MGI:Bcl2l1

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Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000910	cytokinesis	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0001541	ovarian follicle development	MGI:MGI:1860555 PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	From MGI
	GO:0001541	ovarian follicle development	MGI:MGI:1860555 PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	From MGI
	GO:0001541	ovarian follicle development	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	P	From MGI
	GO:0001701	in utero embryonic development	MGI:MGI:1351384 PMID:10618441^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2158303	P	From MGI
	GO:0001836	release of cytochrome c from mitochondria	MGI:MGI:3688960 PMID:17052454^[3]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	From MGI
	GO:0001836	release of cytochrome c from mitochondria	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0005515	protein binding	MGI:MGI:3778846 PMID:18223655^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q61337	F	From MGI
	GO:0005515	protein binding	MGI:MGI:5009772 PMID:21095239^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q61337	F	From MGI
	GO:0005622	intracellular	MGI:MGI:1928555 PMID:11146504^[6]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005737	cytoplasm	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:2671672 PMID:12931191^[7]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:2682130 PMID:14651853^[8]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	C	From MGI
	GO:0005740	mitochondrial envelope	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	C	From MGI
	GO:0005741	mitochondrial outer membrane	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	C	From MGI
	GO:0005813	centrosome	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	C	From MGI
	GO:0005829	cytosol	MGI:MGI:2178871 PMID:11980919^[9]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005856	cytoskeleton	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0206	C	From MGI
	GO:0006915	apoptotic process	MGI:MGI:1351384 PMID:10618441^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:107739	P	From MGI
	GO:0006915	apoptotic process	MGI:MGI:2183839 PMID:12115603^[10]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006916	anti-apoptosis	MGI:MGI:2158953 PMID:11717309^[11]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006916	anti-apoptosis	MGI:MGI:3689797 PMID:15901672^[12]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0006916	anti-apoptosis	MGI:MGI:3700106 PMID:17267035^[13]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006916	anti-apoptosis	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	P	From MGI
	GO:0006916	anti-apoptosis	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0006916	anti-apoptosis	MGI:MGI:69011 PMID:7607090^[14]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0007281	germ cell development	MGI:MGI:1860555 PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	From MGI
	GO:0007281	germ cell development	MGI:MGI:1860555 PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	From MGI
	GO:0007283	spermatogenesis	MGI:MGI:1860555 PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	From MGI
	GO:0008283	cell proliferation	MGI:MGI:892190 PMID:9176392^[15]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0008284	positive regulation of cell proliferation	MGI:MGI:3700106 PMID:17267035^[13]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0008584	male gonad development	MGI:MGI:1860555 PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	From MGI
	GO:0009314	response to radiation	MGI:MGI:2677658 PMID:14517295^[16]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0009566	fertilization	MGI:MGI:1860555 PMID:10894153^[1]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	From MGI
	GO:0009615	response to virus	MGI:MGI:3057092 PMID:15231831^[17]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0016020	membrane	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0472	C	From MGI
	GO:0016020	membrane	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR004725	C	From MGI
	GO:0016021	integral to membrane	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0812	C	From MGI
	GO:0019901	protein kinase binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	F	From MGI
	GO:0031966	mitochondrial membrane	MGI:MGI:2178871 PMID:11980919^[9]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0034097	response to cytokine stimulus	MGI:MGI:892164 PMID:9184696^[18]	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0040007	growth	MGI:MGI:1860555 PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	From MGI
	GO:0042802	identical protein binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	F	From MGI
	GO:0042981	regulation of apoptotic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	P	From MGI
	GO:0043027	cysteine-type endopeptidase inhibitor activity involved in apoptotic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	F	From MGI
	GO:0043065	positive regulation of apoptotic process	MGI:MGI:81233 PMID:8798158^[19]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:1326944 PMID:9867803^[20]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:1351384 PMID:10618441^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2158303	P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:1860555 PMID:10894153^[1]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2176699	P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:2677658 PMID:14517295^[16]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:3057092 PMID:15231831^[17]	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:75819 PMID:7650367^[21]	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:81233 PMID:8798158^[19]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043066	negative regulation of apoptotic process	MGI:MGI:82784 PMID:8798452^[22]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	From MGI
	GO:0043154	negative regulation of cysteine-type endopeptidase activity involved in apoptotic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	P	From MGI
	GO:0043524	negative regulation of neuron apoptotic process	MGI:MGI:1929535 PMID:11150333^[23]	IGI: Inferred from Genetic Interaction	MGI:MGI:1277950	P	From MGI
	GO:0043524	negative regulation of neuron apoptotic process	MGI:MGI:1929535 PMID:11150333^[23]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2158303	P	From MGI
	GO:0043524	negative regulation of neuron apoptotic process	MGI:MGI:3057092 PMID:15231831^[17]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043524	negative regulation of neuron apoptotic process	MGI:MGI:3057092 PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966	P	From MGI
	GO:0043524	negative regulation of neuron apoptotic process	MGI:MGI:72933 PMID:7753802^[24]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043524	negative regulation of neuron apoptotic process	MGI:MGI:79659 PMID:8625820^[25]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043524	negative regulation of neuron apoptotic process	MGI:MGI:86927 PMID:9096145^[26]	IGI: Inferred from Genetic Interaction	MGI:MGI:99702	P	From MGI
	GO:0044429	mitochondrial part	MGI:MGI:69011 PMID:7607090^[14]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0045768	positive regulation of anti-apoptosis	MGI:MGI:3577955 PMID:10652277^[27]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0046898	response to cycloheximide	MGI:MGI:892190 PMID:9176392^[15]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0046902	regulation of mitochondrial membrane permeability	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0046982	protein heterodimerization activity	MGI:MGI:1095590 PMID:7834748^[28]	IPI: Inferred from Physical Interaction	UniProtKB:Q61337 UniProtKB:Q07813	F	From MGI
	GO:0046982	protein heterodimerization activity	MGI:MGI:2385423 PMID:7650488^[29]	IPI: Inferred from Physical Interaction	UniProtKB:Q07813	F	From MGI
	GO:0046982	protein heterodimerization activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	F	From MGI
	GO:0046982	protein heterodimerization activity	MGI:MGI:82784 PMID:8798452^[22]	IPI: Inferred from Physical Interaction	UniProtKB:Q07813	F	From MGI
	GO:0051400	BH domain binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	F	From MGI
	GO:0051434	BH3 domain binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	F	From MGI
	GO:0051881	regulation of mitochondrial membrane potential	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0060154	cellular process regulating host cell cycle in response to virus	MGI:MGI:3057092 PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966	P	From MGI
	GO:0070215	MDM2 binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P53563	F	From MGI
	GO:0071230	cellular response to amino acid stimulus	MGI:MGI:3057092 PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966	P	From MGI
	GO:0071312	cellular response to alkaloid	MGI:MGI:3057092 PMID:15231831^[17]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0071480	cellular response to gamma radiation	MGI:MGI:3057092 PMID:15231831^[17]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0071780	mitotic cell cycle G2/M transition checkpoint	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0090005	negative regulation of establishment of protein localization in plasma membrane	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0090201	negative regulation of release of cytochrome c from mitochondria	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
	GO:0097136	Bcl-2 family protein complex	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	C	From MGI
	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q07817	P	From MGI
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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 ^17.7 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
↑ Li L et al. (1997) The apoptosis and proliferation of SAC-activated B cells by IL-10 are associated with changes in Bcl-2, Bcl-xL, and Mcl-1 expression. Cell Immunol 178: 33-41 PubMed GONUTS page
↑ ^19.0 ^19.1 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
↑ 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
↑ Broome HE et al. (1995) Expression of Bcl-2, Bcl-x, and Bax after T cell activation and IL-2 withdrawal. J Immunol 155: 2311-7 PubMed GONUTS page
↑ ^22.0 ^22.1 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
↑ ^23.0 ^23.1 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
↑ 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
↑ 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: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 ^17.7 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:9184696-17] Li L et al. (1997) The apoptosis and proliferation of SAC-activated B cells by IL-10 are associated with changes in Bcl-2, Bcl-xL, and Mcl-1 expression. Cell Immunol 178: 33-41 PubMed GONUTS page

[PMID:8798158-18] 19.0 ^19.1 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: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:7650367-20] Broome HE et al. (1995) Expression of Bcl-2, Bcl-x, and Bax after T cell activation and IL-2 withdrawal. J Immunol 155: 2311-7 PubMed GONUTS page

[PMID:8798452-21] 22.0 ^22.1 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:11150333-22] 23.0 ^23.1 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:7753802-23] 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:8625820-24] 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:9096145-25] 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:10652277-26] 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:7834748-27] 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:7650488-28] 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

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Species (Taxon ID)	Mus musculus (house mouse) (taxon:10090)
Gene Name(s)	Bcl2l1 ( synonyms: Bcl(X)L, bcl-x, Bcl-XL, Bcl-Xs, BclX )
Protein Name(s)	BCL2-like 1,
External Links
MGI	MGI:88139

MGI:Bcl2l1

Contents

Annotations

Notes

References

a

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