| + |
SHANK3 | up-regulates quantity 
binding
|
GRIA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264602 |
|
|
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 |
| + |
DLGAP2 | up-regulates activity
relocalization
|
SHANK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264591 |
|
|
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
|
SHANK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264600 |
|
|
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
|
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 |
| + |
SHANK3 | up-regulates 
|
Postsynaptic density assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264607 |
|
|
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 |
| Pathways: | Glutamatergic synapse |
| + |
DLGAP4 | up-regulates activity
relocalization
|
SHANK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264597 |
|
|
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 |
| + |
SHANK3 | up-regulates quantity
binding
|
GRIA3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264603 |
|
|
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
|
SHANK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264594 |
|
|
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 |
| + |
SHANK3 | up-regulates quantity
relocalization
|
NMDA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264701 |
|
|
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 |
| + |
SHANK3 | up-regulates quantity
relocalization
|
AMPA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264700 |
|
|
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 |
| + |
SHANK3 | up-regulates quantity
binding
|
GRIA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264601 |
|
|
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 |
| + |
SHANK3 | up-regulates quantity
binding
|
GRIA4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264604 |
|
|
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 |
| + |
HOMER | up-regulates activity
binding
|
SHANK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264697 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17243894 |
It has been shown that Homer, a scaffold protein with a single EVH1 domain that binds to Shank, mGluR1, and other postsynaptic proteins (98) (Figure 3), exists as a tetramer, thus allowing it to cross-link several interacting proteins in the PSD |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
SHANK3 | up-regulates activity
relocalization
|
ACTN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264585 |
|
|
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 |
| + |
CTTNBP2 | up-regulates activity
binding
|
SHANK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269702 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 35562389 |
Synaptopathy, a key feature of autism spectrum disorders (ASD), is likely relevant to the impaired phase separation and/or transition of ASD-linked synaptic proteins. Here, we report that LLPS and zinc-induced liquid-to-gel phase transition regulate the synaptic distribution and protein-protein interaction of cortactin-binding protein 2 (CTTNBP2), an ASD-linked protein. CTTNBP2 forms self-assembled condensates through its C-terminal intrinsically disordered region and facilitates SHANK3 co-condensation at dendritic spines. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
SHANK3
- 
- 