| + |
PLK4 | up-regulates activity 
phosphorylation
|
TUBGCP6 |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262900 |
Ser1060 |
HGHVSDAsIRVGENV |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262901 |
Ser1087 |
HGHVSNAsISLGESV |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262902 |
Ser1114 |
HGHVSNAsIRVGENV |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262903 |
Ser1168 |
HGHVSDAsISLGESV |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262904 |
Ser1176 |
ISLGESVsDMAPARP |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262905 |
Ser1195 |
HGHVSDAsISLGESV |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262906 |
Ser1249 |
HGHVSDAsISLGEPV |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262907 |
Ser1437 |
RYPDSYEsMSEPPIA |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262908 |
Ser1465 |
PVDPQVQsAADETAV |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262909 |
Ser392 |
VSGASPEsISSLLSE |
in vitro |
|
| pmid |
sentence |
| 22302995 |
Plk4 interacts with and phosphorylates GCP6. we show that GCP6 is an integral component of the centriole and required for centriole duplication. Moreover, we find that GCP6 interacts in vitro and in vivo with Plk4. We show that phosphorylation of GCP6 by Plk4 is required for Plk4-induced centriole overduplication. |
|
| Publications: |
10 |
Organism: |
In Vitro |
| + |
PLK4 | down-regulates activity 
phosphorylation
|
FBXW5 |
0.56 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275476 |
Ser151 |
SQFNKDDsLLLASGV |
|
|
| pmid |
sentence |
| 21725316 |
The activity of SCF-FBXW5 is in turn negatively regulated by Polo-like kinase 4 (PLK4), which phosphorylates FBXW5 at Ser 151 to suppress its ability to ubiquitylate HsSAS-6. |
|
| Publications: |
1 |
| + |
PLK4 | up-regulates
phosphorylation
|
PLK4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162559 |
Ser305 |
SSTSISGsLFDKRRL |
Homo sapiens |
|
| pmid |
sentence |
| 20032307 |
Autophosphorylation probably plays a role in the process of centriole duplication, because mimicking s305 phosphorylation enhances the ability of overexpressed plk4 to induce centriole amplification. Importantly, we show that s305-phosphorylated plk4 is specifically sequestered at the centrosome contrary to the nonphosphorylated form. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK4 | up-regulates activity
phosphorylation
|
NEDD1 |
0.577 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272996 |
Ser325 |
PTTVNKRsVNVNAAS |
|
|
| pmid |
sentence |
| 33351100 |
We found that PLK4-mediated phosphorylation of NEDD1 at its S325 amino acid residue directly promotes both NEDD1 binding to SAS-6 and recruiting SAS-6 to the centrosome. |Collectively, our results demonstrate that PLK4-regulated NEDD1 facilitates initiation of the cartwheel assembly and of daughter centriole biogenesis in mammals. |
|
| Publications: |
1 |
| + |
PLK4 | up-regulates
phosphorylation
|
CENPJ |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166007 |
Ser595 |
ISFSSNSsFVLKILE |
Homo sapiens |
|
| pmid |
sentence |
| 20531387 |
Plk2 phosphorylates the s589 and s595 residues of cpap in vitro and in vivo. This phosphorylation is critical for procentriole formation during the centrosome cycle. Plk4 also phosphorylates s595 of cpap |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PLK4
- 
- 