| + |
PRKACA | up-regulates activity 
phosphorylation
|
AKAP12 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271841 |
Ser627 |
KKRVRRPsESDKEDE |
in vitro |
|
| pmid |
sentence |
| 14657015 |
Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271843 |
Ser696 |
KKRARRGsSSDEEGG |
in vitro |
|
| pmid |
sentence |
| 14657015 |
Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271844 |
Ser698 |
RARRGSSsDEEGGPK |
in vitro |
|
| pmid |
sentence |
| 14657015 |
Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271842 |
Ser772 |
LVTPRKKsKSKLEEK |
in vitro |
|
| pmid |
sentence |
| 14657015 |
Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
CyclinB/CDK1 | up-regulates activity
phosphorylation
|
AKAP12 |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271840 |
Thr767 |
ESFKRLVtPRKKSKS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23063527 |
Mass spectrometry, molecular, and cellular approaches show that CDK1/Cyclin B1 phosphorylates Gravin on threonine 766 to prime the recruitment of the polo-like kinase Plk1 at defined phases of mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates activity
phosphorylation
|
AKAP12 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271839 |
Thr767 |
ESFKRLVtPRKKSKS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23063527 |
Mass spectrometry, molecular, and cellular approaches show that CDK1/Cyclin B1 phosphorylates Gravin on threonine 766 to prime the recruitment of the polo-like kinase Plk1 at defined phases of mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKAP12 | up-regulates activity
relocalization
|
PKC |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271838 |
|
|
|
|
| pmid |
sentence |
| 14657015 |
A-kinase-anchoring protein 250 (AKAP250; gravin) acts as a scaffold that binds protein kinase A (PKA), protein kinase C and protein phosphatases, associating reversibly with the beta(2)-adrenergic receptor. |
|
| Publications: |
1 |
| + |
AKAP12 | up-regulates activity
relocalization
|
PKA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271837 |
|
|
|
|
| pmid |
sentence |
| 14657015 |
A-kinase-anchoring protein 250 (AKAP250; gravin) acts as a scaffold that binds protein kinase A (PKA), protein kinase C and protein phosphatases, associating reversibly with the beta(2)-adrenergic receptor. |
|
| Publications: |
1 |
| + |
AKAP12 | up-regulates activity
relocalization
|
PRKCA |
0.471 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271836 |
|
|
|
|
| pmid |
sentence |
| 14657015 |
A-kinase-anchoring protein 250 (AKAP250; gravin) acts as a scaffold that binds protein kinase A (PKA), protein kinase C and protein phosphatases, associating reversibly with the beta(2)-adrenergic receptor. |
|
| Publications: |
1 |
| + |
AKAP12 | up-regulates activity
relocalization
|
PRKACA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271835 |
|
|
|
|
| pmid |
sentence |
| 14657015 |
A-kinase-anchoring protein 250 (AKAP250; gravin) acts as a scaffold that binds protein kinase A (PKA), protein kinase C and protein phosphatases, associating reversibly with the beta(2)-adrenergic receptor. |
|
| Publications: |
1 |
3.0
AKAP12
- 
- 