+ |
AURKA |
phosphorylation
|
TACC3 |
0.934 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263697 |
Ser34 |
PEVTGRSsVLRVSQK |
in vitro |
|
pmid |
sentence |
26134678 |
To address whether the phosphorylation state of TACC3 influenced Aurora-A binding and activation, we generated TACC3 variants in which all three Aurora-A phosphorylation sites (S34, S552 and S558)| The SA mutant had strongly reduced levels of phosphorylation compared to the individual mutations| |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263698 |
Ser552 |
GTSSFKEsALRKQSL |
in vitro |
|
pmid |
sentence |
26134678 |
In humans, Aurora-A phosphorylates TACC3 on three residues (S34, S552 and S558); these sites are conserved in Maskin and the S558 equivalent site is also present in D-TACC [26,27,30]. In mammalian cells, phosphorylation of S558 promotes accumulation of TACC3 on spindle MTs |
|
Publications: |
2 |
Organism: |
In Vitro |
+ |
AURKA | up-regulates activity
phosphorylation
|
TACC3 |
0.934 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262655 |
Ser558 |
ESALRKQsLYLKFDP |
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
17545617 |
We show that this conserved serine on human TACC3 (Ser(558)) is also phosphorylated by Aurora A. Moreover, phosphorylation of TACC3 by Aurora A in human cells is essential for its proper localization to centrosomes and proximal mitotic spindles. Inhibition of Aurora A with the selective small molecule inhibitor MLN8054 in cultured human tumor cells resulted in mislocalization of TACC3 away from mitotic spindles in a concentration-dependent manner. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |