Title : Identification of amino acid residues critical for the Src-homology 2 domain-dependent docking of Stat2 to the interferon alpha receptor.

Pub. Date : 1998 Jul 31

PMID : 9677371






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Upon treatment of cells with interferon alpha (IFNalpha), the IFNaR1 subunit of the IFNalpha receptor becomes tyrosine phosphorylated at position 466. Tyrosine interferon alpha 1 Homo sapiens
2 Upon treatment of cells with interferon alpha (IFNalpha), the IFNaR1 subunit of the IFNalpha receptor becomes tyrosine phosphorylated at position 466. Tyrosine interferon alpha 1 Homo sapiens
3 The region surrounding phosphorylated tyrosine 466 subsequently acts as a docking site for the SH2 domain of Stat2, facilitating phosphorylation of the latter and, thus, the transduction of the IFNalpha signal. Tyrosine interferon alpha 1 Homo sapiens