| + |
CDK5/CDK5R1 |
phosphorylation
|
DCX |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250654 |
Ser28 |
SRMNGLPsPTHSAHC |
in vitro |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. These were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35 (Figure 3D). However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. | Therefore, S28 residue may be a substrate in vitro, but our best efforts failed to detect phosphorylation of S28 in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250655 |
Ser287 |
ATAGPKAsPTPQKTS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250658 |
Ser306 |
GPMRRSKsPADSGND |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250667 |
Ser332 |
STPKSKQsPISTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250673 |
Ser339 |
SPISTPTsPGSLRKH |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250656 |
Thr289 |
AGPKASPtPQKTSAK |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250659 |
Thr326 |
TSSSQLStPKSKQSP |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250660 |
Thr336 |
SKQSPIStPTSPGSL |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
In order to determine the sites of phosphorylation by Cdk5, serine or threonine in the nine potential sites were substituted with alanine by site-directed mutagenesis to create mutant Dcx proteins. hese were analyzed by co-transfection of 293T cells with cdk5/p35. All-sites-A mutant Dcx showed no slower migrating species on Western analysis, indicating that removal of all nine possible sites is sufficient to block the phosphorylation by Cdk5/p35. However, each single mutant Dcx retains the slower migrating species similar to the wild-type Dcx, suggesting that any single mutation is not sufficient to block phosphorylation by Cdk5/p35. |
|
| Publications: |
8 |
Organism: |
In Vitro, Homo Sapiens |
| + |
CDK5/CDK5R1 | up-regulates activity 
phosphorylation
|
DCX |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250657 |
Ser297 |
PQKTSAKsPGPMRRS |
Homo sapiens |
|
| pmid |
sentence |
| 14741103 |
We identified that Ser297 is the major phosphorylation site by Cdk5. Phosphorylation of this site occurs in human. | Mutation of Ser297 blocks the effect of Dcx on migration in a fashion similar to pharmacological inhibition of Cdk5 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | up-regulates activity
phosphorylation
|
DCX |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-170755 |
Ser332 |
STPKSKQsPISTPTS |
Homo sapiens |
|
| pmid |
sentence |
| 21159948 |
Gsk3b phosphorylates dcx at the distinct site of ser327 and thereby contributes to dcx function in the restriction of axon branching. Together, our data define a jip3-regulated gsk3_/dcx signaling pathway that restricts axon branching in the mammalian brain.Gsk3_ induces the phosphorylation of dcx at ser327, which contributes to dcx function in the inhibition of axon branching and self-contact. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | up-regulates activity
phosphorylation
|
DCX |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279217 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21477071 |
DCX phosphorylation by JNK1 is required for glioma suppression. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279228 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28701917 |
In addition, DCX can be phosphorylated by mitogen activated protein kinase 8 (MAPK8 and JNK1) at Thr321, Thr331, and Ser334 sites in humans with corresponding sites at Thr326, Thr336, and Ser339 in mouse. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GDNF | down-regulates quantity by repression 
transcriptional regulation
|
DCX |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252172 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 15212950 |
We characterize the network of 43 genes induced by GDNF overproduction of neuronal progenitor cells (ST14A), which mainly regulate migration and differentiation of neuronal progenitor cells. GDNF down-regulates doublecortin, Paf-ah1b (Lis1), dynamin, and a-tubulin, which are involved in neocortical lamination and cytoskeletal reorganization. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CHD8 | down-regulates quantity 
transcriptional regulation
|
DCX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268915 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 32839322 |
Many of the most significantly up-regulated genes in Chd8+/− and Chd8−/− NPCs are involved in later stages of neuronal development, including Ascl1 [a central driver of neural reprogramming (29)], Dcx, Map2, Nefm, Neurod4, and Neurog1 (Fig. 2 E and F). Additionally, we found that Sox3 is derepressed in both Chd8+/− and Chd8−/− NPCs, and several other Sox TF members (Sox2, Sox7, and Sox11) became derepressed in the Chd8−/− cells |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
4.0
DCX
- 
- 