MGI:Bad

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Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0005515	protein binding	MGI:MGI:2675215 PMID:12944463^[1]	IPI: Inferred from Physical Interaction	UniProtKB:P68254	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3689775 PMID:15694340^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P10415 UniProtKB:Q07817-1	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3694305 PMID:16697956^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P10415	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3778846 PMID:18223655^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P52792	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4453294 PMID:19915011^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9CQV8	F	From MGI
	GO:0005515	protein binding	MGI:MGI:5009772 PMID:21095239^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q64373	F	From MGI
	GO:0005543	phospholipid binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	F	From MGI
	GO:0005737	cytoplasm	MGI:MGI:1928555 PMID:11146504^[7]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:2671672 PMID:12931191^[8]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:3852644 PMID:18614015^[9]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:O35147	C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:F5GY71	C	From MGI
	GO:0005741	mitochondrial outer membrane	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	C	From MGI
	GO:0005829	cytosol	MGI:MGI:2178871 PMID:11980919^[10]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005829	cytosol	MGI:MGI:2663315 PMID:12727206^[11]	ISO: Inferred from Sequence Orthology	UniProtKB:A7MCM4	C	From MGI
	GO:0005829	cytosol	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:O35147	C	From MGI
	GO:0005829	cytosol	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	C	From MGI
	GO:0006007	glucose catabolic process	MGI:MGI:2671672 PMID:12931191^[8]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966 MGI:MGI:3029528	P	From MGI
	GO:0006915	apoptotic process	MGI:MGI:2183839 PMID:12115603^[12]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:2158953 PMID:11717309^[13]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:2663315 PMID:12727206^[11]	ISO: Inferred from Sequence Orthology	UniProtKB:A7MCM4	P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:2675215 PMID:12944463^[1]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:3057092 PMID:15231831^[14]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:O35147	P	From MGI
	GO:0006917	induction of apoptosis	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	MGI:MGI:4453294 PMID:19915011^[5]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0008283	cell proliferation	MGI:MGI:892190 PMID:9176392^[15]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0008289	lipid binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	F	From MGI
	GO:0008624	induction of apoptosis by extracellular signals	MGI:MGI:2671672 PMID:12931191^[8]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966 MGI:MGI:3029528	P	From MGI
	GO:0008624	induction of apoptosis by extracellular signals	MGI:MGI:3057092 PMID:15231831^[14]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0008629	induction of apoptosis by intracellular signals	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0008633	activation of pro-apoptotic gene products	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0008656	cysteine-type endopeptidase activator activity involved in apoptotic process	MGI:MGI:4453294 PMID:19915011^[5]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0008656	cysteine-type endopeptidase activator activity involved in apoptotic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	F	From MGI
	GO:0010918	positive regulation of mitochondrial membrane potential	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0016020	membrane	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0472	C	From MGI
	GO:0019221	cytokine-mediated signaling pathway	MGI:MGI:3032484 PMID:14967141^[16]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0019901	protein kinase binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	F	From MGI
	GO:0019903	protein phosphatase binding	MGI:MGI:2675215 PMID:12944463^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q76MZ3	F	From MGI
	GO:0030346	protein phosphatase 2B binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:O35147	F	From MGI
	GO:0032024	positive regulation of insulin secretion	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0033133	positive regulation of glucokinase activity	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0035774	positive regulation of insulin secretion involved in cellular response to glucose stimulus	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0042593	glucose homeostasis	MGI:MGI:2671672 PMID:12931191^[8]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2675966 MGI:MGI:3029528	P	From MGI
	GO:0042593	glucose homeostasis	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0042981	regulation of apoptotic process	MGI:MGI:1095590 PMID:7834748^[17]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0042981	regulation of apoptotic process	MGI:MGI:3029504 PMID:12431371^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:3029528	P	From MGI
	GO:0042981	regulation of apoptotic process	MGI:MGI:3032484 PMID:14967141^[16]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0043065	positive regulation of apoptotic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:O35147	P	From MGI
	GO:0043065	positive regulation of apoptotic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0043065	positive regulation of apoptotic process	MGI:MGI:5009772 PMID:21095239^[6]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0043280	positive regulation of cysteine-type endopeptidase activity involved in apoptotic process	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0043281	regulation of cysteine-type endopeptidase activity involved in apoptotic process	MGI:MGI:3032484 PMID:14967141^[16]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0043422	protein kinase B binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:O35147	F	From MGI
	GO:0044342	type B pancreatic cell proliferation	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0045579	positive regulation of B cell differentiation	MGI:MGI:3029504 PMID:12431371^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:3029528	P	From MGI
	GO:0045582	positive regulation of T cell differentiation	MGI:MGI:3029504 PMID:12431371^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:3029528	P	From MGI
	GO:0046031	ADP metabolic process	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0046034	ATP metabolic process	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0046902	regulation of mitochondrial membrane permeability	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0046931	pore complex assembly	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0046982	protein heterodimerization activity	MGI:MGI:1095590 PMID:7834748^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P10417 UniProtKB:Q64373	F	From MGI
	GO:0050679	positive regulation of epithelial cell proliferation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0060154	cellular process regulating host cell cycle in response to virus	MGI:MGI:3057092 PMID:15231831^[14]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0071310	cellular response to organic substance	MGI:MGI:2663315 PMID:12727206^[11]	ISO: Inferred from Sequence Orthology	UniProtKB:A7MCM4	P	From MGI
	GO:0071316	cellular response to nicotine	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0090200	positive regulation of release of cytochrome c from mitochondria	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:0097191	extrinsic apoptotic signaling pathway	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:Q92934	P	From MGI
	GO:2000078	positive regulation of type B pancreatic cell development	MGI:MGI:3778846 PMID:18223655^[4]	IMP: Inferred from Mutant Phenotype		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 Chiang CW et al. (2003) Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis. Mol Cell Biol 23: 6350-62 PubMed GONUTS page
↑ Chen L et al. (2005) Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Mol Cell 17: 393-403 PubMed GONUTS page
↑ Certo M et al. (2006) Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. Cancer Cell 9: 351-65 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 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
↑ ^5.0 ^5.1 ^5.2 Quoyer J et al. (2010) GLP-1 mediates antiapoptotic effect by phosphorylating Bad through a beta-arrestin 1-mediated ERK1/2 activation in pancreatic beta-cells. J Biol Chem 285: 1989-2002 PubMed GONUTS page
↑ ^6.0 ^6.1 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
↑ ^8.0 ^8.1 ^8.2 ^8.3 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
↑ Pagliarini DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134: 112-23 PubMed GONUTS page
↑ 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
↑ ^11.0 ^11.1 ^11.2 Hsieh YC et al. (2003) Cloning of zebrafish BAD, a BH3-only proapoptotic protein, whose overexpression leads to apoptosis in COS-1 cells and zebrafish embryos. Biochem Biophys Res Commun 304: 667-75 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
↑ ^14.0 ^14.1 ^14.2 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
↑ 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 ^16.2 Yu C et al. (2004) JNK suppresses apoptosis via phosphorylation of the proapoptotic Bcl-2 family protein BAD. Mol Cell 13: 329-40 PubMed GONUTS page
↑ ^17.0 ^17.1 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
↑ ^18.0 ^18.1 ^18.2 Datta SR et al. (2002) Survival factor-mediated BAD phosphorylation raises the mitochondrial threshold for apoptosis. Dev Cell 3: 631-43 PubMed GONUTS page

[PMID:12944463-0] 1.0 ^1.1 ^1.2 Chiang CW et al. (2003) Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosis. Mol Cell Biol 23: 6350-62 PubMed GONUTS page

[PMID:15694340-1] Chen L et al. (2005) Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Mol Cell 17: 393-403 PubMed GONUTS page

[PMID:16697956-2] Certo M et al. (2006) Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. Cancer Cell 9: 351-65 PubMed GONUTS page

[PMID:18223655-3] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 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:19915011-4] 5.0 ^5.1 ^5.2 Quoyer J et al. (2010) GLP-1 mediates antiapoptotic effect by phosphorylating Bad through a beta-arrestin 1-mediated ERK1/2 activation in pancreatic beta-cells. J Biol Chem 285: 1989-2002 PubMed GONUTS page

[PMID:21095239-5] 6.0 ^6.1 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:11146504-6] 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:12931191-7] 8.0 ^8.1 ^8.2 ^8.3 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:18614015-8] Pagliarini DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134: 112-23 PubMed GONUTS page

[PMID:11980919-9] 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:12727206-10] 11.0 ^11.1 ^11.2 Hsieh YC et al. (2003) Cloning of zebrafish BAD, a BH3-only proapoptotic protein, whose overexpression leads to apoptosis in COS-1 cells and zebrafish embryos. Biochem Biophys Res Commun 304: 667-75 PubMed GONUTS page

[PMID:12115603-11] 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:11717309-12] 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:15231831-13] 14.0 ^14.1 ^14.2 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:9176392-14] 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:14967141-15] 16.0 ^16.1 ^16.2 Yu C et al. (2004) JNK suppresses apoptosis via phosphorylation of the proapoptotic Bcl-2 family protein BAD. Mol Cell 13: 329-40 PubMed GONUTS page

[PMID:7834748-16] 17.0 ^17.1 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:12431371-17] 18.0 ^18.1 ^18.2 Datta SR et al. (2002) Survival factor-mediated BAD phosphorylation raises the mitochondrial threshold for apoptosis. Dev Cell 3: 631-43 PubMed GONUTS page

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Species (Taxon ID)	Mus musculus (house mouse) (taxon:10090)
Gene Name(s)	Bad ( synonyms: Bbc2 )
Protein Name(s)	BCL2-associated agonist of cell death,
External Links
MGI	MGI:1096330

MGI:Bad

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