Linked Life Data

48887BiochemicalReaction3665

Source:http://www.reactome.org/biopax/48887BiochemicalReaction3665

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
biopax3:comment
Authored: Luo, F, 2005-11-10 11:23:18, Edited: Shamovsky, V, 2009-12-16, Human IRF-3 is activated through a two step phosphorylation in the C-terminal domain mediated by TBK1 and/or IKK-i. It requires Ser386 and/or Ser385 (site 1) and a cluster of serine/threonine residues between Ser396 and Ser405 (site 2) [Panne et al 2007]. Phosphorylated residues at site 2 alleviate autoinhibition to allow interaction with CBP (CREB-binding protein) and facilitate phosphorylation at site 1. Phosphorylation at site 1 is required for IRF-3 dimerization.<p>IRF-3 and IRF-7 transcription factors possess distinct structural characteristics; IRF-7 is phosphorylated on Ser477 and Ser479 residues [Lin R et al 2000]. TRAF6 mediated ubiquitination of IRF7 is also required and essential for IRF7 phosphorylation and activation. The K-63 linked ubiquitination occurs on the last three C-terminal lysine sites (positions 444, 446, and 452) of human IRF7 independently of its C-terminal functional phosphorylation sites.[Ning et al 2008].<p>Since the number of serine residues involved into IRF activation remains unclear this reaction represents a minimum stoichiometry to achieve the phosphorylation of at least 3 Ser residues per each IRF transcription factor., Reviewed: Gay, NJ, 2006-04-24 16:48:17
biopax3:xref
biopax3:dataSource
biopax3:displayName
Phosphorylation and Release of IRF3 or IRF7
biopax3:left
biopax3:participantStoichio...
biopax3:right