IL12RB2 in IL12A:IL12RB1:p-Y-TYK2:IL12B:IL12RB2:p-JAK2 is phosphorylated

Stable Identifier
Reaction [omitted]
Homo sapiens
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Phosphorylated residues in the cytoplasmic region of Interleukin-12 receptor subunit beta 2 (IL12RB2) enable binding and activation of Signal transducer and activator of transcription 4 (STAT4) by means of Tyrosine-protein kinase JAK2 (JAK2).
STAT4 was found to bind only phosphorylated tyrosine-800, and not to phosphorylated tyrosines 678 or 767 when phosphorylated. Although required, phosphorylated tyrosine-800 was not sufficient for binding of STAT4, as other residues in IL12RB2, specifically at -4, -1 and +1 relative to the tyrosine, contribute to the specificity of STAT4 binding (Yao et al. 1999).
As the pattern of phosphorylations required for receptor activation is unknown, this is a black box event.

Literature References
PubMed ID Title Journal Year
10415122 Direct interaction of STAT4 with the IL-12 receptor

Yao, BB, Faltynek, CR, Surowy, CS, Niu, P

Arch. Biochem. Biophys. 1999
Catalyst Activity

transmembrane receptor protein tyrosine kinase activity of IL12A:IL12B:IL12RB1:p-Y-TYK2:IL12RB2:p-JAK2 [plasma membrane]

Orthologous Events
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