+ |
PRKACA | up-regulates activity
phosphorylation
|
ITPKA |
0.332 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249994 |
Ser121 |
LQQPRRLsTSSVSST |
in vitro |
|
pmid |
sentence |
9374536 |
Two isoforms of the inositol 1,4,5-trisphosphate 3-kinase have been identified, the A form and the B form. phosphorylation of isoform A by the cyclic AMP-dependent protein kinase increased activity 1.5-fold, whereas phosphorylation of isoform B decreased activity by 45%. major phosphorylation sites in the protein are Ser119 for PKA. Ser119 in the A isoform is conserved in the B isoform as Ser328 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CAMK2A | up-regulates
phosphorylation
|
ITPKA |
0.334 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-48387 |
Thr311 |
EHAQRAVtKPRYMQW |
Homo sapiens |
Neuron |
pmid |
sentence |
9155020 |
D-myo-inositol 1,4,5-trisphosphate 3-kinase a is activated by receptor activation through a calcium:calmodulin-dependent protein kinase ii phosphorylation mechanism. the phosphorylated residue was thr311. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Ovary, Brain |
+ |
PRKCA | down-regulates activity
|
ITPKA |
0.378 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-248991 |
|
|
in vitro |
|
pmid |
sentence |
9374536 |
In contrast, phosphorylation of the A isoform with PKC caused a significant decrease in activity whether assayed in the presence or absence of calcium/calmodulin (to _25% of the unphosphorylated enzyme activity). |
|
Publications: |
1 |
Organism: |
In Vitro |