Induces apoptosis and anoikis. Isoform BimL is more potent than isoform BimEL. Isoform Bim-alpha1, isoform Bim-alpha2 and isoform Bim-alpha3 induce apoptosis, although less potent than isoform BimEL, isoform BimL and isoform BimS. Isoform Bim-gamma induces apoptosis. Isoform Bim-alpha3 induces apoptosis possibly through a caspase-mediated pathway. Isoform BimAC and isoform BimABC lack the ability to induce apoptosis. Forms heterodimers with a number of antiapoptotic Bcl-2 proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1, BHRF1, and BCL2L2/BCLW (PubMed:11997495, PubMed:27013495, PubMed:18812174). 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. Interacts with YWHAZ. When phosphorylated, interacts with TRIM2; this interaction is associated with ubiquitination and degradation (PubMed:21478148). Interacts with MCL1; may sequester BCL2L11 to prevent its pro-apoptotic activity (PubMed:27013495, PubMed:17389404). Interacts with GIMAP5 (PubMed:16509771). Interacts with BCL2L10/BCL-B (PubMed:23235460, PubMed:23563182, PubMed:22498477). Interacts (when phosphorylated) with USP27X; the interaction leads to BCL2L11 deubiquitination and stabilization (PubMed:27013495). Interacts with humanin; the interaction prevents BIM-induced apoptosis. Does not interact with humanin. Interacts with BAX; the interaction may lead to BAX activation through conformational change (PubMed:11997495). Does not interact with humanin (PubMed:15661735). Interacts with BAX; the interaction may lead to BAX activation through conformational change. Associated with intracytoplasmic membranes. Translocates from microtubules to mitochondria on loss of cell adherence. Isoform BimEL, isoform BimL and isoform BimS are the predominant isoforms and are widely expressed with tissue-specific variation. Isoform Bim-gamma is most abundantly expressed in small intestine and colon, and in lower levels in spleen, prostate, testis, heart, liver and kidney. By ER stress in a DDIT3/CHOP-dependent manner. The BH3 motif is required for interaction with Bcl-2 proteins and cytotoxicity. Phosphorylation at Ser-69 by MAPK1/MAPK3 leads to interaction with TRIM2 and polyubiquitination, followed by proteasomal degradation (PubMed:15486195, PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (By similarity). 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.