| + |
UCHL3 | up-regulates activity 
deubiquitination
|
RAD51 |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275907 |
Lys57 |
EAVAYAPkKELINIK |
|
|
| pmid |
sentence |
| 27941124 |
Here we report that ubiquitination of RAD51 hinders RAD51-BRCA2 interaction, while deubiquitination of RAD51 facilitates RAD51-BRCA2 binding and RAD51 recruitment and thus is critical for proper HR. | UCHL3, in turn, deubiquitinates RAD51 and promotes the binding between RAD51 and BRCA2.|Our results suggested that three lysine sites (56, 57, and 63) on RAD51 that are close to E59 are deubiquitinated by UCHL3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275908 |
Lys58 |
AVAYAPKkELINIKG |
|
|
| pmid |
sentence |
| 27941124 |
Here we report that ubiquitination of RAD51 hinders RAD51-BRCA2 interaction, while deubiquitination of RAD51 facilitates RAD51-BRCA2 binding and RAD51 recruitment and thus is critical for proper HR. | UCHL3, in turn, deubiquitinates RAD51 and promotes the binding between RAD51 and BRCA2.|Our results suggested that three lysine sites (56, 57, and 63) on RAD51 that are close to E59 are deubiquitinated by UCHL3. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275909 |
Lys64 |
KKELINIkGISEAKA |
|
|
| pmid |
sentence |
| 27941124 |
Here we report that ubiquitination of RAD51 hinders RAD51-BRCA2 interaction, while deubiquitination of RAD51 facilitates RAD51-BRCA2 binding and RAD51 recruitment and thus is critical for proper HR. | UCHL3, in turn, deubiquitinates RAD51 and promotes the binding between RAD51 and BRCA2.|Our results suggested that three lysine sites (56, 57, and 63) on RAD51 that are close to E59 are deubiquitinated by UCHL3. |
|
| Publications: |
3 |
| + |
Cullin 1-RBX1-Skp1 | up-regulates activity
ubiquitination
|
RAD51 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272453 |
Lys58 |
AVAYAPKkELINIKG |
in vitro |
|
| pmid |
sentence |
| 25585578 |
The F-box DNA helicase 1 (FBH1) is a 3'-5' DNA helicase with a putative function as a negative regulator of HR. It is the only known DNA helicase to contain an F-box, suggesting that one of its functions is to act as a ubiquitin ligase as part of an SCF (SKP1, CUL1 and F-box) complex. Here we report that the central player in HR, RAD51, is ubiquitylated by the SCF(FBH1) complex. Expression of an ubiquitylation-resistant form of RAD51 in human cells leads to hyperrecombination, as well as several phenotypes indicative of an altered response to DNA replication stress. However, K58/64R RAD51 was ubiquitylated much less efficiently by FBH1 in vitro than was wild-type (WT) RAD51 (Fig. 1d), confirming that the primary sites of modification by FBH1 on RAD51 are K58 and K64. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272454 |
Lys64 |
KKELINIkGISEAKA |
in vitro |
|
| pmid |
sentence |
| 25585578 |
The F-box DNA helicase 1 (FBH1) is a 3'-5' DNA helicase with a putative function as a negative regulator of HR. It is the only known DNA helicase to contain an F-box, suggesting that one of its functions is to act as a ubiquitin ligase as part of an SCF (SKP1, CUL1 and F-box) complex. Here we report that the central player in HR, RAD51, is ubiquitylated by the SCF(FBH1) complex. Expression of an ubiquitylation-resistant form of RAD51 in human cells leads to hyperrecombination, as well as several phenotypes indicative of an altered response to DNA replication stress. However, K58/64R RAD51 was ubiquitylated much less efficiently by FBH1 in vitro than was wild-type (WT) RAD51 (Fig. 1d), confirming that the primary sites of modification by FBH1 on RAD51 are K58 and K64. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CHEK1 | up-regulates
phosphorylation
|
RAD51 |
0.837 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133375 |
Thr309 |
LRKGRGEtRICKIYD |
Homo sapiens |
|
| pmid |
sentence |
| 15665856 |
We demonstrate that chk1 interacts with rad51, and that rad51 is phosphorylated on thr 309 in a chk1-dependent manner |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer, FLT3-ITD signaling, Cell cycle: G2/M phase transition |
| + |
BCR-ABL | up-regulates activity
phosphorylation
|
RAD51 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271707 |
Tyr315 |
ETRICKIyDSPCLPE |
Homo sapiens |
32D Cell |
| pmid |
sentence |
| 11684015 |
RAD51 is one of six mitotic human homologs of the E. coli RecA protein (RAD51-Paralogs) that play a central role in homologous recombination and repair of DNA double-strand breaks (DSBs).|Phosphorylation of the RAD51 Tyr-315 residue by BCR/ABL appears essential for enhanced DSB repair and drug resistance. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
ABL1 | up-regulates activity
phosphorylation
|
RAD51 |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247599 |
Tyr315 |
ETRICKIyDSPCLPE |
Mus musculus |
32D Clone3 Cell |
| pmid |
sentence |
| 11684015 |
Phosphorylation of the RAD51 Tyr-315 residue by BCR/ABL appears essential for enhanced DSB repair and drug resistance |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260777 |
Tyr315 |
ETRICKIyDSPCLPE |
Homo sapiens |
|
| pmid |
sentence |
| 10212258 |
Tyrosine Phosphorylation of Rad51 by ABL1 Enhances the Interaction between Rad51 and Rad52 | our studies of Rad51·Rad52 complex formation in vitro and in vivo suggest that the ATM and ABL1-mediated signaling is likely to promote repair given the biochemical evidence that Rad51 acts in concert with Rad52 in homologous recombination |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-247594 |
Tyr315 |
ETRICKIyDSPCLPE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10212258 |
Mutation of Rad51 Tyr315, but not Tyr205, Tyr191, or Tyr54 to phenylalanine abolished Rad51 tyrosine phosphorylation by c-Abl (Fig. 3 b). These results strongly suggest that c-Abl phosphorylates Rad51 Tyr315 in vivo |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251434 |
Tyr315 |
ETRICKIyDSPCLPE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 10212258 |
C-Abl phosphorylates Rad51 in vitro and in vivo. phosphorylation of Rad51 by c-Abl enhances complex formation between Rad51 and Rad52, which cooperates with Rad51 in recombination and repair. c-Abl phosphorylates Rad51 Tyr315 |
|
| Publications: |
4 |
Organism: |
Mus Musculus, Homo Sapiens, Chlorocebus Aethiops |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
ABL1 | down-regulates 
phosphorylation
|
RAD51 |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55482 |
Tyr54 |
HTVEAVAyAPKKELI |
Homo sapiens |
|
| pmid |
sentence |
| 9461559 |
Here we demonstrate that c-abl interacts constitutively with rad51. We show that c-abl phosphorylates rad51 on tyr-54 in vitro. The results also show that treatment of cells with ionizing radiation induces c-abl-dependent phosphorylation of rad51. Phosphorylation of rad51 by c-abl inhibits the binding of rad51 to dna and the function of rad51 in atp-dependent dna strand exchange reactions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
FBH1 | up-regulates activity
binding
|
RAD51 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272451 |
|
|
in vitro |
|
| pmid |
sentence |
| 25585578 |
The F-box DNA helicase 1 (FBH1) is a 3'-5' DNA helicase with a putative function as a negative regulator of HR. It is the only known DNA helicase to contain an F-box, suggesting that one of its functions is to act as a ubiquitin ligase as part of an SCF (SKP1, CUL1 and F-box) complex. Here we report that the central player in HR, RAD51, is ubiquitylated by the SCF(FBH1) complex. Expression of an ubiquitylation-resistant form of RAD51 in human cells leads to hyperrecombination, as well as several phenotypes indicative of an altered response to DNA replication stress. However, K58/64R RAD51 was ubiquitylated much less efficiently by FBH1 in vitro than was wild-type (WT) RAD51 (Fig. 1d), confirming that the primary sites of modification by FBH1 on RAD51 are K58 and K64. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
RAD51 | form complex 
binding
|
BRCC ubiquitin ligase complex |
0.743 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263206 |
|
|
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 |
| + |
RAD51 | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251508 |
|
|
|
|
| pmid |
sentence |
| 27660832 |
Rad51 is a key component of homologous recombination (HR) to repair DNA double-strand breaks and it forms Rad51 recombinase filaments of broken single-stranded DNA to promote HR. In addition to its role in DNA repair and cell cycle progression, Rad51 contributes to the reprogramming process during the generation of induced pluripotent stem cells |
|
| Publications: |
1 |
| Pathways: | Acute Myeloid Leukemia, DNA repair in cancer, FLT3-ITD in AML, Cell cycle: G2/M phase transition |
| + |
XRCC3 | up-regulates activity
relocalization
|
RAD51 |
0.737 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263258 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 23438602 |
We examined the effect of XRCC3 depletion on redistribution of RAD51 upon IR damage|Interestingly, cells expressing the XRCC3 S225A phosphomutant showed compromised chromatin loading of RAD51 upon IR damage (Fig. 4G) while the nuclear and cytosolic fractions of RAD51 were largely unchanged|It is likely that BRCA2 may directly participate in RAD51 recruitment and XRCC3 may stabilize the RAD51 filament which is in part mediated by phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STAT5A | up-regulates quantity by expression
transcriptional regulation
|
RAD51 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261552 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15626738 |
FLT3-ITD-TKD dual mutants induce hyperactivation of STAT5 and up-regulation of its downstream targets Bcl-x(L) and RAD51 in Ba/F3 cells |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling |
| + |
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 |
| + |
XRCC3 | up-regulates quantity by stabilization
binding
|
RAD51 |
0.737 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262667 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23438602 |
XRCC3 activation is essential for the recruitment of RAD51 to the sites of DNA lesions. It is likely that BRCA2 may directly participate in RAD51 recruitment and XRCC3 may stabilize the RAD51 filament which is in part mediated by phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD51AP1 | up-regulates activity
binding
|
RAD51 |
0.762 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261962 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17996711 |
Homologous recombination (HR) repairs chromosome damage and is indispensable for tumor suppression in humans. RAD51 mediates the DNA strand-pairing step in HR. RAD51 associated protein 1 (RAD51AP1) is a RAD51-interacting protein whose function has remained elusive. Biochemical and cytological results show that RAD51AP1 functions at a step subsequent to the assembly of the RAD51-ssDNA nucleoprotein filament. Purified RAD51AP1 binds both dsDNA and a D loop structure and, only when able to interact with RAD51, greatly stimulates the RAD51-mediated D loop reaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAD51 | up-regulates activity
binding
|
SYCP3 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264205 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 10525529 |
The eukaryotic RecA homologues RAD51 and DMC1 function in homology recognition and formation of joint-molecule recombination intermediates during yeast meiosis. We also show that mouse RAD51 and DMC1 establish protein-protein interactions with each other and with the chromosome core component COR1(SCP3) in a two-hybrid system and in vitro binding analyses. These results suggest that the formation of a multiprotein recombination complex associated with the meiotic chromosome cores is essential for the development and fulfillment of the meiotic recombination process. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FLT3 | up-regulates quantity by expression
transcriptional regulation
|
RAD51 |
0.254 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261550 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 15626738 |
FLT3-ITD-TKD dual mutants induce hyperactivation of STAT5 and up-regulation of its downstream targets Bcl-x(L) and RAD51 in Ba/F3 cells |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, FLT3-ITD in AML, FLT3-ITD signaling |
| + |
RAD51 | up-regulates activity
binding
|
Synaptonemal_complex |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264207 |
|
|
Mus musculus |
Spermatocyte |
| pmid |
sentence |
| 10525529 |
The eukaryotic RecA homologues RAD51 and DMC1 function in homology recognition and formation of joint-molecule recombination intermediates during yeast meiosis. We also show that mouse RAD51 and DMC1 establish protein-protein interactions with each other and with the chromosome core component COR1(SCP3) in a two-hybrid system and in vitro binding analyses. These results suggest that the formation of a multiprotein recombination complex associated with the meiotic chromosome cores is essential for the development and fulfillment of the meiotic recombination process. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PALB2 | up-regulates
binding
|
RAD51 |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185656 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19423707 |
We propose that both palb2 chromatin association and its oligomerization serve to secure the brca2 x rad51 repair machinery at the sites of dna damage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | DNA repair in cancer |
| + |
HDLBP | up-regulates activity
binding
|
RAD51 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266697 |
|
|
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 |
| + |
D1-D2-G-X3 complex | up-regulates activity
relocalization
|
RAD51 |
0.682 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263259 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23438602 |
We examined the effect of XRCC3 depletion on redistribution of RAD51 upon IR damage|Interestingly, cells expressing the XRCC3 S225A phosphomutant showed compromised chromatin loading of RAD51 upon IR damage (Fig. 4G) while the nuclear and cytosolic fractions of RAD51 were largely unchanged|It is likely that BRCA2 may directly participate in RAD51 recruitment and XRCC3 may stabilize the RAD51 filament which is in part mediated by phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Caspase 3 complex | down-regulates quantity by destabilization
cleavage
|
RAD51 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271708 |
|
|
Homo sapiens |
32D Cell |
| pmid |
sentence |
| 11684015 |
The RAD51 protein has been shown to be a substrate for caspase-3|he activated caspase-3 fragments (19 kDa and 17 kDa) and caspase-3 cleaved RAD51 fragment (∼23 kDa) was detected by Western analysis (Figure 3E). Activation of caspase-3 and the signature proteolytic degradation product of RAD51 only occurred in parental 32Dcl3 cells after treatment with cisplatin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates
phosphorylation
|
RAD51 |
0.764 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67069 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10212258 |
C-abl phosphorylates rad51 in vitro and in vivo. In assays using purified components, phosphorylation of rad51 by c-abl enhances complex formation between rad51 and rad52, which cooperates with rad51 in recombination and repair |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Cell cycle: G2/M phase transition |
| + |
CASP3 | down-regulates quantity by destabilization
cleavage
|
RAD51 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271709 |
|
|
Homo sapiens |
32D Cell |
| pmid |
sentence |
| 11684015 |
The RAD51 protein has been shown to be a substrate for caspase-3|he activated caspase-3 fragments (19 kDa and 17 kDa) and caspase-3 cleaved RAD51 fragment (∼23 kDa) was detected by Western analysis (Figure 3E). Activation of caspase-3 and the signature proteolytic degradation product of RAD51 only occurred in parental 32Dcl3 cells after treatment with cisplatin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RAD51
- 
- 