+ |
IFNG | up-regulates
binding
|
IFNGR2 |
0.634 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-31013 |
|
|
Homo sapiens |
|
pmid |
sentence |
7673114 |
Ifn-g Binds to the ifn-g Receptor binding subunit (ifn-gR1;receptor chain 1), a species-specific cell surface transmembrane receptor chain (41, 42). A second transmembrane protein (ifn-gR2) (43 45) is required for signal transduction |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
JAK2 | up-regulates activity
binding
|
IFNGR2 |
0.688 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249489 |
|
|
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 |
+ |
JAK1 | up-regulates activity
phosphorylation
|
IFNGR2 |
0.647 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249491 |
|
|
Homo sapiens |
|
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 |
+ |
IFNGR2 | up-regulates activity
binding
|
JAK2 |
0.688 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249504 |
|
|
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 |
+ |
IFNGR2 | form complex
binding
|
IFNGR2/INFGR1 |
0.733 |
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 |