+ |
CREBBP | up-regulates activity
acetylation
|
IFNAR2 |
0.352 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-217783 |
Lys399 |
SGPCERRkSPLQDPF |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17923090 |
By binding to IFNalphaR2 within the region where two adjacent proline boxes bear phospho-Ser364 and phospho-Ser384, CBP acetylates IFNalphaR2 on Lys399, which in turn serves as the docking site for interferon regulatory factor 9 (IRF9)RF9 interacts with the acetyl-Lys399 motif by means of its IRF homology2 (IH2) domain, leading to formation of the ISGF3 complex that includes IRF9, STAT1, and STAT2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFNAR2 | form complex
binding
|
IFNAR |
0.903 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260333 |
|
|
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 |
+ |
IRF9 | up-regulates activity
binding
|
IFNAR2 |
0.717 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-217779 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
17923090 |
By binding to IFNalphaR2 within the region where two adjacent proline boxes bear phospho-Ser364 and phospho-Ser384, CBP acetylates IFNalphaR2 on Lys399, which in turn serves as the docking site for interferon regulatory factor 9 (IRF9)RF9 interacts with the acetyl-Lys399 motif by means of its IRF homology2 (IH2) domain, leading to formation of the ISGF3 complex that includes IRF9, STAT1, and STAT2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
IFNA1 | up-regulates activity
binding
|
IFNAR2 |
0.611 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-219298 |
|
|
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 |
+ |
IFNB1 | up-regulates activity
binding
|
IFNAR2 |
0.662 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-219304 |
|
|
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 |
+ |
IFNB1 | up-regulates
binding
|
IFNAR2 |
0.662 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105934 |
|
|
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 |
+ |
IFNW1 | up-regulates
binding
|
IFNAR2 |
0.751 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105982 |
|
|
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 |
+ |
IFNA1 | up-regulates
binding
|
IFNAR2 |
0.611 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-104641 |
|
|
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 |
+ |
G8RGG88B68 | up-regulates activity
chemical activation
|
IFNAR2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259391 |
|
|
in vitro |
|
pmid |
sentence |
15898717 |
To significantly improve the pharmacological properties of the drug, a pegylated form of IFNalpha(2a) was developed (PEGASYS). This 40 kDa PEG-conjugated IFNalpha(2a) ((40)PEG-IFNalpha(2a)) is obtained by the covalent binding of one 40 kDa branched PEG-polymer to a lysine side-chain of IFNalpha(2a). Here, we report the detailed structural, kinetic, and thermodynamic analysis of the binding to the extracellular domain of the receptor IFNAR2 of (40)PEG-IFNalpha(2a) and its isolated positional isomers modified at K31, K134, K131, K121, K164, and K70, respectively, in comparison with unmodified IFNalpha(2a). |
|
Publications: |
1 |
Organism: |
In Vitro |