Protein Variants | Comment | Organism |
---|---|---|
S17D | phosphomimetic mutation, stimulates MDM2-mediated polyubiquitination of p53. The stimulation is independent of p53 substrate. Mutation alters the conformation of the isolated N-terminus, it induces increased thermostability of the isolated N-terminal domain, it stimulates the allosteric interaction of MDM2 with the DNA-binding domain of p53 and it stimulates a protein-protein interaction with the E2-ubiquitin complex in the absence of substrate p53 that, in turn, increases hydrolysis of the E2-ubiquitin thioester bond | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P51668 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-ubiquitinyl-[UbcH5a]-L-cysteine + [p53]-L-lysine | - |
Homo sapiens | [UbcH5a]-L-cysteine + N6-ubiquitinyl-[p53]-L-lysine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
E3 ubiquitin-protein ligase Mdm2 | - |
Homo sapiens |
Mdm2 | - |
Homo sapiens |