| + |
PLK1 | up-regulates 
phosphorylation
|
BUB1B |
0.834 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157646 |
Ser676 |
LSPIIEDsREATHSS |
Homo sapiens |
|
| pmid |
sentence |
| 17785528 |
We identify s676 as a plk1-specific phosphorylation site on bubr1. These findings describe the first in vivo verified phosphorylation site for human bubr1, identify plk1 as the kinase responsible for causing the characteristic mitotic bubr1 upshift, and attribute a kt-specific function to the hyperphosphorylated form of bubr1 in the stabilization of kt-mt interactions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153863 |
Thr1008 |
LNANDEAtVSVLGEL |
Homo sapiens |
|
| pmid |
sentence |
| 17376779 |
Bubr1 was phosphorylated by plk1 in vitro at two plk1 consensus sites in the kinase domain of bubr1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199222 |
Thr680 |
IEDSREAtHSSGFSG |
Homo sapiens |
|
| pmid |
sentence |
| 23079597 |
Phosphorylation of kard by plk1 promotes direct interaction of bubr1 with the pp2a-b56_ phosphatase that counters excessive aurora b activity at kinetochores. We propose that plk1 and bubr1 cooperate to stabilize kinetochore-microtubule interactions. Phosphorylation of t680 by plk1 is essential for kard function |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153867 |
Thr792 |
PRNSAELtVIKVSSQ |
Homo sapiens |
|
| pmid |
sentence |
| 17376779 |
Bubr1 was phosphorylated by plk1 in vitro at two plk1 consensus sites in the kinase domain of bubr1 |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates
phosphorylation
|
BUB1B |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157642 |
Thr620 |
RAARFVStPFHEIMS |
Homo sapiens |
|
| pmid |
sentence |
| 17785528 |
Here, we demonstrate that bubr1 is phosphorylated on the cdk1 site t620, which triggers the recruitment of plk1 and phosphorylation of bubr1 by plk1 both in vitro and in vivo. Phosphorylation does not appear to be required for spindle checkpoint function but instead is important for the stability of kinetochore-microtubule (kt-mt) interactions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KNL1 | up-regulates
binding
|
BUB1B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158894 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17981135 |
Association of the amino and middle domain of blinkin with the tpr domains in the amino termini of bubr1 and bub1 is essential for bubr1 and bub1 to execute their distinct mitotic functions |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BUB1B | form complex 
binding
|
MCC |
0.978 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265974 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 25092294 |
The mitotic (or spindle assembly) checkpoint system delays anaphase until all chromosomes are correctly attached to the mitotic spindle. When the checkpoint is active, a Mitotic Checkpoint Complex (MCC) assembles and inhibits the ubiquitin ligase Anaphase-Promoting Complex/Cyclosome (APC/C). MCC is composed of the checkpoint proteins Mad2, BubR1, and Bub3 associated with the APC/C activator Cdc20. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CENPE | up-regulates activity
binding
|
BUB1B |
0.84 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252043 |
|
|
Mus musculus |
Fibroblast |
| pmid |
sentence |
| 12925705 |
Without CENP-E, diminished levels of BubR1 are recruited to kinetochores and BubR1 kinase activity remains at basal levels. CENP-E binds to and directly stimulates the kinase activity of purified BubR1 in vitro. Thus, CENP-E is required for enhancing recruitment of its binding partner BubR1 to each unattached kinetochore and for stimulating BubR1 kinase activity, implicating it as an essential amplifier of a basal mitotic checkpoint signal. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266118 |
|
|
in vitro |
|
| pmid |
sentence |
| 12925705 |
CENP-E binds to and directly stimulates the kinase activity of purified BubR1 in vitro. |
|
| Publications: |
2 |
Organism: |
Mus Musculus, In Vitro |
| + |
BUB1B | up-regulates 
|
Mitotic_checkpoint |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168195 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20888775 |
The multidomain protein kinases bub1 and bubr1 (mad3 in yeast, worms and plants) are central components of the mitotic checkpoint for spindle assembly (sac) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5RAP2 | up-regulates quantity by expression
transcriptional regulation
|
BUB1B |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260312 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19282672 |
These data indicate that CDK5RAP2 is a positive regulator of both the BUBR1 promoter and the MAD2 promoter |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BUB1B
- 
- 