anti-Ring Finger Protein 126 (RNF126) Antibodies

Human Ring Finger Protein 126 (RNF126) interaction partners

1. Studies present the solution structure of the RNF126_NZF (N-terminal zinc finger domain) as well as the structure of RNF126_NZF/BAG6_UBL complex and characterize the interaction of RNF126 with the UBL domains from both BAG6 and UBL4A from the BAG6 sortase complex.

2. RNF126 depletion results in frataxin accumulation in cells derived from FRDA patients.

3. These data suggested that RNF126 might be related to the progression of tongue cancer through regulating AKT signaling pathway.

4. RNF126 is a novel regulator of NHEJ that promotes completion of DNA repair by ubiquitylating Ku80 and releasing Ku70/80 from damaged DNA.

5. this results suggest a novel role of RNF126 in promoting Homologous recombination-mediated repair through positive regulation on BRCA1 expression by direct interaction with E2F1.

6. RNF126 is recruited to the N-terminal Ubl domain of Bag6 and preferentially ubiquitinates juxtahydrophobic lysine residues on Bag6-associated clients.

7. The ubiquitin ligase RNF126 has a role in the retrograde sorting of the CI-MPR.

8. RNF126 and Rabring7 play a role in the ubiquitin-dependent sorting and downregulation of membrane receptors.

9. identify a unique cofactor, RING finger protein 126 (RNF126), verify its interaction by traditional techniques, and show that it has functional consequences as RNF126 is able to ubiquitylate activation-induced cytidine deaminase

10. These findings suggest that RNF126 promotes cancer cell proliferation by targeting p21 for ubiquitin-mediated degradation