| + |
PRKDC | down-regulates 
phosphorylation
|
LIG4 |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125869 |
Ser668 |
DVEFCVMsGTDSQPK |
Homo sapiens |
|
| pmid |
sentence |
| 15194694 |
Using tandem mass spectrometry, we identified a dna-pk phosphorylation site at thr-650 in human lig4 and a potential second phosphorylation site at ser-668 or ser-672. Phosphorylation of lig4 per se was not required for lig4 dna end joining activity. Substitution of these amino acids with alanine, individually or in combination, led to changes in lig4 protein stability of mouse lig4. The phosphomimetic mutation s650d returned lig4 stability to that of the wild-type protein. Furthermore dna-pk was found to negatively regulate lig4 protein stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125873 |
Ser672 |
CVMSGTDsQPKPDLE |
Homo sapiens |
|
| pmid |
sentence |
| 15194694 |
Using tandem mass spectrometry, we identified a dna-pk phosphorylation site at thr-650 in human lig4 and a potential second phosphorylation site at ser-668 or ser-672. Phosphorylation of lig4 per se was not required for lig4 dna end joining activity. Substitution of these amino acids with alanine, individually or in combination, led to changes in lig4 protein stability of mouse lig4. The phosphomimetic mutation s650d returned lig4 stability to that of the wild-type protein. Furthermore dna-pk was found to negatively regulate lig4 protein stability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125877 |
Thr650 |
HLKAPNLtNVNKISN |
Homo sapiens |
|
| pmid |
sentence |
| 15194694 |
Using tandem mass spectrometry, we identified a dna-pk phosphorylation site at thr-650 in human lig4 and a potential second phosphorylation site at ser-668 or ser-672. Phosphorylation of lig4 per se was not required for lig4 dna end joining activity. Substitution of these amino acids with alanine, individually or in combination, led to changes in lig4 protein stability of mouse lig4. The phosphomimetic mutation s650d returned lig4 stability to that of the wild-type protein. Furthermore dna-pk was found to negatively regulate lig4 protein stability. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
LIG4 | form complex 
binding
|
Lig4-Xrcc4 complex |
0.95 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264533 |
|
|
in vitro |
|
| pmid |
sentence |
| 19837014 |
The DNA ligase IV-Xrcc4 complex is responsible for the ligation of broken DNA ends in the non-homologous end-joining (NHEJ) pathway of DNA double strand break repair in mammals. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
LIG4
- 
- 