CASP9 is phosphorylated at T412

Stable Identifier
R-HSA-9627089
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Phosphorylation of caspase 9 (CASP9) may contribute to the suppression of apoptosis. A major inhibitory phosphorylation site in CASP9 is Thr412, which forms part of a Thr‑Pro motif (Allan LA & Clarke PR 2007; Martin MC et al. 2008). This motif is targeted by multiple proline‑directed kinases such as ERK1/2 in response to extracellular growth/survival signals or CDK1‑cyclin B1 during mitosis (Allan LA et al. 2003; Allan LA & Clarke PR 2007; Martin MC et al. 2008). Thr412 is also phosphorylated by DYRK1A, which regulates apoptosis during development (Seifert A et al. 2008).
Literature References
PubMed ID Title Journal Year
18083711 The docking interaction of caspase-9 with ERK2 provides a mechanism for the selective inhibitory phosphorylation of caspase-9 at threonine 125

Allan, LA, Clarke, PR, Mancini, EJ, Martin, MC

J. Biol. Chem. 2008
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Catalyst Activity

protein serine/threonine kinase activity of p-T,Y MAPK dimers [cytosol]

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