| + |
MAPK1 | up-regulates activity 
phosphorylation
|
NDE1 |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249421 |
Ser239 |
FRRGLDDsTGGTPLT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12556484 |
Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro. In the case of Nudel, the phosphorylation sites were also located in the S/TP motifs. Detailed mutagenesis study indicated that T219, S242, and T245 were phosphorylated by Cdc2, while T219 and T245 were phosphorylated by Erk2.|Phosphorylation of Nudel in M phase appears to positively modulate dynein motor activity. Both phosphorylated and unphosphorylated forms of Nudel were transported by dynein (Fig. 7 and 9 and data not shown), indicating that neither of them inactivated the dynein motor. On the other hand, both phospho-Nudel and Nudelpmt5 bound Lis1 more strongly than Nudel or Nudelmt5 did |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249422 |
Thr215 |
ATGSVPStPIAHRGP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12556484 |
Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro. In the case of Nudel, the phosphorylation sites were also located in the S/TP motifs. Detailed mutagenesis study indicated that T219, S242, and T245 were phosphorylated by Cdc2, while T219 and T245 were phosphorylated by Erk2.|Phosphorylation of Nudel in M phase appears to positively modulate dynein motor activity. Both phosphorylated and unphosphorylated forms of Nudel were transported by dynein (Fig. 7 and 9 and data not shown), indicating that neither of them inactivated the dynein motor. On the other hand, both phospho-Nudel and Nudelpmt5 bound Lis1 more strongly than Nudel or Nudelmt5 did |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274078 |
|
|
in vitro |
|
| pmid |
sentence |
| 12556484 |
We found that Nudel and NudE were also phosphorylated in M phase (Fig. (Fig.22 and and3).3). First, Nudel and NudE were specifically phosphorylated in M phase. Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro.Due to conservation of the S/TP motifs, NudE may also be phosphorylated at similar sites by these kinases, though it contains an additional potential Cdk site at S282 (SPNR). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens, In Vitro |
| + |
CyclinB/CDK1 | up-regulates quantity by stabilization
phosphorylation
|
NDE1 |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274083 |
Ser282 |
RNLVYDQsPNRTGGP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16682949 |
Here, we demonstrate that Su48 can associate with Nde1. Moreover, we found that Nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative Cdc2 phosphorylation sites in Nde1 and found that alteration of these sites diminishes phosphorylation by Cdc2 in vitro and affects the stability of Su48-Nde1 interactions and the centrosomal localization of Nde1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274087 |
Thr191 |
QKQEKPRtPMPSSVE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16682949 |
Here, we demonstrate that Su48 can associate with Nde1. Moreover, we found that Nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative Cdc2 phosphorylation sites in Nde1 and found that alteration of these sites diminishes phosphorylation by Cdc2 in vitro and affects the stability of Su48-Nde1 interactions and the centrosomal localization of Nde1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274082 |
Thr215 |
ATGSVPStPIAHRGP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16682949 |
Here, we demonstrate that Su48 can associate with Nde1. Moreover, we found that Nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative Cdc2 phosphorylation sites in Nde1 and found that alteration of these sites diminishes phosphorylation by Cdc2 in vitro and affects the stability of Su48-Nde1 interactions and the centrosomal localization of Nde1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274085 |
Thr228 |
GPSSSLNtPGSFRRG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16682949 |
Here, we demonstrate that Su48 can associate with Nde1. Moreover, we found that Nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative Cdc2 phosphorylation sites in Nde1 and found that alteration of these sites diminishes phosphorylation by Cdc2 in vitro and affects the stability of Su48-Nde1 interactions and the centrosomal localization of Nde1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274084 |
Thr243 |
LDDSTGGtPLTPAAR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16682949 |
Here, we demonstrate that Su48 can associate with Nde1. Moreover, we found that Nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative Cdc2 phosphorylation sites in Nde1 and found that alteration of these sites diminishes phosphorylation by Cdc2 in vitro and affects the stability of Su48-Nde1 interactions and the centrosomal localization of Nde1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274086 |
Thr246 |
STGGTPLtPAARISA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16682949 |
Here, we demonstrate that Su48 can associate with Nde1. Moreover, we found that Nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative Cdc2 phosphorylation sites in Nde1 and found that alteration of these sites diminishes phosphorylation by Cdc2 in vitro and affects the stability of Su48-Nde1 interactions and the centrosomal localization of Nde1. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
PRKACA | up-regulates
phosphorylation
|
NDE1 |
0.373 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174410 |
Thr131 |
LERAKRAtIMSLEDF |
Homo sapiens |
|
| pmid |
sentence |
| 21677187 |
Here, we demonstrate that disc1 and pde4 modulate nde1 phosphorylation by camp-dependent protein kinase a (pka) and identify a novel pka substrate site on nde1 at threonine-131 (t131).Since phosphorylated t131 is detectable at multiple subcellular locations (centrosome, nucleus, postsynaptic density, proximal axon), there is potential for disc1/pde4 to influence several important brain processes that critically depend on the nde1/ndel1/lis1 comple |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CDK1 | up-regulates
phosphorylation
|
NDE1 |
0.64 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146734 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16682949 |
We found that nde1 is subjected to phosphorylation in vivo. In particular, we identified six putative cdc2 phosphorylation sites in nde1 and found that alteration of these sites diminishes phosphorylation by cdc2 in vitro and affects the stability of su48-nde1 interactions and the centrosomal localization of nde1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates activity
phosphorylation
|
NDE1 |
0.64 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274077 |
|
|
in vitro |
|
| pmid |
sentence |
| 12556484 |
We found that Nudel and NudE were also phosphorylated in M phase (Fig. (Fig.22 and and3).3). First, Nudel and NudE were specifically phosphorylated in M phase. Moreover, both proteins were phosphorylated by Cdc2 and Erk2 in vitro.Due to conservation of the S/TP motifs, NudE may also be phosphorylated at similar sites by these kinases, though it contains an additional potential Cdk site at S282 (SPNR). |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
NDE1
- 
- 