| + |
CSNK2A1 | up-regulates activity 
phosphorylation
|
XRCC1 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250972 |
Ser475 |
IDIEGVQsEGQDNGA |
Cricetulus griseus |
CHO-EM9 Cell |
| pmid |
sentence |
| 15066279 |
We show that inhibiting XRCC1 phosphorylation by mutation of the CK2 phosphorylation sites or preventing CK2 activity using a highly specific inhibitor ablates the rapid repair of cellular DNA single-strand breaks by XRCC1. | |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
CSNK2A1 | up-regulates
phosphorylation
|
XRCC1 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165419 |
Ser485 |
QDNGAEDsGDTEDEL |
Homo sapiens |
|
| pmid |
sentence |
| 20471329 |
Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165423 |
Ser518 |
GEDPYAGsTDENTDS |
Homo sapiens |
|
| pmid |
sentence |
| 20471329 |
Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128893 |
Ser518 |
GEDPYAGsTDENTDS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15367657 |
Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165427 |
Thr488 |
GAEDSGDtEDELRRV |
Homo sapiens |
|
| pmid |
sentence |
| 20471329 |
Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128897 |
Thr519 |
EDPYAGStDENTDSE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15367657 |
Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165431 |
Thr519 |
EDPYAGStDENTDSE |
Homo sapiens |
|
| pmid |
sentence |
| 20471329 |
Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165435 |
Thr523 |
AGSTDENtDSEEHQE |
Homo sapiens |
|
| pmid |
sentence |
| 20471329 |
Xrcc1 phosphorylation by ck2 is required for its stability and efficient dna repair. Rcc1 is phosphorylated in vivo and in vitro by ck2, and ck2 phosphorylation of xrcc1 on s518, t519, and t523 |
|
| Publications: |
7 |
Organism: |
Homo Sapiens |
| + |
CSNK2A2 | up-regulates activity
phosphorylation
|
XRCC1 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251050 |
Ser518 |
GEDPYAGsTDENTDS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15367657 |
XRCC1 is phosphorylated in vivo and in vitro by CK2, and CK2 phosphorylation of XRCC1 on S518, T519, and T523 largely determines aprataxin binding to XRCC1 though its FHA domain | In addition, we present data to show that the acute loss of aprataxin by small interfering RNA (siRNA) renders HeLa cells sensitive to MMS through a mechanism that destabilizes XRCC1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251051 |
Thr519 |
EDPYAGStDENTDSE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15367657 |
XRCC1 is phosphorylated in vivo and in vitro by CK2, and CK2 phosphorylation of XRCC1 on S518, T519, and T523 largely determines aprataxin binding to XRCC1 though its FHA domain | In addition, we present data to show that the acute loss of aprataxin by small interfering RNA (siRNA) renders HeLa cells sensitive to MMS through a mechanism that destabilizes XRCC1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251052 |
Thr523 |
AGSTDENtDSEEHQE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15367657 |
XRCC1 is phosphorylated in vivo and in vitro by CK2, and CK2 phosphorylation of XRCC1 on S518, T519, and T523 largely determines aprataxin binding to XRCC1 though its FHA domain | In addition, we present data to show that the acute loss of aprataxin by small interfering RNA (siRNA) renders HeLa cells sensitive to MMS through a mechanism that destabilizes XRCC1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CHEK2 | up-regulates
phosphorylation
|
XRCC1 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181816 |
Thr284 |
APTRTPAtAPVPARA |
Homo sapiens |
|
| pmid |
sentence |
| 18971944 |
Chk2 formed a complex with xrcc1, the ber scaffold protein, and phosphorylated xrcc1 in vivo and in vitro at thr(284). our results are consistent with the phosphorylation of xrcc1 by atm-chk2 facilitating recruitment of downstream ber proteins to the initial damage recognition/excision step to promote ber. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC1 | up-regulates activity
binding
|
PARP2 |
0.58 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282649 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 39970298 |
The BRCT2 domain of XRCC1 can directly interact with PARP2. XRCC1 increases the local concentration of PARP2 near DNA breaks, promoting its DNA binding and activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC1 | up-regulates quantity by stabilization
binding
|
LIG3 |
0.943 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282650 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 39970298 |
The XRCC1-BRCT2 domain is also known to bind to the LIG3 C-terminal BRCT domain. This interaction is critical for the stability of nuclear LIG3 protein and involves the arginine 564 residue within the XRCC1-BRCT2 domain.XRCC1 is also essential for the protein stability of nuclear LIG3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC1 | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282653 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28002403 |
XRCC1 is a molecular scaffold protein that assembles multi-protein complexes involved in DNA single-strand break repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PARP1 | up-regulates activity
binding
|
XRCC1 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282654 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14500814 |
Here, we show that the single-strand break repair protein XRCC1 is rapidly assembled into discrete nuclear foci after oxidative DNA damage at sites of poly (ADP-ribose) synthesis. These data demonstrate that PARP-1 is required for the assembly or stability of XRCC1 nuclear foci after oxidative DNA damage and suggest that the formation of these foci is mediated via interaction with poly (ADP-ribose). These results support a model in which the rapid activation of PARP-1 at sites of DNA strand breakage facilitates DNA repair by recruiting the molecular scaffold protein, XRCC1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
XRCC1 | down-regulates activity 
binding
|
PARP1 |
0.597 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282655 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 39970298 |
XRCC1-deficiency causes hyperactivation of PARP1 while attenuating micro-irradiation-induced PARP2 foci. In XRCC1-null cells, the unrepaired single-strand breaks (SSBs) accumulate, leading to persistent PARP1 foci and hyperactivated PARP1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
XRCC1
- 
- 