+ |
PLK1 | up-regulates
phosphorylation
|
KAT7 |
0.516 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160751 |
Ser57 |
SQSSQDSsPVRNLQS |
Homo sapiens |
|
pmid |
sentence |
18250300 |
Here, we show that the interaction between plk1 and hbo1 is mitosis-specific and that plk1 phosphorylates hbo1 on ser-57 in vitro and in vivo. During mitosis, cdk1 phosphorylates hbo1 on thr-85/88, creating a docking site for plk1 to be recruited. Significantly, the overexpression of hbo1 mutated at the plk1 phosphorylation site (s57a) leads to cell-cycle arrest in the g1/s phase, inhibition of chromatin loading of the minichromosome maintenance (mcm) complex, and a reduced dna replication rate. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKD1 | up-regulates quantity by stabilization
phosphorylation
|
KAT7 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277828 |
Thr331 |
LRLQGQItEGSNMIK |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
33014433 |
We show that PKD1 directly interacts and phosphorylates KAT7 at Thr97 and Thr331 in vitro and in vivo. PKD1-mediated phosphorylation of KAT7 enhances its expression levels and stability by reducing its ubiquitination-mediated degradation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277829 |
Thr97 |
KKYPLRQtRSSGSET |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
33014433 |
We show that PKD1 directly interacts and phosphorylates KAT7 at Thr97 and Thr331 in vitro and in vivo. PKD1-mediated phosphorylation of KAT7 enhances its expression levels and stability by reducing its ubiquitination-mediated degradation. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
CDK1 | up-regulates
phosphorylation
|
KAT7 |
0.361 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160743 |
Thr85 |
TRSQQQPtPVTPKKY |
Homo sapiens |
|
pmid |
sentence |
18250300 |
Here, we show that the interaction between plk1 and hbo1 is mitosis-specific and that plk1 phosphorylates hbo1 on ser-57 in vitro and in vivo. During mitosis, cdk1 phosphorylates hbo1 on thr-85/88, creating a docking site for plk1 to be recruited. Significantly, the overexpression of hbo1 mutated at the plk1 phosphorylation site (s57a) leads to cell-cycle arrest in the g1/s phase, inhibition of chromatin loading of the minichromosome maintenance (mcm) complex, and a reduced dna replication rate. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-160747 |
Thr88 |
QQQPTPVtPKKYPLR |
Homo sapiens |
|
pmid |
sentence |
18250300 |
Here, we show that the interaction between plk1 and hbo1 is mitosis-specific and that plk1 phosphorylates hbo1 on ser-57 in vitro and in vivo. During mitosis, cdk1 phosphorylates hbo1 on thr-85/88, creating a docking site for plk1 to be recruited. Significantly, the overexpression of hbo1 mutated at the plk1 phosphorylation site (s57a) leads to cell-cycle arrest in the g1/s phase, inhibition of chromatin loading of the minichromosome maintenance (mcm) complex, and a reduced dna replication rate. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |