| + |
NRXN3 | up-regulates activity 
binding
|
NLGN2 |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265457 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626547 |
The neurexin–NL2 interaction is sufficient to induce GABAergic differentiation and clustering of GABAARs at postsynaptic sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NRXN3 | up-regulates activity
binding
|
NLGN2 |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265456 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626546 |
The neurexin–NL2 interaction is sufficient to induce GABAergic differentiation and clustering of GABAARs at postsynaptic sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NLGN2 | up-regulates activity
binding
|
NRXN2 |
0.825 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264156 |
|
|
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 |
| + |
NRXN1 | up-regulates activity
binding
|
NLGN2 |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265453 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626543 |
The neurexin–NL2 interaction is sufficient to induce GABAergic differentiation and clustering of GABAARs at postsynaptic sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
NLGN2 | up-regulates activity
binding
|
NRXN1 |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264151 |
|
|
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 |
| + |
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 |
| + |
NLGN2 | up-regulates activity
binding
|
NRXN3 |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264171 |
|
|
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
|
NRXN1 |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264146 |
|
|
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 
|
Synaptic_plasticity |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264977 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25882190 |
Gephyrin is believed to act as a scaffold at inhibitory synapses, in a manner analogous to that of the prototypic excitatory synaptic scaffold, PSD-95. The best-known function of gephyrin is to bring the inhibitory synaptic receptors and to stabilize them at the inhibitory synapses. gephyrin interacts with NL-2 and collybistin, suggesting that it may be critical for the maturation or maintenance of inhibitory synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | GABAergic synapse |
| + |
NLGN2 | up-regulates activity
binding
|
MAGI2 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265444 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626542 |
S-SCAM is a member of the membrane-associated guanylate kinase (MAGUK) family of PDZ-domain-containing proteins that include the synaptic organising molecule PSD-95. The PDZ domain of S-SCAM binds to the C-terminal tail of NL2, forming a ternary complex at the cell membrane (Figure 2b). 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 |
| Tissue: |
Brain |
| + |
GPHN | up-regulates activity
binding
|
NLGN2 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264974 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 25882190 |
Gephyrin is believed to act as a scaffold at inhibitory synapses, in a manner analogous to that of the prototypic excitatory synaptic scaffold, PSD-95. The best-known function of gephyrin is to bring the inhibitory synaptic receptors and to stabilize them at the inhibitory synapses. gephyrin interacts with NL-2 and collybistin, suggesting that it may be critical for the maturation or maintenance of inhibitory synapses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | GABAergic synapse |
| + |
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 |
| + |
NLGN2 | up-regulates activity
binding
|
NRXN3 |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264166 |
|
|
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-265454 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626544 |
The neurexin–NL2 interaction is sufficient to induce GABAergic differentiation and clustering of GABAARs at postsynaptic sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NRXN1 | up-regulates activity
binding
|
NLGN2 |
0.82 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265452 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22626542 |
The neurexin–NL2 interaction is sufficient to induce GABAergic differentiation and clustering of GABAARs at postsynaptic sites. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
NLGN2
- 
- 