Induces apoptosis and anoikis. Forms heterodimers with a number of antiapoptotic Bcl-2 proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1, and BCL2L2/BCLW. Does not heterodimerize with proapoptotic proteins such as BAD, BOK or BAK (PubMed:9731710). Identified in a complex containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3 integrity is required for BCL2L1-binding. Interacts with YWHAZ. When phosphorylated, interacts with TRIM2; this interaction is associated with ubiquitination and degradation (PubMed:21478148). Interacts (via BH3) with MCL1; this interaction may sequester BCL2L11 and prevent its pro-apoptotic activity (PubMed:9731710). When phosphorylated, isoform BimEL interacts with USP27X; this interaction leads to BCL2L11 deubiquitination and stabilization (By similarity). Interacts with GIMAP5 (By similarity). Interacts with BCL2L10/BCL-B (By similarity). Associated with intracytoplasmic membranes. Widely expressed. The BH3 motif is required for the interaction with Bcl-2 proteins and cytotoxicity. Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation. Deubiquitination catalyzed by USP27X stabilizes the protein. Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation (PubMed:21478148). Conversely, deubiquitination catalyzed by USP27X stabilizes the protein (By similarity). Produced by alternative initiation at Met-104 of isoform BOD-L. Belongs to the Bcl-2 family.