| Post Translational Modification |
PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-apoptotic activity (PubMed:9115213). Growth factor-stimulated phosphorylation on Ser-70 by PKC is required for the anti-apoptosis activity and occurs during the G2/M phase of the cell cycle (PubMed:9115213). In the absence of growth factors, BCL2 appears to be phosphorylated by other protein kinases such as ERKs and stress-activated kinases (PubMed:9115213). Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70 and Ser-84, wich stimulates starvation-induced autophagy (By similarity). Dephosphorylated by protein phosphatase 2A (PP2A) (PubMed:9852076). {ECO:0000250|UniProtKB:P10415, ECO:0000269|PubMed:9115213, ECO:0000269|PubMed:9852076}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity, causes the release of cytochrome c into the cytosol promoting further caspase activity. {ECO:0000250|UniProtKB:P10415}.; PTM: Monoubiquitinated by PRKN, leading to an increase in its stability (By similarity). Ubiquitinated by SCF(FBXO10), leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P10415}. |