| + |
SCF-FBW7 | up-regulates activity 
ubiquitination
|
XRCC4 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277200 |
Lys296 |
QENQLQEkENSRPDS |
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 | up-regulates activity
phosphorylation
|
XRCC4 |
0.905 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277198 |
Ser327 |
SLETLRNsSPEDLFD |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277199 |
Ser328 |
LETLRNSsPEDLFDE |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
CHD2 | up-regulates quantity
relocalization
|
XRCC4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264528 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 26895424 |
CHD2 Promotes the Recruitment of Core NHEJ Factors. overexpression of ATPase-dead CHD2 (K515R; Figure S5F), but not wild-type CHD2, also reduced the recruitment of XRCC4 (Figure 5E). Together, these findings suggest that the chromatin remodeling activity of CHD2 promotes the efficient assembly of NHEJ complexes at DSBs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC4 | up-regulates activity
binding
|
DNA-PK |
0.815 |
| 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 |
| + |
XRCC4 | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264530 |
|
|
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 | form complex 
binding
|
Lig4-Xrcc4 complex |
0.95 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264532 |
|
|
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
XRCC4
- 
- 