| + |
NLGN3 | up-regulates activity 
binding
|
NRXN1 |
0.836 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264142 |
|
|
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 |
| + |
KHDRBS1 | up-regulates activity
post transcriptional regulation
|
NRXN1 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269057 |
|
|
Mus musculus |
Cerebellum |
| pmid |
sentence |
| 22196734 |
Activity-dependent alternative splicing of Nrxn1 requires the KH-domain RNA binding protein SAM68 which associates with RNA response elements in the Nrxn1 pre-mRNA. Our findings uncover SAM68 as a key regulator of dynamic control of Nrxn1 molecular diversity and activity-dependent alternative splicing in the central nervous system. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NLGN1 | up-regulates activity
binding
|
NRXN1 |
0.836 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264144 |
|
|
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 |
0.821 |
| 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 |
| + |
ASH1L | down-regulates quantity by repression 
transcriptional regulation
|
NRXN1 |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269056 |
|
|
Homo sapiens |
NG-108-15 Cell |
| pmid |
sentence |
| 27229316 |
Our results reveal that a novel process of activity-dependent transcriptional repression exists in neurons and that Ash1L mediates the long-term repression of nrxn1α, thus implicating an important role for epigenetic modification in brain functioning. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NRXN1 | up-regulates activity
binding
|
NLGN2 |
0.821 |
| 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 |
| + |
STXBP1 | up-regulates activity
binding
|
NRXN1 |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264040 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 11036064 |
We propose that all these neurexin complexes can interact with Munc18. Both Mint1 and Mint2 could function as direct adaptors of Munc18 to neurexins, whereas Mint1 in addition could recruit Munc18 to CASK-neurexin (Fig. 5 B). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Neurotransmitters release |
| + |
NRXN1 | up-regulates activity
binding
|
DAG1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265458 |
|
|
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 |
| Tissue: |
Brain |
| + |
NLGN4X | up-regulates activity
binding
|
NRXN1 |
0.765 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264145 |
|
|
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
|
NRXN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264143 |
|
|
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 |
| + |
TCF4 | up-regulates quantity by expression 
transcriptional regulation
|
NRXN1 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255391 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22777675 |
we show that TCF4 can transactivate the NRXN1β and CNTNAP2 promoters in luciferase assays. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APBA2 | up-regulates activity
binding
|
NRXN1 |
0.624 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264039 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11036064 |
Mint1 and Mint2 Interact with the Cytoplasmic Domain of Neurexin I. The interaction of Mint1 with neurexins is mediated by its PDZ domains and allows the formation of mixed CASK-Mint complexes. Both CASK and Mint1 can bind directly to neurexins and to each other. Therefore, the assembly of various multimeric complexes could proceed as CASK could be indirectly recruited to neurexin-bound Mint1 and vice versa. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
NXPH1 | up-regulates
binding
|
NRXN1 |
0.562 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-62775 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9856994 |
Purification of neurexin ialpha revealed that it is tightly complexed to a secreted glycoprotein called neurexophilin 1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APBA1 | up-regulates activity
binding
|
NRXN1 |
0.656 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264038 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 11036064 |
Mint1 and Mint2 Interact with the Cytoplasmic Domain of Neurexin I. The interaction of Mint1 with neurexins is mediated by its PDZ domains and allows the formation of mixed CASK-Mint complexes. Both CASK and Mint1 can bind directly to neurexins and to each other. Therefore, the assembly of various multimeric complexes could proceed as CASK could be indirectly recruited to neurexin-bound Mint1 and vice versa. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| Pathways: | Neurotransmitters release |
| + |
DGC | up-regulates activity
binding
|
NRXN1 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265446 |
|
|
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
NRXN1
- 
- 