ID:B2CL2_HUMAN DESCRIPTION: RecName: Full=Bcl-2-like protein 2; Short=Bcl2-L-2; AltName: Full=Apoptosis regulator Bcl-W; FUNCTION: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. INTERACTION: Q07812:BAX; NbExp=3; IntAct=EBI-707714, EBI-516580; Q9BXH1:BBC3; NbExp=2; IntAct=EBI-707714, EBI-519884; O43521:BCL2L11; NbExp=4; IntAct=EBI-707714, EBI-526406; P55957:BID; NbExp=5; IntAct=EBI-707714, EBI-519672; Q13323:BIK; NbExp=2; IntAct=EBI-707714, EBI-700794; Q91ZE9:Bmf (xeno); NbExp=2; IntAct=EBI-707714, EBI-708032; SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane protein. Note=Loosely associated with the mitochondrial membrane in healthy cells. During apoptosis, tightly bound to the membrane. TISSUE SPECIFICITY: Expressed (at protein level) in a wide range of tissues with highest levels in brain, spinal cord, testis, pancreas, heart, spleen and mammary glands. Moderate levels found in thymus, ovary and small intestine. Not detected in salivary gland, muscle or liver. Also expressed in cell lines of myeloid, fibroblast and epithelial origin. Not detected in most lymphoid cell lines. DOMAIN: The BH4 motif seems to be involved in the anti-apoptotic function. DOMAIN: The BH1 and BH2 motifs form a hydrophobic groove which acts as a docking site for the BH3 domain of some pro-apoptotic proteins. The C-terminal residues of BCL2L2 fold into the BH3- binding cleft and modulate pro-survival activity by regulating ligand access. When BH3 domain-containing proteins bind, they displace the C-terminus, allowing its insertion into the membrane and neutralizing the pro-survival activity of BCL2L2. SIMILARITY: Belongs to the Bcl-2 family. SEQUENCE CAUTION: Sequence=BAA19666.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q92843
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0005515 protein binding GO:0042802 identical protein binding GO:0042803 protein homodimerization activity GO:0046982 protein heterodimerization activity GO:0051400 BH domain binding GO:0097718 disordered domain specific binding
Biological Process: GO:0006915 apoptotic process GO:0007283 spermatogenesis GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage GO:0042981 regulation of apoptotic process GO:0043066 negative regulation of apoptotic process GO:0060011 Sertoli cell proliferation GO:0097192 extrinsic apoptotic signaling pathway in absence of ligand GO:2001243 negative regulation of intrinsic apoptotic signaling pathway