| + |
TRAF6 | up-regulates activity 
ubiquitination
|
IRAK1 |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262298 |
Lys134 |
AEAWSPRkLPSSAST |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 18347055 |
K63-linked polyubiquitination of proximal signaling proteins is a common mechanism used by diverse innate immune receptors for recruiting IKK and activating NF-_B |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252252 |
Lys180 |
SPAPSSTkPGPESSV |
Homo sapiens |
|
| pmid |
sentence |
| 18347055 |
K63-linked polyubiquitination of proximal signaling proteins is a common mechanism used by diverse innate immune receptors for recruiting IKK and activating NF-_B |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Innate Immune Response, IL1 Signaling , Toll like receptors |
| + |
IRAK1 | up-regulates activity
phosphorylation
|
PELI1 |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276137 |
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-96735 |
Ser293 |
FNTLAFPsMKRKDVV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12496252 |
In this article we demonstrate that pellino 1 is phosphorylated at multiple sites by irak1 or irak4 in vitro. The key residues involved in activation are located between residues 76 and 86 (ser-76, ser-78, thr-80, ser-82, and thr-86) and at thr-288 and ser-293, just n-terminal to the ring-like domain that carries the e3 ligase activity. Unusually, we found that the phosphorylation of ser-76 or thr-288 or ser-293 alone was sufficient for maximal activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96739 |
Ser76 |
ISNKDQHsISYTLSR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12496252 |
In this article we demonstrate that pellino 1 is phosphorylated at multiple sites by irak1 or irak4 in vitro. The key residues involved in activation are located between residues 76 and 86 (ser-76, ser-78, thr-80, ser-82, and thr-86) and at thr-288 and ser-293, just n-terminal to the ring-like domain that carries the e3 ligase activity. Unusually, we found that the phosphorylation of ser-76 or thr-288 or ser-293 alone was sufficient for maximal activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276134 |
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-96743 |
Ser78 |
NKDQHSIsYTLSRAQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12496252 |
In this article we demonstrate that pellino 1 is phosphorylated at multiple sites by irak1 or irak4 in vitro. The key residues involved in activation are located between residues 76 and 86 (ser-76, ser-78, thr-80, ser-82, and thr-86) and at thr-288 and ser-293, just n-terminal to the ring-like domain that carries the e3 ligase activity. Unusually, we found that the phosphorylation of ser-76 or thr-288 or ser-293 alone was sufficient for maximal activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276133 |
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-276139 |
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-96747 |
Ser82 |
HSISYTLsRAQTVVV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12496252 |
In this article we demonstrate that pellino 1 is phosphorylated at multiple sites by irak1 or irak4 in vitro. The key residues involved in activation are located between residues 76 and 86 (ser-76, ser-78, thr-80, ser-82, and thr-86) and at thr-288 and ser-293, just n-terminal to the ring-like domain that carries the e3 ligase activity. Unusually, we found that the phosphorylation of ser-76 or thr-288 or ser-293 alone was sufficient for maximal activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96751 |
Thr288 |
QCPVGFNtLAFPSMK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12496252 |
In this article we demonstrate that pellino 1 is phosphorylated at multiple sites by irak1 or irak4 in vitro. The key residues involved in activation are located between residues 76 and 86 (ser-76, ser-78, thr-80, ser-82, and thr-86) and at thr-288 and ser-293, just n-terminal to the ring-like domain that carries the e3 ligase activity. Unusually, we found that the phosphorylation of ser-76 or thr-288 or ser-293 alone was sufficient for maximal activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276136 |
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-276138 |
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-96759 |
Thr86 |
YTLSRAQtVVVEYTH |
Homo sapiens |
|
| pmid |
sentence |
| 12496252 |
In this article we demonstrate that pellino 1 is phosphorylated at multiple sites by irak1 or irak4 in vitro. The key residues involved in activation are located between residues 76 and 86 (ser-76, ser-78, thr-80, ser-82, and thr-86) and at thr-288 and ser-293, just n-terminal to the ring-like domain that carries the e3 ligase activity. Unusually, we found that the phosphorylation of ser-76 or thr-288 or ser-293 alone was sufficient for maximal activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276135 |
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: |
13 |
Organism: |
In Vitro, Homo Sapiens |
| Pathways: | IL1 Signaling |
| + |
IRAK1 | up-regulates activity
phosphorylation
|
IRAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251326 |
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-119212 |
Thr209 |
LCEISRGtHNFSEEL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14625308 |
Sequential autophosphorylation steps in the interleukin-1 receptor-associated kinase-1 regulate its availability as an adapter in interleukin-1 signalingthis identifies irak-1 as a novel type of adapter protein, which employs its own kinase activity to introduce negative charges adjacent to the protein interaction domain, which anchors irak-1 at the active receptor complex. Thus, irak-1 regulates its own availability as an adapter molecule by sequential autophosphorylation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119216 |
Thr387 |
RTQTVRGtLAYLPEE |
Homo sapiens |
|
| pmid |
sentence |
| 14625308 |
Sequential autophosphorylation steps in the interleukin-1 receptor-associated kinase-1 regulate its availability as an adapter in interleukin-1 signalingthis identifies irak-1 as a novel type of adapter protein, which employs its own kinase activity to introduce negative charges adjacent to the protein interaction domain, which anchors irak-1 at the active receptor complex. Thus, irak-1 regulates its own availability as an adapter molecule by sequential autophosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251330 |
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-251327 |
Thr66 |
CERSGQRtASVLWPW |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12138165 |
T66E mutations interfered with the ability of IRAK to autophosphorylate. Thr-66 mutations abolished the capacity of IRAK to dimerize. |
|
| Publications: |
5 |
Organism: |
In Vitro, Homo Sapiens, Chlorocebus Aethiops |
| Pathways: | Innate Immune Response, IL1 Signaling , Toll like receptors |
| + |
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-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. |
|
| 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. |
|
| Publications: |
4 |
Organism: |
In Vitro, Homo Sapiens, Mus Musculus |
| Pathways: | IL1 Signaling |
| + |
IRAK1 | up-regulates activity
phosphorylation
|
GLIPR2 |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262887 |
Ser58 |
ILKHSPEsSRGQCGE |
Homo sapiens |
THP-1 Cell |
| pmid |
sentence |
| 25544559 |
We found that TIRAP-MyD88 dependent kinase IRAK1 phosphorylated GAPR-1 at Serine 58 site. The phosphorylation of GAPR-1 promoted its interaction with TRAM-TRIF dependent inhibitor TMED7, and impaired TMED7-mediated disruption of the TRAM-TRIF complex to trigger IFN-β and the IL10 secretion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IRAK1 | up-regulates
phosphorylation
|
STAT3 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129685 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
|
| pmid |
sentence |
| 15465816 |
Irak1 can directly use stat3 as a substrate and cause stat3 serine 727 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | down-regulates activity 
phosphorylation
|
IRAK1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252551 |
Thr100 |
LRARDIItAWHPPAP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11976320 |
CaMKKc and Akt overexpression increases IRAK1 phosphorylation at Thr100, and point mutation of this site abrogates the inhibitory effect of Akt on IRAK1-mediated NF-kappaB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT | down-regulates activity
phosphorylation
|
IRAK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248008 |
Thr100 |
LRARDIItAWHPPAP |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11976320 |
CaMKKc and Akt overexpression increases IRAK1 phosphorylation at Thr100, and point mutation of this site abrogates the inhibitory effect of Akt on IRAK1-mediated NF-kappaB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL1R1 | up-regulates activity 
|
IRAK1 |
0.912 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119208 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14625308 |
Formation of the signaling il-1 receptor complex results in the activation and hyperphosphorylation of irak-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling |
| + |
MYD88 | up-regulates activity
binding
|
IRAK1 |
0.843 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-67143 |
|
|
Mus musculus |
EL-4 Cell |
| pmid |
sentence |
| 10217414 |
Interleukin-1 (il-1) stimulates the association of the il-1 receptor-associated protein kinase (irak) with the heterodimer of il-iri and il-iracp via the adapter protein myd88. Myd88 binds to both irak (il-1 receptor-associated kinase) and the heterocomplex (the signaling complex) of the two receptor chains and thereby mediates the association of irak with the receptor. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Innate Immune Response, IL1 Signaling , Toll like receptors |
| + |
IRAK1 | up-regulates activity
binding
|
TRAF6 |
0.911 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-44234 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8837778 |
Il-1 treatment of 293 cells induces the association of traf6 with irak. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92994 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12242293 |
We now find that the phosphorylated IRAK in turn recruits TRAF6 to the receptor complex (complex I), which differs from the previous concept that IRAK interacts with TRAF6 after it leaves the receptor. IRAK then brings TRAF6 to TAK1 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Innate Immune Response, IL1 Signaling , Toll like receptors |
| + |
IRAK1 | up-regulates
phosphorylation
|
PELI3 |
0.717 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159052 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17997719 |
Pellino3 physically interacts with il-1r-associated kinase-1, tnf receptor-associated factor-6, tgf-beta-activated kinase-1, and nf-kappab-inducing kinase in an il-1-dependent manner in the present study, we demonstrate that irak1 and irak4 phosphorylate pellino isoforms in vitro and that phosphorylation greatly enhances pellino's e3 ubiquitin ligase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-103983 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12874243 |
Pellino3 physically interacts with il-1r-associated kinase-1, tnf receptor-associated factor-6, tgf-beta-activated kinase-1, and nf-kappab-inducing kinase in an il-1-dependent manner in the present study, we demonstrate that irak1 and irak4 phosphorylate pellino isoforms in vitro and that phosphorylation greatly enhances pellino's e3 ubiquitin ligase activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SOCS1 | down-regulates
binding
|
IRAK1 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95528 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12433373 |
Coimmunoprecipitation analyses demonstrated association of socs-1 with irak...This Finding suggests that socs-1 might suppress myd88-dependent signal pathways at least by binding to irak |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL1RL1 | up-regulates activity
binding
|
IRAK1 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277706 |
|
|
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 |
| + |
PELI3 | up-regulates
ubiquitination
|
IRAK1 |
0.717 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159061 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17997719 |
These studies suggest that pellino isoforms may be the e3 ubiquitin ligases that mediate the il-1-stimulated formation of k63-pub-irak1 in cells, which may contribute to the activation of ikkbeta and the transcription factor nf-kappab, as well as other pathways dependent on irak1/4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TOLLIP | down-regulates activity
binding
|
IRAK1 |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251980 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10854325 |
Binding of IL-1 to its receptor results in rapid assembly of a membrane-proximal signalling complex that consists of two different receptor chains (IL-1Rs), IL-1RI and IL-1RAcP, the adaptor protein MyD88, the serine/threonine kinase IRAK and a new protein, which we have named Tollip. Here we show that, before IL-1β treatment, Tollip is present in a complex with IRAK, and that recruitment of Tollip–IRAK complexes to the activated receptor complex occurs through association of Tollip with IL-1RAcP. Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (and IL-1Rs) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling |
| + |
PELI1 | up-regulates quantity by expression
ubiquitination
|
IRAK1 |
0.758 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159055 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17997719 |
These results were consistent with the observations made in vitro, namely that pellino isoforms are activated by irak1-catalysed phosphorylation and that, once activated, can ubiquitinate irak1 in cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IL1 Signaling |
| + |
PELI2 | up-regulates
ubiquitination
|
IRAK1 |
0.772 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159058 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17997719 |
These studies suggest that pellino isoforms may be the e3 ubiquitin ligases that mediate the il-1-stimulated formation of k63-pub-irak1 in cells, which may contribute to the activation of ikkbeta and the transcription factor nf-kappab, as well as other pathways dependent on irak1/4. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
IRAK1
- 
- 