Reactome | Interaction of E3 with substrate and E2-Ub complex

Interaction of E3 with substrate and E2-Ub complex

Stable Identifier

R-HSA-983157

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol

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Interaction of E3 with substrate and E2-Ub complex

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Ubiquitin E3 ligases confer specificity to ubiquitination by recognizing target substrates and mediating transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to substrate (Raymond et al. 2009). E3 ligases includes a large, diverse set of proteins characterized by several defining motifs which include a HECT (homologous to E6-associated C-terminus), RING (Really Interesting New Gene) and U-box domains. The E3 ligases can be multisubunit complexes rather than a single polypeptide. Presently three different kinds of E3 complexes have been described called SCF, APC, and VHL. E3 ligases binds to both substrate and an E2 thioesterified with ubiquitin (E2-Ub).

Literature References

PubMed ID	Title	Journal	Year
12646216	U-box proteins as a new family of ubiquitin ligases Hatakeyama, S, Nakayama, KI	Biochem Biophys Res Commun	2003
16954532	A novel family of membrane-bound E3 ubiquitin ligases Ohmura-Hoshino, M, Goto, E, Matsuki, Y, Aoki, M, Mito, M, Uematsu, M, Hotta, H, Ishido, S	J Biochem	2006
19489725	RING domain E3 ubiquitin ligases Deshaies, RJ, Joazeiro, CA	Annu Rev Biochem	2009
19028597	Maturation of human dendritic cells is accompanied by functional remodelling of the ubiquitin-proteasome system Ebstein, F, Lange, N, Urban, S, Seifert, U, Krüger, E, Kloetzel, PM	Int. J. Biochem. Cell Biol.	2009