EC Number   |
Protein Variants |
Reference |
|---|
   2.7.1.153 | A1066V |
a common naturally occuring mutation involved in cancer development |
707974 |
| 2.7.1.153 | D1017H |
a common naturally occuring somatic mutation involved in cancer development |
707974 |
| 2.7.1.153 | D910A |
mice with an inactivating knock-in mutation in the p110delta isoform of PI3K, p110deltaD910A, generated on Leishmanina major resistant and susceptible genetic backgrounds. The mutant mice show severely impaired T cell responses, but the mutant mice also show more robust resistance to Leishmanina major infection manifested as significantly reduced lesion size and accelerated parasite clearance. Cells from p110D910A mice were significantly impaired in their ability to make cytokines, particularly IFN-gamma, interleukin-10, and TNF, phenotypes, overview |
709350 |
| 2.7.1.153 | D910A |
site-directed mutagenesis of isoform p110delta, catalytically inactive. Interleukin is unable to induce hyper-responsiveness in tissues expressing the mutant |
694257 |
| 2.7.1.153 | D915A |
complete loss of enzymic activity |
640955 |
| 2.7.1.153 | D933A/F934A |
complete loss of enzymic activity |
640955 |
| 2.7.1.153 | E542K |
a common naturally occuring mutation in the helical domain, the mutation is involved in cancer development, the mutant requires RAS binding but bot p85 binding |
707974 |
| 2.7.1.153 | E542K/E545K |
gain-of-function helical domain mutations result in upregulation of enzyme activity, Akt phosphorylation and cell transformation |
710406 |
| 2.7.1.153 | E542K/E545K |
the mutation disrupts the interaction between residues E545 (helical domain) and K379 (nSH2 domain) |
738217 |
| 2.7.1.153 | E545K |
a common naturally occuring mutation in the helical domain, the mutation is involved in cancer development, the mutant requires RAS binding but bot p85 binding |
707974 |
