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EC Number	Substrates	Commentary Substrates	Products	Commentary (Products)	Reversibility
2.3.2.23	S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine	backside interaction was of Ub non-covalently bound to Ube2D3 via the hydrophobic patch centered on I44, a Ub surface used in many different protein-protein interactions. Although weak in affinity, the interaction promotes an increase in processivity of polyUb chain building by Ube2D3	[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine	-	?
2.3.2.23	S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine	acceptor ubiquitin residue Arg54 participates in Ube2R1-catalyzed Lys48 polyubiquitin chain formation. Significance of the Asp143 Ube2R1/2-Arg54 acceptor ubiquitin ion pair	[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine	-	?
2.3.2.23	S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine	acceptor ubiquitin residue Arg54 participated in Ube2R1-catalyzed Lys 48 polyubiquitin chain formation. Significance of the Asp143 Ube2R1/2-Arg54 acceptor ubiquitin ion pair	[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine	-	?
2.3.2.23	S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine	the E2 ubiquitin-conjugating enzyme acquires the activated ubquitin from the E1 ubiquitin-activating enzyme	[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine	-	?
2.3.2.23	S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [UBE2S]-L-cysteine	-	[E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[UBE2S]-L-cysteine	-	?
2.3.2.23	S-ubiquitinyl-[Uba1]-L-cysteine + [Ubc5a]-L-cysteine	-	[Uba1]-L-cysteine + S-ubiquitinyl-[Ubc5a]-L-cysteine	the E1 enzyme Uba1, the E2 enzyme UbcH5a, and the E3 enzyme TRIP12 are responsible for ubiquitylation of ubiquitin mutant G76V	?
2.3.2.23	[UBE2W]-S-ubiquitinyl-L-cysteine + [Josephin domain of ATXN3]-L-lysine	-	[UBE2W]-L-cysteine + [Josephin domain of ATXN3]-N6-ubiquitinyl-L-lysine	-	?
2.3.2.23	[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein Ubc4]-L-cysteine	binding of Ubc4 to the E1ubiquitin covalent intermediate leads to productive catalysis of ubiquitin transfer to Ubc4 in the form of a thioester linkage. No significant ubiquitination of Ubc4 through formation of lysyl isopeptide bonds is observed	[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin carrier protein Ubc4]-S-ubiquitinyl-L-cysteine	-	?
2.3.2.23	[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin carrier protein UbcH7]-L-cysteine	-	[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin carrier protein UbcH7]-S-ubiquitinyl-L-cysteine	-	?
2.3.2.23	[ubiquitin-activating protein E1]-S-ubiquitinyl-L-cysteine + [ubiquitin-carrier-protein Ube2r]-L-cysteine	-	[ubiquitin-activating protein E1]-L-cysteine + [ubiquitin-carrier-protein Ube2r]-S-ubiquitinyl-L-cysteine	enzyme is capable of forming a thiolester bond with ubiquitin	?

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