| + |
NEK6 | up-regulates activity 
phosphorylation
|
KIF11 |
0.457 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273886 |
Ser1033 |
GINTLERsKVEETTE |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 19001501 |
Nek6 phosphorylated Eg5 at several sites in vitro and one of these sites, Ser1033, is phosphorylated in vivo during mitosis. Whereas CDK1 phosphorylates nearly all Eg5 at Thr926 during mitosis, Nek6 phosphorylates approximately 3% of Eg5, primarily at the spindle poles. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK6 | up-regulates activity
phosphorylation
|
EML4 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273883 |
Ser144 |
QSPQIRAsPSPQPSS |
in vitro |
|
| pmid |
sentence |
| 31409757 |
The mitotic kinases NEK6 and NEK7 phosphorylated the EML4 N-terminal domain at Ser144 and Ser146 in vitro, and depletion of these kinases in cells led to increased EML4 binding to microtubules in mitosis. An S144A-S146A double mutant not only bound inappropriately to mitotic microtubules but also increased their stability and interfered with chromosome congression. In addition, constitutive activation of NEK6 or NEK7 reduced the association of EML4 with interphase microtubules. Together, these data support a model in which NEK6- and NEK7-dependent phosphorylation promotes the dissociation of EML4 from microtubules in mitosis in a manner that is required for efficient chromosome congression. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NEK6 | up-regulates activity
phosphorylation
|
ACD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264424 |
Ser169 |
SNAGLSLsQLLDEMR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 27396482 |
NEK6-mediated phosphorylation of human TPP1 regulates telomere length through telomerase recruitment|Shelterin component TPP1 plays critical roles in chromosome end protection and telomere length regulation. Specifically, TPP1 contains an OB-fold domain that provides an interface to recruit telomerase.| |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK9 | up-regulates activity
phosphorylation
|
NEK6 |
0.676 |
| 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 |
| + |
NEK6 | down-regulates activity 
phosphorylation
|
KIF20A |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273891 |
Ser244 |
LSTSLKRsVYIESRI |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 28630147 |
We show that Nek9, Nek6, and the kinesin Mklp2 form a signaling module, which is required for Mklp2 to localize to the central spindle in anaphase. Nek6 also phosphorylates Mklp2 at Ser244, inhibiting its bundling activity until anaphase onset. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK6 | up-regulates activity
phosphorylation
|
PSMD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273894 |
Ser361 |
ENNRFGGsGSQVDSA |
in vitro |
|
| pmid |
sentence |
| 31843888 |
Seven of these kinases (PIM1/2/3, MAP4K1/2, PKA, and NEK6) directly and robustly phosphorylated recombinant GST-Rpn1 at S361 in vitro (Fig. 3D and SI Appendix, Fig. S3 A and B). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NEK6 | down-regulates activity
phosphorylation
|
BSG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273882 |
Ser368 |
GSAPLKSsGQHQNDK |
Homo sapiens |
|
| pmid |
sentence |
| 31016558 |
These results indicate that NEK6 directly interacts with CD147 and phosphorylates the protein at serine-252 in Huh-7 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NEK6 | up-regulates activity
phosphorylation
|
SGK1 |
0.344 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262954 |
Ser377 |
PPFNPNVsGPNDLRH |
in vitro |
|
| pmid |
sentence |
| 12023960 |
In contrast, we demonstrate for the first time that NEK6 phosphorylates SGK1 efficiently at its hydrophobic motif in vitro and peptide-mapping analysis indicates that this is the major site of phosphorylation (Fig 3). Ser377 is a more minor site of phosphorylation located in the kinase domain of SGK1, which has not been reported to undergo phosphorylation previously. the phosphorylation of the hydrophobic motif of SGK1 in vitro, coupled with the phosphorylation of the T-loop with PDK1, may be a useful way of generating fully active wild type SGK1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250296 |
Ser377 |
PPFNPNVsGPNDLRH |
in vitro |
|
| pmid |
sentence |
| 12023960 |
The present study is the first report of a protein kinase (NEK6) capable of phosphorylating the hydrophobic motif of SGK1, although our data suggest that NEK6 may not mediate this reaction in cells. Nevertheless, the phosphorylation of the hydrophobic motif of SGK1in vitro, coupled with the phosphorylation of the T-loop with PDK1, may be a useful way of generating fully active wild type SGK1. Ser377 and Ser422of SGK1, and the CDK7 T-loop peptide, which are phosphorylated by NEK6. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250297 |
Ser422 |
AEAFLGFsYAPPTDS |
in vitro |
|
| pmid |
sentence |
| 12023960 |
The present study is the first report of a protein kinase (NEK6) capable of phosphorylating the hydrophobic motif of SGK1, although our data suggest that NEK6 may not mediate this reaction in cells. Nevertheless, the phosphorylation of the hydrophobic motif of SGK1in vitro, coupled with the phosphorylation of the T-loop with PDK1, may be a useful way of generating fully active wild type SGK1. Ser377 and Ser422of SGK1, and the CDK7 T-loop peptide, which are phosphorylated by NEK6. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
NEK6 | up-regulates activity
phosphorylation
|
RPS6KB1 |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262953 |
Ser403 |
DDSTLSEsANQVFLG |
in vitro |
|
| pmid |
sentence |
| 12023960 |
Here we demonstrate that in addition to phosphorylating S6K1 and SGK1 at their hydrophobic motif, NEK6 also phosphorylates S6K1 at two other sites and phosphorylates SGK1 at one other site in vitro. Analysis of the peptides phosphorylated by NEK6 (Fig 2), performed in the present study has confirmed this, and identified two novel sites on S6K1 (Ser53 and Ser403) as major sites of NEK6 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262952 |
Ser53 |
EGGQLNEsMDHGGVG |
in vitro |
|
| pmid |
sentence |
| 12023960 |
Here we demonstrate that in addition to phosphorylating S6K1 and SGK1 at their hydrophobic motif, NEK6 also phosphorylates S6K1 at two other sites and phosphorylates SGK1 at one other site in vitro. Analysis of the peptides phosphorylated by NEK6 (Fig 2), performed in the present study has confirmed this, and identified two novel sites on S6K1 (Ser53 and Ser403) as major sites of NEK6 phosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
NEK6 | down-regulates activity
phosphorylation
|
NUP98 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273892 |
Ser608 |
VLKNLNNsNLFSPVN |
in vitro |
|
| pmid |
sentence |
| 21335236 |
To elucidate which of the identified sites can be targeted by CDK1/cyclin B1 and Nek6 in vitro (Figure S1D), we performed phosphorylation reactions using recombinant kinases and unlabeled ATP followed by phosphopeptide mapping (Table S1). MS analysis confirmed phosphorylation of S591 and S822 by Nek6 as well as phosphorylation of T529, T536, S595, S606, and T653 by CDK1. Phosphomimetic Mutants of Nup98 Show Defects in NPC Localization |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273893 |
Ser839 |
TSRCLIKsPDRLADI |
in vitro |
|
| pmid |
sentence |
| 21335236 |
To elucidate which of the identified sites can be targeted by CDK1/cyclin B1 and Nek6 in vitro (Figure S1D), we performed phosphorylation reactions using recombinant kinases and unlabeled ATP followed by phosphopeptide mapping (Table S1). MS analysis confirmed phosphorylation of S591 and S822 by Nek6 as well as phosphorylation of T529, T536, S595, S606, and T653 by CDK1. Phosphomimetic Mutants of Nup98 Show Defects in NPC Localization |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
NEK6 | up-regulates activity
phosphorylation
|
STAT3 |
0.339 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273902 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20595392 |
Our data also show that NEK6 interacts with STAT3, an oncogenic transcription factor, and phosphorylates STAT3 on Ser(727), which is important for transcriptional activation. These results demonstrate that NEK6 interacts with and phosphorylates STAT3, an event that could play an important role in oncogenesis. For the maximal activation of STAT3 signaling, phosphorylation of both Tyr705 and Ser727 is required. Phosphorylation of Tyr705 induces dimerization, nuclear translocation, and DNA binding of the STAT3 protein, whereas phosphorylation of Ser727 is important for transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273901 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20595392 |
Our data also show that NEK6 interacts with STAT3, an oncogenic transcription factor, and phosphorylates STAT3 on Ser(727), which is important for transcriptional activation. These results demonstrate that NEK6 interacts with and phosphorylates STAT3, an event that could play an important role in oncogenesis. For the maximal activation of STAT3 signaling, phosphorylation of both Tyr705 and Ser727 is required. Phosphorylation of Tyr705 induces dimerization, nuclear translocation, and DNA binding of the STAT3 protein, whereas phosphorylation of Ser727 is important for transcriptional activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
NEK6 | up-regulates activity
phosphorylation
|
HSPA1A |
0.436 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273885 |
Thr66 |
VALNPQNtVFDAKRL |
in vitro |
|
| pmid |
sentence |
| 30108182 |
Mitotic phosphorylation of Hsp72 by the kinase NEK6 at Thr66 located in the NBD promotes the localization of Hsp72 to the mitotic spindle and is required for efficient spindle assembly and chromosome congression and segregation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
NEK6
- 
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