+ |
PLK1 | up-regulates activity
phosphorylation
|
MAD1L1 |
0.441 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276173 |
Thr680 |
SKMQLLEtEFSHTVG |
in vitro |
|
pmid |
sentence |
18922800 |
These findings indicate mechanistic roles contributed by protein phosphorylation and Plk1 to the SAC activity of Mad1.Here, we have studied the phosphorylation of Mad1 and mapped using liquid chromatography-tandem mass spectrometry several phosphorylated amino acids in this protein. One phosphorylated residue, Thr680, was characterized to be important for the kinetochore localization of Mad1 and its SAC function. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
CENPE | up-regulates activity
|
MAD1L1 |
0.62 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252044 |
|
|
Mus musculus |
Fibroblast |
pmid |
sentence |
12925705 |
CENP-E is required for efficient recruitment of BubR1, Mad1, and Mad2 to attached and newly unattached kinetochores |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
TPR | up-regulates
binding
|
MAD1L1 |
0.498 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-181918 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
18981471 |
Tpr directly binds to mad1 and mad2. / depletion of tpr decreases the levels of mad1 at kinetochores during prometaphase, correlating with the inability of mad1 to activate mad2, which is required for inhibiting apc(cdc20). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
MAX | up-regulates activity
binding
|
MAD1L1 |
0.305 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-240357 |
|
|
Homo sapiens |
|
pmid |
sentence |
7954804 |
the role MAX plays in transcription is thought to be primarily as a cofactor for DNA binding. In this capacity, however, it appears to be essential for most, if not all, the known biological activities of MYC. MAX also functions as a cofactor for DNA binding for a group of bHLHZip proteins related to MYC, including MNT, MXD1-4 (formerly Mad1, Mxi1, Mad3 and Mad4), and MGA. Like MYC, these proteins do not homodimerize and appear to be incapable of binding DNA on their own, but when bound to MAX, they recognize E-box sequences. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BUB1 | up-regulates activity
relocalization
|
MAD1L1 |
0.717 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252017 |
|
|
|
|
pmid |
sentence |
11402067 |
Spindle checkpoint protein Bub1 is required for kinetochore localization of Mad1, Mad2, Bub3, and CENP-E, independently of its kinase activity |
|
Publications: |
1 |
+ |
RPS6KA3 | up-regulates activity
|
MAD1L1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252038 |
|
|
Homo sapiens |
|
pmid |
sentence |
20383198 |
We also show that this kinase might also participate in the maintenance of the SAC in mammalian cells as Rsk2 knockdown in these cells prevents the kinetochore localization of Mad1, Mad2 and CENP-E under checkpoint conditions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |