Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex. Inhibits IRAK1 phosphorylation and kinase activity. Oligomerizes. Binds to TLR2 and the TLR4-MD2 complex via its C-terminus. Exists as complex with IRAK1 in unstimulated cells. Upon IL-1 signaling, Tollip binds to the activated IL-1 receptor complex containing IL-1RI, IL-1RacP and the adapter protein MyD88, where it interacts with the TIR domain of IL-1RacP. MyD88 then triggers IRAK1 autophosphorylation, which in turn leads to the dissociation of IRAK1 from Tollip and IL-1RAcP. Interacts with TOM1L2. Belongs to the tollip family. Note: This description may include information from UniProtKB.
Protein type: Vesicle protein; Inhibitor protein
Cellular Component: nuclear body; interleukin-1 receptor complex; perinuclear region of cytoplasm; cytoplasm; interleukin-18 receptor complex; cytosol
Molecular Function: signal transducer activity; protein binding; SUMO binding; ubiquitin conjugating enzyme binding; ubiquitin protein ligase binding; interleukin-1, Type I receptor binding; kinase binding
Biological Process: positive regulation of protein sumoylation; epithelial cell differentiation; cell-cell signaling; innate immune response; inflammatory response; signal transduction; phosphorylation; leukocyte activation
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.