| + |
CDK2 | up-regulates 
phosphorylation
|
ORC2 |
0.744 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116364 |
Thr116 |
LASELAKtPQKSVSF |
Homo sapiens |
|
| pmid |
sentence |
| 11931757 |
We also found that horc2p is phosphorylated in vitro by cyclin a/cdk2, specifically at residues thr116 and thr226. These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196048 |
Thr226 |
SAPVGKEtPSKRMKR |
Homo sapiens |
|
| pmid |
sentence |
| 22334659 |
Phosphorylation at thr-116 and thr-226 of orc2 occurs by cyclin-dependent kinase during the s phase and is maintained until the m phase. Phosphorylation of orc2 at thr-116 and thr-226 dissociated the orc2-5 from chromatin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116476 |
Thr226 |
SAPVGKEtPSKRMKR |
Homo sapiens |
|
| pmid |
sentence |
| 11931757 |
We also found that horc2p is phosphorylated in vitro by cyclin a/cdk2, specifically at residues thr116 and thr226. These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CyclinA2/CDK2 | up-regulates
phosphorylation
|
ORC2 |
0.699 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217296 |
Thr116 |
LASELAKtPQKSVSF |
Homo sapiens |
|
| pmid |
sentence |
| 11931757 |
We also found that horc2p is phosphorylated in vitro by cyclin a/cdk2, specifically at residues thr116 and thr226. These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217308 |
Thr226 |
SAPVGKEtPSKRMKR |
Homo sapiens |
|
| pmid |
sentence |
| 11931757 |
We also found that horc2p is phosphorylated in vitro by cyclin a/cdk2, specifically at residues thr116 and thr226. These data combined strongly suggest that skp2 promotes horc1p turnover and that the n-terminal domain of horc1p, containing most of the phosphorylation sites and overlapping with one of the skp2-interacting domains, is a regulatory element for horc1p stability. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ORC2 | form complex 
binding
|
ORC |
0.97 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267566 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32808929 |
The dynamic nature of the human origin recognition complex revealed through five cryoEM structures|Genome replication is initiated from specific origin sites established by dynamic events. The Origin Recognition Complex (ORC) is necessary for orchestrating the initiation process by binding to origin DNA, recruiting CDC6, and assembling the MCM replicative helicase on DNA. Here we report five cryoEM structures of the human ORC (HsORC) that illustrate the native flexibility of the complex. |The very first step of this initiation process is accomplished by DNA association with the Origin Recognition Complex (ORC), a six-subunit protein that forms a partial ring around origin DNA |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ORC2
- 
- 