+ |
TYK2 | up-regulates activity
phosphorylation
|
IFNAR1 |
0.908 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246934 |
Tyr466 |
VFLRCINyVFFPSLK |
in vitro |
|
pmid |
sentence |
8605876 |
We demonstrate that, in vitro, p135tyk2 phosphorylates two tyrosines on IFNaR1. A phosphopeptide corresponding to the major phosphorylation site (Tyr466) binds STAT2, but not STAT1, in an SH-2-dependent manner. Furthermore, only latent, non-phosphorylated STAT2 interacts with this phosphopeptide. When this phosphopeptide is introduced into permeabilized cells, the IFN alpha-dependent tyrosine phosphorylation of both STATs is blocked. Finally, mutant versions of IFNaR1, in which Tyr466 is changed to phenylalanine, can act in a dominant negative manner to inhibit phosphorylation of STAT2. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-246939 |
Tyr481 |
PSSSIDEyFSEQPLK |
Homo sapiens |
|
pmid |
sentence |
7526154 |
In this report, we demonstrate that the alpha subunit of the type I IFN receptor (IFN-R) corresponds to the product of a previously cloned receptor subunit cDNA and, further, that the p135tyk2 tyrosine kinase directly binds and tyrosine phosphorylates this receptor subunit.These data support the hypothesis that the Tyk2 protein functions as part of a receptor complex to initiate intracellular signaling in response to type I IFNs |
|
Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
+ |
IFNW1 | up-regulates
binding
|
IFNAR1 |
0.719 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105979 |
|
|
Homo sapiens |
|
pmid |
sentence |
11278538 |
Ifn-alpha, ifn-beta, and ifn-omega, induce somewhat different cellular effects but act through a common receptor complex, ifnar, composed of subunits ifnar-1 and ifnar-2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFNAR1 | form complex
binding
|
IFNAR |
0.903 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260332 |
|
|
Homo sapiens |
|
pmid |
sentence |
11278538 |
The human type I interferons, IFN-alpha, IFN-beta, and IFN-omega, induce somewhat different cellular effects but act through a common receptor complex, IFNAR, composed of subunits IFNAR-1 and IFNAR-2. Human IFNAR-2 binds all type I IFNs but with lower affinity and different specificity than the IFNAR complex. Human IFNAR-1 has low intrinsic binding of human IFNs but strongly affects the affinity and differential ligand specificity of the IFNAR complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFNB1 | up-regulates
binding
|
IFNAR1 |
0.862 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104663 |
|
|
Homo sapiens |
|
pmid |
sentence |
11278538 |
Ifn-alpha, ifn-beta, and ifn-omega, induce somewhat different cellular effects but act through a common receptor complex, ifnar, composed of subunits ifnar-1 and ifnar-2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFNAR1 | up-regulates activity
phosphorylation
|
PI3K |
0.331 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260435 |
|
|
Homo sapiens |
|
pmid |
sentence |
21631354 |
These results indicate that NF-κB activation by IFN via the PI3K pathway is distinct from the ISRE-driven mechanism in regulating gene expression. Activation of PI3K/AKT by IFN has also been described through the insulin receptor substrate 1 (Uddin and others 1997) and through the direct interaction of PI3K with IFNAR1, which also leads to induction of NF-κB activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFNA1 | up-regulates
binding
|
IFNAR1 |
0.649 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-36622 |
|
|
Homo sapiens |
|
pmid |
sentence |
8181059 |
The present study describes a novel type i ifn receptor having the ability to bind and respond to several subtypes of ifn-a as well as to ifn-8. This 102 kda-51 kda receptor is essential for the activity of many type i ifns, as demonstrated with anti-receptor antibodies. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFNB1 | up-regulates activity
binding
|
IFNAR1 |
0.862 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-219301 |
|
|
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
11278538 |
Ifn-alpha, ifn-beta, and ifn-omega, induce somewhat different cellular effects but act through a common receptor complex, ifnar, composed of subunits ifnar-1 and ifnar-2. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |