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Literature summary for 3.1.3.16 extracted from
- Protein phosphatase 2A inactivates Bcl2s antiapoptotic function by dephosphorylation and up-regulation of Bcl2-p53 binding (2009), Blood, 113, 422-428.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| C2-ceramide | potent PP2A activator | Homo sapiens |  |
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | activating PP2A to dephosphorylate Bcl2 and/or increase Bcl2/p53 binding may represent an efficient and novel approach for treatment of hematologic malignancies | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphorylated Bcl2 + H2O | PP2A-mediated dephosphorylation of Bcl2 promotes its direct interaction with p53 as well as a conformational change in Bcl2, PP2A directly interacts with the BH4 domain of Bcl2 as a docking site to potentially bridge PP2A to Bcl2's flexible loop domain containing the target serine 70 phosphorylation site | Homo sapiens | Bcl2 + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PP2A | - |
Homo sapiens |
| protein phosphatase 2A | - |
Homo sapiens |
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