+ |
NEK7 | up-regulates activity
phosphorylation
|
KIF11 |
0.418 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273890 |
Ser1033 |
GINTLERsKVEETTE |
Mus musculus |
Neuron |
pmid |
sentence |
29899413 |
NEK7 regulates these processes in part through phosphorylation of the kinesin Eg5/KIF11, promoting its accumulation on microtubules in distal dendrites. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
NEK7 | up-regulates quantity by stabilization
phosphorylation
|
TERF1 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273903 |
Ser114 |
AIIHGLSsLTACQLR |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
28216227 |
Mechanistically, Nek7 interacts with and phosphorylates TRF1 on Ser114, which prevents TRF1 from binding to Fbx4, an Skp1-Cul1-F box E3 ligase subunit, thereby alleviating proteasomal degradation of TRF1, leading to a stable association of TRF1 with Tin2 to form a shelterin complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEK7 | up-regulates activity
phosphorylation
|
KIF14 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266420 |
Ser1217 |
PIKNLHSsHSSGLMD |
Homo sapiens |
HEL Cell |
pmid |
sentence |
28630147 |
Nek7 direct phosphorylation is required for the anaphase localization of Kif14. we generated an EGFP-Kif14-5A construct in which Ser56, Ser607, Ser1217, Ser1219, and Ser1220 were all mutated to Ala. When transfected into HeLa cells, EGFP-Kif14-5A was expressed to similar levels as WT Kif14 (Fig. S3 C), but its localization to the central spindle in anaphase cells was completely abolished (Fig. 6 C). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266419 |
Ser1219 |
KNLHSSHsSGLMDKS |
Homo sapiens |
HEL Cell |
pmid |
sentence |
28630147 |
Nek7 direct phosphorylation is required for the anaphase localization of Kif14. we generated an EGFP-Kif14-5A construct in which Ser56, Ser607, Ser1217, Ser1219, and Ser1220 were all mutated to Ala. When transfected into HeLa cells, EGFP-Kif14-5A was expressed to similar levels as WT Kif14 (Fig. S3 C), but its localization to the central spindle in anaphase cells was completely abolished (Fig. 6 C). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266418 |
Ser1220 |
NLHSSHSsGLMDKSS |
Homo sapiens |
HEL Cell |
pmid |
sentence |
28630147 |
Nek7 direct phosphorylation is required for the anaphase localization of Kif14. we generated an EGFP-Kif14-5A construct in which Ser56, Ser607, Ser1217, Ser1219, and Ser1220 were all mutated to Ala. When transfected into HeLa cells, EGFP-Kif14-5A was expressed to similar levels as WT Kif14 (Fig. S3 C), but its localization to the central spindle in anaphase cells was completely abolished (Fig. 6 C). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266416 |
Ser56 |
NDDPLLRsAGKVRDI |
Homo sapiens |
HEL Cell |
pmid |
sentence |
28630147 |
Nek7 direct phosphorylation is required for the anaphase localization of Kif14. we generated an EGFP-Kif14-5A construct in which Ser56, Ser607, Ser1217, Ser1219, and Ser1220 were all mutated to Ala. When transfected into HeLa cells, EGFP-Kif14-5A was expressed to similar levels as WT Kif14 (Fig. S3 C), but its localization to the central spindle in anaphase cells was completely abolished (Fig. 6 C). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266417 |
Ser607 |
NLIDLAGsERCSTAH |
Homo sapiens |
HEL Cell |
pmid |
sentence |
28630147 |
Nek7 direct phosphorylation is required for the anaphase localization of Kif14. we generated an EGFP-Kif14-5A construct in which Ser56, Ser607, Ser1217, Ser1219, and Ser1220 were all mutated to Ala. When transfected into HeLa cells, EGFP-Kif14-5A was expressed to similar levels as WT Kif14 (Fig. S3 C), but its localization to the central spindle in anaphase cells was completely abolished (Fig. 6 C). |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
NEK7 | up-regulates activity
phosphorylation
|
EML4 |
0.277 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273884 |
Ser146 |
PQIRASPsPQPSSQP |
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 |
+ |
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 |