| + |
BRCA1-BARD1 complex | up-regulates activity 
ubiquitination
|
BRCA1-BARD1 complex |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263233 |
|
|
in vitro |
|
| pmid |
sentence |
| 12485996 |
Auto‐ubiquitylation stimulates the ubiquitin ligase activity of BRCA1/BARD1|Secondly, BRCA1/BARD1 catalyses the formation of multiple polyubiquitin chains on itself. Remarkably, this auto‐polyubiquitylation potentiates the E3 ubiquitin ligase activity of the BRCA1/BARD1 complex >20‐fold. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BRCA1-BARD1 complex | down-regulates quantity by destabilization 
ubiquitination
|
LARP7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275581 |
|
|
|
|
| pmid |
sentence |
| 32726637 |
Here, we demonstrate that upon genotoxic stress, BRCA1 together with BARD1 catalyzes the K48 polyubiquitination on LARP7, a 7SK RNA binding protein known to control RNAPII pausing, and thereby degrades it through the 26S ubiquitin-proteasome pathway. |
|
| Publications: |
1 |
| + |
BRCA1-BARD1 complex | up-regulates activity
ubiquitination
|
FANCD2 |
0.699 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263237 |
|
|
Homo sapiens |
HCC-1937 Cell |
| pmid |
sentence |
| 12485996 |
The major genetic evidence supporting ubiquitin ligase function for BRCA1 in vivo comes from studies on the FANCD2 protein. Whereas in wild‐type cells the FANCD2 protein co‐localizes with BRCA1 in nuclear foci and becomes monoubiquitylated in response to DNA damage, HCC1937 cells, which encode a mutated form of BRCA1, are largely defective for both monoubiquitylation of FANCD2 and foci formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | form complex 
binding
|
BRCA1-BARD1 complex |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263224 |
|
|
|
|
| pmid |
sentence |
| 25400280 |
Intriguingly, another BRCA1 complex, the BRCA1–A complex, which itself contains RAP80 along with MERIT40, BRCC36/45 and Abraxas, has been reported to inhibit DNA end resection, suggesting that, in some contexts, BRCA1 may function to limit and/or prevent over resection of DNA breaks. |
|
| Publications: |
1 |
| + |
BARD1 | form complex
binding
|
BRCA1-BARD1 complex |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263223 |
|
|
|
|
| pmid |
sentence |
| 25400280 |
Intriguingly, another BRCA1 complex, the BRCA1–A complex, which itself contains RAP80 along with MERIT40, BRCC36/45 and Abraxas, has been reported to inhibit DNA end resection, suggesting that, in some contexts, BRCA1 may function to limit and/or prevent over resection of DNA breaks. |
|
| Publications: |
1 |
| + |
BRCA1-BARD1 complex | form complex
binding
|
BRCA1-B complex |
0.773 |
| 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 |
| + |
BRCA1-BARD1 complex | up-regulates activity
ubiquitination
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263235 |
|
|
in vitro |
|
| pmid |
sentence |
| 12485996 |
Strikingly, as well as H2AX, the nucleosome core histones H2A, H2B, H3 and H4 were all ubiquitylated efficiently by BRCA1/BARD1, while the linker histone H1 was not (Figure 3).| Generally, histone proteins are required for compaction of nuclear DNA into chromatin, and their modification is thought to loosen this compaction. Therefore, one might envisage that ubiquitylation of γH2AX by BRCA1/BARD1 at DNA breaks modulates local chromatin packaging to facilitate the action of DNA repair enzymes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BRCA1-BARD1 complex | form complex
binding
|
BRCA1-A complex |
0.761 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263216 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20656690 |
We and others showed previously that BRCC36 is a component of the BRCA1-A complex, which consists of RAP80, CCDC98/ABRAXAS, BRCC45/BRE, MERIT40/NBA1, BRCC36, and BRCA1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1-BARD1 complex | form complex
binding
|
BRCA1-C complex |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263222 |
|
|
|
|
| pmid |
sentence |
| 25400280 |
The BRCA1–C complex consisting of BRCA1, Mre11:Rad50:Nbs1 (collectively known as the MRN complex) and CtIP plays a role in DSB end resection, a process that also involves EXO1 and DNA2 |
|
| Publications: |
1 |
| + |
BRCA1-BARD1 complex | up-regulates activity
ubiquitination
|
H4C1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263234 |
|
|
in vitro |
|
| pmid |
sentence |
| 12485996 |
Strikingly, as well as H2AX, the nucleosome core histones H2A, H2B, H3 and H4 were all ubiquitylated efficiently by BRCA1/BARD1, while the linker histone H1 was not (Figure 3).| Generally, histone proteins are required for compaction of nuclear DNA into chromatin, and their modification is thought to loosen this compaction. Therefore, one might envisage that ubiquitylation of γH2AX by BRCA1/BARD1 at DNA breaks modulates local chromatin packaging to facilitate the action of DNA repair enzymes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BRCA1-BARD1 complex | form complex
binding
|
BRCC ubiquitin ligase complex |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263208 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14636569 |
These findings identify BRCC as a ubiquitin E3 ligase complex that enhances cellular survival following DNA damage.|Reconstitution of a recombinant four-subunit complex containing BRCA1/BARD1/BRCC45/BRCC36 revealed an enhanced E3 ligase activity compared to that of BRCA1/BARD1 heterodimer |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BRCA1-BARD1 complex
CPX-715