EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.3.2.25 | more |
Ube2w is not reactive toward free lysine and contains novel residues in its active site that are important for activity |
Homo sapiens |
? |
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 |
? |
| 2.3.2.25 | more |
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 |
Homo sapiens |
? |
- |
- |
| 2.3.2.25 | more |
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 |
Homo sapiens |
? |
- |
- |
| 2.3.2.25 | S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid |
- |
Homo sapiens |
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein] |
- |
? |
| 2.3.2.25 | S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid |
- |
Mus musculus |
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein] |
- |
? |
| 2.3.2.25 | S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid |
- |
Mus musculus C57BL/6 |
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein] |
- |
? |
| 2.3.2.25 | S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid |
- |
Mus musculus C57 |
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein] |
- |
? |
| 2.3.2.25 | S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [alpha-synuclein]-N-terminal-amino acid |
full-length alpha-synuclein |
Homo sapiens |
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[alpha-synuclein] |
- |
? |
| 2.3.2.25 | S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid |
- |
Mus musculus |
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin] |
- |
? |
| 2.3.2.25 | S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid |
the relatively disordered nature of the N-terminal domain of HTT predicts it to be a potential candidate target for Ube2W |
Mus musculus |
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin] |
- |
? |
