| + |
ZDHHC2 | up-regulates activity 
palmitoylation
|
DLG4 |
0.389 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262296 |
Cys3 |
cLCIVTTK |
Homo sapiens |
|
| pmid |
sentence |
| 23836932 |
Plasma membrane targeting of DHHC2 palmitoyltransferase rapidly recruited PSD-95 to the plasma membrane and proved essential for postsynaptic nanodomain formation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261290 |
Cys5 |
cIVTTKKY |
Homo sapiens |
|
| pmid |
sentence |
| 23836932 |
Plasma membrane targeting of DHHC2 palmitoyltransferase rapidly recruited PSD-95 to the plasma membrane and proved essential for postsynaptic nanodomain formation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates
phosphorylation
|
DLG4 |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205120 |
Tyr523 |
REDSVLSyETVTQME |
Homo sapiens |
|
| pmid |
sentence |
| 24981431 |
These results indicate that psd-95 phosphorylation by src facilitates the integration of pyk2 to psd-95 signal complex, the activation of pyk2/src, as well as the subsequent tyrosine phosphorylation of nr2a, which ultimately results in the upregulation of nmda receptor function and synaptic transmission. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | up-regulates
phosphorylation
|
DLG4 |
0.58 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-180449 |
Tyr523 |
REDSVLSyETVTQME |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18721130 |
Psd-95 is phosphorylated either by purified src/fyn kinases in vitro or by co-expression of constitutively active src/fyn in cos7 cells. psd-95 tyr(523) phosphorylation contributes to the post-ischaemic over-activation of nmda receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NMDA receptor_2C | up-regulates activity
binding
|
DLG4 |
0.738 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264224 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Another central component of the NMDA receptor signaling complex is the scaffold protein PSD-95 (also referred to as SAP-90). The first and second PDZ domains bind tightly to the tails of the NR2 subunits of the NMDA receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYNGAP1 | up-regulates activity
binding
|
DLG4 |
0.615 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264229 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 26356309 |
The reversible removal of AIDA-1 from the PSD core under excitatory conditions is similar to the redistribution of another abundant PSD protein, SynGAP. Both SynGAP-alpha1 and AIDA-1 are known to bind PSD-95. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
LRRC4B | up-regulates activity
binding
|
DLG4 |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264052 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19467332 |
A possible function for the NGL–PSD-95 interaction is to couple trans-synaptic adhesion events to the recruitment of PSD-95 and other PSD-95-associated postsynaptic proteins. PSD-95 and liprin-α may be key synaptic scaffolding proteins that couple trans-synaptic adhesions to the assembly of synaptic proteins/vesicles |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates activity
binding
|
LRFN2 |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264094 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 21736948 |
SALMs 1-3 contain a C-terminal PDZ-binding motif, which interacts with PSD-95, an abundant postsynaptic scaffolding protein, whereas SALM4 and SALM5 lack PDZ binding. Interactions between SALMs 1–3 and PSD-95 family proteinscould serve a number of functions. SALM1 and SALM2, which lack the ability to interact with a presynaptic ligand and thus cannot be directly targeted to sites of early synaptic adhesion, may require PSD-95 binding for their localization to early synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates activity
relocalization
|
GRIN2B |
0.817 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264195 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9278515 |
The PDZ domains of PSD-95 and related proteins interact with the COOH-terminal sequences of K+channels and NMDA2 receptors (3). By these interactions, PSD-95 may mediate the clustering of K+ channels and NMDA receptors at synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRFN4 | up-regulates activity
binding
|
DLG4 |
0.67 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264096 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 21736948 |
SALMs 1-3 contain a C-terminal PDZ-binding motif, which interacts with PSD-95, an abundant postsynaptic scaffolding protein, whereas SALM4 and SALM5 lack PDZ binding. One possibility is that SALM3, which is capable of inducing presynaptic differentiation in contacting axons [19], recruits PSD-95 or SAP102 to the sites of early synaptic adhesion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NMDA receptor_2D | up-regulates activity
binding
|
DLG4 |
0.731 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264225 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Another central component of the NMDA receptor signaling complex is the scaffold protein PSD-95 (also referred to as SAP-90). The first and second PDZ domains bind tightly to the tails of the NR2 subunits of the NMDA receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates activity
binding
|
TANC2 |
0.317 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266895 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 21068316 |
In the present study, we provide evidence that TANC1 and its close relative TANC2 regulate dendritic spines and excitatory synapses. our results indicate that TANC-dependent spine/synapse maintenance requires TANC binding to PSD-95, which promotes synaptic localization of TANC proteins. Thus, it is likely that interaction with PSD-95 concentrates TANC proteins at synapses, where they play a role in mediating PSD-95-dependent maintenance of spines and synapses. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Tissue: |
Brain |
| + |
DLG4 | up-regulates 
|
Synaptic_plasticity |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264053 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19075115 |
Postsynaptic density 95 (PSD-95) is an important regulator of synaptic structure and plasticity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
DLGAP4 | up-regulates activity
binding
|
DLG4 |
0.794 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264212 |
|
|
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 |
| + |
UBE3A | down-regulates quantity by destabilization 
ubiquitination
|
DLG4 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271397 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17121805 |
E6-induced degradation of DLG4 depends on E6AP in vivo. Our findings as a whole indicate that E6AP is involved in E6-mediated ubiquitination and degradation of DLG4 both in vivo and in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLGAP2 | up-regulates activity
binding
|
DLG4 |
0.692 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264210 |
|
|
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 |
| + |
NLGN3 | up-regulates activity
relocalization
|
DLG4 |
0.746 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264189 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. 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). A possible role of these interactions is to recruit postsynaptic adaptor proteins to the site of synaptic junctions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FMR1 | up-regulates quantity
post transcriptional regulation
|
DLG4 |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262108 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 32118033 |
These results point toward a novel mechanism by which FUS targets neuronal mRNA and given that these PSD-95 and Shank1 3'-UTR G quadruplex structures are also targeted by the fragile X mental retardation protein (FMRP), they raise the possibility that FUS and FMRP might work together to regulate the translation of these neuronal mRNA targets. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
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 |
| + |
DLG4 | up-regulates activity
relocalization
|
GRIN2A |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264194 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9278515 |
The PDZ domains of PSD-95 and related proteins interact with the COOH-terminal sequences of K+channels and NMDA2 receptors (3). By these interactions, PSD-95 may mediate the clustering of K+ channels and NMDA receptors at synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IQSEC2 | up-regulates activity
relocalization
|
DLG4 |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264907 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 18164504 |
Here, we characterized IQ-ArfGEF/BRAG1, a guanine nucleotide exchange factor (GEF) for Arf6, in the mouse brain. In vivo Arf pull down assay demonstrated that IQ-ArfGEF/BRAG1 activated Arf6 more potently than Arf1.IQ-ArfGEF/BRAG1 is a guanine nucleotide exchange factor for Arf6 that interacts with PSD-95 at postsynaptic density of excitatory synapses. Taken together, IQ-ArfGEF/BRAG1 forms a postsynaptic protein complex containing PSD-95 and NMDA receptors at excitatory synapses, where it may function as a GEF for Arf6. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
NMDA receptor_2B | up-regulates activity
binding
|
DLG4 |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264223 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Another central component of the NMDA receptor signaling complex is the scaffold protein PSD-95 (also referred to as SAP-90). The first and second PDZ domains bind tightly to the tails of the NR2 subunits of the NMDA receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLGN4Y | up-regulates activity
relocalization
|
DLG4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264190 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. 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). A possible role of these interactions is to recruit postsynaptic adaptor proteins to the site of synaptic junctions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates
|
Postsynaptic density assembly |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264230 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17243894 |
PSD-95 (the best-studied scaffold protein of the PSD, which binds to NR2 subunits of NMDA receptors) was found to be highly abundant in the adult forebrain PSD |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
ANKS1B | up-regulates activity
binding
|
DLG4 |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264228 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 26356309 |
The reversible removal of AIDA-1 from the PSD core under excitatory conditions is similar to the redistribution of another abundant PSD protein, SynGAP. Both SynGAP-alpha1 and AIDA-1 are known to bind PSD-95. |
|
| 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 |
| + |
DLG4 | up-regulates activity
binding
|
TANC1 |
0.616 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266894 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 21068316 |
In the present study, we provide evidence that TANC1 and its close relative TANC2 regulate dendritic spines and excitatory synapses. our results indicate that TANC-dependent spine/synapse maintenance requires TANC binding to PSD-95, which promotes synaptic localization of TANC proteins. Thus, it is likely that interaction with PSD-95 concentrates TANC proteins at synapses, where they play a role in mediating PSD-95-dependent maintenance of spines and synapses. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Tissue: |
Brain |
| + |
NMDA receptor_2A | up-regulates activity
binding
|
DLG4 |
0.794 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264222 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Another central component of the NMDA receptor signaling complex is the scaffold protein PSD-95 (also referred to as SAP-90). The first and second PDZ domains bind tightly to the tails of the NR2 subunits of the NMDA receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLGN4X | up-regulates activity
relocalization
|
DLG4 |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264192 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. 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). A possible role of these interactions is to recruit postsynaptic adaptor proteins to the site of synaptic junctions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates activity
binding
|
LRFN1 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264095 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 21736948 |
SALMs 1-3 contain a C-terminal PDZ-binding motif, which interacts with PSD-95, an abundant postsynaptic scaffolding protein, whereas SALM4 and SALM5 lack PDZ binding. Interactions between SALMs 1–3 and PSD-95 family proteinscould serve a number of functions. SALM1 and SALM2, which lack the ability to interact with a presynaptic ligand and thus cannot be directly targeted to sites of early synaptic adhesion, may require PSD-95 binding for their localization to early synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LRRC4C | up-regulates activity
binding
|
DLG4 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264050 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19467332 |
A possible function for the NGL–PSD-95 interaction is to couple trans-synaptic adhesion events to the recruitment of PSD-95 and other PSD-95-associated postsynaptic proteins. PSD-95 and liprin-α may be key synaptic scaffolding proteins that couple trans-synaptic adhesions to the assembly of synaptic proteins/vesicles |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLG4 | up-regulates activity
binding
|
NOS1 |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264227 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Neuronal NOS, a Ca2+-activated form of NOS, can bind to PSD-95 through a class III PDZ domain interaction in which its own amino-terminal PDZ domain binds to a PDZ domain of PSD-95. PSD-95 may concentrate nNOS near the NMDA receptor at postsynaptic sites in these neurons. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NMDA | up-regulates activity
binding
|
DLG4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264801 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Another central component of the NMDA receptor signaling complex is the scaffold protein PSD-95 (also referred to as SAP-90). The first and second PDZ domains bind tightly to the tails of the NR2 subunits of the NMDA receptor |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264704 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11052931 |
Another central component of the NMDA receptor signaling complex is the scaffold protein PSD-95 (also referred to as SAP-90). The first and second PDZ domains bind tightly to the tails of the NR2 subunits of the NMDA receptor |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
DLG4 | form complex 
binding
|
Scribble_complex_DLG4-LLGL2_variant |
0.453 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270889 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KIRREL3 | up-regulates activity
binding
|
DLG4 |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269079 |
|
|
Mus musculus |
Dopaminergic Neuron |
| pmid |
sentence |
| 28381988 |
We here report that, through its C-terminal PDZ domain-binding motif, Neph2 directly interacts with postsynaptic density (PSD)-95, an abundant excitatory postsynaptic scaffolding protein. Moreover, Neph2 protein is detected in the brain PSD fraction and interacts with PSD-95 in synaptosomal lysates. Functionally, loss of Neph2 in mice leads to age-specific defects in the synaptic connectivity of DG neurons. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NLGN2 | up-regulates activity
relocalization
|
DLG4 |
0.751 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264193 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. 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). A possible role of these interactions is to recruit postsynaptic adaptor proteins to the site of synaptic junctions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTCHD1 | up-regulates quantity
binding
|
DLG4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266652 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 29118110 |
Using Western blotting, we validated our MS approach confirming the binding of Dgl4 (also known as PSD95) and VPS35 to the recombinant Ptchd1 C terminus. Endogenous DLG4 and VPS35 from membrane and soluble mouse brain fractions were recovered specifically on the GST fusion proteins containing the cytoplasmic but not the extracellular, negative control sequences of Ptchd1 (Fig. 5E). Binding of DLG4 was dependent on the PDZ-binding motif in Ptchd1, whereas VPS35 binding was not (Fig. 5E). These results demonstrate a biochemical interaction of Ptchd1 with postsynaptic trafficking proteins in the mouse brain. Together, these data suggest that loss of Ptchd1 results in severe alterations in synaptic function in the dentate gyrus |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
FUS | up-regulates quantity
post transcriptional regulation
|
DLG4 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262103 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 32118033 |
These results point toward a novel mechanism by which FUS targets neuronal mRNA and given that these PSD-95 and Shank1 3'-UTR G quadruplex structures are also targeted by the fragile X mental retardation protein (FMRP), they raise the possibility that FUS and FMRP might work together to regulate the translation of these neuronal mRNA targets.|As seen in Figure 7 (top panel), both PSD-95 Q1-Q2 and Shank1a GQ probes pulled down endogenous FUS, whereas their M2 mutants did not, indicating that the GQ structure is sufficient for recognition. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Brain |
| + |
LRRC4 | up-regulates activity
binding
|
DLG4 |
0.436 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264051 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 19467332 |
A possible function for the NGL–PSD-95 interaction is to couple trans-synaptic adhesion events to the recruitment of PSD-95 and other PSD-95-associated postsynaptic proteins. PSD-95 and liprin-α may be key synaptic scaffolding proteins that couple trans-synaptic adhesions to the assembly of synaptic proteins/vesicles |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLGAP3 | up-regulates activity
binding
|
DLG4 |
0.748 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264211 |
|
|
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 |
| + |
DLGAP5 | up-regulates activity
binding
|
DLG4 |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264213 |
|
|
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 |
| + |
KIF5A | up-regulates activity
binding
|
DLG4 |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264065 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31753031 |
Postsynaptic density protein 95 (PSD-95) is transported by KIF5 to dendritic regions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLGN1 | up-regulates activity
relocalization
|
DLG4 |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264191 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Like NRXNs, NLGNs bind to intracellular PDZ-domain proteins, but in contrast to NRXNs, NLGNs bind to class I PDZ domains such as those contained in PSD95, a postsynaptic MAGUK protein65. PSD95 and its homologues are centrally involved in recruiting glutamate receptors at postsynaptic sites66. 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). A possible role of these interactions is to recruit postsynaptic adaptor proteins to the site of synaptic junctions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Glutamatergic synapse |
| + |
DLG4 | form complex
binding
|
Scribble_complex_DLG4-LLGL1_variant |
0.458 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270905 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23397623 |
The Scribble polarity complex or module is one of the three polarity modules that regulate cell polarity in multiple epithelia including blood-tissue barriers. This protein complex is composed of Scribble, Lethal giant larvae (Lgl) and Discs large (Dlg), which are well conserved across species from fruitflies and worms to mammals. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DLG4
- 
- 