+ |
RNF168 |
ubiquitination
|
H2AX |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262063 |
Lys14 |
TGGKARAkAKSRSSR |
Homo sapiens |
|
pmid |
sentence |
22980979 |
We find that K63 ubiquitin chains are conjugated to RNF168-dependent H2A/H2AX monoubiquitination at K13-15 and not on K118-119. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
UBR5 | down-regulates quantity
ubiquitination
|
RNF168 |
0.454 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266782 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
22884692 |
Here, we show that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage. We find that RNF168 can be saturated by increasing amounts of DSBs. Depletion of TRIP12 and UBR5 allows accumulation of RNF168 to supraphysiological levels, followed by massive spreading of ubiquitin conjugates and hyperaccumulation of ubiquitin-regulated genome caretakers such as 53BP1 and BRCA1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Histone H2B | up-regulates
binding
|
RNF168 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265372 |
|
|
Homo sapiens |
|
pmid |
sentence |
19203578 |
Rnf168 is recruited to sites of dna damage by binding to ubiquitylated histone h2a. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RNF168 | down-regulates
polyubiquitination
|
H1-2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272927 |
|
|
Homo sapiens |
MDA-MB-231 Cell |
pmid |
sentence |
30517763 |
ITCH biochemically antagonized RNF168 and RNF8 in polyubiquitination of histone H1.2 ITCH interacts with and ubiquitinates linker histone H1.2 at K46. ITCH biochemically competes with RNF168 and RNF8 to polyubiquitinate histone H1.2. Both RNF168 and RNF8 elicited higher Ubn levels of K46R-H1.2 compared to WT-H1.2, suggesting that Ubn of H1.2 by both E3 ligases occurs at a site apart from K46. |
|
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 |
+ |
RNF168 | up-regulates quantity
ubiquitination
|
Histone H2A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266784 |
|
|
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 |
+ |
DGCR8 | up-regulates activity
binding
|
RNF168 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277309 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
34188037 |
Specifically, radiation-induced ATM-dependent phosphorylation of DGCR8 at serine 677 facilitates USP51 to bind, deubiquitinate, and stabilize DGCR8, which leads to the recruitment of DGCR8 and DGCR8's binding partner RNF168 to MDC1 and RNF8 at DSBs. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
L3MBTL2 | down-regulates quantity
binding
|
RNF168 |
0.248 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266788 |
|
|
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 |
+ |
TRIP12 | down-regulates activity
ubiquitination
|
RNF168 |
0.478 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266783 |
|
|
Homo sapiens |
U2-OS Cell |
pmid |
sentence |
22884692 |
Here, we show that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage. We find that RNF168 can be saturated by increasing amounts of DSBs. Depletion of TRIP12 and UBR5 allows accumulation of RNF168 to supraphysiological levels, followed by massive spreading of ubiquitin conjugates and hyperaccumulation of ubiquitin-regulated genome caretakers such as 53BP1 and BRCA1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
Ub:E2 | up-regulates activity
ubiquitination
|
RNF168 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271029 |
|
|
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 |
+ |
RNF168 | up-regulates
|
DNA_repair |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266789 |
|
|
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 |
+ |
H2AC11 | up-regulates
binding
|
RNF168 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-183890 |
|
|
Homo sapiens |
|
pmid |
sentence |
19203578 |
Rnf168 is recruited to sites of dna damage by binding to ubiquitylated histone h2a. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |