+ |
ATM | up-regulates
phosphorylation
|
PNKP |
0.476 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176008 |
Ser114 |
EETRTPEsQPDTPPG |
Homo sapiens |
|
pmid |
sentence |
21824916 |
We demonstrate that pnkp is phosphorylated by the dna-dependent protein kinase (dna-pk) and ataxia-telangiectasia mutated (atm) in vitro. The major phosphorylation site for both kinases was serine 114, with serine 126 being a minor site. Purified pnkp protein with mutation of serines 114 and 126 had decreased dna kinase and dna phosphatase activities and reduced affinity for dna in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176012 |
Ser126 |
PPGTPLVsQDEKRDA |
Homo sapiens |
|
pmid |
sentence |
21824916 |
We demonstrate that pnkp is phosphorylated by the dna-dependent protein kinase (dna-pk) and ataxia-telangiectasia mutated (atm) in vitro. The major phosphorylation site for both kinases was serine 114, with serine 126 being a minor site. Purified pnkp protein with mutation of serines 114 and 126 had decreased dna kinase and dna phosphatase activities and reduced affinity for dna in vitro. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKDC | up-regulates
phosphorylation
|
PNKP |
0.636 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176016 |
Ser114 |
EETRTPEsQPDTPPG |
Homo sapiens |
|
pmid |
sentence |
21824916 |
We demonstrate that pnkp is phosphorylated by the dna-dependent protein kinase (dna-pk) and ataxia-telangiectasia mutated (atm) in vitro. The major phosphorylation site for both kinases was serine 114, with serine 126 being a minor site. Purified pnkp protein with mutation of serines 114 and 126 had decreased dna kinase and dna phosphatase activities and reduced affinity for dna in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-176020 |
Ser126 |
PPGTPLVsQDEKRDA |
Homo sapiens |
|
pmid |
sentence |
21824916 |
We demonstrate that pnkp is phosphorylated by the dna-dependent protein kinase (dna-pk) and ataxia-telangiectasia mutated (atm) in vitro. The major phosphorylation site for both kinases was serine 114, with serine 126 being a minor site. Purified pnkp protein with mutation of serines 114 and 126 had decreased dna kinase and dna phosphatase activities and reduced affinity for dna in vitro. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |