces unanchored, isopeptde-linked, and thioester-linked polyubiquitin chains
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?
additional information
?
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E3-independent ubiquitination by Ube2K produces unanchored but also Ube2K-linked polyubiquitins through thioester and isopeptide bonds. E3-independent assembly of polyubiquitins on the catalytic cysteine of Ube2K strongly supports the possibility of en bloc transfer for polyubiquitination. Different lengths of polyubiquitins are linked to different E2s through thioester bond. In vitro E3-independent ubiquitination by Ube2K simultaneously produces unanchored, isopeptde-linked, and thioester-linked polyubiquitin chains
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?
additional information
?
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E3-independent ubiquitination by Ube2K produces unanchored but also Ube2K-linked polyubiquitins through thioester and isopeptide bonds. E3-independent assembly of polyubiquitins on the catalytic cysteine of Ube2K strongly supports the possibility of en bloc transfer for polyubiquitination. Different lengths of polyubiquitins are linked to different E2s through thioester bond. In vitro E3-independent ubiquitination by Ube2K simultaneously produces unanchored, isopeptde-linked, and thioester-linked polyubiquitin chains
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?
additional information
?
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isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
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?
additional information
?
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isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
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?
additional information
?
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isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
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?
additional information
?
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ubiquitin thiol ester forms of at least four of five E2s tested catalyze ubiquitin transfer to a number of small amines, in a reaction that does not require E3 enzyme, and only primary amines on primary carbons can serve as ubiquitin acceptors. E3-independent ubiquitin transfer to the small, basic proteins histones H2A and H2B, and cytochrome c, is also observed
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?
additional information
?
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E2-EPF ubiquitin carrier protein (UCP) possesses E3 ubiquitin ligase activity via its cysteine 118 residue. E2-EPF UCP elongates E3-independent polyubiquitin chains on the lysine residues of von Hippel-Lindau protein (pVHL) and its own lysine residues both in vitro and in vivo. The initiation of the ubiquitin reaction depends on not only Lys11 linkage but also the Lys6, Lys48 and Lys63 residues of ubiquitin, which are involved in polyubiquitin chain formation on UCP itself. UCP self-association occurred through the UBC domain, which also contributes to the interaction with pVHL. The polyubiquitin chains appears on the N-terminus of UCP in vivo, which indicates that the N-terminus of UCP contains target lysines for polyubiquitination. The Lys76 residue of UCP is the most critical site for auto-ubiquitination, whereas the polyubiquitin chain formation on pVHL occurrs on all three of its lysines (Lys159, Lys171 and Lys196). Polyubiquitin chain formation requires the coordination of Cys95 and Cys118 between two interacting molecules. The mechanism of the polyubiquitin chain reaction of UCP may involve the transfer of ubiquitin from Cys95 to Cys118 by trans-thiolation, with polyubiquitin chains forming at Cys118 by reversible thioester bonding. The polyubiquitin chains are then moved to the lysine residues of the substrate by irreversible isopeptide bonding. During the elongation of the ubiquitin chain, an active Cys118 residue is required in both parts of UCP, namely, the catalytic enzyme and the substrate
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additional information
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the enzyme interacts with E3 ligases of types RING and RBR, and with its own N-terminus
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additional information
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UBE2O is an E2/E3 hybrid enzyme and exhibits both the E2 and E3 activities. UBE2O performs monoubiquitination, multi-monoubiquitination, and polyubiquitination of different substrates, mechanisms, overview. A consensus sequence analysis of the UBE2O-mediated ubiquitination sites discovers the VLI patch-containing bipartite NLS as the putative UBE2O recognition sequence
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additional information
?
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UBE2O is an E2/E3 hybrid enzyme and exhibits both the E2 and E3 activities. UBE2O performs monoubiquitination, multi-monoubiquitination, and polyubiquitination of different substrates, mechanisms, overview. A consensus sequence analysis of the UBE2O-mediated ubiquitination sites discovers the VLI patch-containing bipartite NLS as the putative UBE2O recognition sequence
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additional information
?
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beta-lactoglobulin and reduced carboxymethylated bovine serum albumin rcmBSA are not conjugates
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?
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2.3.2.24 (E3-independent) E2 ubiquitin-conjugating enzyme
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