+ |
CAMK2A | down-regulates quantity by destabilization
phosphorylation
|
DLGAP1 |
0.407 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276429 |
Ser356 |
KAMGDEDsGDSDTSP |
in vitro |
|
pmid |
sentence |
23143515 |
CaMKIIα activated by the NMDA receptor phosphorylates GKAP Ser54 to induce polyubiquitination of GKAP. |
|
Publications: |
1 |
Organism: |
In Vitro |
Pathways: | Glutamatergic synapse |
+ |
DLGAP1 | up-regulates activity
relocalization
|
SHANK2 |
0.82 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264587 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
28179641 |
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DLGAP1 | up-regulates activity
relocalization
|
SHANK1 |
0.851 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264586 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
28179641 |
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glutamatergic synapse |
+ |
DLG4 | up-regulates activity
relocalization
|
DLGAP1 |
0.93 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264196 |
|
|
Homo sapiens |
|
pmid |
sentence |
18923512 |
Similarly to CASK, PSD95 binds to intracellular adaptor proteins, and especially to GKAP (a protein that binds to the guanylate-kinase domain of PSD95), which, in turn, binds to SHANK proteins (Fig. 1b). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glutamatergic synapse |
+ |
DLGAP1 | up-regulates activity
binding
|
DLG4 |
0.93 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264209 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
9115257 |
SAPAPs are specifically expressed in neuronal cells and enriched in the PSD fraction. SAPAPs induce the enrichment of PSD-95/SAP90 to the plasma membrane in transfected cells. Thus, SAPAPs may have a potential activity to maintain the structure of PSD by concentrating its components to the membrane area. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glutamatergic synapse |
+ |
DLGAP1 | up-regulates activity
relocalization
|
SHANK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264588 |
|
|
Homo sapiens |
Neuron |
pmid |
sentence |
28179641 |
SHANK proteins are ‘master’ scaffolding proteins that tether and organize intermediate scaffolding proteins. They are located at excitatory synapses, where they are crucial for proper synaptic development and function. SAPAP proteins subsequently bind to the PDZ domain of members of the SHANK protein family. SHANK proteins then bind to the actin cytoskeleton and to Homer protein, which in turn interacts with mGluRs. Through these extended links, PSD95, SAPAP, SHANK and Homer proteins form a quaternary complex that brings together mGluR and NMDAR complexes in the PSD (FIG. 3). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Glutamatergic synapse |