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RNF125 encodes a novel E3 ubiquitin ligase that contains a RING finger domain in the N-terminus and three zinc-binding and one ubiquitin-interacting motif in the C-terminus. Additionally we are shipping RNF125 Antibodies (55) and many more products for this protein.
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Data indicate that brain from Japanese encephalitis virus (JEV)-infection showed a reciprocal correlation between microRNA miR-15b levels and the ex (show MLXIP Proteins)pression of ring finger protein 125 (RNF125).
RNF125 is enhanced by IFN, these functions constitute a negative regulatory loop circuit for IFN production
we identified the downregulation of the ubiquitin ligase RNF125 in BRAFi-resistant melanomas
Results indicate that the nucleotide sequence in the 3' untranslated region (3' UTR) of ring finger protein 125 (RNF125) is a potential microRNA miR (show MLXIP Proteins)-15b targeting site.
studies of the RNF125 pathway point to upregulation of RIG-I (show DDX58 Proteins)-IPS1 (show MAVS Proteins)-MDA5 (show IFIH1 Proteins) and/or disruption of the PI3K (show PIK3CA Proteins)-AKT (show AKT1 Proteins) and interferon (show IFNA Proteins) signaling pathways as the putative final effectors
In controls, RNF125 is the highest expressed gene, whereas in HIV infection progressors, RIG-I (show DDX58 Proteins) is either the highest expressed gene or is expressed similarly to RNF125 and TRIM25 (show TRIM25 Proteins).
study reports human bocavirus VP2 modulates IFN pathway by targeting the ring finger protein 125, a negative regulator of type I IFN signaling, which conjugates Lys (show LYZ Proteins)(48)-linked ubiquitination to retinoic acid-inducible gene-I (show DDX58 Proteins) and leads to the proteasome-dependent degradation of RIG-I (show DDX58 Proteins)
These results suggest that RNF125/TRAC-1 could function to recruit host factor(s) controlling HIV-1 transcription to the ubiquitin-proteasome pathway.
TRAC-1 associates with membranes and is excluded from the nucleus through myristoylation
This gene encodes a novel E3 ubiquitin ligase that contains a RING finger domain in the N-terminus and three zinc-binding and one ubiquitin-interacting motif in the C-terminus. As a result of myristoylation, this protein associates with membranes and is primarily localized to intracellular membrane systems. The encoded protein may function as a positive regulator in the T-cell receptor signaling pathway.
E3 ubiquitin-protein ligase RNF125
, T-cell RING activation protein 1
, T-cell ring protein identified in activation screen