STAT4 is phosphorylated by p-JAK2 and/or p-Y-TYK2 after IL12:IL12R interaction

Stable Identifier
R-HSA-8950354
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Inferred from mouse:
Signal transducer and activator of transcription 4 (STAT4) is activated via interaction with tyrosine-800 of Interleukin-12 receptor beta 2 subunit (IL12RB2). Based on experiments with murine-specific peptides, STAT4 activation depends on interaction with the peptide sequence pYLPSNID, where pY represents phosphotyrosine. STAT1 and STAT3 are not activated directly through the Interleukin-12 heterodimeric receptor (Naeger et al. 1999).
As the pattern of phosphorylations required for this event is unclear, it is represented here as a black box event.
Literature References
PubMed ID Title Journal Year
9890938 Identification of a STAT4 binding site in the interleukin-12 receptor required for signaling

Hoey, T, McKinney, J, Salvekar, A, Naeger, LK

J. Biol. Chem. 1999
Participants
Participates
Catalyst Activity

transmembrane receptor protein tyrosine kinase activity of IL12A:IL12B:IL12RB1:p-Y800-IL12RB2:p-Y-TYK2:p-JAK2:2xSTAT4 [plasma membrane]

Inferred From
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