Reactome | TRAF6 E3 ubiquitin ligase activity was shown to be essential...

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created	[InstanceEdit:975168] Shamovsky, V, 2010-09-22
dbId	975096
displayName	TRAF6 E3 ubiquitin ligase activity was shown to be essential...
literatureReference	[LiteratureReference:933491] Interferon-alpha induction through Toll-like receptors involves a direct interaction of IRF7 with MyD88 and TRAF6 [LiteratureReference:500618] TRAF6 and the three C-terminal lysine sites on IRF7 are required for its ubiquitination-mediated activation by the tumor necrosis factor receptor family member latent membrane protein 1
schemaClass	Summation
text	TRAF6 E3 ubiquitin ligase activity was shown to be essential for IRF7 activation, although the role of TRAF6-dependent ubiquitination remains unclear [Kawai T et al 2004]. It has been demonstrated that IRF7 is ubiquitinated by TRAF6 at multiple sites both in vitro and in vivo[Ning et al 2008].It has been also shown that K63-linked ubiquitination of IRF7 is independent of its C-terminal functional phosphorylation sites.

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