| + |
IFNGR1 | form complex 
binding
|
IFNGR2/INFGR1 |
0.734 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249485 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 19041276 |
The activation of this signaling pathway involves the binding of IFN-g to two IFN-g receptor (IFN-gR) subunits, made up of respective IFNgR1:IFNgR2 pairs, which dimerize upon IFN-g binding to form the IFN-gR complex. Two JAKs, JAK1and JAK2,which bind to each IFN-gR subunits, respectively through their N-terminal domains, both become activated by tyrosine phosphorylation in a JAK2-dependent process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAK2 | up-regulates activity 
phosphorylation
|
IFNGR2/INFGR1 |
0.694 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249493 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, Macrophage polarization |
| + |
JAK1 | up-regulates activity
phosphorylation
|
IFNGR2/INFGR1 |
0.669 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249492 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 19041276 |
The activation of this signaling pathway involves the binding of IFN-g to two IFN-g receptor (IFN-gR) subunits, made up of respective IFNgR1:IFNgR2 pairs, which dimerize upon IFN-g binding to form the IFN-gR complex. Two JAKs, JAK1and JAK2,which bind to each IFN-gR subunits, respectively through their N-terminal domains, both become activated by tyrosine phosphorylation in a JAK2-dependent process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, SARS-CoV CYTOKINE STORM |
| + |
LMP2 | down-regulates quantity by destabilization 
|
IFNGR2/INFGR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266825 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19718044 |
The EBV-encoded Latent Membrane Proteins, LMP2A and LMP2B, Limit the Actions of Interferon by Targeting Interferon Receptors for Degradation. LMP2A and LMP2B increase the turnover and degradation of IFNAR1 and IFNGR1. LMP2A and LMP2B reduce the half-life of IFNAR1 and IFNGR1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
IFNGR2/INFGR1 | up-regulates activity
phosphorylation
|
STAT1 |
0.666 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249494 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, SARS-CoV CYTOKINE STORM |
| + |
IFNGR2/INFGR1 | up-regulates activity
binding
|
JAK2 |
0.694 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249506 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection, Macrophage polarization |
| + |
IFNGR2 | form complex
binding
|
IFNGR2/INFGR1 |
0.734 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249486 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 19041276 |
The activation of this signaling pathway involves the binding of IFN-g to two IFN-g receptor (IFN-gR) subunits, made up of respective IFNgR1:IFNgR2 pairs, which dimerize upon IFN-g binding to form the IFN-gR complex. Two JAKs, JAK1and JAK2,which bind to each IFN-gR subunits, respectively through their N-terminal domains, both become activated by tyrosine phosphorylation in a JAK2-dependent process. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IFNG | up-regulates activity
binding
|
IFNGR2/INFGR1 |
0.757 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249487 |
|
|
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 23898330 |
In the classical model of IFNgamma signaling, dimeric IFNgamma cross-links the IFNGR1 receptor subunit that results in allosteric changes in receptor cytoplasmic domain. This results in movement of JAK2 from receptor subunit IFNGR2 to IFNGR1. The JAKs autophosphorylate and then phosphorylate IFNGR1 cytoplasmic domain. This results in binding, phosphorylation, and dimer formation of STAT1_. The dimeric STAT1_ dissociates from receptor and undergoes nuclear translocation via an intrinsic NLS for specific gene activation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Macrophage polarization, SARS-CoV CYTOKINE STORM |
3.0
IFNGR2/INFGR1