| + |
CDK5 | up-regulates activity 
phosphorylation
|
NDEL1 |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250675 |
Ser198 |
TRKSAPSsPTLDCEK |
Mus musculus |
Brain |
| pmid |
sentence |
| 12796778 |
Three specific phosphorylation sites (Ser198, Thr219 and Ser231) and two weak phosphorylation sites (Ser242 and Thr245) for CDK5/p35 are located in this region of NUDEL | Each single or double mutant compromised,and the triple mutant completely eliminated, interaction with 14-3-3ε. | 14-3-3ε sustains NUDEL phosphorylation and protects it from phosphatase.e dynein motor function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250676 |
Ser231 |
GTENTFPsPKAIPNG |
Mus musculus |
|
| pmid |
sentence |
| 12796778 |
Three specific phosphorylation sites (Ser198, Thr219 and Ser231) and two weak phosphorylation sites (Ser242 and Thr245) for CDK5/p35 are located in this region of NUDEL | Each single or double mutant compromised,and the triple mutant completely eliminated, interaction with 14-3-3ε. | 14-3-3ε sustains NUDEL phosphorylation and protects it from phosphatase.e dynein motor function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250677 |
Ser242 |
IPNGFGTsPLTPSAR |
Mus musculus |
Brain |
| pmid |
sentence |
| 12796778 |
Three specific phosphorylation sites (Ser198, Thr219 and Ser231) and two weak phosphorylation sites (Ser242 and Thr245) for CDK5/p35 are located in this region of NUDEL | Each single or double mutant compromised,and the triple mutant completely eliminated, interaction with 14-3-3ε. | 14-3-3ε sustains NUDEL phosphorylation and protects it from phosphatase.e dynein motor function. |
|
| Publications: |
3 |
Organism: |
Mus Musculus |
| + |
CDK1 | up-regulates activity
phosphorylation
|
NDEL1 |
0.646 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274073 |
Ser242 |
IPNGFGTsPLTPSAR |
in vitro |
|
| pmid |
sentence |
| 12556484 |
In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274074 |
Thr219 |
ASLSLPAtPVGKGTE |
in vitro |
|
| pmid |
sentence |
| 12556484 |
In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274072 |
Thr245 |
GFGTSPLtPSARISA |
in vitro |
|
| pmid |
sentence |
| 12556484 |
In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
AURKA | down-regulates quantity by destabilization 
phosphorylation
|
NDEL1 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263159 |
Ser251 |
LTPSARIsALNIVGD |
Mus musculus |
|
| pmid |
sentence |
| 17060449 |
Here, we show that Aurora-A phosphorylates NDEL1 at Ser251 at the beginning of mitotic entry. Interestingly, NDEL1 phosphorylated by Aurora-A was rapidly downregulated thereafter by ubiquitination-mediated protein degradation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PPP4C | down-regulates activity
dephosphorylation
|
NDEL1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248550 |
Thr219 |
ASLSLPAtPVGKGTE |
Homo sapiens |
|
| pmid |
sentence |
| 18347064 |
Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and microtubule organization via NDEL1 dephosphorylation|PP4c selectively dephosphorylates NDEL1 at Cdk1 sites. We also demonstrate that PP4c negatively regulates Cdk1 activity at the centrosome.|We next examined the ability of PP4c to dephosphorylate a Cdk1 phosphorylation site, phospho-T219 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5/CDK5R1 | up-regulates activity
phosphorylation
|
NDEL1 |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250678 |
Thr219 |
ASLSLPAtPVGKGTE |
Mus musculus |
Brain |
| pmid |
sentence |
| 12796778 |
Three specific phosphorylation sites (Ser198, Thr219 and Ser231) and two weak phosphorylation sites (Ser242 and Thr245) for CDK5/p35 are located in this region of NUDEL | Each single or double mutant compromised,and the triple mutant completely eliminated, interaction with 14-3-3ε. | 14-3-3ε sustains NUDEL phosphorylation and protects it from phosphatase.e dynein motor function. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
NDEL1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274076 |
Thr219 |
ASLSLPAtPVGKGTE |
in vitro |
|
| pmid |
sentence |
| 12556484 |
In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-274075 |
Thr245 |
GFGTSPLtPSARISA |
in vitro |
|
| pmid |
sentence |
| 12556484 |
In this case, only NudelS2 and NudelS5 were phosphorylated. Therefore, T219, S242, and T245 of Nudel were phosphorylation sites of Cdc2 in vitro. In contrast, Erk2 only phosphorylated T219 and T245. These two sites, with surrounding sequences such as PATP from residues 217 to 220 and PLTP from 243 to 246, respectively, are indeed typical MAPK sites |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CyclinD1/CDK6 | up-regulates activity
phosphorylation
|
NDEL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250652 |
Thr245 |
GFGTSPLtPSARISA |
Mus musculus |
Brain |
| pmid |
sentence |
| 12796778 |
Three specific phosphorylation sites (Ser198, Thr219 and Ser231) and two weak phosphorylation sites (Ser242 and Thr245) for CDK5/p35 are located in this region of NUDEL | Each single or double mutant compromised,and the triple mutant completely eliminated, interaction with 14-3-3ε. | 14-3-3ε sustains NUDEL phosphorylation and protects it from phosphatase.e dynein motor function. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PAFAH1B1 | up-regulates activity
binding
|
NDEL1 |
0.838 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252157 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 11163259 |
We demonstrate that LIS1 directly interacts with the cytoplasmic dynein heavy chain (CDHC) and NUDEL. LIS1 is required for the proper distribution of NUDEL and cellular components regulated by CDHC function. Reduction of LIS1 leads to mislocalization of NUDEL, CDHC, β-tubulin, and the Golgi complex |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
NDEL1 | up-regulates activity
binding
|
DYNC1H1 |
0.709 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252159 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 11163259 |
LIS1 specifically binds the P1 loop domain of CDHC, while NUDEL binds the C-terminal region as well as a distinct binding site in the P1 loop domain. LIS1 and NUDEL regulate CDHC localization and motor function. Reduction of LIS1 leads to mislocalization of NUDEL, CDHC, β-tubulin, and the Golgi complex |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
DISC1 | up-regulates activity
binding
|
NDEL1 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252162 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17202468 |
Disrupted-In-Schizophrenia 1 (DISC1) is a candidate gene for susceptibility to schizophrenia. DISC1 is reported to interact with NudE-like (NUDEL), which forms a complex with lissencephaly-1 (LIS1) and 14-3-3ε. 14-3-3ε is involved in the proper localization of NUDEL and LIS1 in axons. the association with NUDEL and LIS1 supports the notion that DISC1 contributes to the neuronal development and morphology |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAE | up-regulates activity
binding
|
NDEL1 |
0.652 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252160 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17202468 |
14-3-3epsilon is involved in the proper localization of NUDEL and LIS1 in axons. 14-3-3ε binds to NUDEL phosphorylated by cyclin-dependent kinase (cdk5) and maintains NUDEL phosphorylation. Deficiency of 14-3-3ε causes mislocalization of the NUDEL/LIS1 complex from axons, suggesting that 14-3-3ε regulates the axonal targeting of the NUDEL/LIS1 complex by sustaining NUDEL phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NDEL1
- 
- 