+ |
AKT | down-regulates activity
phosphorylation
|
ADAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266357 |
Thr1033 |
RLGERLRtMSCSDKI |
in vitro |
|
pmid |
sentence |
31095429 |
AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively, and overexpression of the phosphomimic mutants ADAR1p110 (T738D) and ADAR2 (T553D) resulted in a 50-100% reduction in editase activity. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
AKT1 | down-regulates activity
phosphorylation
|
ADAR |
0.286 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276193 |
Thr1033 |
RLGERLRtMSCSDKI |
in vitro |
|
pmid |
sentence |
31095429 |
AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
AKT3 | down-regulates activity
phosphorylation
|
ADAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276191 |
Thr1033 |
RLGERLRtMSCSDKI |
in vitro |
|
pmid |
sentence |
31095429 |
AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
AKT2 | down-regulates activity
phosphorylation
|
ADAR |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276192 |
Thr1033 |
RLGERLRtMSCSDKI |
in vitro |
|
pmid |
sentence |
31095429 |
AKT-dependent phosphorylation of the adenosine deaminases ADAR-1 and -2 inhibits deaminase activity. Coimmunoprecipitation studies and in vitro kinase assays revealed that AKT-1, -2, and -3 interact with both ADAR1p110 and ADAR2 and phosphorylate these RNA editases. Using site-directed mutagenesis of suspected AKT phosphorylation sites, AKT was found to primarily phosphorylate ADAR1p110 and ADAR2 on T738 and T553, respectively |
|
Publications: |
1 |
Organism: |
In Vitro |