| + |
CASP3 | down-regulates quantity by destabilization 
cleavage
|
BRCA1 |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256326 |
Asp1155 |
ETPDDLLdDGEIKED |
Homo sapiens |
|
| pmid |
sentence |
| 12149654 |
We demonstrate the cleavage and the consequential downregulation of full-length BRCA1 by caspase-3 during UV-induced apoptosis. Finally, mutation of a caspase-3 specific cleavage site (D/A1154) rendered BRCA1 non-cleavable. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Caspase 3 complex | down-regulates quantity by destabilization
cleavage
|
BRCA1 |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256432 |
Asp1155 |
ETPDDLLdDGEIKED |
Homo sapiens |
|
| pmid |
sentence |
| 12149654 |
We demonstrate the cleavage and the consequential downregulation of full-length BRCA1 by caspase-3 during UV-induced apoptosis. Finally, mutation of a caspase-3 specific cleavage site (D/A1154) rendered BRCA1 non-cleavable. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATR | up-regulates activity 
phosphorylation
|
BRCA1 |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250581 |
Ser1143 |
PMGSSHAsQVCSETP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 11114888 |
Of the four potential phosphoacceptor sites in the BRCA1 (1005–1313) fragment (Ser 1143, Ser 1239, Ser 1280, Ser 1298), Ala substitutions at two sites, Ser 1143 and Ser 1280, reduced the in vitro phosphorylation of GST–BRCA1 (1005–1313) by ATR, whereas substitution of Ser 1239 or Ser 1298 with Ala had little or no effect (Fig. 2C; data not shown). A Ser 1143/Ser 1280 double mutant was a poor substrate for ATR, suggesting that these are the two major in vitro phosphorylation sites on this BRCA1 fragment. | Together, these results demonstrate that ATR and BRCA1 are components of the same genotoxic stress-responsive pathway, and that ATR directly phosphorylates BRCA1 in response to damaged DNA or stalled DNA replication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250582 |
Ser1280 |
QVILAKAsQEHHLSE |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 11114888 |
Of the four potential phosphoacceptor sites in the BRCA1 (1005–1313) fragment (Ser 1143, Ser 1239, Ser 1280, Ser 1298), Ala substitutions at two sites, Ser 1143 and Ser 1280, reduced the in vitro phosphorylation of GST–BRCA1 (1005–1313) by ATR, whereas substitution of Ser 1239 or Ser 1298 with Ala had little or no effect (Fig. 2C; data not shown). A Ser 1143/Ser 1280 double mutant was a poor substrate for ATR, suggesting that these are the two major in vitro phosphorylation sites on this BRCA1 fragment. | Together, these results demonstrate that ATR and BRCA1 are components of the same genotoxic stress-responsive pathway, and that ATR directly phosphorylates BRCA1 in response to damaged DNA or stalled DNA replication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106432 |
Ser1387 |
EDCSGLSsQSDILTT |
Homo sapiens |
Lymphoblastoid Cell Line |
| pmid |
sentence |
| 11278964 |
Brca1 is phosphorylated at ser-1423 and ser-1524 after ir and uv;however, ser-1387 is specifically phosphorylated after ir, and ser-1457 is predominantly phosphorylated after uv.atr controls brca1 phosphorylation in vivo. Taken together, our results support a model in which atm and atr act in parallel but somewhat overlapping pathways of dna damage signaling but respond primarily to different types of dna lesion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106436 |
Ser1423 |
AVLEQHGsQPSNSYP |
Homo sapiens |
Lymphoblastoid Cell Line |
| pmid |
sentence |
| 11278964 |
Brca1 is phosphorylated at ser-1423 and ser-1524 after ir and uv;however, ser-1387 is specifically phosphorylated after ir, and ser-1457 is predominantly phosphorylated after uv.atr controls brca1 phosphorylation in vivo. Taken together, our results support a model in which atm and atr act in parallel but somewhat overlapping pathways of dna damage signaling but respond primarily to different types of dna lesion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106440 |
Ser1457 |
SEKAVLTsQKSSEYP |
Homo sapiens |
Lymphoblastoid Cell Line |
| pmid |
sentence |
| 11278964 |
Brca1 is phosphorylated at ser-1423 and ser-1524 after ir and uv;however, ser-1387 is specifically phosphorylated after ir, and ser-1457 is predominantly phosphorylated after uv.atr controls brca1 phosphorylation in vivo. Taken together, our results support a model in which atm and atr act in parallel but somewhat overlapping pathways of dna damage signaling but respond primarily to different types of dna lesion. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250583 |
Thr1394 |
SQSDILTtQQRDTMQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 11114888 |
Although no single mutation eliminated the GST–BRCA1 (1314–1863) electrophoretic mobility shift, a quadruple mutant (GST–BRCA14A) containing Ala substitutions at Ser 1387, Thr 1394, Ser 1423, and Ser 1457 showed no alteration in electrophoretic mobility after phosphorylation by ATR-containing immune complexes (Fig.2D). The total incorporation of 32Pi into the GST–BRCA14Asubstrate was reduced by 70% relative to that obtained with wild-type GST–BRCA1 (1314–1863), suggesting that these four residues account for most, but not all of the phosphorylation sites in this fragment. | Together, these results demonstrate that ATR and BRCA1 are components of the same genotoxic stress-responsive pathway, and that ATR directly phosphorylates BRCA1 in response to damaged DNA or stalled DNA replication. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
CDK1 | up-regulates
phosphorylation
|
BRCA1 |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187595 |
Ser1189 |
QKGELSRsPSPFTHT |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 19683496 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72083 |
Ser1189 |
QKGELSRsPSPFTHT |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187599 |
Ser1191 |
GELSRSPsPFTHTHL |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 19683496 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72087 |
Ser1497 |
EPGVERSsPSKCPSL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187603 |
Ser1497 |
EPGVERSsPSKCPSL |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 19683496 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates
phosphorylation
|
BRCA1 |
0.813 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72048 |
Ser1330 |
QMRHQSEsQGVGLSD |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
The brca1 (breast cancer gene 1) tumor suppressor protein is phosphorylated in response to dna damage. phosphorylation of brca1 by the checkpoint kinase atm may be critical for proper responses to dna double-strand breaks |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91482 |
Ser1387 |
EDCSGLSsQSDILTT |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12183412 |
Phosphorylation of serine 1387 in brca1 is specifically required for the atm-mediated s-phase checkpoint after ionizing irradiation.We recently reported that brca1 function is required for appropriate cell cycle arrests after ionizing irradiation in both the s-phase and the g2 phase of the cell cycle. We also found that mutation of serine 1423 in brca1, a target of atm phosphorylation, abrogates the g2-m checkpoint but not the ionizing irradiation-induced s-phase checkpoint. Here we demonstrate that mutation of serine 1387 in brca1, another target of atm phosphorylation, conversely abrogates the radiation-induced s-phase arrest but does not affect the g2-m checkpoint. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72052 |
Ser1423 |
AVLEQHGsQPSNSYP |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
Phosphorylation of serine 1387 in brca1 is specifically required for the atm-mediated s-phase checkpoint after ionizing irradiation.We recently reported that brca1 function is required for appropriate cell cycle arrests after ionizing irradiation in both the s-phase and the g2 phase of the cell cycle. We also found that mutation of serine 1423 in brca1, a target of atm phosphorylation, abrogates the g2-m checkpoint but not the ionizing irradiation-induced s-phase checkpoint. Here we demonstrate that mutation of serine 1387 in brca1, another target of atm phosphorylation, conversely abrogates the radiation-induced s-phase arrest but does not affect the g2-m checkpoint. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72056 |
Ser1457 |
SEKAVLTsQKSSEYP |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
The brca1 (breast cancer gene 1) tumor suppressor protein is phosphorylated in response to dna damage. phosphorylation of brca1 by the checkpoint kinase atm may be critical for proper responses to dna double-strand breaks |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72060 |
Ser1466 |
KSSEYPIsQNPEGLS |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
The brca1 (breast cancer gene 1) tumor suppressor protein is phosphorylated in response to dna damage. phosphorylation of brca1 by the checkpoint kinase atm may be critical for proper responses to dna double-strand breaks |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187591 |
Ser1497 |
EPGVERSsPSKCPSL |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 19683496 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72064 |
Ser1497 |
EPGVERSsPSKCPSL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72068 |
Ser1524 |
LQNRNYPsQEELIKV |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
The brca1 (breast cancer gene 1) tumor suppressor protein is phosphorylated in response to dna damage. phosphorylation of brca1 by the checkpoint kinase atm may be critical for proper responses to dna double-strand breaks. Phosphorylation of brca1 on ser1423 and ser1524 by atm |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72072 |
Ser1542 |
EEQQLEEsGPHDLTE |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
The brca1 (breast cancer gene 1) tumor suppressor protein is phosphorylated in response to dna damage. phosphorylation of brca1 by the checkpoint kinase atm may be critical for proper responses to dna double-strand breaks. Phosphorylation of brca1 on ser1423 and ser1524 by atm |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87845 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12024016 |
Results from this study indicate that the checkpoint protein kinase atm (mutated in ataxia telangiectasia) was required for phosphorylation of brca1 in response to ionizing radiation. Brca1 is phosphorylated at tyrosine residues in an atm-dependent, radiation-dependent manner. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72075 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
Results from this study indicate that the checkpoint protein kinase atm (mutated in ataxia telangiectasia) was required for phosphorylation of brca1 in response to ionizing radiation. Brca1 is phosphorylated at tyrosine residues in an atm-dependent, radiation-dependent manner. |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
PPP1CA | down-regulates activity
dephosphorylation
|
BRCA1 |
0.384 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248561 |
Ser1423 |
AVLEQHGsQPSNSYP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17603999 |
Protein kinases involved in the DNA damage checkpoint control, such as ATM, ATR, and hCds1/Chk2, have been shown to phosphorylate and activate BRCA1 upon DNA damage. |Altogether, these results indicate that PP1α specifically dephosphorylates BRCA1 at multiple serine sites, including S988 [12], S1423, and S1524. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248562 |
Ser1524 |
LQNRNYPsQEELIKV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17603999 |
Protein kinases involved in the DNA damage checkpoint control, such as ATM, ATR, and hCds1/Chk2, have been shown to phosphorylate and activate BRCA1 upon DNA damage. |Altogether, these results indicate that PP1α specifically dephosphorylates BRCA1 at multiple serine sites, including S988 [12], S1423, and S1524. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248560 |
Ser988 |
PPLFPIKsFVKTKCK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17603999 |
Protein kinases involved in the DNA damage checkpoint control, such as ATM, ATR, and hCds1/Chk2, have been shown to phosphorylate and activate BRCA1 upon DNA damage. |Altogether, these results indicate that PP1α specifically dephosphorylates BRCA1 at multiple serine sites, including S988 [12], S1423, and S1524. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK2 | up-regulates
phosphorylation
|
BRCA1 |
0.664 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-187607 |
Ser1497 |
EPGVERSsPSKCPSL |
Homo sapiens |
Lung Cancer Cell |
| pmid |
sentence |
| 19683496 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72091 |
Ser1497 |
EPGVERSsPSKCPSL |
Homo sapiens |
|
| pmid |
sentence |
| 10550055 |
However, shrna-mediated depletion of cdk1 alone or small molecule cdk1 inhibition abrogated s phase cell-cycle arrest and the phosphorylation of a subset of atr/atm targets after dna damage. Loss of dna damage-induced checkpoint control was caused by a reduction in formation of brca1-containing foci. Mutation of brca1 at s1497 and s1189/s1191 resulted in loss of cdk1-mediated phosphorylation and also compromised formation of brca1-containing foci. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ATM |
phosphorylation
|
BRCA1 |
0.813 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72079 |
Ser1524 |
LQNRNYPsQEELIKV |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10550055 |
The brca1 (breast cancer gene 1) tumor suppressor protein is phosphorylated in response to dna damage. Results from this study indicate that the checkpoint protein kinase atm (mutated in ataxia telangiectasia) was required for phosphorylation of brca1 in response to ionizing radiation. Atm resides in a complex with brca1 and phosphorylated brca1 in vivo and in vitro in a region that contains clusters of serine-glutamine residues. Phosphorylation of this domain appears to be functionally important because a mutated brca1 protein lacking two phosphorylation sites failed to rescue the radiation hypersensitivity of a brca1-deficient cell line.Atm-dependent phosphorylation of ser1423 or ser1524 also occurred in vivo, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
CSNK2A1 |
phosphorylation
|
BRCA1 |
0.379 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250832 |
Ser1572 |
ESGISLFsDDPESDP |
in vitro |
|
| pmid |
sentence |
| 10403822 |
Subsequent studies showed that BRCA1 was phosphorylated in vitro by CK2. An analysis by site directed mutagenesis of BRCA1 showed that in vitro phosphorylation by CK2 required a serine at aa1572. These data implicate CK2 as a potential mediator of BRCA1 activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSNK2B |
phosphorylation
|
BRCA1 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251055 |
Ser1572 |
ESGISLFsDDPESDP |
in vitro |
|
| pmid |
sentence |
| 10403822 |
Subsequent studies showed that BRCA1 was phosphorylated in vitro by CK2. An analysis by site directed mutagenesis of BRCA1 showed that in vitro phosphorylation by CK2 required a serine at aa1572. These data implicate CK2 as a potential mediator of BRCA1 activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AURKA | up-regulates
phosphorylation
|
BRCA1 |
0.663 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123065 |
Ser308 |
KAEFCNKsKQPGLAR |
Homo sapiens |
|
| pmid |
sentence |
| 14990569 |
Previous studies have shown that the brca1 breast cancer tumor suppressor also localizes to the centrosome and that brca1 inactivation results in loss of the g(2)-m checkpoint. We demonstrate here that aurora-a physically binds to and phosphorylates brca1. We propose that brca1 phosphorylation by aurora-a plays a role in g(2) to m transition of cell cycle |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK4 | down-regulates
phosphorylation
|
BRCA1 |
0.651 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153450 |
Ser632 |
LVVSRNLsPPNCTEL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17334399 |
In particular, we have identified ser 632 of brca1 as a cyclin d1/cdk4 phosphorylation site in vitro. Using chromatin immunoprecipitation assays, we observed that the inhibition of cyclin d1/cdk4 activity resulted in increased brca1 dna binding at particular promoters in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinD/CDK4 | down-regulates
phosphorylation
|
BRCA1 |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216984 |
Ser632 |
LVVSRNLsPPNCTEL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17334399 |
In particular, we have identified ser 632 of brca1 as a cyclin d1/cdk4 phosphorylation site in vitro. Using chromatin immunoprecipitation assays, we observed that the inhibition of cyclin d1/cdk4 activity resulted in increased brca1 dna binding at particular promoters in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
AKT1 | up-regulates
phosphorylation
|
BRCA1 |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163472 |
Ser694 |
QTSKRHDsDTFPELK |
Homo sapiens |
|
| pmid |
sentence |
| 20085797 |
We identify a novel akt phosphorylation site in brca1 at s694 which is responsive to activation of these signaling pathways. These data suggest akt phosphorylation of brca1 increases total protein expression by preventing proteasomal degradation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154312 |
Thr509 |
LKRKRRPtSGLHPED |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17428466 |
Phosphatidylinositol 3-kinase/akt signaling enhances nuclear localization and transcriptional activity of brca1. mutation of threonine 509 in brca1, the site of akt phosphorylation, to an alanine, attenuates the ability of heregulin to induce brca1 nuclear accumulation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT | up-regulates
phosphorylation
|
BRCA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244164 |
Ser694 |
QTSKRHDsDTFPELK |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20085797 |
We identify a novel akt phosphorylation site in brca1 at s694 which is responsive to activation of these signaling pathways. These data suggest akt phosphorylation of brca1 increases total protein expression by preventing proteasomal degradation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244168 |
Thr509 |
LKRKRRPtSGLHPED |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17428466 |
Phosphatidylinositol 3-kinase/akt signaling enhances nuclear localization and transcriptional activity of brca1. mutation of threonine 509 in brca1, the site of akt phosphorylation, to an alanine, attenuates the ability of heregulin to induce brca1 nuclear accumulation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
CHEK2 | up-regulates
phosphorylation
|
BRCA1 |
0.78 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120575 |
Ser988 |
PPLFPIKsFVKTKCK |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 14701743 |
In this study, we tested the hypothesis that the brca1-mediated regulation of recombination requires the chk2- and atm-dependent phosphorylation sites. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
FRK | up-regulates quantity by stabilization
phosphorylation
|
BRCA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275454 |
Tyr1552 |
HDLTETSyLPRQDLE |
Homo sapiens |
HCC-1937 Cell |
| pmid |
sentence |
| 29156836 |
Herein, we demonstrate that Fyn-related kinase (Frk)/Rak plays an important role in maintaining genomic stability, possibly in part through positively regulating BRCA1 protein stability and function via tyrosine phosphorylation on BRCA1 Tyr1552. Rak-mediated tyrosine phosphorylation of BRCA1 is essential for its stability and function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | up-regulates activity
ubiquitination
|
FANCD2 |
0.839 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263236 |
|
|
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 | down-regulates activity 
|
ESR1 |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253974 |
|
|
Homo sapiens |
Breast Cancer Cell Line, Prostate Cancer Cell Line |
| pmid |
sentence |
| 11244506 |
The BRCA1 gene was previously found to inhibit the transcriptional activity of the estrogen receptor [ER-alpha] in human breast and prostate cancer cell lines. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UIMC1 | up-regulates
binding
|
BRCA1 |
0.907 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155201 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17525342 |
Rap80 specifically recruits brca1 to dna damage sites and functions with brca1 in g2/m checkpoint control |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXO44 | down-regulates quantity by destabilization
binding
|
BRCA1 |
0.376 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272037 |
|
|
in vitro |
|
| pmid |
sentence |
| 23086937 |
The F-box protein FBXO44 mediates BRCA1 ubiquitination and degradation. The Skp1-Cul1-F-box-protein44 (SCF(FBXO44)) complex ubiquitinates full-length BRCA1 in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ABRAXAS1 | up-regulates
binding
|
BRCA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155144 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17525340 |
Full length abraxas binds the brct-repeats of brca1the rap80-abraxas complex may help recruit brca1 to dna damage sites in part through recognition of ubiquitinated proteins |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Cullin 1-RBX1-Skp1 | down-regulates quantity by destabilization
polyubiquitination
|
BRCA1 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272039 |
|
|
in vitro |
|
| pmid |
sentence |
| 23086937 |
The F-box protein FBXO44 mediates BRCA1 ubiquitination and degradation. The Skp1-Cul1-F-box-protein44 (SCF(FBXO44)) complex ubiquitinates full-length BRCA1 in vitro. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PALB2 | up-regulates activity
binding
|
BRCA1 |
0.846 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244487 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 19369211 |
The BRCA1-PALB2 interaction is required for homologous recombination repair.Here, we report that PALB2, the partner and localizer of BRCA2, binds directly to BRCA1, and serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
CTBP1 | down-regulates quantity by repression
transcriptional regulation
|
BRCA1 |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259194 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23303449 |
Our findings suggest an important role of CtBP1 in the transcriptional control of p16INK4a and Brca1[.]. Breast Cancer Susceptibility Gene 1(Brca1), a core protein in DNA damage repair, was repressed by CtBP1 in melanoma cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BARD1 | up-regulates
binding
|
BRCA1 |
0.785 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162499 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20029420 |
Brac1 dimerizes with brca1?associated Ring domain protein 1 (bard1) to yield a functional e3 ligase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251500 |
|
|
|
|
| pmid |
sentence |
| 15549093 |
The BRCA1 protein also contributes to cell-cycle arrest and DNA repair by homologous recombination |
|
| Publications: |
1 |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
BRCA1 | down-regulates quantity by destabilization
ubiquitination
|
TOP1 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277353 |
|
|
Homo sapiens |
HCT-15 Cell |
| pmid |
sentence |
| 28415827 |
Here, we show that the Ku70/Ku80 heterodimer binds with topoI, and that the DNA-dependent protein kinase (DNA-PKcs) phosphorylates topoI on serine 10 (topoI-pS10), which is subsequently ubiquitinated by BRCA1. Taken together, we conclude that BRCA1 is the E3 ligase for topoI, and the rate of topoI proteasomal degradation determines CPT response. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | down-regulates quantity by destabilization
polyubiquitination
|
ERCC6 |
0.452 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272754 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21756275 |
BRCA1 polyubiquitinates CSB and this polyubiquitination and subsequent degradation of CSB occur following UV irradiation, even in the absence of Cockayne syndrome A (CSA) protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | up-regulates quantity by expression
transcriptional regulation
|
CDKN1B |
0.352 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-142888 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 16331276 |
We identified a foxa1 binding site within the brca1-responsive element of the p27(kip1) promoter and showed that foxa1 activated the promoter alone and in conjunction with brca1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
BRCA1 | up-regulates activity
binding
|
MRE11/RAD50/NBS1 |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251501 |
|
|
|
|
| pmid |
sentence |
| 10426999 |
BRCA1 encodes a tumor suppressor that is mutated in familial breast and ovarian cancers. Here, it is shown that BRCA1 interacts in vitro and in vivo with hRad50, which forms a complex with hMre11 and p95/nibrin. Upon irradiation, BRCA1 was detected in discrete foci in the nucleus, which colocalize with hRad50.| These data suggest that BRCA1 is important for the cellular responses to DNA damage that are mediated by the hRad50-hMre11-p95 complex. |
|
| Publications: |
1 |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
BRCA1 | up-regulates quantity by expression
transcriptional regulation
|
ATM |
0.813 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198467 |
|
|
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 22832221 |
Brca1/e2f1/ctipbinding to atm promoter activates atm transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
CTBP1 | down-regulates quantity by repression
transcriptional regulation
|
BRCA1 |
0.586 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259196 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21681822 |
Carboxyl-terminal binding protein 1 (CtBP1) is a transcriptional co-repressor with oncogenic potential. We found CtBP1 was recruited to the promoter regions of Brca1 and E-cadherin genes in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | down-regulates
|
Cell_cycle_progress |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267282 |
|
|
|
|
| pmid |
sentence |
| 15549093 |
The BRCA1 protein also contributes to cell-cycle arrest and DNA repair by homologous recombination |
|
| Publications: |
1 |
| + |
BRCA1 | up-regulates quantity by expression
transcriptional regulation
|
RNASEL |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253762 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15940267 |
We propose that BRCA1 may be an upstream regulator of RNaseL, acting in concert with IFN-gamma to transcriptionally activate 2,5 OAS, leading to the downstream activation of RNaseL and apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | down-regulates quantity by repression
transcriptional regulation
|
CTSD |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253759 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 11244506 |
BRCA1 blocked the expression of two endogenous estrogen-regulated gene products in human breast cancer cells: pS2 and cathepsin D. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | down-regulates quantity by destabilization
ubiquitination
|
AKT |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252458 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 19074868 |
The BRCA1-BRCT domains bind to phosphorylated AKT (pAKT) and lead to its ubiquitination toward protein degradation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
ASPM | up-regulates quantity by expression
transcriptional regulation
|
BRCA1 |
0.276 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253936 |
|
|
|
|
| pmid |
sentence |
| 16123590 |
Here, we report that downregulation of endogenous ASPM by siRNA decreases protein levels of endogenous BRCA1. ASPM localizes to the centrosome in interphase and to the spindle poles from prophase through telophase. These findings indicate that ASPM may be involved in mitotic spindle function, possibly, through regulation of BRCA1. |
|
| Publications: |
1 |
| + |
BRCA1 | down-regulates quantity by repression
transcriptional regulation
|
FOXC2 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253760 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 22120723 |
We show that the BRCA1-GATA3 interaction is important for the repression of genes associated with triple-negative and basal-like breast cancer (BLBCs) including FOXC1, and that GATA3 interacts with a C-terminal region of BRCA1. We demonstrate that this BRCA1-GATA3 repression complex is not a FOXC1-specific phenomenon as a number of other genes associated with BLBCs such as FOXC2, CXCL1 and p-cadherin were also repressed in a similar manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | up-regulates
|
Cell_cycle_block |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251499 |
|
|
|
|
| pmid |
sentence |
| 15549093 |
The BRCA1 protein also contributes to cell-cycle arrest and DNA repair by homologous recombination |
|
| Publications: |
1 |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
BRCA1 | up-regulates
ubiquitination
|
RBBP8 |
0.836 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16818604 |
In conclusion, our data show that ctip is a physiological substrate of the brca1 e3 ligase. Brca1 recruits ctip through its c-terminal brct domains and promotes ctip ubiquitination through its n-terminal ring domain. The ubiquitinated ctip is not targeted for degradation. Instead, ubiquitinated ctip binds to chromatin following dna damage and is likely to be involved in dna damage checkpoint control. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | form complex 
binding
|
BRCA1-BARD1 complex |
0.785 |
| 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 |
| + |
HDLBP | up-regulates activity
binding
|
BRCA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266698 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 33941620 |
We show that vigilin interacts with the DNA damage response (DDR) proteins RAD51 and BRCA1, and vigilin depletion impairs their recruitment to DSB sites. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRIP1 | up-regulates activity
binding
|
BRCA1 |
0.787 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259185 |
|
|
Homo sapiens |
MCF-7 Cell, HCC-1937 Cell |
| pmid |
sentence |
| 11301010 |
BRCA1 interacts in vivo with a novel protein, BACH1, a member of the DEAH helicase family. BACH1 binds directly to the BRCT repeats of BRCA1. Moreover, BACH1 likely contributes to the DNA repair function of BRCA1 []. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | down-regulates activity
binding
|
ACACA |
0.563 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267474 |
|
|
in vitro |
|
| pmid |
sentence |
| 16698035 |
ACCA binds BRCA1 when phosphorylated onSer1263, thus supporting a model in which controlof lipid synthesis would be mediated at least in part,viaphosphorylation of the Ser1263. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BRCA1 | down-regulates quantity by repression
transcriptional regulation
|
TFF1 |
0.304 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253937 |
|
|
Homo sapiens |
Breast Cancer Cell Line, Prostate Cancer Cell Line |
| pmid |
sentence |
| 11244506 |
In addition, BRCA1 blocked the expression of two endogenous estrogen-regulated gene products in human breast cancer cells: pS2 and cathepsin D. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATR | up-regulates
phosphorylation
|
BRCA1 |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201050 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23422745 |
The phosphorylation of atr and atm substrates, chk1, chk2, h2ax, and brca1 was significantly reduced or abrogated in mutant cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer, Cell cycle: G2/M phase transition |
| + |
RAD50 | up-regulates
binding
|
BRCA1 |
0.779 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69701 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10426999 |
Brca1 interacts in vitro and in vivo with hrad50. Brca1 is important for the cellular responses to dna damage that are mediated by the hrad50-hmre11-p95 complex. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
RBBP8 | up-regulates activity
relocalization
|
BRCA1 |
0.836 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263203 |
|
|
|
|
| pmid |
sentence |
| 24832651 |
DNA damage activates ATM and CHK2 kinases, which mediate phosphorylation of CtIP and BRCA1. Phosphorylated CtIP associates with BRCA1 and with the MRN complex leading to the recruitment of the BRCC complex at the site of DNA damage where HR is initiated. |
|
| Publications: |
1 |
| + |
Fanconi anemia ID complex | up-regulates
|
BRCA1 |
0.826 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263271 |
|
|
|
|
| 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 |
| + |
BRCA1 | down-regulates quantity by destabilization
ubiquitination
|
AKT1 |
0.521 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252435 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 19074868 |
The BRCA1-BRCT domains bind to phosphorylated AKT (pAKT) and lead to its ubiquitination toward protein degradation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
BRCA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271105 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 34199813 |
The ubiquitination process is mediated sequentially by three classes of enzymes consisting of a Ub-activating enzyme E1, a Ub-conjugating enzyme E2, and a Ub ligase E3. Ub is first activated by E1 in an adenosine 5′-triphosphate (ATP)-dependent manner t |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRCA1 | down-regulates quantity by repression
transcriptional regulation
|
HSPA5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253761 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 18776923 |
We report here that glucose-regulated protein (GRP)-78, a critical regulator of the unfolded protein response (UPR), is a novel downstream target of BRCA1. We showed that overexpression of wild-type BRCA1 suppressed the expression of GRP78, whereas expression of mutant BRCA1 gene or targeted inhibition of endogenous BRCA1 using small-interfering RNA (siRNA) enhanced GRP78 expression. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BRCA1
- 
- 