interleukin-1 receptor associated kinase 1 (IRAK1)

Function: - binds to the IL-1 type I receptor following IL-1 engagement, triggering intracellular signaling cascades leading to transcriptional up-regulation & mRNA stabilization - isoform 1 binds rapidly but is then degraded allowing isoform 2 to mediate a slower, more sustained response to the IL-1 - isoform 2 is inactive suggesting that the kinase activity of this enzyme is not required for IL-1 signaling - once phosphorylated, IRAK1 recruits the adapter protein PELI1 - IL-1 stimulation leads to the formation of a signaling complex which dissociates from the IL-1 receptor following the binding of PELI1 - interacts with IL1RL1 - interacts with IRAK1BP1 - autophosphorylation or phosphorylation by IRAK4 following recruitment to the IL-1RI is linked to ubiquitination & degradation of isoform 1 Cofactor: Mg⁺² Structure: - belongs to the protein kinase superfamily, TKL Ser/Thr protein kinase family, Pelle subfamily - contains 1 protein kinase domain Alternative splicing: named isoforms=3 Expression: - isoform 1 & isoform 2 are ubiquitously expressed in all tissues examined - isoform 1 is more strongly expressed than isoform 2

Properties

SIZE: entity length = 712 aa MW = 77 kD STATE: active state MOTIF: Ser phosphorylation site {S131} kinase domain SITE: 212-521 MOTIF: ATP-binding site NAME: ATP-binding site SITE: 218-226 ATP-binding site NAME: ATP-binding site SITE: 239-239 aspartate residue {D340} Ser phosphorylation site {S371} Ser phosphorylation site {S568}

Database Correlations

OMIM 300283 UniProt P51617 PFAM correlations Entrez Gene 3654 Kegg hsa:3654 ENZYME 2.7.11.1

References

UniProt :accession P51617