+ |
AKT1 | down-regulates activity
phosphorylation
|
ADARB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276194 |
Thr553 |
LQGERLLtMSCSDKI |
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
|
ADARB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276195 |
Thr553 |
LQGERLLtMSCSDKI |
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
|
ADARB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276196 |
Thr553 |
LQGERLLtMSCSDKI |
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 |
+ |
AKT | down-regulates activity
phosphorylation
|
ADARB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266358 |
Thr553 |
LQGERLLtMSCSDKI |
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 |
+ |
FUS | down-regulates quantity by repression
post transcriptional regulation
|
ADARB1 |
0.258 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262805 |
|
|
Mus musculus |
|
pmid |
sentence |
28515487 |
This conclusion is also supported by the analysis of alternative splicing events in hFUS+/+; Smn+/− mice. As shown in Fig. 6b, the splicing of Dusp22, Mphosph9, Adarb1, hnRNP A2/B1, Gria4, Vps16, Atxn2 and Agrin, which are significantly affected in hFUS+/+ mice, is not further modified by SMN decrease |
|
Publications: |
1 |
Organism: |
Mus Musculus |
Tissue: |
Spinal Cord |
+ |
ADARB1 | up-regulates activity
binding
|
EIF2AK2 |
0.469 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266359 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
19605474 |
Both forms of ADAR1 show enhanced interactions with PKR at the peak of HIV infection, suggesting a role for this protein in the regulation of PKR activation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |