+ |
CAMK2A | up-regulates activity
phosphorylation
|
SYNGAP1 |
0.439 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262687 |
Ser1073 |
PPLQRGKsQQLTVSA |
in vitro |
|
pmid |
sentence |
14970204 |
Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. The Major Phosphorylation Sites, Serines 764/765, 1058, and 1123, All Contribute to Regulation of GAP Activity of synGAP by CaMKII |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262688 |
Ser1138 |
PSITKQHsQTPSTLN |
in vitro |
|
pmid |
sentence |
14970204 |
Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. We identify four major sites of phosphorylation, serines 1123, 1058, 750/751/756, and 764/765. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262689 |
Ser779 |
FMARGLNsSMDMARL |
in vitro |
|
pmid |
sentence |
14970204 |
Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. The Major Phosphorylation Sites, Serines 764/765, 1058, and 1123, All Contribute to Regulation of GAP Activity of synGAP by CaMKII |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262690 |
Ser780 |
MARGLNSsMDMARLP |
in vitro |
|
pmid |
sentence |
14970204 |
Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. We identify four major sites of phosphorylation, serines 1123, 1058, 750/751/756, and 764/765. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262691 |
Thr1077 |
RGKSQQLtVSAAQKP |
in vitro |
|
pmid |
sentence |
15358237 |
Certain phosphopeptides were detected only in samples phosphorylated in vitro under conditions that favor CaMKII activity (Mg2+-ATP, Ca2+, calmodulin, and peptide inhibitors of PKA and PKC). In samples phosphorylated in vitro in the presence of Ca2+/calmodulin, we also detected the peptide (R)GKS*QQLT*VSAAQKPR with phosphorylated residues corresponding to S-1058 and T-1062 of synaptic ras GTPase activating protein (SynGAP). |
|
Publications: |
5 |
Organism: |
In Vitro |
Pathways: | Glutamatergic synapse |
+ |
SYNGAP1 | up-regulates activity
binding
|
DLG4 |
0.615 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264229 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
26356309 |
The reversible removal of AIDA-1 from the PSD core under excitatory conditions is similar to the redistribution of another abundant PSD protein, SynGAP. Both SynGAP-alpha1 and AIDA-1 are known to bind PSD-95. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glutamatergic synapse |