EC Number   |
Application |
Reference |
|---|
   2.3.2.31 | analysis |
co-crystal structure of HOIP RBR domain with single-domain antibody, use as a platform for soaking of ligands that target the active site cysteine of HOIP |
756380 |
| 2.3.2.31 | analysis |
development of activity-based probes by reengineering of a ubiquitin-charged E2 conjugating enzyme using tosyl-substituted doubly activated genes and application in profiling the transthiolation activity of the RBR E3 ligase Parkin in vitro and in cellular extracts |
757731 |
| 2.3.2.31 | analysis |
development of chemical probes, ubiquitin C-terminal fluorescein thioesters UbMES and UbFluor, to qualitatively and quantitatively assess the activity of the RBR E3 ligase PARKIN in a simple experimental setup and in real time using fluorescence polarization. UbFluor quantitatively detects naturally occurring activation states of parkin caused by Ser65 phosphorylation and phosphorylated ubiquitin |
757182 |
| 2.3.2.31 | medicine |
isoform RNF144A interacts with poly(ADP-ribose) polymerase PARP1 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 | medicine |
parkin patient disease-associated mutation largely mediate their effect by altering transthiolation activity |
757731 |
| 2.3.2.31 | medicine |
upon infection, Trichinella spiralis secretes E2 Ub-conjugating protein UBE2L3, located in the secretory organ of the parasite during the muscle stages of infection. UBE2L3 but specifically binds to a panel of human RING E3 ligases, including the RBR E3 ARIH2 with which it interacts with a higher affinity than the mammalian ortholog UbcH7/UBE2L3. Expression of UBE2L3 in skeletal muscle cells causes a global downregulation in protein ubiquitination, most predominantly affecting motor, sarcomeric and extracellular matrix proteins, thus mediating their stabilization with regards to proteasomal degradation |
758193 |
