| + |
PLK1 | down-regulates activity 
phosphorylation
|
BRCA2 |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102486 |
Ser193 |
AEVDPDMsWSSSLAT |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102490 |
Ser205 |
LATPPTLsSTVLIVR |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102494 |
Ser206 |
ATPPTLSsTVLIVRN |
Homo sapiens |
|
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102498 |
Thr203 |
SSLATPPtLSSTVLI |
Homo sapiens |
|
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102502 |
Thr207 |
TPPTLSStVLIVRNE |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
M phase-specific phosphorylation of brca2 by polo-like kinase 1 correlates with the dissociation of the brca2-p/caf complex.Plk1 interacts with brca2 in vivo, and mutation of ser193, ser205/206, and thr203/207 to ala in br-n1 abolished plk1 phosphorylation, suggesting that brca2 is the substrate of plk1 |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
PLK1 |
phosphorylation
|
BRCA2 |
0.555 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249217 |
Ser193 |
AEVDPDMsWSSSLAT |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
Plk1 interacts with BRCA2 in vivo, and mutation of Ser193, Ser205/206, and Thr203/207 to Ala in BR-N1 abolished Plk1 phosphorylation, suggesting that BRCA2 is the substrate of Plk1. Furthermore, both the hyperphosphorylated and hypophosphorylated forms of BRCA2 bind to RAD51, whereas the M phase hyperphosphorylated form of BRCA2 no longer associates with the P/CAF, suggesting that the dissociation of P/CAF-BRCA2 complex is regulated by phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249218 |
Ser205 |
LATPPTLsSTVLIVR |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
Plk1 interacts with BRCA2 in vivo, and mutation of Ser193, Ser205/206, and Thr203/207 to Ala in BR-N1 abolished Plk1 phosphorylation, suggesting that BRCA2 is the substrate of Plk1. Furthermore, both the hyperphosphorylated and hypophosphorylated forms of BRCA2 bind to RAD51, whereas the M phase hyperphosphorylated form of BRCA2 no longer associates with the P/CAF, suggesting that the dissociation of P/CAF-BRCA2 complex is regulated by phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249219 |
Ser206 |
ATPPTLSsTVLIVRN |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
Plk1 interacts with BRCA2 in vivo, and mutation of Ser193, Ser205/206, and Thr203/207 to Ala in BR-N1 abolished Plk1 phosphorylation, suggesting that BRCA2 is the substrate of Plk1. Furthermore, both the hyperphosphorylated and hypophosphorylated forms of BRCA2 bind to RAD51, whereas the M phase hyperphosphorylated form of BRCA2 no longer associates with the P/CAF, suggesting that the dissociation of P/CAF-BRCA2 complex is regulated by phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249220 |
Thr203 |
SSLATPPtLSSTVLI |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
Plk1 interacts with BRCA2 in vivo, and mutation of Ser193, Ser205/206, and Thr203/207 to Ala in BR-N1 abolished Plk1 phosphorylation, suggesting that BRCA2 is the substrate of Plk1. Furthermore, both the hyperphosphorylated and hypophosphorylated forms of BRCA2 bind to RAD51, whereas the M phase hyperphosphorylated form of BRCA2 no longer associates with the P/CAF, suggesting that the dissociation of P/CAF-BRCA2 complex is regulated by phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249221 |
Thr207 |
TPPTLSStVLIVRNE |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 12815053 |
Plk1 interacts with BRCA2 in vivo, and mutation of Ser193, Ser205/206, and Thr203/207 to Ala in BR-N1 abolished Plk1 phosphorylation, suggesting that BRCA2 is the substrate of Plk1. Furthermore, both the hyperphosphorylated and hypophosphorylated forms of BRCA2 bind to RAD51, whereas the M phase hyperphosphorylated form of BRCA2 no longer associates with the P/CAF, suggesting that the dissociation of P/CAF-BRCA2 complex is regulated by phosphorylation. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
BRCA2 | form complex 
binding
|
BRCC ubiquitin ligase complex |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263207 |
|
|
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 |
| + |
BRCA2 | up-regulates activity 
binding
|
RAD51 |
0.945 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259905 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17515904 |
We suggest that interactions of the BRCA2 C-terminal region with RAD51 may facilitate efficient nucleation of RAD51 multimers on DNA and thereby stimulate recombination-mediated repair. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
BRCA2 | form complex
binding
|
D1-D2-G-X3 complex |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263256 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 18212739 |
These results argue that FANCG has a role independent of the FA core complex, and we propose that phosphorylation of serine 7 is the signalling event required for forming a discrete complex comprising FANCD1/BRCA2-FANCD2-FANCG-XRCC3 (D1-D2-G-X3). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PALB2 | up-regulates
binding
|
BRCA2 |
0.94 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147217 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 16793542 |
Palb2 colocalizes with brca2 in nuclear foci, promotes its localization and stability in key nuclear structures (e.g., chromatin and nuclear matrix), and enables its recombinational repair and checkpoint functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
EMSY | down-regulates activity
binding
|
BRCA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263915 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 14651845 |
The EMSY protein interacts precisely with a highly conserved transactivating region at the N terminus of the breast cancer protein BRCA2, and has endogenous transcriptional repressor activity when recruited to a high basal promoter. We have suggested that the independent activation domain of BRCA2 within exon 3 might have some role in transcription (Milner et al., 1997). The identification of the repressor protein EMSY, which binds and silences this domain, is consistent with such a function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA2 | up-regulates
binding
|
POLH |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-204538 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24485656 |
Palb2 and brca2 interact with pol_ and are required to sustain the recruitment of pol_ at blocked replication forks. Palb2 and brca2 stimulate pol_-dependent dna synthesis on d loop substrates |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
FANCD2 | up-regulates activity
relocalization, binding
|
BRCA2 |
0.805 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263253 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15199141 |
FANCD2-Ub then promotes BRCA2 loading into a chromatin complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263238 |
|
|
Homo sapiens |
Fanconi Anemia Disease Specific Cell Type |
| pmid |
sentence |
| 19861535 |
Fanconi anemia complementation group FANCD2 protein serine 331 phosphorylation is important for fanconi anemia pathway function and BRCA2 interaction |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
Fanconi anemia ID complex | up-regulates 
|
BRCA2 |
0.783 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263270 |
|
|
|
|
| pmid |
sentence |
| 18985065 |
Once monoubiquitinated, the ID complex becomes associated with chromatin and is redistributed to DNA-damage sites, forming foci that are visible by immunofluorescence and colocalizing with other DNA-repair molecules, notably BRCA1, BRCA2 and γH2AX. |
|
| Publications: |
1 |
3.0
BRCA2
- 
- 