loading...| Preferred Name | Hyperphosphorylated IRAK1 associates with TRAF6 | |
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Authored: Ray, KP, 2010-05-17 Hyperphosphorylated IRAK1, still within the receptor complex, binds TRAF6 through multiple regions including the death domain, the undefined domain and the C-terminal C1 domain (Li et al. 2001). The C-terminal region of IRAK-1 contains three potential TRAF6-binding sites; mutation of the amino acids (Glu544, Glu587, Glu706) in these sites to alanine greatly reduces activation of NFkappaB (Ye et al. 2002). Reviewed: Pinteaux, E, 2010-05-17 Edited: Jupe, S, 2010-05-17 |
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http://purl.obolibrary.org/obo/HINO_0007194 |
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Authored: Ray, KP, 2010-05-17 Hyperphosphorylated IRAK1, still within the receptor complex, binds TRAF6 through multiple regions including the death domain, the undefined domain and the C-terminal C1 domain (Li et al. 2001). The C-terminal region of IRAK-1 contains three potential TRAF6-binding sites; mutation of the amino acids (Glu544, Glu587, Glu706) in these sites to alanine greatly reduces activation of NFkappaB (Ye et al. 2002). Reviewed: Pinteaux, E, 2010-05-17 Edited: Jupe, S, 2010-05-17 |
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Pubmed8837778 Pubmed12140561 Pubmed18070982 Reactome, http://www.reactome.org Pubmed11287640 |
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Hyperphosphorylated IRAK1 associates with TRAF6 |
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HINO:0007194 |
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Hyperphosphorylated IRAK1 associates with TRAF6 |
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Reactome Database ID Release 43446862 ReactomeREACT_22311 |
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