Ubiquitin-like proteins (Ubl's) are conjugated to target proteins or lipids to regulate their
activity, stability, subcellular localization, or macromolecular interactions. Similar to ubiquitin …

E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of
ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct …

The regulation of protein fate by modification with the small ubiquitin-related modifier
(SUMO) plays an essential and crucial role in most cellular pathways. Sumoylation is highly …

Ubiquitin is the founding member of a family of structurally conserved proteins that regulate
a host of processes in eukaryotic cells. Ubiquitin and its relatives carry out their functions …

Familial cylindromatosis is an autosomal dominant predisposition to tumours of skin
appendages called cylindromas. Familial cylindromatosis is caused by mutations in a gene …

Ubiquitin-binding domains (UBDs) are a collection of modular protein domains that non-
covalently bind to ubiquitin. These recently discovered motifs interpret and transmit …

The covalent modification of proteins by ubiquitination is a major regulatory mechanism of
protein degradation and quality control, endocytosis, vesicular trafficking, cell-cycle control …

It is generally assumed that a specific ubiquitin ligase (E3) links protein substrates to
polyubiquitin chains containing a single type of isopeptide linkage, and that chains …

Ubiquitin is a highly conserved 76-aminoacid polypeptide that is found throughout the
eukaryotic kingdom. The covalent conjugation of ubiquitin (often in the form of a polymer) to …

Modification by Lys63-linked ubiquitin (UbK63) chains is the second most abundant form of
ubiquitylation. In addition to their role in DNA repair or kinase activation, UbK63 chains …