| + |
NRXN2 | up-regulates activity 
binding
|
DAG1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265461 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626542 |
The DGC is potentially recruited to the postsynaptic membrane though a direct neurexin–dystroglycan interaction and an indirect interaction with NL2 via the synaptic scaffolding protein S-SCAM. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLGN3 | up-regulates activity
binding
|
NRXN2 |
0.826 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264157 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Pre- and postsynaptic plasma membranes are always precisely aligned, and are separated by a synaptic cleft of ~20 nm. The cleft contains an undefined proteinaceous material in the middle, and is presumably bridged by synaptic cell-adhesion molecules such as Nrxns and Nlgns that align the pre- and postsynaptic elements and mediate trans-synaptic signaling.|Nlgns bind to both alpha- and beta-Nrxns with nanomolar affinities; binding involves the sixth LNS-domain of alpha-Nrxns which corresponds to the only LNS-domain of beta-Nrxns52. The binding affinities differ characteristically between various pairs of Nlgns and Nrxns, and are controlled by alternative splicing of both Nrxns and Nlgns (Figure 1c) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NRXN2 | up-regulates activity
binding
|
NLGN2 |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265455 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626545 |
The neurexin–NL2 interaction is sufficient to induce GABAergic differentiation and clustering of GABAARs at postsynaptic sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NLGN1 | up-regulates activity
binding
|
NRXN2 |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264159 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Pre- and postsynaptic plasma membranes are always precisely aligned, and are separated by a synaptic cleft of ~20 nm. The cleft contains an undefined proteinaceous material in the middle, and is presumably bridged by synaptic cell-adhesion molecules such as Nrxns and Nlgns that align the pre- and postsynaptic elements and mediate trans-synaptic signaling.|Nlgns bind to both alpha- and beta-Nrxns with nanomolar affinities; binding involves the sixth LNS-domain of alpha-Nrxns which corresponds to the only LNS-domain of beta-Nrxns52. The binding affinities differ characteristically between various pairs of Nlgns and Nrxns, and are controlled by alternative splicing of both Nrxns and Nlgns (Figure 1c) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLGN4X | up-regulates activity
binding
|
NRXN2 |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264160 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Pre- and postsynaptic plasma membranes are always precisely aligned, and are separated by a synaptic cleft of ~20 nm. The cleft contains an undefined proteinaceous material in the middle, and is presumably bridged by synaptic cell-adhesion molecules such as Nrxns and Nlgns that align the pre- and postsynaptic elements and mediate trans-synaptic signaling.|Nlgns bind to both alpha- and beta-Nrxns with nanomolar affinities; binding involves the sixth LNS-domain of alpha-Nrxns which corresponds to the only LNS-domain of beta-Nrxns52. The binding affinities differ characteristically between various pairs of Nlgns and Nrxns, and are controlled by alternative splicing of both Nrxns and Nlgns (Figure 1c) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLGN4Y | up-regulates activity
binding
|
NRXN2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264158 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Pre- and postsynaptic plasma membranes are always precisely aligned, and are separated by a synaptic cleft of ~20 nm. The cleft contains an undefined proteinaceous material in the middle, and is presumably bridged by synaptic cell-adhesion molecules such as Nrxns and Nlgns that align the pre- and postsynaptic elements and mediate trans-synaptic signaling.|Nlgns bind to both alpha- and beta-Nrxns with nanomolar affinities; binding involves the sixth LNS-domain of alpha-Nrxns which corresponds to the only LNS-domain of beta-Nrxns52. The binding affinities differ characteristically between various pairs of Nlgns and Nrxns, and are controlled by alternative splicing of both Nrxns and Nlgns (Figure 1c) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NLGN2 | up-regulates activity
binding
|
NRXN2 |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264161 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18923512 |
Pre- and postsynaptic plasma membranes are always precisely aligned, and are separated by a synaptic cleft of ~20 nm. The cleft contains an undefined proteinaceous material in the middle, and is presumably bridged by synaptic cell-adhesion molecules such as Nrxns and Nlgns that align the pre- and postsynaptic elements and mediate trans-synaptic signaling.|Nlgns bind to both alpha- and beta-Nrxns with nanomolar affinities; binding involves the sixth LNS-domain of alpha-Nrxns which corresponds to the only LNS-domain of beta-Nrxns52. The binding affinities differ characteristically between various pairs of Nlgns and Nrxns, and are controlled by alternative splicing of both Nrxns and Nlgns (Figure 1c) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DGC | up-regulates activity
binding
|
NRXN2 |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265449 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11470830 |
In brain, dystroglycan and dystrophin are expressed on neurons and astrocytes, and some muscular dystrophies cause cognitive dysfunction. Our data indicate that dystroglycan is a physiological ligand for neurexins and that neurexins' tightly regulated interaction could mediate cell adhesion between brain cells. these results suggest that α- and β-neurexins represent ligands for dystroglycan via interactions of their LNS domains, analogous to interaction of the LNS-domain in laminin, agrin, and perlecan with dystroglycan. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
NRXN2
- 
- 