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Literature summary for 2.3.2.23 extracted from
- Trim-Away ubiquitinates and degrades lysine-less and N-terminally acetylated substrates (2023), Nat. Commun., 14, 2160.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure of the RING domain of TRIM21 in complex with Ube2W dimerization mutant V30K/D67K/C91K. Two copies of each Ube2W and RING are found in the asymmetric unit, with the two RINGs forming a homodimer | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| V30K/D67K/C91K | dimerization mutant, the active site is additionally replaced with lysine | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q96B02 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | TRIM21 RING is monoubiquitinated by UBE2W at its N-terminus and. Ubiquitination can be inhibited by N-terminal acetylation | Homo sapiens | ? | - |
- |
 |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| UBE2W | - |
Homo sapiens |
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