B-Cell CLL/Lymphoma 2 Like Protein (Bcl2L) Antibody – Mouse Monoclonal

Function: Potent inhibitor of cell death. Inhibits activation of caspases

By similarity. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis. Ref.3 Ref.4 Ref.6

Subunit structure: Homodimer

By similarity. Isoform Bcl-X(L) forms heterodimers with BAX, BAK or BCL2. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity. Interacts with BAD. Interacts with P53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with P53/TP53. Interacts (isoform Bcl-X(L)) with SIVA1 (isoform 1); the interaction inhibits the anti-apoptotic activity. Interacts with BECN1 and PGAM5. Interacts (isoform Bcl-X(L)) with BAX (isoform Sigma). Interacts with BCL2L11

By similarity. Isoform Bcl-X(L) interacts with IKZF3

By similarity. Interacts with HEBP2

By similarity. Isoform Bcl-X(L) interacts with BOP

By similarity. Interacts with DMN1L; the interaction stimulates the GTPase activity of DMN1L in synapses and increases the number of axonal mitochondria and the size and number of synaptic vesicle clusters. Ref.6

Subcellular location: Mitochondrion membrane; Single-pass membrane protein

By similarity. Nucleus membrane; Single-pass membrane protein; Cytoplasmic side

By similarity. Cytoplasm › cytoskeleton › microtubule organizing center › centrosome

By similarity. Note: Mitochondrial membranes and perinuclear envelope

By similarity.

Tissue specificity: Expressed in most tissues. Bcl-X(beta) is specifically expressed in cerebellum, heart, and thymus. In the ovary, the predominant form is Bcl-X(L), with a small but detectable level of Bcl-X(S).

Domain: The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death.

Post-translational modification: Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity

By similarity.Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis

By similarity.

Sequence similarities: Belongs to the Bcl-2 family.

Sequence caution: The sequence AAC60701.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.The sequence AAC60702.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.