| + |
ABL1 | up-regulates activity 
phosphorylation
|
RAD52 |
0.672 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251435 |
Tyr104 |
DLNNGKFyVGVCAFV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12379650 |
C-Abl tyrosine kinase associates with and phosphorylates Rad52 on tyrosine 104. he functional significance of c-Abl-dependent phosphorylation of Rad52 is underscored by our findings that cells that express the phosphorylation-resistant Rad52 mutant, in which tyrosine 104 is replaced by phenylalanine, exhibit compromised nuclear foci formation in response to IR. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247661 |
Tyr104 |
DLNNGKFyVGVCAFV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12379650 |
We show here that c-Abl tyrosine kinase associates with and phosphorylates Rad52 on tyrosine 104. Importantly, the very same site of Rad52 is phosphorylated on exposure of cells to ionizing radiation (IR). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
BCR-ABL | up-regulates activity
phosphorylation
|
RAD52 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262531 |
Tyr104 |
DLNNGKFyVGVCAFV |
Homo sapiens |
|
| pmid |
sentence |
| 23836560 |
Have found that BCR-ABL1 interacts with the C-terminal portion of RAD52, resulting in tyrosine phosphorylation of Y104 located in RAD52 DNA II and enhanced nuclear foci formation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD52 | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251507 |
|
|
|
|
| pmid |
sentence |
| 27649245 |
Homologous recombination (HR) plays an important role in maintaining genomic integrity. It is responsible for repair of the most harmful DNA lesions, DNA double-strand breaks and inter-strand DNA cross-links. HR function is also essential for proper segregation of homologous chromosomes in meiosis, maintenance of telomeres, and resolving stalled replication forks. Defects in HR often lead to genetic diseases and cancer. Rad52 is one of the key HR proteins, which is evolutionarily conserved from yeast to humans| in mammals, Rad52 knockouts showed no significant DNA repair or recombination phenotype. |These new findings indicate an important backup role for Rad52, which complements the main HR mechanism in mammals. |
|
| Publications: |
1 |
| Pathways: | Cell cycle: G2/M phase transition |
3.0
RAD52
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- 