Phosphorylation of PKC-theta

Stable Identifier
R-HSA-2730882
Type
Reaction
Species
Homo sapiens
Compartment
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Raft localized PKC-theta is phosphorylated and is activated. Phosphorylation of both tyrosine and serine-threonine residues is important in the regulation of PKC function. Six phosphorylation sites have been identified on PKC-theta: Y90, T219, T538, S676, S685, and S695. Phosphorylation of Y90 positively regulates NF-AT and NF-kB activation in T-cells. In mast cells Src family members Src and LYN have been shown to be involved in phosphorylating Y90 (Wang et al. 2012, Liu et al. 2001).

Literature References
PubMed ID Title Journal Year
16978534 Selective function of PKC-theta in T cells

Gupta, S, Manicassamy, S, Sun, Z

Cell Mol Immunol 2006
12473184 Protein kinase C-theta (PKC theta): a key enzyme in T cell life and death

Villalba, M, Altman, A

J Biochem (Tokyo) 2002
Participants
Participates
Catalyst Activity

protein tyrosine kinase activity of Allergen:p-LYN:p-FCERI:IgE aggregate [plasma membrane]

Orthologous Events
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