A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

IndraLab

Statements

databases
phosphosite cbn pc11 biopax bel_lc signor biogrid tas lincs_drug hprd trrust | geneways tees isi trips rlimsp medscan sparser reach
reading

SRC phosphorylates AKT1 on Y315. 5 / 5
2 3 |
hprd
No evidence text available
signor
"We also showed that phosphorylation of Tyr-315 in Akt induced by Src or EGF is dependent on the integrity of this proline-rich motif. Furthermore, the Akt mutant lacking this proline motif fails to block the transcription activity of Forkhead in 293 cells and poorly stimulates the proliferation of Madin-Darby canine kidney cells. Taken together, our data suggest that the interaction between the SH3 domain of Src family kinases and the proline-rich motif in the C-terminal regulatory region of Akt is required for tyrosine phosphorylation of Akt and its subsequent activation."
signor
"Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity."
hprd
No evidence text available
hprd
No evidence text available
SRC phosphorylates AKT1 on Y326. 4 / 4
1 3 |
hprd
No evidence text available
signor
"Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity."
hprd
No evidence text available
hprd
No evidence text available
SRC phosphorylates AKT1 at position 308. 2 / 2
2 |
biopax:inoh
No evidence text available
biopax:inoh
No evidence text available
SRC phosphorylates AKT1 at position 473. 2 / 2
2 |
biopax:inoh
No evidence text available
biopax:inoh
No evidence text available
SRC leads to the phosphorylation of AKT1. 1 / 1
| 1
reach
"PI3K and AKT kinase inhibitor Ly294-002, Syc kinase inhibitor Bay61, Src kinase inhibitor PP2, but not the respective control PP3, also specifically blocked AKT1 phosphorylation in human platelets induced by CAPs at very low concentrations (XREF_FIG)."
SRC phosphorylates AKT1 on tyrosine. 1 / 1
| 1
reach
"Additionally, RET-PTC also phosphorylates a Y315 residue in protein kinase B (PKB), which is known to be phosphorylated by the Src tyrosine kinase."