| + |
CyclinA2/CDK2 | down-regulates quantity by destabilization 
phosphorylation
|
BLM |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276910 |
Ser175 |
SFVTPPQsHFVRVST |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276907 |
Thr171 |
ETSKSFVtPPQSHFV |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates quantity by destabilization
phosphorylation
|
BLM |
0.262 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276911 |
Ser175 |
SFVTPPQsHFVRVST |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276906 |
Thr171 |
ETSKSFVtPPQSHFV |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CHEK1 | up-regulates 
phosphorylation
|
BLM |
0.772 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167534 |
Ser646 |
LKHERFQsLSFPHTK |
Homo sapiens |
|
| pmid |
sentence |
| 20719863 |
Hese results indicated that chk1-mediated phosphorylation on blm at ser(646) might be a determinant for regulating subnuclear localization and could act as a marker for the activation status of blm in response to dna damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK1 | down-regulates quantity by destabilization
phosphorylation
|
BLM |
0.772 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276909 |
Thr182 |
SHFVRVStAQKSKKG |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates.Phosphorylation on BLM Thr171 and Ser175 depends on prior phosphorylation at Thr182 by Chk1/Chk2. Thr182 phosphorylation not only controls BLM ubiquitylation and degradation during mitosis but is also a determinant for its localization on the ultrafine bridges. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CHEK2 | down-regulates quantity by destabilization
phosphorylation
|
BLM |
0.543 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276908 |
Thr182 |
SHFVRVStAQKSKKG |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates.Phosphorylation on BLM Thr171 and Ser175 depends on prior phosphorylation at Thr182 by Chk1/Chk2. Thr182 phosphorylation not only controls BLM ubiquitylation and degradation during mitosis but is also a determinant for its localization on the ultrafine bridges. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATM | up-regulates
phosphorylation
|
BLM |
0.767 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88010 |
Thr99 |
NAPAGQEtQRGGSKS |
Homo sapiens |
|
| pmid |
sentence |
| 12034743 |
Mitotic phosphorylation of blm was partially dependent on atm, and phosphorylation sites on blm were identified. A phosphospecific antibody against one of these sites (thr-99) revealed radiation-induced phosphorylation, which was defective in ataxia-telangiectasia cells. These data suggest that atm and blm function together in recognizing abnormal dna structures by direct interaction and that these phosphorylation sites in blm are important for radiosensitivity status but not for sce frequency. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MSH6 | up-regulates
binding
|
BLM |
0.618 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123705 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15064730 |
We show that the recombinant hmsh2/6 protein complex stimulated the ability of the bloom's syndrome gene product, blm, to process holliday junctions in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MSH2/MSH6 | up-regulates
binding
|
BLM |
0.61 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217223 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15064730 |
We show that the recombinant hmsh2/6 protein complex stimulated the ability of the bloom's syndrome gene product, blm, to process holliday junctions in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MSH2 | up-regulates
binding
|
BLM |
0.601 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123699 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15064730 |
We show that the recombinant hmsh2/6 protein complex stimulated the ability of the bloom's syndrome gene product, blm, to process holliday junctions in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
BLM |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276912 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 26028025 |
We now provide evidence that BLM undergoes K48-linked ubiquitylation and subsequent degradation during mitosis due to the E3 ligase, Fbw7α. Fbw7α carries out its function after GSK3β- and CDK2/cyclin A2-dependent phosphorylation events on Thr171 and Ser175 of BLM which lies within a well-defined phosphodegron, a sequence which is conserved in all primates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BLM | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261824 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28912125 |
The BLM gene product, BLM, is a RECQ helicase that is involved in DNA replication and repair of DNA double-strand breaks by the homologous recombination (HR) pathway. During HR, BLM has both pro- and anti-recombinogenic activities, either of which may contribute to maintenance of genomic integrity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF168 | up-regulates activity
ubiquitination
|
BLM |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272114 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 23708797 |
Here, we demonstrate that the ubiquitin/SUMO-dependent DNA damage response (UbS-DDR), controlled by the E3 ligases RNF8/RNF168, triggers BLM recruitment to sites of replication fork stalling via ubiquitylation in the N-terminal region of BLM and subsequent BLM binding to the ubiquitin-interacting motifs of RAP80. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | up-regulates activity
ubiquitination
|
BLM |
0.343 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272115 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 23708797 |
Here, we demonstrate that the ubiquitin/SUMO-dependent DNA damage response (UbS-DDR), controlled by the E3 ligases RNF8/RNF168, triggers BLM recruitment to sites of replication fork stalling via ubiquitylation in the N-terminal region of BLM and subsequent BLM binding to the ubiquitin-interacting motifs of . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BLM | up-regulates activity
binding
|
UIMC1 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272116 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 23708797 |
Here, we demonstrate that the ubiquitin/SUMO-dependent DNA damage response (UbS-DDR), controlled by the E3 ligases RNF8/RNF168, triggers BLM recruitment to sites of replication fork stalling via ubiquitylation in the N-terminal region of BLM and subsequent BLM binding to the ubiquitin-interacting motifs of . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BRIP1 | up-regulates quantity by stabilization
binding
|
BLM |
0.642 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259186 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21240188 |
In this work, FANCJ and BLM were found to interact physically and functionally in human cells and co-localize to nuclear foci in response to replication stress. The cellular level of BLM is strongly dependent upon FANCJ, and BLM is degraded by a proteasome-mediated pathway when FANCJ is depleted. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
BLM
- 
- 