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Subunit: Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs, and is necessary for anti-apoptotic activity (By similarity). Interacts with EI24 (By similarity). Also interacts with APAF1, BBC3, BCL2L1, BNIPL, MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the mitochondria and probably interferes with the binding of BCL2 to its targets. Interacts with BAG1 in an ATP-dependent manner. Interacts with RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated form). Interacts (via the BH4 domain) with EGLN3; the interaction prevents the formation of the BAX-BCL2 complex and inhibits the anti-apoptotic activity of BCL2. Interacts with G0S2; this interaction also prevents the formation of the anti-apoptotic BAX-BCL2 complex. Interacts with BOP Selected PDB 3D structures from [IMAGE] and Proteopedia [IMAGE] for BCL2 (see all 13): 1G5M (3D) [IMAGE] 1GJH (3D) [IMAGE] 1YSW (3D) [IMAGE] 2O21 (3D) [IMAGE] 2O22 (3D) [IMAGE] 2O2F (3D) [IMAGE]
Tissue specificity: Expressed in a variety of tissues [IMAGE] Pathway & Disease-focused RT2 Profiler PCR Arrays including BCL2 (see all 34): Neurogenesis in human mouse rat Lung Cancer in human mouse rat Multiple Sclerosis in human mouse rat Lymphoma in human mouse rat Infla
Function: UniProtKB/Swiss-Prot Summary: BCL2_HUMAN, P10415 Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1)
Similarity: Belongs to the Bcl-2 family [IMAGE]
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