J Biol Chem 1999,
PMID: 9890938
Naeger, L K; McKinney, J; Salvekar, A; Hoey, T
The specificity of the various STAT SH2 domains for different tyrosine-containing peptides enables cytokines to activate different signaling pathways and to induce distinct patterns of gene expression. We show that STAT4 has a unique peptide specificity and binds to the peptide sequence pYLPSNID (where pY represents phosphotyrosine). This motif is found at tyrosine residue 800 in the beta2 subunit of the interleukin-12 receptor and is required for DNA binding and transcriptional activity of STAT4. Our data demonstrate that transfection of interleukin-12 receptor beta1 and beta2 subunits is sufficient for STAT4 activation but not for STAT1 or STAT3 activation.
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Text Mining Data
Dashed line = No text mining data
Manually curated Databases
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IRef Intact Interaction:
IL12RB2
—
STAT4
(association, fluorescence polarization spectroscopy)
-
NCI Pathway Database IL12-mediated signaling events:
STAT4 (STAT4)
→
STAT4 (dimer) complex (STAT4)
(modification, collaborate)
Evidence: mutant phenotype, assay, other species
-
NCI Pathway Database IL12-mediated signaling events:
STAT4 (STAT4)
→
IL12/IL12R/TYK2/JAK2 complex (IL12A-IL12B-IL12RB1-IL12RB2-TYK2-JAK2)
(modification, collaborate)
Evidence: mutant phenotype, assay, other species
-
NCI Pathway Database IL12-mediated signaling events:
STAT4 (STAT4)
→
RIP2 (RIPK2)
(modification, collaborate)
Evidence: mutant phenotype, assay, other species
-
NCI Pathway Database IL12-mediated signaling events:
IL12/IL12R/TYK2/JAK2 complex (IL12A-IL12B-IL12RB1-IL12RB2-TYK2-JAK2)
→
RIP2 (RIPK2)
(modification, activates)
Evidence: mutant phenotype, assay, other species
In total, 29 gene pairs are associated to this article in curated databases