| + |
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 |
| + |
DLGAP5 | up-regulates activity
relocalization
|
SHANK2 |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264599 |
|
|
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 |
| + |
SHANK2 | up-regulates activity
relocalization
|
ACTN1 |
0.301 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264584 |
|
|
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 |
| + |
DLGAP3 | up-regulates activity
relocalization
|
SHANK2 |
0.779 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264593 |
|
|
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 |
| + |
DLGAP4 | up-regulates activity
relocalization
|
SHANK2 |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264596 |
|
|
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 |
| + |
SHANK2 | up-regulates 
|
Postsynaptic density assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264606 |
|
|
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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLGAP2 | up-regulates activity
relocalization
|
SHANK2 |
0.843 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264590 |
|
|
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 |
3.0
SHANK2
- 
- 