+ |
PLK1 | down-regulates
phosphorylation
|
CENPU |
0.731 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-150453 |
Ser77 |
TFDPPLHsTAIYADE |
Homo sapiens |
|
pmid |
sentence |
17081991 |
S77 and t78 of pbip1 are important for plk1-dependent pbip1 phosphorylation and degradation. Here, we demonstrate that a pbd-binding protein, pbip1, is crucial for recruiting plk1 to the interphase and mitotic kinetochores. Unprecedentedly, plk1 phosphorylated pbip1 at t78. Later in mitosis, plk1 also induced pbip1 degradation in a t78-dependent manner, thereby enabling itself to interact with other components critical for proper kinetochore functions |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-150457 |
Thr78 |
FDPPLHStAIYADEE |
Homo sapiens |
|
pmid |
sentence |
17081991 |
S77 and t78 of pbip1 are important for plk1-dependent pbip1 phosphorylation and degradation. Here, we demonstrate that a pbd-binding protein, pbip1, is crucial for recruiting plk1 to the interphase and mitotic kinetochores. Unprecedentedly, plk1 phosphorylated pbip1 at t78. Later in mitosis, plk1 also induced pbip1 degradation in a t78-dependent manner, thereby enabling itself to interact with other components critical for proper kinetochore functions |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CENPU | form complex
binding
|
CCAN complex |
0.807 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265203 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18007590 |
CENP-A NAC/CAD components have been subdivided into either NAC proteins (nucleosome-associated complex; CENP-C, CENP-H, CENP-50CENP−U, CENP-M, CENP-T and Chl4RCENP−N) or CAD proteins (CENP-A Distal; CENP-I, Mcm21RCENP−O, Fta1RCENP−L, Sim4RCENP−K, CENP-P, CENP-Q, CENP-R and CENP-S). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |