| + |
CDK1 | up-regulates activity 
phosphorylation
|
NINL |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259830 |
Ser185 |
NRHSPSWsPDGRRRQ |
Homo sapiens |
|
| pmid |
sentence |
| 20890132 |
In this study, we show that Nlp can be phosphorylated by cell cycle protein kinase Cdc2/cyclin B1. The phosphorylation sites of Nlp are mapped at Ser185 and Ser589. Interestingly, the Cdc2/cyclin B1 phosphorylation site Ser185 of Nlp is required for its recognition by PLK1, which enable Nlp depart from centrosomes to allow the establishment of a mitotic scaffold at the onset of mitosis . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKB | up-regulates
phosphorylation
|
NINL |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168045 |
Ser185 |
WDSEDFGsPQKSCSP |
Homo sapiens |
|
| pmid |
sentence |
| 20864540 |
Importantly, nlp is characterized as a novel substrate of aurora b and can be phosphorylated by aurora b. The specific phosphorylation sites are mapped at ser-185, ser-448, and ser-585. The phosphorylation at ser-448 and ser-585 is likely required for nlp association with aurora b and localization at midbody. Meanwhile, the phosphorylation at ser-185 is vital to nlp protein stability. Disruptions of these phosphorylation sites abolish cytokinesis and lead to chromosomal instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168049 |
Ser448 |
QGYRERLsLLRSEVE |
Homo sapiens |
|
| pmid |
sentence |
| 20864540 |
Importantly, nlp is characterized as a novel substrate of aurora b and can be phosphorylated by aurora b. The specific phosphorylation sites are mapped at ser-185, ser-448, and ser-585. The phosphorylation at ser-448 and ser-585 is likely required for nlp association with aurora b and localization at midbody. Meanwhile, the phosphorylation at ser-185 is vital to nlp protein stability. Disruptions of these phosphorylation sites abolish cytokinesis and lead to chromosomal instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168053 |
Ser585 |
RLPKNRHsPSWSPDG |
Homo sapiens |
|
| pmid |
sentence |
| 20864540 |
Importantly, nlp is characterized as a novel substrate of aurora b and can be phosphorylated by aurora b. The specific phosphorylation sites are mapped at ser-185, ser-448, and ser-585. The phosphorylation at ser-448 and ser-585 is likely required for nlp association with aurora b and localization at midbody. Meanwhile, the phosphorylation at ser-185 is vital to nlp protein stability. Disruptions of these phosphorylation sites abolish cytokinesis and lead to chromosomal instability. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates quantity by destabilization 
phosphorylation
|
NINL |
0.397 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259831 |
Ser589 |
NRHSPSWsPDGRRRQ |
Homo sapiens |
|
| pmid |
sentence |
| 20890132 |
In this study, we show that Nlp can be phosphorylated by cell cycle protein kinase Cdc2/cyclin B1. The phosphorylation sites of Nlp are mapped at Ser185 and Ser589. the phosphorylation at the site Ser589 by Cdc2/cyclin B1 plays an important role in Nlp protein stability probably due to its effect on protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | down-regulates activity
phosphorylation
|
NINL |
0.688 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103348 |
Ser686 |
LEELHEKsQEVIWGL |
in vitro |
|
| pmid |
sentence |
| 12852856 |
Here, we identify a centrosomal plk1 substrate, termed nlp (ninein-like protein), whose properties suggest an important role in microtubule organization. Nlp interacts with two components of the gamma-tubulin ring complex and stimulates microtubule nucleation. Plk1 phosphorylates nlp and disrupts both its centrosome association and its gamma-tubulin interaction |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103352 |
Ser87 |
VRPSDEDsSSLESAA |
in vitro |
|
| pmid |
sentence |
| 12852856 |
Here, we identify a centrosomal plk1 substrate, termed nlp (ninein-like protein), whose properties suggest an important role in microtubule organization. Nlp interacts with two components of the gamma-tubulin ring complex and stimulates microtubule nucleation. Plk1 phosphorylates nlp and disrupts both its centrosome association and its gamma-tubulin interaction |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103356 |
Ser88 |
RPSDEDSsSLESAAS |
in vitro |
|
| pmid |
sentence |
| 12852856 |
Here, we identify a centrosomal plk1 substrate, termed nlp (ninein-like protein), whose properties suggest an important role in microtubule organization. Nlp interacts with two components of the gamma-tubulin ring complex and stimulates microtubule nucleation. Plk1 phosphorylates nlp and disrupts both its centrosome association and its gamma-tubulin interaction |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103364 |
Thr161 |
SDEEAEStKEAQNEL |
in vitro |
|
| pmid |
sentence |
| 12852856 |
Here, we identify a centrosomal plk1 substrate, termed nlp (ninein-like protein), whose properties suggest an important role in microtubule organization. Nlp interacts with two components of the gamma-tubulin ring complex and stimulates microtubule nucleation. Plk1 phosphorylates nlp and disrupts both its centrosome association and its gamma-tubulin interaction |
|
| Publications: |
4 |
Organism: |
In Vitro |
3.0
NINL
- 
- 