Cloned (Comment) | Organism |
---|---|
- |
Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | phosphorylation of Ser472 and phosphorylation of Thr305 appears to contribute to the activation of Akt-3 because mutation of both these residues to aspartate increases the catalytic activity of Akt-3, whereas mutation to alanine inhibits activation | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ro 31-8220 | - |
Homo sapiens | |
staurosporine | - |
Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9Y243 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | Akt-3 also possess a C-terminal 'tail' that contains a phosphorylation site Ser472 thought to be involved in the activation of Akt kinases. In addition to phosphorylation of Ser472, phosphorylation of Thr305 also appears to contribute to the activation of Akt-3 | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
liver | not highly expressed | Homo sapiens | - |
additional information | expressed widely | Homo sapiens | - |
skeletal muscle | not highly expressed | Homo sapiens | - |
Synonyms | Comment | Organism |
---|---|---|
Akt-3 | - |
Homo sapiens |
RAC-gamma serine/threonine protein kinase | - |
Homo sapiens |