+ |
IFNA2 | up-regulates quantity by stabilization
|
ISGF3 complex |
0.47 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-240684 |
|
|
Homo sapiens |
|
pmid |
sentence |
22171011 |
IFN-I (IFN-_ and IFN-_) induces the assembly of IFN-stimulated gene factor 3 (ISGF3), a multimeric transcriptional activation complex composed of STAT1, STAT2, and IFN regulatory factor 9. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ISGF3 complex | up-regulates quantity by expression
transcriptional regulation
|
EIF2AK2 |
0.491 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260158 |
|
|
Homo sapiens |
|
pmid |
sentence |
27712625 |
The activated kinases then phosphorylate the signal transducers and transcription factors STAT1 and STAT2, which form a complex with IRF9 (ISGF3) that enters the nucleus to transactivate promoters of an antiviral gene expression program. Genes that are specifically upregulated by IFNs are collectively called ISGs (IFN-stimulated genes). The kinase PKR is an ISG product acting as a signaling PRR on one hand (see earlier), but its main function in antiviral defense is the inhibition of protein synthesis.PKR has a broad antiviral spectrum. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Inflammosome Activation, SARS-CoV CYTOKINE STORM, SARS-CoV INFLAMMATORY RESPONSE |
+ |
STAT1 | form complex
binding
|
ISGF3 complex |
0.672 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-240606 |
|
|
in vitro |
|
pmid |
sentence |
8943351 |
The first STAT-containing transcription factor to be studied, the alpha-interferon-induced ISGF3, is composed of a Stat1:2 heterodimer and a weak DNA-binding protein, p48. The p48 and Stat1:2 heterodimer do not associate stably in the absence of DNA, but we show that amino acids approximately 150 to 250 of Stat1 and a COOH-terminal portion of p48 exhibit physical interaction, implying contact that stabilizes ISGF3 |
|
Publications: |
1 |
Organism: |
In Vitro |
Pathways: | SARS-CoV CYTOKINE STORM |
+ |
STAT2 | form complex
binding
|
ISGF3 complex |
0.726 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-240603 |
|
|
in vitro |
|
pmid |
sentence |
8943351 |
The first STAT-containing transcription factor to be studied, the alpha-interferon-induced ISGF3, is composed of a Stat1:2 heterodimer and a weak DNA-binding protein, p48. The p48 and Stat1:2 heterodimer do not associate stably in the absence of DNA, but we show that amino acids approximately 150 to 250 of Stat1 and a COOH-terminal portion of p48 exhibit physical interaction, implying contact that stabilizes ISGF3 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
IRF9 | form complex
binding
|
ISGF3 complex |
0.865 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-240600 |
|
|
in vitro |
|
pmid |
sentence |
8943351 |
The first STAT-containing transcription factor to be studied, the alpha-interferon-induced ISGF3, is composed of a Stat1:2 heterodimer and a weak DNA-binding protein, p48. The p48 and Stat1:2 heterodimer do not associate stably in the absence of DNA, but we show that amino acids approximately 150 to 250 of Stat1 and a COOH-terminal portion of p48 exhibit physical interaction, implying contact that stabilizes ISGF3 |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
TYK2 | up-regulates activity
phosphorylation
|
ISGF3 complex |
0.72 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260148 |
|
|
Homo sapiens |
|
pmid |
sentence |
15120645 |
Despite signaling through distinct receptor complexes, type I IFNs and IFN-lambda activate similar signaling events and biological activities, consistent with their common ability to mediate an antiviral state in cells (Fig. 6). In both cases, receptor engagement leads via the activation of the Jak kinases Jak1 and Tyk2 to the activation of the IFN-stimulated gene factor 3 (ISGF3) transcription complex, composed of latent transcriptional factors of the Signal Transducers and Activators of Transcription (STAT) family, Stat1 and Stat2, and of the interferon regulatory factor (IRF) IRF9 (ISGF3g or p48). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Inflammosome Activation, SARS-CoV INFLAMMATORY RESPONSE |
+ |
JAK1 | up-regulates activity
phosphorylation
|
ISGF3 complex |
0.715 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260149 |
|
|
Homo sapiens |
|
pmid |
sentence |
15120645 |
Despite signaling through distinct receptor complexes, type I IFNs and IFN-lambda activate similar signaling events and biological activities, consistent with their common ability to mediate an antiviral state in cells (Fig. 6). In both cases, receptor engagement leads via the activation of the Jak kinases Jak1 and Tyk2 to the activation of the IFN-stimulated gene factor 3 (ISGF3) transcription complex, composed of latent transcriptional factors of the Signal Transducers and Activators of Transcription (STAT) family, Stat1 and Stat2, and of the interferon regulatory factor (IRF) IRF9 (ISGF3g or p48). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | COVID-19 Causal Network, Inflammosome Activation, SARS-CoV CYTOKINE STORM, SARS-CoV INFLAMMATORY RESPONSE |
+ |
IFNA1 | up-regulates quantity by stabilization
|
ISGF3 complex |
0.464 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-240610 |
|
|
Homo sapiens |
|
pmid |
sentence |
22171011 |
IFN-I (IFN-_ and IFN-_) induces the assembly of IFN-stimulated gene factor 3 (ISGF3), a multimeric transcriptional activation complex composed of STAT1, STAT2, and IFN regulatory factor 9. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | SARS-CoV CYTOKINE STORM |
+ |
KPNB1 | up-regulates activity
relocalization
|
ISGF3 complex |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260274 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
17596301 |
Although ORF6 causes a relocalization of KPNA2 from the cytosol to the ER/Golgi membrane, KPNA2 is not directly involved in the translocation of the STAT1:STAT2:IRF9 (ISGF3) complex into the nucleus; rather, KPNA1 interacts with KPNB1 to initiate ISGF3's nuclear localization. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |