+ |
IRAK4 | up-regulates
phosphorylation
|
NCF1 |
0.394 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152011 |
Ser288 |
QKSGQDVsQAQRQIK |
Homo sapiens |
Neutrophil |
pmid |
sentence |
17217339 |
Phosphorylation of the cytosolic factor p47phox is essential for activation of the nadph oxidase.We found that thr133, ser288 and thr356, targets for irak-4 phosphorylation in vitro, are also phosphorylated in endogenous p47phox after lps stimulation. We conclude that irak-4 phosphorylates p47phox and regulates nadph oxidase activation after lps stimulation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152015 |
Ser320 |
QRSRKRLsQDAYRRN |
Homo sapiens |
Neutrophil |
pmid |
sentence |
17217339 |
Phosphorylation of the cytosolic factor p47phox is essential for activation of the nadph oxidase.These results strongly support the observation that irak-4 is a kinase for p47phox in vivo. We also detected the signature of phosphorylation at ser320 and ser345 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152019 |
Ser345 |
QARPGPQsPGSPLEE |
Homo sapiens |
Neutrophil |
pmid |
sentence |
17217339 |
Phosphorylation of the cytosolic factor p47phox is essential for activation of the nadph oxidase.These results strongly support the observation that irak-4 is a kinase for p47phox in vivo. We also detected the signature of phosphorylation at ser320 and ser345 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152023 |
Thr133 |
KLPTDNQtKKPETYL |
Homo sapiens |
Neutrophil |
pmid |
sentence |
17217339 |
Phosphorylation of the cytosolic factor p47phox is essential for activation of the nadph oxidase.We found that thr133, ser288 and thr356, targets for irak-4 phosphorylation in vitro, are also phosphorylated in endogenous p47phox after lps stimulation. We conclude that irak-4 phosphorylates p47phox and regulates nadph oxidase activation after lps stimulation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-152027 |
Thr356 |
PLEEERQtQRSKPQP |
Homo sapiens |
Neutrophil |
pmid |
sentence |
17217339 |
Phosphorylation of the cytosolic factor p47phox is essential for activation of the nadph oxidase.We found that thr133, ser288 and thr356, targets for irak-4 phosphorylation in vitro, are also phosphorylated in endogenous p47phox after lps stimulation. We conclude that irak-4 phosphorylates p47phox and regulates nadph oxidase activation after lps stimulation. |
|
Publications: |
5 |
Organism: |
Homo Sapiens |
+ |
IRAK4 | up-regulates activity
phosphorylation
|
IRAK4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204653 |
Ser346 |
FAQTVMTsRIVGTTA |
Homo sapiens |
Monocyte |
pmid |
sentence |
24567333 |
We show irak4 autophosphorylation occurs by an intermolecular reaction and that autophosphorylation is required for full catalytic activity of the kinase. Phosphorylation of any two of the residues thr-342, thr-345, and ser-346 is required for full activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-151006 |
Thr342 |
ASEKFAQtVMTSRIV |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17141195 |
The present data indicate that the kinase activity of irak-4 is dependent on the autophosphorylations at t342 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204657 |
Thr342 |
ASEKFAQtVMTSRIV |
Homo sapiens |
Monocyte |
pmid |
sentence |
24567333 |
We show irak4 autophosphorylation occurs by an intermolecular reaction and that autophosphorylation is required for full catalytic activity of the kinase. Phosphorylation of any two of the residues thr-342, thr-345, and ser-346 is required for full activity |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204661 |
Thr345 |
KFAQTVMtSRIVGTT |
Homo sapiens |
Monocyte |
pmid |
sentence |
24567333 |
We show irak4 autophosphorylation occurs by an intermolecular reaction and that autophosphorylation is required for full catalytic activity of the kinase. Phosphorylation of any two of the residues thr-342, thr-345, and ser-346 is required for full activity |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
Pathways: | IL1 Signaling |
+ |
IRAK4 | up-regulates activity
phosphorylation
|
IRAK1 |
0.667 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251328 |
Ser376 |
GSSPSQSsMVARTQT |
in vitro |
|
pmid |
sentence |
11960013 |
In vitro the IRAK-1 activation loop is a good substrate for IRAK-4, and that T387 and S376 are the main sites of phosphorylation by both IRAK-1 and IRAK-4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251329 |
Thr387 |
RTQTVRGtLAYLPEE |
in vitro |
|
pmid |
sentence |
11960013 |
In vitro the IRAK-1 activation loop is a good substrate for IRAK-4, and that T387 and S376 are the main sites of phosphorylation by both IRAK-1 and IRAK-4. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153458 |
|
|
Mus musculus |
Macrophage |
pmid |
sentence |
17337443 |
Analyses of embryonic fibroblasts and macrophages obtained from IRAK-4 KD mice demonstrate lack of cellular responsiveness to stimulation with IL-1beta or a Toll-like receptor 7 (TLR7) agonist. IRAK-4 kinase deficiency prevents the recruitment of IRAK-1 to the IL-1 receptor complex and its subsequent phosphorylation and degradation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-117315 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
11960013 |
In addition, IRAK-4 is able to phosphorylate IRAK-1, and overexpression of dominant-negative IRAK-4 is blocking the IL-1-induced activation and modification of IRAK-1, suggesting a role of IRAK-4 as a central element in the early signal transduction of Toll/IL-1 receptors, upstream of IRAK-1. |
|
Publications: |
4 |
Organism: |
In Vitro, Mus Musculus, Homo Sapiens |
Pathways: | IL1 Signaling |
+ |
MYD88 | up-regulates activity
binding
|
IRAK4 |
0.945 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252097 |
|
|
Homo sapiens |
|
pmid |
sentence |
12297423 |
Signaling between MyD88 and TRAF6 is mediated by members of the IL-1R-associated kinase (IRAK) family; however, the exact function of each IRAK protein remains controversial. IRAK-1 is required for the optimal transduction of IL-1R- and TLR-mediated signals, but IRAK-1 can be replaced by other IRAKs. Surprisingly, gene targeting studies show that the newest IRAK protein, IRAK-4, has an essential role in mediating signals initiated by IL-1R and TLR engagement. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-155385 |
|
|
Homo sapiens |
B-lymphocyte |
pmid |
sentence |
17548806 |
St2825 interfered with recruitment of irak1 and irak4 by myd88, causing inhibition of il-1beta-mediated activation of nf-kappab transcriptional activity. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | IL1 Signaling |
+ |
IRAK3 | down-regulates
binding
|
IRAK4 |
0.695 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-205434 |
|
|
Homo sapiens |
|
pmid |
sentence |
25290089 |
Irak3 exerts negative regulatory effects through preventing (i) the dissociation of irak1 and irak4 from myd88 irak3 negatively regulates irak signalling through suppression of irak4 and irak1 activation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IRAK4 | up-regulates
phosphorylation
|
PELI2 |
0.618 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-103717 |
|
|
Homo sapiens |
|
pmid |
sentence |
12860405 |
Pellino2 is one of the firstsubstrates identified for irak1 andirak4. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |