EC Number   |
General Information |
Reference |
|---|
   2.3.2.31 | physiological function |
a short extension of ARIH1 RING1, Zn2+-loop II, acts as a steric wedge to disrupt closed E2-ubiquitin, resulting in open E2-ubiquitin that favors ubiquitin transfer to the E3 active site |
758488 |
| 2.3.2.31 | physiological function |
ARIH1 predominantly and extensively interacts with activated cullin-RING E3 enzymes and acts as a monoubiquitin conjugating enzyme for neddylated CUL3-RBX1 substrate SEC13-SEC31A. Efficient neddylated cullin-RING E3 substrate polyubiquitylation can be achieved by UBCH7-ARIH1-mediated priming and CDC34-mediated chain elongation |
744643 |
| 2.3.2.31 | physiological function |
downregulation of isoform RNF144B in kidney with small siRNA upregulates polyinosinic:polycytidylic acid poly(I:C)-induced inflammatory cytokines production, including IFN-I, TNF-alpha, IL-6, and transcription factor IRF3 |
756749 |
| 2.3.2.31 | physiological function |
isoform RNF144A interacts with poly(ADP-ribose) polymerase PARP1, a DNA repair protein, through its carboxy-terminal region containing the transmembrane domain, and targets PARP1 for ubiquitination and subsequent proteasomal degradation. Induced expression of RNF144A decreases PARP1 protein levels and renders breast cancer cells resistant to the clinical-grade PARP inhibitor olaparib. Knockdown of endogenous RNF144A increases PARP1 protein levels and enhances cellular sensitivity to olaparib |
757893 |
| 2.3.2.31 | physiological function |
miR-218 targets parkin and negatively regulates PINK1/parkin-mediated mitophagy. Overexpression of microRNA miR-218 reduces parkin mRNA levels, reducing protein content and deregulating the E3 ubiquitin ligase action. Following miR-218 overexpression, mitochondria result less ubiquitylated and the autophagy machinery fails to proceed with correct mitochondrial clearance |
757005 |
| 2.3.2.31 | physiological function |
parkin does not require an E2 enzyme for substrate ubiquitination, lysine selection, and polyubiquitin chain formation. Both phosphorylated ubiquitin and the ubiquitin-accepting substrate contribute to maximal ubiquitin conjugation turnover of phosphorylated parkin. Phosphorylated ubiquitin enhances the transthiolation step, whereas the substrate clears the phosphorylated parkin-ubiquitin thioester intermediate |
757182 |
| 2.3.2.31 | physiological function |
RING Finger ABA-Related1 (RFA1) and RFA4 E3 ubiquitin ligases are key regulators of abscisic acid receptor stability in root and leaf tissues, targeting abscisic acid receptors for degradation in different subcellular locations. Endogenous levels of PYR1 and PYL4 abscisic acid receptors are higher in the Rfa1 Rfa4 double mutant than in wild-type plants. UBC26 is the cognate nuclear E2 enzyme that interacts with the RFA4 E3 ligase and forms UBC26-RFA4-receptor complexes in nuclear speckles. Loss-of-function Ubc26 alleles and the Rfa1Rrfa4 double mutant show enhanced sensitivity to abscisic acid and accumulation of abscisic acid receptors compared with the wild-type |
758055 |
| 2.3.2.31 | physiological function |
RING1 domains of HHARI promote open sate E2-ubiquitin conjugates. RING1 opening of E2-ubiquitin enforces ubiquitin transfer via the RING2 active site Cys. The hydrophobic surface of ubiquitin is required for transfer of ubiquitin to the RBR active site. Mutations that ablate ubiquitin binding to HHARI RING2 also decrease RBR ligase activity |
756593 |
| 2.3.2.31 | physiological function |
RING1 domains of RNF144 promote open sate E2-ubiquitin conjugates. RING1 opening of E2-ubiquitin enforces ubiquitin transfer via the RING2 active site Cys |
756593 |
| 2.3.2.31 | physiological function |
the activity of inactive parkin molecules can be stimulated by the presence of activated parkin molecules, molecules can function together to ligate ubiquitin |
757792 |
