+ |
TOPBP1 | form complex
binding
|
BRCA1-B complex |
0.661 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263218 |
|
|
|
|
pmid |
sentence |
25400280 |
Another BRCA1 complex, the BRCA1–B complex containing BRCA1/TopBP1 and BACH1 (also known and BRIP1/FANCJ) has been reported to play a role in HR and S‐phase cell cycle arrest. The exact role of this complex in HR remains unclear, although it is assumed that BACH1, a DNA helicase, contributes to end resection (possibly through its helicase activity) and RPA loading, whereas TopBP1 is required for ATR activation and subsequent S‐phase checkpoint activation |
|
Publications: |
1 |
+ |
BRIP1 | form complex
binding
|
BRCA1-B complex |
0.661 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263219 |
|
|
|
|
pmid |
sentence |
25400280 |
Another BRCA1 complex, the BRCA1–B complex containing BRCA1/TopBP1 and BACH1 (also known and BRIP1/FANCJ) has been reported to play a role in HR and S‐phase cell cycle arrest. The exact role of this complex in HR remains unclear, although it is assumed that BACH1, a DNA helicase, contributes to end resection (possibly through its helicase activity) and RPA loading, whereas TopBP1 is required for ATR activation and subsequent S‐phase checkpoint activation |
|
Publications: |
1 |
+ |
BRCA1-B complex | up-regulates
|
G1/S_transition_checkpoint |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263225 |
|
|
|
|
pmid |
sentence |
25400280 |
Another BRCA1 complex, the BRCA1–B complex containing BRCA1/TopBP1 and BACH1 (also known and BRIP1/FANCJ) has been reported to play a role in HR and S‐phase cell cycle arrest. The exact role of this complex in HR remains unclear, although it is assumed that BACH1, a DNA helicase, contributes to end resection (possibly through its helicase activity) and RPA loading, whereas TopBP1 is required for ATR activation and subsequent S‐phase checkpoint activation |
|
Publications: |
1 |
+ |
BRCA1-B complex | up-regulates activity
binding
|
ATR |
0.64 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263231 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
16530042 |
These results establish that TopBP1 can activate both Xenopus and human ATR. Furthermore, these experiments provide conclusive evidence that the kinase activity that is induced by TopBP1 is intrinsic to the ATR protein itself and is not due to a kinase that associates with ATR. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BRCA1-BARD1 complex | form complex
binding
|
BRCA1-B complex |
0.766 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263217 |
|
|
|
|
pmid |
sentence |
25400280 |
Another BRCA1 complex, the BRCA1–B complex containing BRCA1/TopBP1 and BACH1 (also known and BRIP1/FANCJ) has been reported to play a role in HR and S‐phase cell cycle arrest. The exact role of this complex in HR remains unclear, although it is assumed that BACH1, a DNA helicase, contributes to end resection (possibly through its helicase activity) and RPA loading, whereas TopBP1 is required for ATR activation and subsequent S‐phase checkpoint activation |
|
Publications: |
1 |
+ |
tetra-mu3-sulfido-tetrairon | form complex
binding
|
BRCA1-B complex |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269475 |
|
|
|
|
pmid |
sentence |
25400280 |
Another BRCA1 complex, the BRCA1–B complex containing BRCA1/TopBP1 and BACH1 (also known and BRIP1/FANCJ) has been reported to play a role in HR and S‐phase cell cycle arrest. The exact role of this complex in HR remains unclear, although it is assumed that BACH1, a DNA helicase, contributes to end resection (possibly through its helicase activity) and RPA loading, whereas TopBP1 is required for ATR activation and subsequent S‐phase checkpoint activation |
|
Publications: |
1 |