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BAD (mouse)

Overview BAD a proapoptotic member of the Bcl-2 family. Displaces Bax from binding to Bcl-2 and Bcl-xL, resulting in cell death. Survival factors such as IL-3 can inhibit the apoptotic activity of Bad inducing the phosphorylation of Bad by Akt and p90RSK. 14-3-3 proteins bind phosphorylated Bad, inhibiting its binding to Bcl-2 and Bcl-xL. Phosphorylation by mitochondria-anchored PKA in the BH3 domain can block the dimerization of Bad and Bcl-xL. Note: This description may include information from UniProtKB. Protein type: Apoptosis Cellular Component: mitochondrial outer membrane; membrane; mitochondrion; cytoplasm; cytosol Molecular Function: protein kinase B binding; protein binding; protein heterodimerization activity; phospholipid binding; caspase activator activity; protein phosphatase binding; protein kinase binding; lipid binding; protein phosphatase 2B binding Biological Process: caspase activation; positive regulation of apoptosis; apoptosis; cytokine and chemokine mediated signaling pathway; positive regulation of insulin secretion; ADP metabolic process; positive regulation of caspase activity; regulation of caspase activity; cellular process regulating host cell cycle in response to virus; glucose homeostasis; ATP metabolic process; regulation of apoptosis; cell proliferation; glucose catabolic process; positive regulation of T cell differentiation; induction of apoptosis; positive regulation of B cell differentiation; pore complex biogenesis; regulation of mitochondrial membrane permeability; positive regulation of epithelial cell proliferation; positive regulation of glucokinase activity Reference #:  Q61337 (UniProtKB) Alt. Names/Synonyms: AI325008; BAD; Bbc2; Bbc6; Bcl-2-binding component 6; Bcl-associated death promoter; Bcl-xL/Bcl-2-associated death promoter; Bcl2 antagonist of cell death; BCL2-associated agonist of cell death; OTTMUSP00000017561 Gene Symbols: Bad Molecular weight: 22,080 Da Basal Isoelectric point: 9.15  Predict pI for various phosphorylation states CST Pathways:  Apoptosis  |  ErbB/HER Signaling  |  Inhibition of Apoptosis  |  Insulin Receptor Signaling  |  MAPK/Erk in Growth and Differentiation  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below BAD 2BZW - B=137-163 (mouse) 1G5J - B=103-127 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
apoptosis, altered: S112‑p, S136‑p, S155‑p apoptosis, induced: S128‑p apoptosis, inhibited: S112‑p, S136‑p, S155‑p, S170‑p, T201‑p cell cycle regulation: S170‑p cell growth, altered: S136‑p cell growth, inhibited: S170‑p activation: S112‑p, S136‑p, T201‑p inhibition: S136‑p intracellular localization: S112‑p, S136‑p molecular association, regulation: S112‑p, S128‑p, S136‑p, S155‑p, T201‑p phosphorylation: S136‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			mouse
1	0		S26-p	KSDPGIRsLGSDAGG
0	3		S67	TDRGLGPSLTEDQPG
0	1		G74	SLTEDQPGPyLAPGL
0	3		Y76-p	TEDQPGPyLAPGLLG
0	1		-	gap
1	0		T94-p	HQQGRAAtNsHHGGA
1	0		S96-p	QGRAAtNsHHGGAGA
0	23		S108-p	AGAMETRsRHssyPA
1	69		S111-p	METRsRHssyPAGtE
112	169		S112-p	ETRsRHssyPAGtEE
0	44		Y113-p	TRsRHssyPAGtEED
1	21		T117-p	HssyPAGtEEDEGME
7	24		S128-p	EGMEEELsPFRGRsR
1	17		S134-p	LsPFRGRsRsAPPNL
110	206		S136-p	PFRGRsRsAPPNLWA
0	1		Y147	NLWAAQRYGRELRRM
43	155		S155-p	GRELRRMsDEFEGSF
1	1		S161	MsDEFEGSFKGLPRP
6	8		S170-p	KGLPRPKsAGtATQM
2	0		T173-p	PRPKsAGtATQMRQS
0	1		G182	TQMRQSAGWTRIIQS
0	4		K197	WWDRNLGKGGStPSQ
3	0		T201-p	NLGKGGStPSQ____

	human
-	gap
S25-p	AERGLGPsPAGDGPs
S32-p	sPAGDGPsGsGkHHR
S34-p	AGDGPsGsGkHHRQA
K36-a	DGPsGsGkHHRQAPG
S57	HQQEQPTSSSHHGGA
S59	QEQPTSSSHHGGAGA
S71-p	AGAVEIRsRHssyPA
S74-p	VEIRsRHssyPAGtE
S75-p	EIRsRHssyPAGtED
Y76-p	IRsRHssyPAGtEDD
T80-p	HssyPAGtEDDEGMG
S91-p	EGMGEEPsPFRGRsR
S97-p	PsPFRGRsRsAPPNL
S99-p	PFRGRsRsAPPNLWA
Y110-p	NLWAAQRyGRELRRM
S118-p	GRELRRMsDEFVDsF
S124-p	MsDEFVDsFKKGLPR
S134-p	KGLPRPKsAGtATQM
T137-p	PRPKsAGtATQMRQS
S146-p	TQMRQSSsWTRVFQS
R161-m1	WWDRNLGrGSSAPSQ
A165	NLGrGSSAPSQ____

	rat
S26	KSDPGIRSLGSDAGG
S67	TDRGLGPSLTEDQPG
G74	SLTEDQPGPYLAPGL
Y76	TEDQPGPYLAPGLLG
-	gap
N95	QQPGQAANNSHHGGA
S97	PGQAANNSHHGGAGT
S109	AGTMETRSRHSsYPA
S112	METRSRHSsYPAGtE
S113-p	ETRSRHSsYPAGtEE
Y114	TRSRHSsYPAGtEED
T118-p	HSsYPAGtEEDEGME
S129-p	EGMEEELsPFRGRSR
S135	LsPFRGRSRsAPPNL
S137-p	PFRGRSRsAPPNLWA
Y148	NLWAAQRYGRELRRM
S156-p	GRELRRMsDEFEGSF
S162	MsDEFEGSFKGLPRP
S171	KGLPRPKSAGTATQM
T174	PRPKSAGTATQMRQS
S183	TQMRQSASWTRIIQS
K198	WWDRNLGKGGSTPSQ
T202	NLGKGGSTPSQ____

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