Relation Results

Summary

Name RNF168
Full Name E3 ubiquitin-protein ligase RNF168
Synonyms hRNF168, RING finger protein 168
Primary ID Q8IYW5
Links - -
Type protein
Relations 13
Function E3 ubiquitin-protein ligase required for accumulation of repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to amplify the RNF8-dependent h ...
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Type: Score: Layout: SPV 
0.20.20.70.20.2470.4730.8190.20.2640.20.20.20.449RNF168H2AXUb:E2DNA_repairHistone H2BL3MBTL2TRIP12TP53BP1Histone H2ABLMH2AC11H1-2DGCR8UBR5

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ RNF168 img/unknown.png ubiquitination H2AX 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-262063 Lys14 TGGKARAkAKSRSSR Homo sapiens
pmid sentence
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
+ Ub:E2up-regulates activity img/direct-activation.png ubiquitination RNF168 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271029 Homo sapiens
pmid sentence
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
+ RNF168up-regulates img/indirect-activation.png DNA_repair 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-266789 Homo sapiens
pmid sentence
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
+ Histone H2Bup-regulates img/direct-activation.png binding RNF168 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265372 Homo sapiens
pmid sentence
Rnf168 is recruited to sites of dna damage by binding to ubiquitylated histone h2a.
Publications: 1 Organism: Homo Sapiens
+ L3MBTL2down-regulates quantity img/direct_inhibition.png binding RNF168 0.247
Identifier Residue Sequence Organism Cell Line
SIGNOR-266788 Homo sapiens
pmid sentence
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
+ TRIP12down-regulates activity img/direct_inhibition.png ubiquitination RNF168 0.473
Identifier Residue Sequence Organism Cell Line
SIGNOR-266783 Homo sapiens U2-OS Cell
pmid sentence
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
+ RNF168up-regulates quantity img/direct-activation.png ubiquitination TP53BP1 0.819
Identifier Residue Sequence Organism Cell Line
SIGNOR-278777 Homo sapiens
pmid sentence
E3 ligase RNF168-mediated 53BP1 ubiquitination through activated the mechanistic target of rapamycin (mTOR)-ribosomal S6 kinase (S6K) signaling and increased 53BP1 protein stability in response to IR|We further found that overexpression of RNF168 enhanced 53BP1 ubiquitination inhibited by G0S2 overexpression in U87 and LN229 cells in response to IR (Fig. xref f).
Publications: 1 Organism: Homo Sapiens
+ RNF168up-regulates quantity img/direct-activation.png ubiquitination Histone H2A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-266784 Homo sapiens
pmid sentence
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
+ RNF168up-regulates activity img/direct-activation.png ubiquitination BLM 0.264
Identifier Residue Sequence Organism Cell Line
SIGNOR-272114 Homo sapiens U2-OS Cell
pmid sentence
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
+ H2AC11up-regulates img/direct-activation.png binding RNF168 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-183890 Homo sapiens
pmid sentence
Rnf168 is recruited to sites of dna damage by binding to ubiquitylated histone h2a.
Publications: 1 Organism: Homo Sapiens
+ RNF168down-regulates img/direct_inhibition.png polyubiquitination H1-2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272927 Homo sapiens MDA-MB-231 Cell
pmid sentence
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
+ DGCR8up-regulates activity img/direct-activation.png binding RNF168 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277309 Homo sapiens HEK-293T Cell
pmid sentence
 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
+ UBR5down-regulates quantity img/direct_inhibition.png ubiquitination RNF168 0.449
Identifier Residue Sequence Organism Cell Line
SIGNOR-266782 Homo sapiens U2-OS Cell
pmid sentence
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
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