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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
Substrates: -
Products: -
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2 N6-monoubiquitinyl-[Ube2K]-L-lysine
N6-diubiquitinyl-[Ube2K]-L-lysine + [Ube2K]-L-lysine
Substrates: -
Products: -
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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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Substrates: -
Products: -
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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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Substrates: -
Products: 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
Substrates: -
Products: 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
Substrates: -
Products: 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
Substrates: -
Products: 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
Substrates: -
Products: -
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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
Substrates: -
Products: -
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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
Substrates: -
Products: -
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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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Substrates: -
Products: 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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Substrates: -
Products: 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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Substrates: -
Products: 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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Substrates: -
Products: 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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Substrates: -
Products: 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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Substrates: -
Products: 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
Substrates: polyubiquitination of AMPKalpha2
Products: -
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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
Substrates: -
Products: -
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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
Substrates: 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
Products: -
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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
Substrates: polyubiquitination of o-Maf
Products: -
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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
Substrates: polyubiquitination of protein MLL
Products: -
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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
Substrates: monoubiquitination of SMAD6
Products: -
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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
Substrates: polyubiquitination of TRAF6 K63
Products: -
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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
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Substrates: 42% relative activity compared to cytochrome c as substrate
Products: -
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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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Substrates: 12% with human and 15% with bovine alpha-lactalbumin, relative activity compared to cytochrome c as substrate
Products: -
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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
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Substrates: yeast cytochrome c, ubiquitin from human blood
Products: -
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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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Substrates: -
Products: -
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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
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Substrates: 5% relative activity compared to cytochrome c as substrate
Products: -
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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
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Substrates: substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
Products: -
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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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Substrates: substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
Products: -
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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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Substrates: substrate protein Stam2 contains a N-terminal ubiquitin-interacting motif and VHS domain, it is most strongly ubiquitinated by E2 isoform UbcH5A
Products: -
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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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Substrates: substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
Products: -
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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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Substrates: substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
Products: -
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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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Substrates: substrate protein Pol tau contains two C-terminal ubiquitin-associated domains. It is ubiquitinated by all E2 isoforms tested
Products: -
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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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Substrates: substrate protein Eps15 contains two C-terminal ubiquitin-interacting motifs. It is potently ubiquitinated by UbcH5 isoforms and less well by UbcH2 and UbcH6
Products: -
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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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Substrates: substrate protein Pol k contains two C-terminal ubiquitin-binding zinc finger domains. It is ubiquitinated by UbcH2, UbcH5 isoforms and UbcH6
Products: -
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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
Substrates: -
Products: 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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Substrates: -
Products: 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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Substrates: -
Products: 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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Substrates: -
Products: 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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Substrates: -
Products: 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
Substrates: -
Products: -
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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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Substrates: -
Products: -
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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
Substrates: -
Products: -
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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
Substrates: mapping of the BMAL1-interacting domain in UBE2O
Products: -
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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
Substrates: polyubiquitination of BMAL1
Products: -
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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
Substrates: 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
Products: -
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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
Substrates: -
Products: -
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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
Substrates: the polyubiquitin chain formation on Hippel-Lindau protein (pVHL) occurrs on all three of its lysines (Lys159, Lys171 and Lys196)
Products: -
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additional information
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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: polyubiquitin chain formation catalyzed by E2 enzymes, in the absence of an E3 protein and a target protein substrate
Products: 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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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
Products: -
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additional information
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Substrates: isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
Products: -
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additional information
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Substrates: isoform UbcH10 does not preassemble polyubiquitin chains on its acitve site cysteine
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: the enzyme interacts with E3 ligases of types RING and RBR, and with its own N-terminus
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: beta-lactoglobulin and reduced carboxymethylated bovine serum albumin rcmBSA are not conjugates
Products: -
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Adenocarcinoma of Lung
UBE2V2 Positively Correlates With PD-L1 Expression and Confers Poor Patient Survival in Lung Adenocarcinoma.
Anemia
UBE2O remodels the proteome during terminal erythroid differentiation.
Autoimmune Diseases
Variants on the UBE2L3-YDJC autoimmune disease risk haplotype increase UBE2L3 gene expression by modulating CTCF and YY1 binding.
Breast Neoplasms
UBE2O promotes the proliferation, EMT and stemness properties of breast cancer cells through the UBE2O/AMPK?2/mTORC1-MYC positive feedback loop.
Carcinogenesis
A new duet in cancer biology: AMPK the typical and UBE2O the atypical.
Carcinogenesis
A UBE2O-AMPK?2 Axis that Promotes Tumor Initiation and Progression Offers Opportunities for Therapy.
Carcinogenesis
UBE2O promotes the proliferation, EMT and stemness properties of breast cancer cells through the UBE2O/AMPK?2/mTORC1-MYC positive feedback loop.
Carcinogenesis
UBE2O targets Mxi1 for ubiquitination and degradation to promote lung cancer progression and radioresistance.
Carcinoma
Deregulation of E2-EPF ubiquitin carrier protein in papillary renal cell carcinoma.
Carcinoma
The predictive role of E2-EPF ubiquitin carrier protein in esophageal squamous cell carcinoma.
Carcinoma
UBE2O Promotes Progression and Epithelial-Mesenchymal Transition in Head and Neck Squamous Cell Carcinoma.
Carcinoma
[Roles of hMMS2 gene in reversing the oxaliplatin tolerance of human colon carcinoma cells].
Carcinoma, Hepatocellular
Overexpression of ubiquitin-conjugating enzyme E2 L3 in hepatocellular carcinoma potentiates apoptosis evasion by inhibiting the GSK3?/p65 pathway.
Carcinoma, Hepatocellular
Prognostic value of ubiquitin-conjugating enzyme E2 S overexpression in hepatocellular carcinoma.
Carcinoma, Hepatocellular
Stabilization of E2-EPF UCP protein is implicated in hepatitis B virus-associated hepatocellular carcinoma progression.
Carcinoma, Renal Cell
Deregulation of E2-EPF ubiquitin carrier protein in papillary renal cell carcinoma.
Carcinoma, Squamous Cell
UBE2O Promotes Progression and Epithelial-Mesenchymal Transition in Head and Neck Squamous Cell Carcinoma.
Colorectal Neoplasms
[Roles of hMMS2 gene in reversing the oxaliplatin tolerance of human colon carcinoma cells].
Diabetes Mellitus, Type 2
A muscle-specific UBE2O/AMPK?2 axis promotes insulin resistance and metabolic syndrome in obesity.
Diabetes, Gestational
Putative association between UBE2E2 polymorphisms and the risk of gestational diabetes mellitus.
Esophageal Neoplasms
Role of interleukin 1 beta in esophageal squamous cell carcinoma.
Esophageal Neoplasms
The predictive role of E2-EPF ubiquitin carrier protein in esophageal squamous cell carcinoma.
Esophageal Squamous Cell Carcinoma
The predictive role of E2-EPF ubiquitin carrier protein in esophageal squamous cell carcinoma.
Glioma
Ectopic High Expression of E2-EPF Ubiquitin Carrier Protein Indicates a More Unfavorable Prognosis in Brain Glioma.
Hepatitis B
Stabilization of E2-EPF UCP protein is implicated in hepatitis B virus-associated hepatocellular carcinoma progression.
Infections
The ubiquitin-conjugating enzyme UBE2O modulates c-Maf stability and induces myeloma cell apoptosis.
Infections
Ubiquitin-Conjugating Enzyme E2 L3 is Downregulated by the Chikungunya Virus nsP2 Protease.
Intellectual Disability
A novel UBE2A mutation causes X-linked intellectual disability type Nascimento.
Leukemia
Diverse roles of the E2/E3 hybrid enzyme UBE2O in the regulation of protein ubiquitination, cellular functions, and disease onset.
Lung Neoplasms
Epigenome-wide DNA methylation signature of benzo[a]pyrene exposure and their mediation roles in benzo[a]pyrene-associated lung cancer development.
Lung Neoplasms
UBE2O targets Mxi1 for ubiquitination and degradation to promote lung cancer progression and radioresistance.
Metabolic Syndrome
A muscle-specific UBE2O/AMPK?2 axis promotes insulin resistance and metabolic syndrome in obesity.
Multiple Myeloma
The ubiquitin-conjugating enzyme UBE2O modulates c-Maf stability and induces myeloma cell apoptosis.
Neoplasm Metastasis
A UBE2O-AMPK?2 Axis that Promotes Tumor Initiation and Progression Offers Opportunities for Therapy.
Neoplasm Metastasis
E2-EPF UCP targets pVHL for degradation and associates with tumor growth and metastasis.
Neoplasm Metastasis
Stabilization of E2-EPF UCP protein is implicated in hepatitis B virus-associated hepatocellular carcinoma progression.
Neoplasm Metastasis
UBE2O promotes the proliferation, EMT and stemness properties of breast cancer cells through the UBE2O/AMPK?2/mTORC1-MYC positive feedback loop.
Neoplasms
A new duet in cancer biology: AMPK the typical and UBE2O the atypical.
Neoplasms
A UBE2O-AMPK?2 Axis that Promotes Tumor Initiation and Progression Offers Opportunities for Therapy.
Neoplasms
AMPK variant, a candidate of novel predictor for chemotherapy in metastatic colorectal cancer: A meta-analysis using TRIBE, MAVERICC and FIRE3.
Neoplasms
An Oncogenic Role for the Ubiquitin Ligase UBE2O by Targeting AMPK-?2 for Degradation.
Neoplasms
Autodeubiquitination Protects the Tumor Suppressor BAP1 from Cytoplasmic Sequestration Mediated by the Atypical Ubiquitin Ligase UBE2O.
Neoplasms
Deregulation of E2-EPF ubiquitin carrier protein in papillary renal cell carcinoma.
Neoplasms
Diverse roles of the E2/E3 hybrid enzyme UBE2O in the regulation of protein ubiquitination, cellular functions, and disease onset.
Neoplasms
E2-EPF UCP targets pVHL for degradation and associates with tumor growth and metastasis.
Neoplasms
Egr-1 and serum response factor are involved in growth factors- and serum-mediated induction of E2-EPF UCP expression that regulates the VHL-HIF pathway.
Neoplasms
Mechanism of muscle protein degradation induced by a cancer cachectic factor.
Neoplasms
Prognostic value of ubiquitin-conjugating enzyme E2 S overexpression in hepatocellular carcinoma.
Neoplasms
Role of interleukin 1 beta in esophageal squamous cell carcinoma.
Neoplasms
Stabilization of E2-EPF UCP protein is implicated in hepatitis B virus-associated hepatocellular carcinoma progression.
Neoplasms
The Positive Correlations between the Expression of Histopathological Ubiquitin-Conjugating Enzyme 2O Staining and Prostate Cancer Advancement.
Neoplasms
The ubiquitin-conjugating enzyme UBE2O modulates c-Maf stability and induces myeloma cell apoptosis.
Neoplasms
UBE2D3 Activates SHP-2 Ubiquitination to Promote Glycolysis and Proliferation of Glioma via Regulating STAT3 Signaling Pathway.
Neoplasms
UBE2O Promotes Progression and Epithelial-Mesenchymal Transition in Head and Neck Squamous Cell Carcinoma.
Neoplasms
UBE2O promotes the proliferation, EMT and stemness properties of breast cancer cells through the UBE2O/AMPK?2/mTORC1-MYC positive feedback loop.
Neoplasms
UBE2O targets Mxi1 for ubiquitination and degradation to promote lung cancer progression and radioresistance.
Obesity
A muscle-specific UBE2O/AMPK?2 axis promotes insulin resistance and metabolic syndrome in obesity.
Osteosarcoma
Ubiquitin-conjugating enzyme UBE2O regulates cellular clock function by promoting the degradation of the transcription factor BMAL1.
Ovarian Neoplasms
UBE2N Regulates Paclitaxel Sensitivity of Ovarian Cancer via Fos/P53 Axis.
Prostatic Neoplasms
Diverse roles of the E2/E3 hybrid enzyme UBE2O in the regulation of protein ubiquitination, cellular functions, and disease onset.
Prostatic Neoplasms
The Positive Correlations between the Expression of Histopathological Ubiquitin-Conjugating Enzyme 2O Staining and Prostate Cancer Advancement.
Skin Abnormalities
A novel UBE2A mutation causes X-linked intellectual disability type Nascimento.
Squamous Cell Carcinoma of Head and Neck
UBE2O Promotes Progression and Epithelial-Mesenchymal Transition in Head and Neck Squamous Cell Carcinoma.
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evolution
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
ubiquitin-conjugating enzyme E2 O (UBE2O) is a member of the E2 family of the ubiquitin-proteasome system (UPS). Unlike most members of this family which are about 20 to 25 kDa in molecular weight, UBE2O is unusually large, with a molecular weight of 141 kDa
malfunction
a UCP mutant in which Cys118 is changed to alanine (UCPC118A) does not form a polyubiquitin chain but strongly accumulates mono- and di-ubiquitin via auto-ubiquitination
malfunction
inhibition of UBE2O or depletion of UBE2O leads to the reduced growth of breast and prostate cancer cells, but inactivation of AMPKalpha2 abrogates the beneficial effect caused by the UBE2O loss
malfunction
UBE2O knockdown elevates the amplitude of the circadian clock in human osteosarcoma U2OS cells. Full-length UBE2O and the CR2 truncation rescue the effect of UBE2O knockdown on the BMAL1 protein level
metabolism
the ubiquitin-proteasome system is an important regulatory machinery involved in proteostasis and cellular signaling. Proteins are ubiquitinated via the concerted action of E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin ligases. UBE2O is an E2/E3 hybrid enzyme and exhibits both the E2 and E3 activities. Role of UBE2O in the development of hematological disorders and cancers, overview
metabolism
UBE2O is a critical regulator in the ubiquitin-proteasome system, which modulates BMAL1 transcriptional activity and circadian function by promoting BMAL1 ubiquitination and degradation under normal physiological conditions. UBE2O regulates BMAL1 protein level and stability
metabolism
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
physiological function
-
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
physiological function
E2 enzyme HIP2-ubiquitin thioester complexes remain predominantly monomeric in solution
physiological function
E2 enzyme HIP2-ubiquitin thioester complexes remain predominantly monomeric in solution. Models of the HIP2-ubiquitin complex show an open or backbent conformation similar to UbcH5b-ubiquitin where the ubiquitin-associated UBA domain and covalently attached ubiquitin reside on opposite ends of the catalytic domain. Full length HIP2 exhibits a fivefold increase in the formation rate of diubiquitin compared to a HIP2 lacking the UBA domain
physiological function
dysregulation of the circadian rhythm is associated with many diseases, including diabetes, obesity, and cancer. Aryl hydrocarbon receptor nuclear translocator-like protein 1 (Arntl or Bmal1) is the only clock gene whose loss disrupts circadian locomotor behavior in constant darkness. BMAL1 transcription factor levels are affected by proteasomal inhibition and by several enzymes in the ubiquitin-proteasome system. Specific interaction between BMAL1 and ubiquitin-conjugating enzyme E2 O (UBE2O), an E3-independent E2 ubiquitin-conjugating enzyme (i.e. hybrid E2/E3 enzyme) is detetcted, UBE2O expression reduces BMAL1 levels by promoting its ubiquitination and degradation. UBE2O expression/knockdown diminishes/increases, respectively, BMAL1-mediated transcriptional activity but does not affect BMAL1 gene expression. The conserved region 2 (CR2) in UBE2O significantly enhances BMAL1 ubiquitination and decreases BMAL1 protein levels. The CR2 domain alone can enhance BMAL1 ubiquitination and its protein level
physiological function
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
the ubiquitin-conjugating enzyme E2 O (UBE2O) is an E3-independent E2 (i.e. an E2/E3 hybrid enzyme), can directly mediate the ubiquitination of many substrates, e.g. 5'-AMP-activated protein kinase catalytic subunit alpha2 (AMPKalpha2), tumor suppressor ubiquitin carboxyl-terminal hydrolase BAP1, mixed-lineage leukemia (MLL) protein, SMAD family member 6 (SMAD6), transcription factor c-Maf and aryl hydrocarbon receptor nuclear translocator-like protein 1 (ARNTL or BMAL1), and free ribosomal proteins, which are ubiquitinated in distinct ways, thereby associating UBE2O with a variety of biological functions. The presence of multifunctional domains in UBE2O suggests that it might act on a broad spectrum of targets and execute diverse biological functions. Although UBE2O is first identified as an E2 enzyme, it is subsequently discovered that it also functions as an E2/E3 hybrid enzyme. UBE2O also functions as an E3 enzyme which is fused to an E2 enzyme and carries out the E3-independent ubiquitination. UBE2O may involve an intramolecular thiol relay mechanism. UBE2O mediates monoubiquitination, multi-monoubiquitination, and polyubiquitination of different substrates and thereby performs its diverse functions. UBE2O specifically targets AMPKalpha2 but not AMPKalpha1 for the formation of K48-linked polyubiquitin chains and for its subsequent degradation by the 26S proteasome, importance of UBE2O-mediated ubiquitination of AMPKalpha2 on tumor cell growth
physiological function
UCP possesses not only E2 ubiquitin conjugating enzyme activity but also E3 ubiquitin ligase activity, and Cys118 is critical for polyubiquitin chain formation
additional information
E2 structure-function analysis, overview. Enzyme UBE2O is a large multidomain E2/E3 hybrid performing the E2 and the E3 reaction
additional information
homology modeling of UBE2O, using the recombinant enzyme and structure of the MZM-REP domains of Mind bomb 1 (Mib1, PDB ID 4XI6) and the UBC domain of baculoviral IAP repeat-containing protein 6 (BIRC6, PDB ID 3CEG), respectively, overview. UBE2O also displays nonenzymatic functions, and as a protein-interacting partner it can block protein ubiquitination. The N-terminus of UBE2O interacts efficiently with the TRAF domain in TNF receptor-associated factor 6 (TRAF6), prevents its K63-linked polyubiquitination, competes with myeloid differentiation primary response protein MyD88 for TRAF6, and thus suppresses the activation of NF-kappaB induced by lipopolysaccharide and interleukin-1beta. Loss of the UBC domain in UBE2O does not affect this regulation, indicating that its nonenzymatic function prevents TRAF6 ubiquitination
additional information
-
homology modeling of UBE2O, using the recombinant enzyme and structure of the MZM-REP domains of Mind bomb 1 (Mib1, PDB ID 4XI6) and the UBC domain of baculoviral IAP repeat-containing protein 6 (BIRC6, PDB ID 3CEG), respectively, overview. UBE2O also displays nonenzymatic functions, and as a protein-interacting partner it can block protein ubiquitination. The N-terminus of UBE2O interacts efficiently with the TRAF domain in TNF receptor-associated factor 6 (TRAF6), prevents its K63-linked polyubiquitination, competes with myeloid differentiation primary response protein MyD88 for TRAF6, and thus suppresses the activation of NF-kappaB induced by lipopolysaccharide and interleukin-1beta. Loss of the UBC domain in UBE2O does not affect this regulation, indicating that its nonenzymatic function prevents TRAF6 ubiquitination
additional information
UCP ubiquitinates itself independent of E3 ubiquitin ligase in vitro using mixed lysine linkages. 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. Residue Cys118 plays a key role in the autoubiquitination of UCP. Reaction mechanism, overview
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