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RNF168 encodes an E3 ubiquitin ligase protein that contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. Additionally we are shipping RNF168 Antibodies (57) and many more products for this protein.
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RNF168, in complex with RAD6A (show ube2a Proteins) or RAD6B (show UBE2B Proteins), is activated in the DNA-damage-induced protein ubiquitination cascade.
Rnf168 is important for maintaining genomic integrity, and it cooperates with p53 (show TP53 Proteins) in suppressing tumorigenesis.
The association of RNF168 with PML (show PML Proteins) NBs (show NBN Proteins) resulted in increased ubiquitylation.
Results reveal an important role of USP7 (show USP7 Proteins) in regulating ubiquitin-dependent signaling via stabilization of RNF168.
CK2 (show CSNK2A1 Proteins)/WIP1 (show PPM1D Proteins)-mediated modulation of LSD1 (show KDM1A Proteins) phosphorylation facilitates RNF168-dependent ubiquitination and recruitment of 53BP1 (show TP53BP1 Proteins) to the DNA damage sites.
The ubiquitin ligase RNF168 is strictly dependent on the activity that UbK27 is required to promote chromatin ubiquitination following DNA damage.
Finding that RNF8 (show RNF8 Proteins) is less abundant than RNF168 identifies RNF8 (show RNF8 Proteins) as a rate-limiting determinant of focal repair complex assembly
Depletion of RNF8 (show RNF8 Proteins) or RNF168 blocks the degradation of diffusely localized nuclear 53BP1 (show TP53BP1 Proteins).
The E3 ligase RNF168 promotes both H2A ubiquitylation and neddylation. RNF168 is itself a substrate for NEDD8, and neddylation of RNF168 is necessary for its E3 ubiquitin activity.
The acidic patch functions within the nucleosome as nucleosomes containing a mutated acidic patch exhibit defective H2A/H2AXub by RNF168 and RING1B (show RNF2 Proteins)/BMI1 (show BMI1 Proteins) in vitro
Taken together, the results suggested that USP3 (show USP3 Proteins) is a negative regulator of ubiquitination signaling, counteracting RNF168- and RNF8 (show RNF8 Proteins)-mediated ubiquitination
Before their localization to DNA double strand breaks, RNF168 interacts with 53BP1 and modifies it through the addition of a chain of ubiquitin-polypeptides.
This gene encodes an E3 ubiquitin ligase protein that contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-DNA and protein-protein interactions. The protein is involved in DNA double-strand break (DSB) repair. Mutations in this gene result in Riddle syndrome.
E3 ubiquitin-protein ligase RNF168
, ring fnger protein 168