MOUSE:B2CL1

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Species (Taxon ID)	Mus musculus (Mouse). (10090)
Gene Name(s)	Bcl2l1 (synonyms: Bcl2l, Bclx)
Protein Name(s)	Bcl-2-like protein 1 Bcl2-L-1 Apoptosis regulator Bcl-X
External Links
UniProt	Q64373
EMBL	X83574 L35049 L35048 U10102 U10101 U10100 U51278 U51279 U78031 U78030
IPI	IPI00133454 IPI00227922 IPI00227924 IPI00406354
PIR	I49055 I49056 I49057
RefSeq	NP_033873.3
UniGene	Mm.238213
PDB	1PQ0 1PQ1 2BZW 3IHC 3IHD 3IHE 3IHF 3IIG 3IIH 3ILB 3ILC
PDBsum	1PQ0 1PQ1 2BZW 3IHC 3IHD 3IHE 3IHF 3IIG 3IIH 3ILB 3ILC
ProteinModelPortal	Q64373
SMR	Q64373
IntAct	Q64373
MINT	MINT-87027
STRING	Q64373
PhosphoSite	Q64373
PRIDE	Q64373
Ensembl	ENSMUST00000007803 ENSMUST00000109820 ENSMUST00000134902 ENSMUST00000140436
GeneID	12048
KEGG	mmu:12048
UCSC	uc008ngi.1 uc008ngn.1
CTD	598
MGI	MGI:88139
OMA	NGSPSWH
OrthoDB	EOG47PX6Z
NextBio	280335
PMAP-CutDB	Q64373
ArrayExpress	Q64373
Bgee	Q64373
CleanEx	MM_BCL2L1
Genevestigator	Q64373
GermOnline	ENSMUSG00000007659
GO	GO:0005829 GO:0016021 GO:0031966 GO:0046982 GO:0006916 GO:0008283 GO:0060154 GO:0071312 GO:0071230 GO:0071480 GO:0009566 GO:0007281 GO:0040007 GO:0001701 GO:0008584 GO:0043066 GO:0043524 GO:0001541 GO:0045768 GO:0043065 GO:0008284 GO:0001836 GO:0046898 GO:0007283
InterPro	IPR013279 IPR002475 IPR000712 IPR020717 IPR020726 IPR020728 IPR003093 IPR020731 IPR004725
KO	K04570
Pfam	PF00452 PF02180
PRINTS	PR01864 PR01862
SMART	SM00337 SM00265
TIGRFAMs	TIGR00865
PROSITE	PS50062 PS01080 PS01258 PS01259 PS01260 PS50063

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000910	cytokinesis	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q07817	P	Seeded From UniProt
	GO:0001541	ovarian follicle development	PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	Seeded From UniProt
	GO:0001541	ovarian follicle development	PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	Seeded From UniProt
	GO:0001701	in utero embryonic development	PMID:10618441^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2158303	P	Seeded From UniProt
	GO:0001836	release of cytochrome c from mitochondria	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	P	Seeded From UniProt
	GO:0001836	release of cytochrome c from mitochondria	PMID:17052454^[3]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	Seeded From UniProt
	GO:0005515	protein binding	PMID:18223655^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q61337	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21095239^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q61337	F	Seeded From UniProt
	GO:0005622	intracellular	PMID:11146504^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C	Seeded From UniProt
	GO:0005739	mitochondrion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0496	C	Seeded From UniProt
	GO:0005739	mitochondrion	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	C	Seeded From UniProt
	GO:0005739	mitochondrion	PMID:12931191^[7]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005739	mitochondrion	PMID:14651853^[8]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005813	centrosome	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q07817	C	Seeded From UniProt
	GO:0005815	microtubule organizing center	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0048	C	Seeded From UniProt
	GO:0005829	cytosol	PMID:11980919^[9]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005856	cytoskeleton	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0206	C	Seeded From UniProt
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P	Seeded From UniProt
	GO:0006915	apoptosis	PMID:10618441^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:107739	P	Seeded From UniProt
	GO:0006915	apoptosis	PMID:12115603^[10]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006916	anti-apoptosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	P	Seeded From UniProt
	GO:0006916	anti-apoptosis	PMID:11717309^[11]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006916	anti-apoptosis	PMID:15901672^[12]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006916	anti-apoptosis	PMID:17267035^[13]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006916	anti-apoptosis	PMID:7607090^[14]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0007281	germ cell development	PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	Seeded From UniProt
	GO:0007281	germ cell development	PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	Seeded From UniProt
	GO:0007283	spermatogenesis	PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	Seeded From UniProt
	GO:0008283	cell proliferation	PMID:9176392^[15]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008284	positive regulation of cell proliferation	PMID:17267035^[13]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008584	male gonad development	PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	Seeded From UniProt
	GO:0009314	response to radiation	PMID:14517295^[16]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0009566	fertilization	PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	Seeded From UniProt
	GO:0009615	response to virus	PMID:15231831^[17]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR004725	C	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C	Seeded From UniProt
	GO:0031966	mitochondrial membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0171	C	Seeded From UniProt
	GO:0031966	mitochondrial membrane	PMID:11980919^[9]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0034097	response to cytokine stimulus	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	P	Seeded From UniProt
	GO:0040007	growth	PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	Seeded From UniProt
	GO:0042802	identical protein binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	F	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000712	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002475	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003093	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR004725	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR013279	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020717	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020726	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020728	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020731	P	Seeded From UniProt
	GO:0043065	positive regulation of apoptosis	PMID:8798158^[18]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	PMID:10618441^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2158303	P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	PMID:14517295^[16]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	PMID:8798158^[18]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	PMID:8798452^[19]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	Seeded From UniProt
	GO:0043066	negative regulation of apoptosis	PMID:9867803^[20]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043524	negative regulation of neuron apoptosis	PMID:11150333^[21]	IGI: Inferred from Genetic Interaction	MGI:MGI:1277950	P	Seeded From UniProt
	GO:0043524	negative regulation of neuron apoptosis	PMID:11150333^[21]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2158303	P	Seeded From UniProt
	GO:0043524	negative regulation of neuron apoptosis	PMID:15231831^[17]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043524	negative regulation of neuron apoptosis	PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966	P	Seeded From UniProt
	GO:0043524	negative regulation of neuron apoptosis	PMID:7753802^[22]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043524	negative regulation of neuron apoptosis	PMID:8625820^[23]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043524	negative regulation of neuron apoptosis	PMID:9096145^[24]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	Seeded From UniProt
	GO:0044429	mitochondrial part	PMID:7607090^[14]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0045768	positive regulation of anti-apoptosis	PMID:10652277^[25]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0046898	response to cycloheximide	PMID:9176392^[15]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0046902	regulation of mitochondrial membrane permeability	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	P	Seeded From UniProt
	GO:0046982	protein heterodimerization activity	PMID:7650488^[26]	IPI: Inferred from Physical Interaction	UniProtKB:Q07813	F	Seeded From UniProt
	GO:0046982	protein heterodimerization activity	PMID:7834748^[27]	IPI: Inferred from Physical Interaction	UniProtKB:Q07813	F	Seeded From UniProt
	GO:0046982	protein heterodimerization activity	PMID:7834748^[27]	IPI: Inferred from Physical Interaction	UniProtKB:Q61337	F	Seeded From UniProt
	GO:0046982	protein heterodimerization activity	PMID:8798452^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q07813	F	Seeded From UniProt
	GO:0051434	BH3 domain binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	F	Seeded From UniProt
	GO:0051881	regulation of mitochondrial membrane potential	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	P	Seeded From UniProt
	GO:0060154	cellular process regulating host cell cycle in response to virus	PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966	P	Seeded From UniProt
	GO:0071230	cellular response to amino acid stimulus	PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966	P	Seeded From UniProt
	GO:0071312	cellular response to alkaloid	PMID:15231831^[17]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0071480	cellular response to gamma radiation	PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0071780	mitotic cell cycle G2/M transition checkpoint	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q07817	P	Seeded From UniProt
	GO:0090005	negative regulation of establishment of protein localization in plasma membrane	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	P	Seeded From UniProt
	GO:0097136	Bcl-2 family protein complex	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSP00000365230	C	Seeded From UniProt
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 Rucker EB 3rd et al. (2000) Bcl-x and Bax regulate mouse primordial germ cell survival and apoptosis during embryogenesis. Mol Endocrinol 14: 1038-52 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Roth KA et al. (2000) Epistatic and independent functions of caspase-3 and Bcl-X(L) in developmental programmed cell death. Proc Natl Acad Sci U S A 97: 466-71 PubMed GONUTS page
↑ Walensky LD et al. (2006) A stapled BID BH3 helix directly binds and activates BAX. Mol Cell 24: 199-210 PubMed GONUTS page
↑ Danial NN et al. (2008) Dual role of proapoptotic BAD in insulin secretion and beta cell survival. Nat Med 14: 144-53 PubMed GONUTS page
↑ Deng H et al. (2011) Phosphorylation of Bcl-associated death protein (Bad) by erythropoietin-activated c-Jun N-terminal protein kinase 1 contributes to survival of erythropoietin-dependent cells. Int J Biochem Cell Biol 43: 409-15 PubMed GONUTS page
↑ Dominov JA et al. (2001) Pro- and anti-apoptotic members of the Bcl-2 family in skeletal muscle: a distinct role for Bcl-2 in later stages of myogenesis. Dev Dyn 220: 18-26 PubMed GONUTS page
↑ Danial NN et al. (2003) BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424: 952-6 PubMed GONUTS page
↑ Mootha VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 115: 629-40 PubMed GONUTS page
↑ ^9.0 ^9.1 Putcha GV et al. (2002) Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant mice. J Cell Biol 157: 441-53 PubMed GONUTS page
↑ Ayllón V et al. (2002) The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad. Eur J Immunol 32: 1847-55 PubMed GONUTS page
↑ Dramsi S et al. (2002) Identification of a novel phosphorylation site, Ser-170, as a regulator of bad pro-apoptotic activity. J Biol Chem 277: 6399-405 PubMed GONUTS page
↑ Willis SN et al. (2005) Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev 19: 1294-305 PubMed GONUTS page
↑ ^13.0 ^13.1 Chen M et al. (2007) Regulation of the lifespan in dendritic cell subsets. Mol Immunol 44: 2558-65 PubMed GONUTS page
↑ ^14.0 ^14.1 González-García M et al. (1994) bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria. Development 120: 3033-42 PubMed GONUTS page
↑ ^15.0 ^15.1 Tzung SP et al. (1997) Expression of Bcl-2 family during liver regeneration and identification of Bcl-x as a delayed early response gene. Am J Pathol 150: 1985-95 PubMed GONUTS page
↑ ^16.0 ^16.1 Maclean KH et al. (2003) c-Myc augments gamma irradiation-induced apoptosis by suppressing Bcl-XL. Mol Cell Biol 23: 7256-70 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 ^17.6 Seo SY et al. (2004) BAD is a pro-survival factor prior to activation of its pro-apoptotic function. J Biol Chem 279: 42240-9 PubMed GONUTS page
↑ ^18.0 ^18.1 Heermeier K et al. (1996) Bax and Bcl-xs are induced at the onset of apoptosis in involuting mammary epithelial cells. Mech Dev 56: 197-207 PubMed GONUTS page
↑ ^19.0 ^19.1 Simonian PL et al. (1996) Bax can antagonize Bcl-XL during etoposide and cisplatin-induced cell death independently of its heterodimerization with Bcl-XL. J Biol Chem 271: 22764-72 PubMed GONUTS page
↑ Chen G et al. (1999) Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins. J Biol Chem 274: 7-10 PubMed GONUTS page
↑ ^21.0 ^21.1 Zaidi AU et al. (2001) Bcl-X(L)-caspase-9 interactions in the developing nervous system: evidence for multiple death pathways. J Neurosci 21: 169-75 PubMed GONUTS page
↑ González-García M et al. (1995) bcl-x is expressed in embryonic and postnatal neural tissues and functions to prevent neuronal cell death. Proc Natl Acad Sci U S A 92: 4304-8 PubMed GONUTS page
↑ Middleton G et al. (1996) Bax promotes neuronal survival and antagonises the survival effects of neurotrophic factors. Development 122: 695-701 PubMed GONUTS page
↑ Shindler KS et al. (1997) Bax deficiency prevents the increased cell death of immature neurons in bcl-x-deficient mice. J Neurosci 17: 3112-9 PubMed GONUTS page
↑ Kieslinger M et al. (2000) Antiapoptotic activity of Stat5 required during terminal stages of myeloid differentiation. Genes Dev 14: 232-44 PubMed GONUTS page
↑ Chao DT et al. (1995) Bcl-XL and Bcl-2 repress a common pathway of cell death. J Exp Med 182: 821-8 PubMed GONUTS page
↑ ^27.0 ^27.1 Yang E et al. (1995) Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80: 285-91 PubMed GONUTS page

[PMID:10894153-0] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 Rucker EB 3rd et al. (2000) Bcl-x and Bax regulate mouse primordial germ cell survival and apoptosis during embryogenesis. Mol Endocrinol 14: 1038-52 PubMed GONUTS page

[PMID:10618441-1] 2.0 ^2.1 ^2.2 Roth KA et al. (2000) Epistatic and independent functions of caspase-3 and Bcl-X(L) in developmental programmed cell death. Proc Natl Acad Sci U S A 97: 466-71 PubMed GONUTS page

[PMID:17052454-2] Walensky LD et al. (2006) A stapled BID BH3 helix directly binds and activates BAX. Mol Cell 24: 199-210 PubMed GONUTS page

[PMID:18223655-3] Danial NN et al. (2008) Dual role of proapoptotic BAD in insulin secretion and beta cell survival. Nat Med 14: 144-53 PubMed GONUTS page

[PMID:21095239-4] Deng H et al. (2011) Phosphorylation of Bcl-associated death protein (Bad) by erythropoietin-activated c-Jun N-terminal protein kinase 1 contributes to survival of erythropoietin-dependent cells. Int J Biochem Cell Biol 43: 409-15 PubMed GONUTS page

[PMID:11146504-5] Dominov JA et al. (2001) Pro- and anti-apoptotic members of the Bcl-2 family in skeletal muscle: a distinct role for Bcl-2 in later stages of myogenesis. Dev Dyn 220: 18-26 PubMed GONUTS page

[PMID:12931191-6] Danial NN et al. (2003) BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis. Nature 424: 952-6 PubMed GONUTS page

[PMID:14651853-7] Mootha VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 115: 629-40 PubMed GONUTS page

[PMID:11980919-8] 9.0 ^9.1 Putcha GV et al. (2002) Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant mice. J Cell Biol 157: 441-53 PubMed GONUTS page

[PMID:12115603-9] Ayllón V et al. (2002) The anti-apoptotic molecules Bcl-xL and Bcl-w target protein phosphatase 1alpha to Bad. Eur J Immunol 32: 1847-55 PubMed GONUTS page

[PMID:11717309-10] Dramsi S et al. (2002) Identification of a novel phosphorylation site, Ser-170, as a regulator of bad pro-apoptotic activity. J Biol Chem 277: 6399-405 PubMed GONUTS page

[PMID:15901672-11] Willis SN et al. (2005) Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev 19: 1294-305 PubMed GONUTS page

[PMID:17267035-12] 13.0 ^13.1 Chen M et al. (2007) Regulation of the lifespan in dendritic cell subsets. Mol Immunol 44: 2558-65 PubMed GONUTS page

[PMID:7607090-13] 14.0 ^14.1 González-García M et al. (1994) bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria. Development 120: 3033-42 PubMed GONUTS page

[PMID:9176392-14] 15.0 ^15.1 Tzung SP et al. (1997) Expression of Bcl-2 family during liver regeneration and identification of Bcl-x as a delayed early response gene. Am J Pathol 150: 1985-95 PubMed GONUTS page

[PMID:14517295-15] 16.0 ^16.1 Maclean KH et al. (2003) c-Myc augments gamma irradiation-induced apoptosis by suppressing Bcl-XL. Mol Cell Biol 23: 7256-70 PubMed GONUTS page

[PMID:15231831-16] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 ^17.6 Seo SY et al. (2004) BAD is a pro-survival factor prior to activation of its pro-apoptotic function. J Biol Chem 279: 42240-9 PubMed GONUTS page

[PMID:8798158-17] 18.0 ^18.1 Heermeier K et al. (1996) Bax and Bcl-xs are induced at the onset of apoptosis in involuting mammary epithelial cells. Mech Dev 56: 197-207 PubMed GONUTS page

[PMID:8798452-18] 19.0 ^19.1 Simonian PL et al. (1996) Bax can antagonize Bcl-XL during etoposide and cisplatin-induced cell death independently of its heterodimerization with Bcl-XL. J Biol Chem 271: 22764-72 PubMed GONUTS page

[PMID:9867803-19] Chen G et al. (1999) Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins. J Biol Chem 274: 7-10 PubMed GONUTS page

[PMID:11150333-20] 21.0 ^21.1 Zaidi AU et al. (2001) Bcl-X(L)-caspase-9 interactions in the developing nervous system: evidence for multiple death pathways. J Neurosci 21: 169-75 PubMed GONUTS page

[PMID:7753802-21] González-García M et al. (1995) bcl-x is expressed in embryonic and postnatal neural tissues and functions to prevent neuronal cell death. Proc Natl Acad Sci U S A 92: 4304-8 PubMed GONUTS page

[PMID:8625820-22] Middleton G et al. (1996) Bax promotes neuronal survival and antagonises the survival effects of neurotrophic factors. Development 122: 695-701 PubMed GONUTS page

[PMID:9096145-23] Shindler KS et al. (1997) Bax deficiency prevents the increased cell death of immature neurons in bcl-x-deficient mice. J Neurosci 17: 3112-9 PubMed GONUTS page

[PMID:10652277-24] Kieslinger M et al. (2000) Antiapoptotic activity of Stat5 required during terminal stages of myeloid differentiation. Genes Dev 14: 232-44 PubMed GONUTS page

[PMID:7650488-25] Chao DT et al. (1995) Bcl-XL and Bcl-2 repress a common pathway of cell death. J Exp Med 182: 821-8 PubMed GONUTS page

[PMID:7834748-26] 27.0 ^27.1 Yang E et al. (1995) Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 80: 285-91 PubMed GONUTS page

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MOUSE:B2CL1

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