Ubiquitination is a post-translational modification pathway involved in myriad cellular
regulation and disease pathways. The Ub (ubiquitin) transfer cascade requires three …

DSS1/Sem1 is a versatile intrinsically disordered protein. Besides being a bona fide subunit
of the 26S proteasome, DSS1 associates with other protein complexes, including BRCA2 …

Most E3 ligases use a RING domain to activate a thioester-linked E2∼ ubiquitin-like protein
(UBL) intermediate and promote UBL transfer to a remotely bound target protein …

E3 ubiquitin ligases, in collaboration with E2 ubiquitin-conjugating enzymes, modify proteins
with poly-ubiquitin chains. Cullin-RING ligase (CRL) E3s use Cdc34/UBE2R-family E2s to …

Cullin-RING ligases (CRLs) ubiquitylate specific substrates selected from other cellular
proteins. Substrate discrimination and ubiquitin transferase activity were thought to be strictly …

Polyubiquitination by E2 and E3 enzymes is a predominant mechanism regulating protein
function. Some RING E3s, including anaphase-promoting complex/cyclosome (APC) …

The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic
cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition …

UCH37, also known as UCHL5, is a highly conserved deubiquitinating enzyme (DUB) that
associates with the 26S proteasome. Recently, it was reported that UCH37 activity is …

Attachment of ubiquitin to substrate is typically thought to occur via formation of an
isopeptide bond between the C-terminal glycine residue of ubiquitin and a lysine residue in …

Ubiquitin is a small, globular protein that is conjugated to other proteins as a
posttranslational event. A palette of small, folded domains recognizes and binds ubiquitin to …