| + |
IRAK4 | up-regulates 
phosphorylation
|
NCF1 |
0.39 |
| 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
|
PELI1 |
0.643 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276130 |
Ser293 |
FNTLAFPsMKRKDVV |
in vitro |
|
| pmid |
sentence |
| 19264966 |
The E3 ubiquitin ligase Pellino can be activated by phosphorylation in vitro, catalyzed by IL-1 receptor-associated kinase 1 (IRAK1) or IRAK4. Here, we show that phosphorylation enhances the E3 ligase activity of Pellino 1. Unusually, the full activation of Pellino 1 can be achieved by phosphorylating any one of several different sites (Ser-76, Thr-86, Thr-288, or Ser-293) or a combination of other sites (Ser-78, Thr-80, and Ser-82). Here, we show that Pellino is phosphorylated at multiple sites by IRAK1 and IRAK4 and that activation can be achieved by phosphorylating any one of several sites or a combination of other sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276127 |
Ser76 |
ISNKDQHsISYTLSR |
in vitro |
|
| pmid |
sentence |
| 19264966 |
The E3 ubiquitin ligase Pellino can be activated by phosphorylation in vitro, catalyzed by IL-1 receptor-associated kinase 1 (IRAK1) or IRAK4. Here, we show that phosphorylation enhances the E3 ligase activity of Pellino 1. Unusually, the full activation of Pellino 1 can be achieved by phosphorylating any one of several different sites (Ser-76, Thr-86, Thr-288, or Ser-293) or a combination of other sites (Ser-78, Thr-80, and Ser-82). Here, we show that Pellino is phosphorylated at multiple sites by IRAK1 and IRAK4 and that activation can be achieved by phosphorylating any one of several sites or a combination of other sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276126 |
Ser78 |
NKDQHSIsYTLSRAQ |
in vitro |
|
| pmid |
sentence |
| 19264966 |
The E3 ubiquitin ligase Pellino can be activated by phosphorylation in vitro, catalyzed by IL-1 receptor-associated kinase 1 (IRAK1) or IRAK4. Here, we show that phosphorylation enhances the E3 ligase activity of Pellino 1. Unusually, the full activation of Pellino 1 can be achieved by phosphorylating any one of several different sites (Ser-76, Thr-86, Thr-288, or Ser-293) or a combination of other sites (Ser-78, Thr-80, and Ser-82). Here, we show that Pellino is phosphorylated at multiple sites by IRAK1 and IRAK4 and that activation can be achieved by phosphorylating any one of several sites or a combination of other sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276132 |
Ser82 |
HSISYTLsRAQTVVV |
in vitro |
|
| pmid |
sentence |
| 19264966 |
The E3 ubiquitin ligase Pellino can be activated by phosphorylation in vitro, catalyzed by IL-1 receptor-associated kinase 1 (IRAK1) or IRAK4. Here, we show that phosphorylation enhances the E3 ligase activity of Pellino 1. Unusually, the full activation of Pellino 1 can be achieved by phosphorylating any one of several different sites (Ser-76, Thr-86, Thr-288, or Ser-293) or a combination of other sites (Ser-78, Thr-80, and Ser-82). Here, we show that Pellino is phosphorylated at multiple sites by IRAK1 and IRAK4 and that activation can be achieved by phosphorylating any one of several sites or a combination of other sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276129 |
Thr288 |
QCPVGFNtLAFPSMK |
in vitro |
|
| pmid |
sentence |
| 19264966 |
The E3 ubiquitin ligase Pellino can be activated by phosphorylation in vitro, catalyzed by IL-1 receptor-associated kinase 1 (IRAK1) or IRAK4. Here, we show that phosphorylation enhances the E3 ligase activity of Pellino 1. Unusually, the full activation of Pellino 1 can be achieved by phosphorylating any one of several different sites (Ser-76, Thr-86, Thr-288, or Ser-293) or a combination of other sites (Ser-78, Thr-80, and Ser-82). Here, we show that Pellino is phosphorylated at multiple sites by IRAK1 and IRAK4 and that activation can be achieved by phosphorylating any one of several sites or a combination of other sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276131 |
Thr80 |
DQHSISYtLSRAQTV |
in vitro |
|
| pmid |
sentence |
| 19264966 |
The E3 ubiquitin ligase Pellino can be activated by phosphorylation in vitro, catalyzed by IL-1 receptor-associated kinase 1 (IRAK1) or IRAK4. Here, we show that phosphorylation enhances the E3 ligase activity of Pellino 1. Unusually, the full activation of Pellino 1 can be achieved by phosphorylating any one of several different sites (Ser-76, Thr-86, Thr-288, or Ser-293) or a combination of other sites (Ser-78, Thr-80, and Ser-82). Here, we show that Pellino is phosphorylated at multiple sites by IRAK1 and IRAK4 and that activation can be achieved by phosphorylating any one of several sites or a combination of other sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276128 |
Thr86 |
YTLSRAQtVVVEYTH |
in vitro |
|
| pmid |
sentence |
| 19264966 |
The E3 ubiquitin ligase Pellino can be activated by phosphorylation in vitro, catalyzed by IL-1 receptor-associated kinase 1 (IRAK1) or IRAK4. Here, we show that phosphorylation enhances the E3 ligase activity of Pellino 1. Unusually, the full activation of Pellino 1 can be achieved by phosphorylating any one of several different sites (Ser-76, Thr-86, Thr-288, or Ser-293) or a combination of other sites (Ser-78, Thr-80, and Ser-82). Here, we show that Pellino is phosphorylated at multiple sites by IRAK1 and IRAK4 and that activation can be achieved by phosphorylating any one of several sites or a combination of other sites. |
|
| Publications: |
7 |
Organism: |
In Vitro |
| Pathways: | IL1 Signaling |
| + |
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 |
0.673 |
| 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 |
| + |
IRAK3 | down-regulates 
binding
|
IRAK4 |
0.7 |
| 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 |
| + |
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 |
| + |
IRAK4 | up-regulates
phosphorylation
|
PELI2 |
0.623 |
| 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 |
| + |
IL1RL1 | up-regulates activity
binding
|
IRAK4 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277705 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16286016 |
As shown in Figure 3D, MyD88, IRAK, IRAK4, and TRAF6 are all recruited to ST2 upon IL-33 stimulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
IRAK4
- 
- 