| + |
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 |
| + |
TUBGCP6 | form complex 
binding
|
g-TuRC complex |
0.775 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262330 |
|
|
in vitro |
|
| pmid |
sentence |
| 31862189 |
Here, we present a cryo-EM reconstruction of the native human gamma-TuRC at 3.8A resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the gamma-TuRC “seam.” |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
TUBGCP6
- 
- 