| + |
RNF8 | up-regulates quantity by stabilization 
polyubiquitination
|
ACD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272722 |
Lys147 |
QDLDVQKkLYDCLEE |
Homo sapiens |
|
| pmid |
sentence |
| 22101936 |
The Rnf8 RING-finger domain is essential for Tpp1 stability and retention at telomeres. Rnf8 physically interacts with Tpp1 to generate Ubc13-dependent Lys63 polyubiquitin chains that stabilize Tpp1 at telomeres. The conserved Tpp1 residue Lys233 is important for Rnf8-mediated Tpp1 ubiquitylation and localization to telomeres. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | up-regulates activity
ubiquitination
|
XRN2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277195 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 37697435 |
Mechanistically, RNF8 interacts with XRN2, which is crucial for transcription termination and R-loop resolution. We report that RNF8 ubiquitylates XRN2 to facilitate its recruitment to R-loop-prone genomic loci and that RNF8 deficiency in BRCA1-mutant breast cancer cells decreases XRN2 occupancy at R-loop-prone sites, thereby promoting R-loop accumulation, transcription-replication collisions, excessive genomic instability, and cancer cell death. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | up-regulates
ubiquitination
|
H2AX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159309 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18001824 |
Rnf8 can ubiquitylate histone h2a and h2ax, |
|
| 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 |
| + |
RNF8 | up-regulates 
|
DNA_repair |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266790 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31225475 |
L3MBTL2 links RNF8 and RNF168 in the DNA double strand break response. The protein kinase ATM phosphorylates L3MBTL2, which recruits it to the DNA lesion by promoting the interaction between MDC1 and L3MBTL2. L3MBTL2 is subsequently ubiquitinated by RNF8, which acts as a docking site for RNF168, thereby recruiting the ubiquitin ligase to the damage site. RNF168, in turn, ubiquitinates H2A-type histones to amplify the DNA damage response and recruit downstream DNA repair proteins for proper DSB signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | up-regulates
ubiquitination
|
H2AC11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166174 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20551964 |
Rnf8 and ubc13 ubiquitylate h2a and h2ax, but other substrates probably exist. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MDC1 | up-regulates
relocalization
|
RNF8 |
0.749 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179820 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18678647 |
Rnf8 relocalizes to dna damage sites via a phospho-dependent interaction with mdc1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | up-regulates
binding
|
UBE2N |
0.74 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179823 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18678647 |
The rnf8 ring domain signals ubc13 to sites of damage, which is sufficient for dna damage signal transduction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | down-regulates 
polyubiquitination
|
H1-2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272928 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 30517763 |
ITCH interacts with and ubiquitinates linker histone H1.2 at K46. ITCH biochemically competes with RNF168 and RNF8 to polyubiquitinate histone H1.2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | up-regulates
binding
|
RAD18 |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185593 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19396164 |
Rnf8 depletion also significantly reduced the accumulation of rad18 to chromatin fraction after ir |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF8 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270987 |
|
|
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 |
| + |
RNF8 | up-regulates activity
ubiquitination
|
L3MBTL2 |
0.244 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266787 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31225475 |
L3MBTL2 links RNF8 and RNF168 in the DNA double strand break response. The protein kinase ATM phosphorylates L3MBTL2, which recruits it to the DNA lesion by promoting the interaction between MDC1 and L3MBTL2. L3MBTL2 is subsequently ubiquitinated by RNF8, which acts as a docking site for RNF168, thereby recruiting the ubiquitin ligase to the damage site. RNF168, in turn, ubiquitinates H2A-type histones to amplify the DNA damage response and recruit downstream DNA repair proteins for proper DSB signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF8 | up-regulates
ubiquitination
|
Histone H2A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20551964 |
Rnf8 and ubc13 ubiquitylate h2a and h2ax, but other substrates probably exist. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
RNF8
- 
- 