| + |
PKC | down-regulates activity 
phosphorylation
|
AQP4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276260 |
Ser180 |
TIFASCDsKRTDVTG |
in vitro |
|
| pmid |
sentence |
| 19761816 |
Taken together this data shows that AQP4 in gliomas is the target of PKC phosphorylation, and albeit significantly phosphorylated at rest, phosphorylation can be further enhanced by PKC activation.This data suggests that in gliomas water permeability through AQP4 is under the regulation of PKC via phosphorylation of S180. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSNK2A2 | down-regulates activity
phosphorylation
|
AQP4 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250974 |
Ser276 |
AAQQTKGsYMEVEDN |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 11742978 |
We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. | To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4‐Cter proteins in which only one out of the three C‐terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250975 |
Ser285 |
MEVEDNRsQVETDDL |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 11742978 |
We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. | To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4‐Cter proteins in which only one out of the three C‐terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250976 |
Ser316 |
EKKGKDQsGEVLSSV |
Canis lupus familiaris |
|
| pmid |
sentence |
| 11742978 |
We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. | To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4‐Cter proteins in which only one out of the three C‐terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII. |
|
| Publications: |
3 |
Organism: |
Canis Lupus Familiaris |
| + |
CSNK2A1 | down-regulates activity
phosphorylation
|
AQP4 |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250826 |
Ser276 |
AAQQTKGsYMEVEDN |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 11742978 |
We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. AQP4 phosphorylation by CKII may thus provide a mechanism that regulates AQP4 cell surface expression. | To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4-Cter proteins in which only one out of the three C-terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250827 |
Ser285 |
MEVEDNRsQVETDDL |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 11742978 |
We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. AQP4 phosphorylation by CKII may thus provide a mechanism that regulates AQP4 cell surface expression. | To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4-Cter proteins in which only one out of the three C-terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250828 |
Ser316 |
EKKGKDQsGEVLSSV |
Canis lupus familiaris |
MDCK Cell |
| pmid |
sentence |
| 11742978 |
We found that the stress-induced kinase casein kinase (CK)II phosphorylates the Ser276 immediately preceding the tyrosine motif, increasing AQP4-mu 3A interaction and enhancing AQP4-lysosomal targeting and degradation. AQP4 phosphorylation by CKII may thus provide a mechanism that regulates AQP4 cell surface expression. | To determine whether Ser276 is an actual CKII substrate, we used GST–AQP4-Cter proteins in which only one out of the three C-terminal CKII consensus sites was sequentially conserved (Ser276, Ser285 and Ser315, respectively). Figure 7B (right panel) shows that the three serine residues, including Ser276, were indeed efficiently phosphorylated by CKII. |
|
| Publications: |
3 |
Organism: |
Canis Lupus Familiaris |
| + |
DGC | up-regulates quantity 
binding
|
AQP4 |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265443 |
|
|
Homo sapiens |
Neuron, Glial Cell |
| pmid |
sentence |
| 22626543 |
In brain, the DGC is involved in the organisation of GABA(A) receptors (GABA(A)Rs) and aquaporin-4 (AQP4)-containing protein complexes in neurons and glia, respectively. DGC-like complexes function in the postsynaptic clustering and stabilisation of GABAARs in a subset of inhibitory GABAergic synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
AQP4
- 
- 