[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=8761287 [NCBI, ExPASy, EBI, Israel, Japan]
Gibson L.,
Holmgreen S.P.,
Huang D.C.,
Bernard O.,
Copeland N.G.,
Jenkins N.A.,
Sutherland G.R.,
Baker E.,
Adams J.M.,
Cory S.;
"bcl-w, a novel member of the bcl-2 family, promotes cell survival.";
Oncogene 13:665-675(1996).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1093/dnares/3.5.321; PubMed=9039502 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T.,
Seki N.,
Ishikawa K.,
Ohira M.,
Kawarabayasi Y.,
Ohara O.,
Tanaka A.,
Kotani H.,
Miyajima N.,
Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N.,
Chen X.,
Rolfs A.,
Halleck A.,
Hines L.,
Eisenstein S.,
Koundinya M.,
Raphael J.,
Moreira D.,
Kelley T.,
LaBaer J.,
Lin Y.,
Phelan M.,
Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[5]
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SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1038/sj.cdd.4400835; PubMed=11423909 [NCBI, ExPASy, EBI, Israel, Japan]
O'Reilly L.A.,
Print C.,
Hausmann G.,
Moriishi K.,
Cory S.,
Huang D.C.S.,
Strasser A.;
"Tissue expression and subcellular localization of the pro-survival molecule Bcl-w.";
Cell Death Differ. 8:486-494(2001).
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[6]
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SUBCELLULAR LOCATION.
DOI=10.1083/jcb.200302144; PubMed=12952938 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Annan J.,
O'Reilly L.A.,
Crawford S.A.,
Hausmann G.,
Beaumont J.G.,
Parma L.P.,
Chen L.,
Lackmann M.,
Lithgow T.,
Hinds M.G.,
Day C.L.,
Adams J.M.,
Huang D.C.S.;
"Proapoptotic BH3-only proteins trigger membrane integration of prosurvival Bcl-w and neutralize its activity.";
J. Cell Biol. 162:877-887(2003).
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[7]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K.,
Sugiyama N.,
Kyono Y.,
Tomita M.,
Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
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[8]
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STRUCTURE BY NMR OF 1-183.
DOI=10.1093/emboj/cdg144; PubMed=12660157 [NCBI, ExPASy, EBI, Israel, Japan]
Hinds M.G.,
Lackmann M.,
Skea G.L.,
Harrison P.J.,
Huang D.C.S.,
Day C.L.;
"The structure of Bcl-w reveals a role for the C-terminal residues in modulating biological activity.";
EMBO J. 22:1497-1507(2003).
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[9]
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STRUCTURE BY NMR OF 2-171.
DOI=10.1074/jbc.M301798200; PubMed=12651847 [NCBI, ExPASy, EBI, Israel, Japan]
Denisov A.Y.,
Madiraju M.S.R.,
Chen G.,
Khadir A.,
Beauparlant P.,
Attardo G.,
Shore G.C.,
Gehring K.;
"Solution structure of human BCL-w: modulation of ligand binding by the C-terminal helix.";
J. Biol. Chem. 278:21124-21128(2003).
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- FUNCTION: Promotes cell survival. Blocks dexamethasone-induced apoptosis. Mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX.
- INTERACTION:
Q92934:BAD; NbExp=1; IntAct=EBI-707714, EBI-700771;
Q61337:Bad (xeno); NbExp=1; IntAct=EBI-707714, EBI-400328;
Q9BXH1:BBC3; NbExp=2; IntAct=EBI-707714, EBI-519884;
O43521:BCL2L11; NbExp=1; IntAct=EBI-707714, EBI-526406;
O54918:Bcl2l11 (xeno); NbExp=1; IntAct=EBI-707714, EBI-526067;
P55957:BID; NbExp=2; IntAct=EBI-707714, EBI-519672;
P70444:Bid (xeno); NbExp=1; IntAct=EBI-707714, EBI-783400;
Q13323:BIK; NbExp=2; IntAct=EBI-707714, EBI-700794;
Q8WYM1:bim-alpha1; NbExp=1; IntAct=EBI-707714, EBI-1002160;
Q91ZE9:Bmf (xeno); NbExp=2; IntAct=EBI-707714, EBI-708032;
O00198:HRK; NbExp=1; IntAct=EBI-707714, EBI-701322;
- 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.
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