| + |
DNA-PK | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264531 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10854421 |
The DNA-dependent protein kinase (DNA-PK), consisting of Ku and the DNA-PK catalytic subunit (DNA-PKcs), and the DNA ligase IV-XRCC4 complex function together in the repair of DNA double-strand breaks by non-homologous end joining. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC4 | up-regulates activity 
binding
|
DNA-PK |
0.816 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277201 |
|
|
Homo sapiens |
MiaPaCa-2 Cell |
| pmid |
sentence |
| 26774286 |
In response to ionizing radiation, ATM phosphorylates FBXW7 at serine 26 to recruit it to DNA double-strand break (DSB) sites, whereas activated DNA-PKcs phosphorylates XRCC4 at serines 325/326, which promotes binding of XRCC4 to FBXW7. SCF(FBXW7) E3 ligase then promotes polyubiquitylation of XRCC4 at lysine 296 via lysine 63 linkage for enhanced association with the Ku70/80 complex to facilitate NHEJ repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKDC | form complex 
binding
|
DNA-PK |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226026 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17308091 |
Complexes formed by interactions between Ku70, Ku80, and DNA-PKcs were well-established |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC5 | form complex
binding
|
DNA-PK |
0.957 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226019 |
|
|
Homo sapiens |
SK-BR-3 Cell |
| pmid |
sentence |
| 17308091 |
complexes formed by interactions between Ku70, Ku80, and DNA-PKcs were well-established |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC6 | form complex
binding
|
DNA-PK |
0.963 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-226023 |
|
|
Homo sapiens |
SK-BR-3 Cell |
| pmid |
sentence |
| 17308091 |
complexes formed by interactions between Ku70, Ku80, and DNA-PKcs were well-established |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NF90-NF45 | up-regulates activity
binding
|
DNA-PK |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268489 |
|
|
in vitro |
|
| pmid |
sentence |
| 9442054 |
These proteins are NF90 and NF45, which are the 90- and 45-kDa subunits of a protein known to bind specifically to the antigen receptor response element of the interleukin 2 promoter, and the alpha, beta, and gamma subunits of eukaryotic translation initiation factor eIF-2. We also show that NF90, NF45, and eIF-2 beta are substrates for DNA-PK in vitro. In addition, recombinant NF90 promotes formation of a complex between DNA-PKcs, Ku, and DNA, and antibodies to recombinant NF90 or recombinant NF45 immunoprecipitate DNA-PKcs in vitro. Together, our data suggest that NF90, in complex with NF45, interacts with DNA-PKcs and Ku on DNA and that NF90 and NF45 may be important for the function of DNA-PK. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
DNA-PK
CPX-3403