Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent. Forms heterodimers with a number of antiapoptotic Bcl-2 proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1, and BCL2L2/BCLW (PubMed:16543145, PubMed:27013495, PubMed:14499110). Interacts with BAX (in vitro); this interaction may induce the conformationally active form of BAX (PubMed:14499110). Does not heterodimerize with proapoptotic proteins such as BAD, BOK or BAK. Identified in a complex containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3 integrity is required for BCL2L1-binding (PubMed:21478148, PubMed:27013495, PubMed:14499110). 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:16543145, PubMed:27013495). When phosphorylated, isoform BimEL interacts with USP27X; this interaction leads to BCL2L11 deubiquitination and stabilization (PubMed:27013495). Interacts with GIMAP5 (PubMed:16509771). Interacts with BCL2L10/BCL-B (By similarity). Associated with intracytoplasmic membranes. Expressed in a number of B- and T-lymphoid cell lines. By ER stress. 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 (PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (PubMed:27013495). Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation. Conversely, deubiquitination catalyzed by USP27X stabilizes the protein. Belongs to the Bcl-2 family.