| + |
IPO5 | up-regulates activity 
relocalization
|
DSCAML1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264274 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30745319 |
DSCAM and DSCAML1 specifically interacted with the importin beta IPO5, whereas deletion of the identified NLSs abolished this specific interaction and suppressed nuclear translocation of the DSCAM/L1 ICDs in cell lines and cultured neurons. This suggests a direct role of IPO5 in the nuclear import of the DSCAM/L1 ICDs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DSCAML1 | down-regulates 
|
Neurite_outgrowth |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264275 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30745319 |
Nuclear DSCAM and DSCAML1 impair neurite outgrowth. this demonstrates that enhanced nuclear translocation of the DSCAM and DSCAML1 ICDs profoundly impairs neurite outgrowth and development of primary cortical neurons |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DSCAML1 | up-regulates activity
binding
|
STAT3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264278 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30745319 |
Our findings now further suggest that STAT3 and the adaptor protein SH2D2A interact with tyrosine‐containing motifs within the DSCAM/L1 ICDs. The SH2 domains of both STAT3 and SH2D2A are known to bind to phosphorylated tyrosine residues in the context of such motifs. Thus, the interactions between DSCAMs and SH2‐domain containing proteins seem to play a central and conserved role in Dscam signaling in the context of dynamic changes of tyrosine‐phosphorylation levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DSCAML1 | down-regulates
|
Synaptic_plasticity |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264281 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30745321 |
The DSCAM/L1 transcriptome data sets also contained a significant number of genes known to regulate synapse formation or function.Increased nuclear DSCAM levels inhibit synapse formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
gamma-secretase | down-regulates quantity 
cleavage
|
DSCAML1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264272 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30745319 |
γ‐secretase‐mediated intra‐membrane cleavage of DSCAM receptors results in the release of the DSCAM ICD, which is likely proceeded by shedding of the DSCAM ectodomain. Interaction of IPO5 with the NLS of DSCAM then leads to importin‐mediated nuclear import of the DSCAM ICD. In the nucleus, the DSCAM ICD may regulate the transcription of genes involved in neuronal development and function, thereby regulating processes such as neurite outgrowth, branching, and repulsion, as well as synapse formation, axon guidance, and neuronal cell death and survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DSCAML1 | up-regulates activity
binding
|
AQP9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264280 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30745319 |
Our findings now further suggest that STAT3 and the adaptor protein SH2D2A interact with tyrosine‐containing motifs within the DSCAM/L1 ICDs. The SH2 domains of both STAT3 and SH2D2A are known to bind to phosphorylated tyrosine residues in the context of such motifs. Thus, the interactions between DSCAMs and SH2‐domain containing proteins seem to play a central and conserved role in Dscam signaling in the context of dynamic changes of tyrosine‐phosphorylation levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DSCAML1
- 
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