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Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)

 BAD_MOUSE               Reviewed;         204 AA.
Q61337;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 157.
RecName: Full=Bcl2-associated agonist of cell death;
Short=BAD;
AltName: Full=Bcl-2-binding component 6;
AltName: Full=Bcl-xL/Bcl-2-associated death promoter;
AltName: Full=Bcl2 antagonist of cell death;
Name=Bad; Synonyms=Bbc6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain, and Thymus;
PubMed=7834748; DOI=10.1016/0092-8674(95)90411-5;
Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., Korsmeyer S.J.;
"Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and
promotes cell death.";
Cell 80:285-291(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[3]
PHOSPHORYLATION AT SER-112 AND SER-136, AND MUTAGENESIS OF SER-112 AND
SER-136.
PubMed=9381178; DOI=10.1126/science.278.5338.687;
Del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G.;
"Interleukin-3-induced phosphorylation of BAD through the protein
kinase Akt.";
Science 278:687-689(1997).
[4]
PHOSPHORYLATION AT SER-112 AND SER-136.
PubMed=10679322; DOI=10.1016/S0960-9822(00)00310-9;
Shimamura A., Ballif B.A., Richards S.A., Blenis J.;
"Rsk1 mediates a MEK-MAP kinase cell survival signal.";
Curr. Biol. 10:127-135(2000).
[5]
MUTAGENESIS OF SERINE RESIDUES.
PubMed=10949026; DOI=10.1016/S1097-2765(05)00012-2;
Datta S.R., Katsov A., Hu L., Petros A., Fesik S.W., Yaffe M.B.,
Greenberg M.E.;
"14-3-3 proteins and survival kinases cooperate to inactivate BAD by
BH3 domain phosphorylation.";
Mol. Cell 6:41-51(2000).
[6]
PHOSPHORYLATION AT SER-112 AND SER-136.
PubMed=10611223; DOI=10.1128/MCB.20.2.453-461.2000;
Schurmann A., Mooney A.F., Sanders L.C., Sells M.A., Wang H.G.,
Reed J.C., Bokoch G.M.;
"p21-activated kinase 1 phosphorylates the death agonist bad and
protects cells from apoptosis.";
Mol. Cell. Biol. 20:453-461(2000).
[7]
PHOSPHORYLATION AT SER-112.
PubMed=11278362; DOI=10.1074/jbc.M007753200;
Jakobi R., Moertl E., Koeppel M.A.;
"p21-activated protein kinase gamma-PAK suppresses programmed cell
death of BALB3T3 fibroblasts.";
J. Biol. Chem. 276:16624-16634(2001).
[8]
PHOSPHORYLATION AT SER-136.
PubMed=11342610; DOI=10.4049/jimmunol.166.10.5955;
Villalba M., Bushway P., Altman A.;
"Protein kinase C-theta mediates a selective T cell survival signal
via phosphorylation of BAD.";
J. Immunol. 166:5955-5963(2001).
[9]
PHOSPHORYLATION AT SER-136.
PubMed=11493700; DOI=10.1073/pnas.171301998;
Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.;
"p70S6 kinase signals cell survival as well as growth, inactivating
the pro-apoptotic molecule BAD.";
Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001).
[10]
PHOSPHORYLATION AT SER-155 AND SER-170, MUTAGENESIS OF SER-112;
SER-155 AND SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11717309; DOI=10.1074/jbc.M109990200;
Dramsi S., Scheid M.P., Maiti A., Hojabrpour P., Chen X., Schubert K.,
Goodlett D.R., Aebersold R., Duronio V.;
"Identification of a novel phosphorylation site, Ser-170, as a
regulator of bad pro-apoptotic activity.";
J. Biol. Chem. 277:6399-6405(2002).
[11]
PHOSPHORYLATION AT SER-112 BY PIM2.
PubMed=12954615; DOI=10.1074/jbc.M307933200;
Yan B., Zemskova M., Holder S., Chin V., Kraft A., Koskinen P.J.,
Lilly M.;
"The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-
induced cell death.";
J. Biol. Chem. 278:45358-45367(2003).
[12]
PHOSPHORYLATION AT SER-112 BY RAF1.
PubMed=15849194; DOI=10.1074/jbc.M413374200;
Jin S., Zhuo Y., Guo W., Field J.;
"p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1
regulates its mitochondrial localization, phosphorylation of BAD, and
Bcl-2 association.";
J. Biol. Chem. 280:24698-24705(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-155 AND
SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
INTERACTION WITH HIF3A, AND SUBCELLULAR LOCATION.
PubMed=21546903; DOI=10.1038/cdd.2011.47;
Torii S., Goto Y., Ishizawa T., Hoshi H., Goryo K., Yasumoto K.,
Fukumura H., Sogawa K.;
"Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a
negative regulator of HIF-1, through binding to pro-survival Bcl-2
family proteins.";
Cell Death Differ. 18:1711-1725(2011).
-!- FUNCTION: Promotes cell death. Successfully competes for the
binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level
of heterodimerization of these proteins with BAX. Can reverse the
death repressor activity of Bcl-X(L), but not that of Bcl-2.
Appears to act as a link between growth factor receptor signaling
and the apoptotic pathways.
-!- SUBUNIT: Forms heterodimers with the anti-apoptotic proteins, Bcl-
X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity).
The Ser-112/Ser-136 phosphorylated form binds 14-3-3 proteins.
Interacts with AKT1 and PIM3 (By similarity). Interacts (via BH3
domain) with NOL3 (via CARD domain); preventing the association of
BAD with BCL2 (By similarity). Interacts with HIF3A isoform 2 (via
C-terminus domain); the interaction reduces the binding between
BAD and BAX (PubMed:21546903). {ECO:0000250|UniProtKB:O35147,
ECO:0000269|PubMed:21546903}.
-!- INTERACTION:
P10415:BCL2 (xeno); NbExp=6; IntAct=EBI-400328, EBI-77694;
Q07817-1:BCL2L1 (xeno); NbExp=3; IntAct=EBI-400328, EBI-287195;
Q64373-1:Bcl2l1; NbExp=2; IntAct=EBI-400328, EBI-526380;
P63104:YWHAZ (xeno); NbExp=3; IntAct=EBI-400328, EBI-347088;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm
{ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform
2 in the cytoplasm (PubMed:21546903). Upon phosphorylation,
locates to the cytoplasm. {ECO:0000269|PubMed:21546903}.
-!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX
for their pro-apoptotic activity and for their interaction with
anti-apoptotic members of the Bcl-2 family.
-!- PTM: Phosphorylated on one or more of Ser-112, Ser-136, Ser-155
and Ser-170 in response to survival stimuli, which blocks its pro-
apoptotic activity. Phosphorylation on Ser-136 or Ser-112 promotes
heterodimerization with 14-3-3 proteins. This interaction then
facilitates the phosphorylation at Ser-155, a site within the BH3
motif, leading to the release of Bcl-X(L) and the promotion of
cell survival. Ser-136 is the major site of AKT/PKB
phosphorylation, Ser-155 the major site of protein kinase A (CAPK)
phosphorylation. {ECO:0000269|PubMed:10611223,
ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11278362,
ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:11493700,
ECO:0000269|PubMed:11717309, ECO:0000269|PubMed:12954615,
ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:9381178}.
-!- PTM: Methylation at Arg-131 and Arg-133 by PRMT1 inhibits Akt-
mediated phosphorylation at Ser-136. {ECO:0000269|PubMed:10611223,
ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11342610,
ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:9381178}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- CAUTION: The protein name 'Bcl2 antagonist of cell death' may be
misleading. The protein antagonises Bcl2-mediated repression of
cell death, hence it promotes apoptosis. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L37296; AAA64465.1; -; mRNA.
EMBL; BC006762; AAH06762.1; -; mRNA.
CCDS; CCDS29513.1; -.
PIR; A55671; A55671.
RefSeq; NP_031548.1; NM_007522.3.
UniGene; Mm.4387; -.
PDB; 2BZW; X-ray; 2.30 A; B=137-163.
PDBsum; 2BZW; -.
DisProt; DP00563; -.
ProteinModelPortal; Q61337; -.
SMR; Q61337; -.
BioGrid; 198296; 7.
ComplexPortal; CPX-2019; BAD:BCL-2 complex.
ComplexPortal; CPX-2021; BAD:BCL-XL complex.
CORUM; Q61337; -.
DIP; DIP-273N; -.
ELM; Q61337; -.
IntAct; Q61337; 16.
MINT; Q61337; -.
STRING; 10090.ENSMUSP00000025910; -.
BindingDB; Q61337; -.
ChEMBL; CHEMBL5385; -.
iPTMnet; Q61337; -.
PhosphoSitePlus; Q61337; -.
EPD; Q61337; -.
MaxQB; Q61337; -.
PaxDb; Q61337; -.
PRIDE; Q61337; -.
DNASU; 12015; -.
Ensembl; ENSMUST00000025910; ENSMUSP00000025910; ENSMUSG00000024959.
GeneID; 12015; -.
KEGG; mmu:12015; -.
UCSC; uc008gjn.2; mouse.
CTD; 572; -.
MGI; MGI:1096330; Bad.
eggNOG; ENOG410IXUQ; Eukaryota.
eggNOG; ENOG410Y2J3; LUCA.
GeneTree; ENSGT00390000010740; -.
HOGENOM; HOG000095169; -.
HOVERGEN; HBG001653; -.
InParanoid; Q61337; -.
KO; K02158; -.
OMA; IQSWWDR; -.
OrthoDB; EOG091G0Z5T; -.
PhylomeDB; Q61337; -.
TreeFam; TF102001; -.
Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
EvolutionaryTrace; Q61337; -.
PMAP-CutDB; Q61337; -.
PRO; PR:Q61337; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024959; Expressed in 265 organ(s), highest expression level in colon.
CleanEx; MM_BAD; -.
ExpressionAtlas; Q61337; baseline and differential.
Genevisible; Q61337; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0030346; F:protein phosphatase 2B binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0046031; P:ADP metabolic process; IMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0046034; P:ATP metabolic process; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IDA:MGI.
GO; GO:0071247; P:cellular response to chromate; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071396; P:cellular response to lipid; IEP:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071316; P:cellular response to nicotine; ISS:UniProtKB.
GO; GO:0071310; P:cellular response to organic substance; ISO:MGI.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
GO; GO:0006007; P:glucose catabolic process; IMP:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:0046931; P:pore complex assembly; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; IDA:MGI.
GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0033133; P:positive regulation of glucokinase activity; IMP:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
GO; GO:1902220; P:positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IDA:CAFA.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
GO; GO:2000078; P:positive regulation of type B pancreatic cell development; IMP:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:MGI.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0034201; P:response to oleic acid; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:MGI.
GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:UniProtKB.
InterPro; IPR018868; BAD.
PANTHER; PTHR28540; PTHR28540; 1.
Pfam; PF10514; Bcl-2_BAD; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Cytoplasm; Membrane;
Methylation; Mitochondrion; Mitochondrion outer membrane;
Phosphoprotein; Reference proteome.
CHAIN 1 204 Bcl2-associated agonist of cell death.
/FTId=PRO_0000143104.
MOTIF 147 161 BH3.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 112 112 Phosphoserine; by PKA, PKB, PIM2, PIM3,
PAK1, PAK2, PAK4, PAK5, RPS6KA1 AND RAF1.
{ECO:0000269|PubMed:10611223,
ECO:0000269|PubMed:10679322,
ECO:0000269|PubMed:11278362,
ECO:0000269|PubMed:12954615,
ECO:0000269|PubMed:15849194,
ECO:0000269|PubMed:9381178}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 131 131 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 133 133 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:O35147}.
MOD_RES 136 136 Phosphoserine; by PKA, PKB, PAK1,
RPS6KA1, RPS6KB1 and PKC/PRKCQ.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10611223,
ECO:0000269|PubMed:10679322,
ECO:0000269|PubMed:11342610,
ECO:0000269|PubMed:11493700,
ECO:0000269|PubMed:9381178}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 155 155 Phosphoserine; by PKA and PKB.
{ECO:0000244|PubMed:21183079,
ECO:0000305|PubMed:11717309}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:11717309}.
MUTAGEN 112 112 S->A: Enhances pro-apoptotic activity; no
phosphorylation.
{ECO:0000269|PubMed:11717309,
ECO:0000269|PubMed:9381178}.
MUTAGEN 136 136 S->A: No phosphorylation.
{ECO:0000269|PubMed:9381178}.
MUTAGEN 155 155 S->A: Enhances pro-apoptotic activity; no
phosphorylation; interacts with Bcl-X(L).
{ECO:0000269|PubMed:11717309}.
MUTAGEN 155 155 S->D: No pro-apoptotic activity, no
interaction with Bcl-X(L).
{ECO:0000269|PubMed:11717309}.
MUTAGEN 170 170 S->A: Enhances pro-apoptotic activity.
{ECO:0000269|PubMed:11717309}.
MUTAGEN 170 170 S->D: No pro-apoptotic activity; even
when associated with A-112.
{ECO:0000269|PubMed:11717309}.
HELIX 139 141 {ECO:0000244|PDB:2BZW}.
HELIX 142 160 {ECO:0000244|PDB:2BZW}.
SEQUENCE 204 AA; 22080 MW; 6C2BA910205053F7 CRC64;
MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE PSEQEDASAT
DRGLGPSLTE DQPGPYLAPG LLGSNIHQQG RAATNSHHGG AGAMETRSRH SSYPAGTEED
EGMEEELSPF RGRSRSAPPN LWAAQRYGRE LRRMSDEFEG SFKGLPRPKS AGTATQMRQS
AGWTRIIQSW WDRNLGKGGS TPSQ


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