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Literature summary for 2.7.11.13 extracted from
- Kinetic analysis of the interaction of the C1 domain of protein kinase C with lipid membranes by stopped-flow spectroscopy (2008), J. Biol. Chem., 283, 7885-7893.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phorbol 12-myristate 13-acetate | - |
Rattus norvegicus |  |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y123W | the mutation in the C1 domain of PKC leads to measurable changes upon membrane binding | Rattus norvegicus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | dependent on | Rattus norvegicus | |
| Zn2+ | the C1 domain of PKC requires two Zn2+ ions for proper folding and stability | Rattus norvegicus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| C1Bbeta | C1 domain of PKC | Rattus norvegicus |
| PKC | - |
Rattus norvegicus |
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Release 2023.1 (January 2023)
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