| + |
NEK9 | up-regulates activity 
phosphorylation
|
NEK7 |
0.701 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103030 |
Ser195 |
SKTTAAHsLVGTPYY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12840024 |
Nercc1 catalyzes the phosphorylation of nek6 (ser206) and the equivalent site on nek7 (ser195), resulting in a 20-25-fold activation of nek6/7 kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK9 | up-regulates activity
phosphorylation
|
NEK6 |
0.675 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102996 |
Ser206 |
SETTAAHsLVGTPYY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12840024 |
Nercc1/nek9 activates the nek6 and nek7 kinases. Nercc1 catalyzes the direct phosphorylation of prokaryotic recombinant nek6 at ser206 in vitro concomitant with 20-25-fold activation of nek6 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK9 | up-regulates activity
phosphorylation
|
NEDD1 |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263016 |
Ser377 |
EKAGLPRsINTDTLS |
in vitro |
|
| pmid |
sentence |
| 22818914 |
Nek9 phosphorylates NEDD1 on Ser377 driving its recruitment and thereby that of γ-tubulin to the centrosome in mitotic cells. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NEK9 | up-regulates
phosphorylation
|
NEK9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173026 |
Ser944 |
GQQVGMHsKGTQTAK |
Homo sapiens |
|
| pmid |
sentence |
| 21454704 |
We find that the interaction of lc8 with nek9 depends on a (k/r)xtqt motif adjacent to the nek9 c-terminal coiled coil motif, results in nek9 multimerization, and increases the rate of nek9 autoactivation. Lc8 binding to nek9 is regulated by nek9 activity through the autophosphorylation of ser(944), a residue immediately n-terminal to the (k/r)xtqt motif. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119897 |
Thr210 |
SEYSMAEtLVGTPYY |
Homo sapiens |
|
| pmid |
sentence |
| 14660563 |
A previous study (19) using the peptide substrate demonstrated that nek9 was able to phosphorylate in vitro the thr210 residue within the activation loop, thus indicating the potential ability of nek9 to autophosphorylate.Nek9 forms a stable, approximately 600-kda complex with fact in the interphase nuclei. Its active form is characterized by phosphorylation-dependent electrophoretic mobility shift and phosphorylation at a conserved residue within the activation loop (thr(210)) |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates activity
phosphorylation
|
NEK9 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273889 |
Thr210 |
SEYSMAEtLVGTPYY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21642957 |
We now identify Plk1 as Nek9 direct activator and propose a two-step activation mechanism that involves Nek9 sequential phosphorylation by CDK1 and Plk1. while CDK1 activity is necessary for Nek9 phosphorylation in mitosis and the resulting change in electrophoretical mobility, Nek9 Thr210 phosphorylation and mitotic activation requires both CDK1 and Plk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates activity
phosphorylation
|
NEK9 |
0.593 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273888 |
Thr210 |
SEYSMAEtLVGTPYY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21642957 |
We now identify Plk1 as Nek9 direct activator and propose a two-step activation mechanism that involves Nek9 sequential phosphorylation by CDK1 and Plk1. while CDK1 activity is necessary for Nek9 phosphorylation in mitosis and the resulting change in electrophoretical mobility, Nek9 Thr210 phosphorylation and mitotic activation requires both CDK1 and Plk1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK9 | down-regulates activity 
phosphorylation
|
MAP1LC3B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273904 |
Thr50 |
QLPVLDKtKFLVPDH |
in vitro |
|
| pmid |
sentence |
| 31857374 |
LC3B is phosphorylated at Thr-50 within the LDS by serine/threonine kinase (STK) 3 and STK4. Here, we identified LIR motifs in STK3 and atypical protein kinase Cζ (PKCζ) and never in mitosis A (NIMA)-related kinase 9 (NEK9). All three kinases phosphorylated LC3B Thr-50 in vitro A phospho-mimicking substitution of Thr-50 impaired binding of several LIR-containing proteins, such as ATG4B, FYVE, and coiled-coil domain-containing 1 (FYCO1), and autophagy cargo receptors p62/sequestosome 1 (SQSTM1) and neighbor of BRCA1 gene (NBR1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
dabrafenib | down-regulates activity
chemical inhibition
|
NEK9 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261072 |
|
|
Homo sapiens |
1205-Lu Cell |
| pmid |
sentence |
| 29112787 |
We have identified dabrafenib as a potent inhibitor of NEK9 and CDK16, and our studies suggest that inhibition of these kinases may have activity against cancers that do not harbor BRAF mutations. We confirmed NEK9 to be a potent target of dabrafenib by in vitro kinase assays, with inhibition of NEK9 observed in the single-digit nanomolar range. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NEK9
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