Domain

Cullin protein, neddylation domain (IPR019559)

Short name: Cullin_neddylation_domain

Domain relationships

Description

This is the neddylation site of cullin proteins, which are a family of structurally related proteins containing an evolutionarily conserved cullin domain. With the exception of APC2, each member of the cullin family is modified by Nedd8 and several cullins function in Ubiquitin-dependent proteolysis, a process in which the 26S proteasome recognises and subsequently degrades a target protein tagged with K48-linked poly-ubiquitin chains. Cullins are molecular scaffolds responsible for assembling the ROC1/Rbx1 RING-based E3 ubiquitin ligases, of which several play a direct role in tumorigenesis. Nedd8/Rub1 is a small ubiquitin-like protein, which was originally found to be conjugated to Cdc53, a cullin component of the SCF (Skp1-Cdc53/CUL1-F-box protein) E3 Ub ligase complex in Saccharomyces cerevisiae (Baker's yeast), and Nedd8 modification has now emerged as a regulatory pathway of fundamental importance for cell cycle control and for embryogenesis in metazoans. The only identified Nedd8 substrates are cullins. Neddylation results in covalent conjugation of a Nedd8 moiety onto a conserved cullin lysine residue [PMID: 15021886].

GO terms

Biological Process

GO:0006511 ubiquitin-dependent protein catabolic process

Molecular Function

GO:0031625 ubiquitin protein ligase binding

Cellular Component

GO:0031461 cullin-RING ubiquitin ligase complex

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam
SMART