+ |
AURKB | up-regulates activity
phosphorylation
|
SKA3 |
0.464 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262661 |
Ser159 |
SPRSPQLsDFGLERY |
in vitro |
|
pmid |
sentence |
22371557 |
Aurora B directly phosphorylated Ska1 and Ska3 in vitro, and expression of phosphomimetic mutants of Ska1 and Ska3 impaired Ska KT recruitment and formation of stable KT-MT fibers (K-fibers), disrupting mitotic progression. We propose that Aurora B phosphorylation antagonizes the interaction between the Ska complex and the KMN network, thereby controlling Ska recruitment to KTs and stabilization of KT-MT attachments. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CDK1 | up-regulates activity
phosphorylation
|
SKA3 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278376 |
Thr358 |
SYENLLRtPTPPEVT |
Homo sapiens |
|
pmid |
sentence |
28479321 |
Cdk1 treatment further enhanced the binding of Ska3 2D to Ndc80, suggesting that phosphorylation of other Cdk1 sites in Ska3 further contributes to the Ndc80C-Ska3 interaction, although this contribution is not apparent in our kinetochore localization assay.We next purified the GST-Ndc80C Bonsai construct that lacks the loop region of Ndc80 as well as the coiled coil regions of Ndc80C [17].|Thus, Ska3 can be phosphorylated by Cdk1 on T358 and T360 sites in vitro.We next tested whether Ska3 was required for Ska1 or Ska2 localization. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278375 |
Thr360 |
ENLLRTPtPPEVTKI |
Homo sapiens |
|
pmid |
sentence |
28479321 |
Cdk1 treatment further enhanced the binding of Ska3 2D to Ndc80, suggesting that phosphorylation of other Cdk1 sites in Ska3 further contributes to the Ndc80C-Ska3 interaction, although this contribution is not apparent in our kinetochore localization assay.We next purified the GST-Ndc80C Bonsai construct that lacks the loop region of Ndc80 as well as the coiled coil regions of Ndc80C [17].|Thus, Ska3 can be phosphorylated by Cdk1 on T358 and T360 sites in vitro.We next tested whether Ska3 was required for Ska1 or Ska2 localization. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SKA3 | form complex
binding
|
SKA complex |
0.917 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265196 |
|
|
in vitro |
|
pmid |
sentence |
22483620 |
We show that the structure of the Ska core complex is a W-shaped dimer of coiled coils, formed by intertwined interactions between Ska1, Ska2, and Ska3. |
|
Publications: |
1 |
Organism: |
In Vitro |