A ubiquitin ligase, or E3, promotes transfer of ubiquitin to a selected substrate within the ubiquitination system. Many E3s provide substrate recognition, while the detailed chemistry differs between E3 families. A ubiquitin-conjugating enzyme supplies activated ubiquitin. The resulting modification can signal protein degradation or other fates depending on substrate, linkage and context, so ubiquitination is not synonymous with immediate destruction. [ref]
A substrate-recognition protein in an iron-sensitive ubiquitin-ligase pathway controlling IRP2. Its stability depends on iron and oxygen conditions.[ref]
A substrate-recognition component of a ubiquitin ligase that recognizes phosphorylated substrates, including Sic1.
As part of an SCF-type assembly, it links a substrate’s phosphorylation state to ubiquitin-dependent turnover. The recognition step explains why adding phosphate can change protein lifetime without directly destroying the modified protein. [ref]
Molecular Biology of the Cell, 4th edition by Bruce Alberts and others. Chapters 3, 6 and 15, protein function, translation and cell signalling
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