Phosphorylation of PKC-theta

Stable Identifier
R-HSA-2730882
Type
Reaction [transition]
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
12473184 Protein kinase C-theta (PKC theta): a key enzyme in T cell life and death

Altman, A, Villalba, M

J Biochem (Tokyo) 2002
16978534 Selective function of PKC-theta in T cells

Manicassamy, S, Gupta, S, Sun, Z

Cell Mol Immunol 2006
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein tyrosine kinase activity of Allergin:p-LYN:p-FCERI:IgE aggregate [plasma membrane]
Physical Entity
Activity
Orthologous Events
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Reviewed
Created