Phosphorylation of STAT1

Stable Identifier
Reaction [transition]
Homo sapiens
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Phosphotyrosine on STAT2 acts as docking site for STAT1 molecules. STAT1 binds to phosphorylated STAT2 and this is followed by STAT1 phosphorylation on tyrosine residue 701 (Y701). These STATs recruited to the phosporylated IFNAR1 form two distinct transcriptional activator complexes, namely, IFN-alpha-activated factor (AAF) and IFN-stimulated gene factor 3 (ISGF3). AAF is a homodimer of STAT1, whereas ISGF3 is a heterotrimeric complex of STAT1, STAT2 and IRF9 (also known as p48 or ISGF3gamma) (Honda et al. 2005).

SARS-CoV-2 nucleoprotein (N) binds to both STAT1 and STAT2, prevents their phosphorylation, and suppresses their nuclear translocation induced by IFN (Mu J et al. 2020).

Protein tyrosine phosphatases SHP-1 and SHP-2 dephosphorylate JAK1 and STAT1 and suppress their signaling.

Literature References
PubMed ID Title Journal Year
10982844 Regulation of STAT1 nuclear export by Jak1

David, M, Mowen, K

Mol Cell Biol 2000
8232552 The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and -gamma signal transduction

Witthuhn, BA, Barbieri, G, Ziemiecki, A, Briscoe, J, Harpur, AG, Laxton, C, Muller, M, Silvennoinen, O, Schindler, C, Guschin, D

Nature 1993
Catalyst Activity

protein tyrosine kinase activity of IFNA/B:IFNAR2:p-JAK1:STAT2:p-IFNAR1:p-TYK2:p-STAT2 [plasma membrane]

This event is regulated
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