Human Interaction Network Ontology

Last uploaded: June 27, 2014
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Id http://purl.obolibrary.org/obo/HINO_0007284
http://purl.obolibrary.org/obo/HINO_0007284
Preferred Name

Pellino ubiquitinates IRAK1
Definitions
has a Stoichiometric coefficient of 2 Authored: Ray, KP, 2010-05-17 IL1 induces the poly-ubiquitination and degradation of IRAK1. This was believed to be K48-linked polyubiquitination, targeting IRAK1 for proteolysis by the proteasome, but recently IL-1R signaling has been shown to lead to K63-linked polyubiquitination of IRAK1 (Windheim et al. 2008; Conze et al. 2008), and demonstrated to have a role in the activation of NF-kappaB. IRAK1 is ubiquitinated on K134 and K180; mutation of these sites impairs IL1R-mediated ubiquitylation of IRAK1 (Conze et al. 2008). Some authors have proposed a role for TRAF6 as the E3 ubiquitin ligase that catalyzes polyubiquitination of IRAK1 (Conze et al. 2008) but this view has been refuted (Windheim et al. 2008; Xiao et al. 2008). There is stronger agreement that Pellino proteins have a role as IRAK1 E3 ubiquitin ligases. <br>Pellino1-3 possess E3 ligase activity and are believed to directly catalyse polyubiquitylation of IRAK1 (Xiao et al. 2008; Butler et al. 2007; Ordureau et al. 2008). They are capable of catalysing the formation of K63- and K48-linked polyubiquitin chains; the type of linkage is controlled by the collaborating E2 enzyme. All the Pellino proteins can combine with the E2 heterodimer UbcH13–Uev1a to catalyze K63-linked ubiquitylation (Ordureau et al. 2008). Reviewed: Pinteaux, E, 2010-05-17 Edited: Jupe, S, 2010-05-17
Type http://www.w3.org/2002/07/owl#Class

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label
Pellino ubiquitinates IRAK1
comment
has a Stoichiometric coefficient of 2
Authored: Ray, KP, 2010-05-17
IL1 induces the poly-ubiquitination and degradation of IRAK1. This was believed to be K48-linked polyubiquitination, targeting IRAK1 for proteolysis by the proteasome, but recently IL-1R signaling has been shown to lead to K63-linked polyubiquitination of IRAK1 (Windheim et al. 2008; Conze et al. 2008), and demonstrated to have a role in the activation of NF-kappaB. IRAK1 is ubiquitinated on K134 and K180; mutation of these sites impairs IL1R-mediated ubiquitylation of IRAK1 (Conze et al. 2008). Some authors have proposed a role for TRAF6 as the E3 ubiquitin ligase that catalyzes polyubiquitination of IRAK1 (Conze et al. 2008) but this view has been refuted (Windheim et al. 2008; Xiao et al. 2008). There is stronger agreement that Pellino proteins have a role as IRAK1 E3 ubiquitin ligases. <br>Pellino1-3 possess E3 ligase activity and are believed to directly catalyse polyubiquitylation of IRAK1 (Xiao et al. 2008; Butler et al. 2007; Ordureau et al. 2008). They are capable of catalysing the formation of K63- and K48-linked polyubiquitin chains; the type of linkage is controlled by the collaborating E2 enzyme. All the Pellino proteins can combine with the E2 heterodimer UbcH13–Uev1a to catalyze K63-linked ubiquitylation (Ordureau et al. 2008).
Reviewed: Pinteaux, E, 2010-05-17
Edited: Jupe, S, 2010-05-17
prefLabel
Pellino ubiquitinates IRAK1
definition source
Pubmed18347055
Reactome, http://www.reactome.org
Pubmed19022706
Pubmed18180283
Pubmed18326498
Pubmed17997719
Pubmed16884718
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prefixIRI
HINO:0007284
seeAlso
EC Number: 6.3.2.19
Reactome Database ID Release 43451418
ReactomeREACT_22381
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