| + |
CyclinA2/CDK2 | down-regulates activity 
phosphorylation
|
POLM |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273597 |
Ser12 |
RRRARVGsPSGDAAS |
in vitro |
|
| pmid |
sentence |
| 23933132 |
In vitro kinase assays showed that the S phase-associated Cdk2/cyclin A complex was able to phosphorylate Polμ. We identified Ser12, Thr21 (located in the BRCT domain) and Ser372 (located in loop1) as the target residues. Mutation of these residues to alanine indicated that Ser372 is the main phosphorylation site.Our evidences suggest that Polμ could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273596 |
Ser372 |
HQHSCCEsPTRLAQQ |
in vitro |
|
| pmid |
sentence |
| 23933132 |
In vitro kinase assays showed that the S phase-associated Cdk2/cyclin A complex was able to phosphorylate Polμ. We identified Ser12, Thr21 (located in the BRCT domain) and Ser372 (located in loop1) as the target residues. Mutation of these residues to alanine indicated that Ser372 is the main phosphorylation site.Our evidences suggest that Polμ could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273598 |
Thr21 |
SGDAASStPPSTRFP |
in vitro |
|
| pmid |
sentence |
| 23933132 |
In vitro kinase assays showed that the S phase-associated Cdk2/cyclin A complex was able to phosphorylate Polμ. We identified Ser12, Thr21 (located in the BRCT domain) and Ser372 (located in loop1) as the target residues. Mutation of these residues to alanine indicated that Ser372 is the main phosphorylation site.Our evidences suggest that Polμ could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1. |
|
| Publications: |
3 |
Organism: |
In Vitro |
3.0
POLM
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