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Ifngr1

Function

Receptor subunit for interferon gamma/INFG that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (, PubMed:20926559, PubMed:27286456). Associates with transmembrane accessory factor IFNGR2 to form a functional receptor (PubMed:2137461, PubMed:2530216, PubMed:2530582, PubMed:2531896, PubMed:2532365). Upon ligand binding, the intracellular domain of IFNGR1 opens out to allow association of downstream signaling components JAK1 and JAK2. In turn, activated JAK1 phosphorylates IFNGR1 to form a docking site for STAT1. Subsequent phosphorylation of STAT1 leads to its dimerization, translocation to the nucleus, and stimulation of target gene transcription (PubMed:19889125). STAT3 can also be activated in a similar manner although activation seems weaker (PubMed:15284232). IFNGR1 intracellular domain phosphorylation also provides a docking site for SOCS1 that regulates the JAK-STAT pathway by competing with STAT1 binding to IFNGR1 (PubMed:15522878).

Post-translational modifications

Phosphorylated at Ser/Thr residues. Phosphorylation of Tyr-445 is required for IFNG receptor signal transduction. Influenza virus infection leads to phosphorylation in a CSNK1A1-dependent manner.

Ubiquitinated after phosphorylation in a CSNK1A1-dependent manner, leading to the lysosome-dependent degradation. Proteasomally degraded through 'Lys-48'-mediated ubiquitination. Ubiquitination is necessary for efficient IFNGR1 signaling.

Sequence Similarities

Belongs to the type II cytokine receptor family.

Cellular localization

Alternative names

CD119, Ifngr, Ifngr1, Interferon gamma receptor 1, IFN-gamma receptor 1, IFN-gamma-R1, Interferon gamma receptor alpha-chain, IFN-gamma-R-alpha

swissprot:P15261 entrezGene:15979

Other research areas