2.3.2.25: N-terminal E2 ubiquitin-conjugating enzyme
This is an abbreviated version!
For detailed information about N-terminal E2 ubiquitin-conjugating enzyme, go to the full flat file.
Word Map on EC 2.3.2.25
Reaction
Synonyms
E2 Ube2w, E2 ubiquitin-conjugating enzyme, Ubc16, UbcH6, UBE2E1, UBE2O, UBE2W, ubiquitin conjugating enzyme, ubiquitin conjugating enzyme E2, ubiquitin-conjugating enzyme (E2), ubiquitin-conjugating enzyme E2, ubiquitin-protein ligase W
ECTree
2.3.2.25 N-terminal E2 ubiquitin-conjugating enzymeAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.3.2.25 - N-terminal E2 ubiquitin-conjugating enzyme
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [alpha-synuclein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[alpha-synuclein]
full-length alpha-synuclein
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
NLRP1B inflammasome is ubiquitinylated at the N-terminal Leu248
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-leucine248
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
NLRP1B inflammasome
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Rnf4]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Rnf4]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [SUMO-2]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[SUMO-2]
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N-terminal mono-ubiquitylation of SUMO-2 primes it for poly-ubiquitylation by the Ubc13-UEV1 (ubiquitin-conjugating enzyme E2 variant 1) heterodimer
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [tau tetra-repeat domain]-N-terminal-Lys18
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[tau tetra-repeat domain]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Ube2W]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Ube2W]
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isoform Ube2W ubiquitylates its own N-terminus
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?
S-ubiquitinyl-[N-terminal E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [CARP2 protein]-N-terminal-amino acid
[N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine + N-ubiquitinyl-[ CARP2 protein]-N-terminal amino acid
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?
S-ubiquitinyl-[N-terminal E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [cIAP2 protein]-N-terminal-amino acid
[N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine + N-ubiquitinyl-[ cIAP2 protein]-N-terminal amino acid
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?
S-ubiquitinyl-[N-terminal E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [MDM2 protein]-N-terminal-amino acid
[N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine + N-ubiquitinyl-[ MDM2 protein]-N-terminal amino acid
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [ataxin-3]-NH2
[ubiquitin-carrier protein E2]-L-cysteine + N-terminal-ubiquitinyl-[ataxin-3]
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [protein-tau]-NH2
[ubiquitin-carrier protein E2]-L-cysteine + N-terminal-ubiquitinyl-[protein-tau]
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?
[ubiquitin-carrier protein Ubc16]-S-ubiquitinyl-L-cysteine + [CHIP]-NH2
[ubiquitin-carrier protein Ubc16]-L-cysteine + N-terminal-ubiquitinyl-[CHIP]
CHIP is a U-box E3 ubiquitin ligase known to interact productively with many E2 enzymes
isoform Ubc16 N-terminally mono-ubiquitinates the ubiquitin E3 ligase CHIP
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?
[ubiquitin-carrier protein Ubc16]-S-ubiquitinyl-L-cysteine + [SUMO-2]-NH2
[ubiquitin-carrier protein Ubc16]-L-cysteine + N-terminal-ubiquitinyl-[SUMO-2]
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isoform Ubc16 shows specific protein N-terminal monoubiquitylation activity. Ubc16 conjugates ubiquitin not only to its own N-terminus, but also to that of the small ubiquitin-like modifier SUMO in a manner dependent on the SUMO-targeted ubiquitin ligase RNF4, i.e. RING finger protein 4. N-terminal mono-ubiquitylation of SUMO-2 primes it for poly-ubiquitylation by the Ubc13-UEV1 ubiquitin-conjugating enzyme E2 variant 1 heterodimer
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
the relatively disordered nature of the N-terminal domain of HTT predicts it to be a potential candidate target for Ube2W
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
the relatively disordered nature of the N-terminal domain of HTT predicts it to be a potential candidate target for Ube2W
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Rnf4]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Rnf4]
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?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Rnf4]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Rnf4]
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?
additional information
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Ube2w is not reactive toward free lysine and contains novel residues in its active site that are important for activity
to confirm N-terminal ubiquitination lysine-less and N-terminally blocked substrates are generated. The lysine-less substrate is ubiquinated, but not the N-terminally blocked one
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?
additional information
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in vitro, UBE2W can modify the N-terminus of both alpha-synuclein and a tau tetra-repeat domain with a single ubiquitin. The reaction does not continue beyond monoubiquitination as UBE2W specifically recognizes disordered sequences at the N-terminus of the substrate
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additional information
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the enzyme UBE2W is specific for N-terminal amine group, it interacts with E3 ligase of type RING, HECT, and RBR. Ube2W exhibits no intrinsic activity towards free lysine. Instead, Ube2W attaches Ub to the N-terminal alpha-amino group of proteins to form a Ub-fusion protein product.While still an aminolysis reaction and therefore not fundamentally different from the reaction with lysine, intrinsic reactivity assays revealed that Ube2W can transfer Ub to the alpha-amino group of small lysine-less peptides but not to free lysine. The preference for N-terminal modification by Ube2W may not be absolute, as the retroviral restriction RING E3 TRIM5alpha is monoubiquitylated by Ube2W despite being acetylated on its N-terminus. Ube2W may also facilitate isopeptide bond formation, possibly if an N-terminus is blocked. Nevertheless, the preference of Ube2W for disordered N-termini gives it a (so far) unique target selection mechanism for a primary modification event that can subsequently be exploited by other E2 enzymes to form Ub chains. The E2 Ube2W shows unique ability to monoubiquitylate proteins on their N-termini. Ube2W appears to monoubiquitylate the RING E3 ligases TRIM5alpha and TRIM21, a prerequisite for their K63 polyubiquitylation by Ube2N/Ube2V2
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