| + |
CSNK2A3 | up-regulates activity 
phosphorylation
|
SCN2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275751 |
Ser1112 |
VPIAVGEsDFENLNT |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19064667 |
We found that the ankyrin-binding motif of Na(v)1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Na(v) channel interaction with ankyrins. | inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275755 |
Ser1124 |
LNTEEFSsESDMEES |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19064667 |
We found that the ankyrin-binding motif of Na(v)1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Na(v) channel interaction with ankyrins. | inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275759 |
Ser1126 |
TEEFSSEsDMEESKE |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19064667 |
We found that the ankyrin-binding motif of Na(v)1.2 that determines channel concentration at the AIS depends on a glutamate residue (E1111), but also on several serine residues (S1112, S1124, and S1126). We showed that phosphorylation of these residues by protein kinase CK2 (CK2) regulates Na(v) channel interaction with ankyrins. | inhibition of CK2 activity reduced sodium channel accumulation at the AIS of neurons. In conclusion, CK2 contributes to sodium channel organization by regulating their interaction with ankyrin G. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CSNK2A3 | down-regulates activity 
phosphorylation
|
F8 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263649 |
Ser1656 |
GRTERLCsQNPPVLK |
in vitro |
|
| pmid |
sentence |
| 8427963 |
Our findings suggest that phosphorylation of factors Va and VIIIa by a platelet casein kinase II-like kinase may downregulate the activity of the two cofactors.| Recombinant human factor VIII also showed incorporation of radioactivity in the presence of purified casein kinase II at the acidic NH2-terminal portion of factor VIII light chain (residues 1648 through 1689). Based on all the considerations reported above Se1657 is the most likely candidate within this region capable of incorporation of radioactivity |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSNK2A3 | up-regulates activity
phosphorylation
|
FGF14 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275742 |
Ser228 |
PGVTPSKsTSASAIM |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 26917740 |
Bioluminescence-based screening of small molecule modulators of the FGF14:Nav1.6 complex identified 4,5,6,7 -: tetrabromobenzotriazole (TBB), a potent casein kinase 2 (CK2) inhibitor, as a strong suppressor of FGF14:Nav1.6 interaction. Inhibition of CK2 through TBB reduces the interaction of FGF14 with Nav1.6 and Nav1.2 channels. Mass spectrometry confirmed direct phosphorylation of FGF14 by CK2 at S228 and S230, and mutation to alanine at these sites modified FGF14 modulation of Nav1.6-mediated currents. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275743 |
Ser230 |
VTPSKSTsASAIMNG |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 26917740 |
Bioluminescence-based screening of small molecule modulators of the FGF14:Nav1.6 complex identified 4,5,6,7 -: tetrabromobenzotriazole (TBB), a potent casein kinase 2 (CK2) inhibitor, as a strong suppressor of FGF14:Nav1.6 interaction. Inhibition of CK2 through TBB reduces the interaction of FGF14 with Nav1.6 and Nav1.2 channels. Mass spectrometry confirmed direct phosphorylation of FGF14 by CK2 at S228 and S230, and mutation to alanine at these sites modified FGF14 modulation of Nav1.6-mediated currents. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
CSNK2A3
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