| + |
TTK | up-regulates 
phosphorylation
|
CDCA8 |
0.472 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186143 |
Thr169 |
KRSSRANtVTPAVGR |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
First, we confirmed that wild-type borealin is phosphorylated at the previously described sites t88, t94, t169, and t230 when present in complex with survivin borealin might be a substrate for mps1. In the case of wild-type borealin, the fast exchange between the monomeric and dimeric forms may allow mps1 to phosphorylate the monomer. In turn, mps1 may regulate borealin function by unfolding the c-terminal domain and/or shifting the population to the monomeric form. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186147 |
Thr230 |
DSKEIFLtVPVGGGE |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
We found that substitutions at borealin t230, recently identified as an mps1 phosphorylation site, can modulate the dimerization state of borealin. Mutation of this single residue to alanine or valine impairs aurora b activity during mitosis and causes chromosome segregation defects |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186151 |
Thr88 |
QALEEAAtADLDITE |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
First, we confirmed that wild-type borealin is phosphorylated at the previously described sites t88, t94, t169, and t230 when present in complex with survivin borealin might be a substrate for mps1. In the case of wild-type borealin, the fast exchange between the monomeric and dimeric forms may allow mps1 to phosphorylate the monomer. In turn, mps1 may regulate borealin function by unfolding the c-terminal domain and/or shifting the population to the monomeric form. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186155 |
Thr94 |
ATADLDItEINKLTA |
Homo sapiens |
|
| pmid |
sentence |
| 19530738 |
First, we confirmed that wild-type borealin is phosphorylated at the previously described sites t88, t94, t169, and t230 when present in complex with survivin borealin might be a substrate for mps1. In the case of wild-type borealin, the fast exchange between the monomeric and dimeric forms may allow mps1 to phosphorylate the monomer. In turn, mps1 may regulate borealin function by unfolding the c-terminal domain and/or shifting the population to the monomeric form. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160604 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18243099 |
Direct phosphorylation of the aurora b regulator borealin by mps1 enhances aurora b activity and is essential for chromosome alignment |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
CDCA8 | form complex 
binding
|
CPC |
0.85 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275423 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23175282 |
It is now known that the chromosomal passenger complex (CPC) is composed of four subunits: the enzymatic component Aurora B and the three regulatory and targeting components INCENP, Survivin and Borealin (also known as Dasra)5–7 (Figure 1A). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDCA8
- 
- 