BAD_MOUSE
ID BAD_MOUSE Reviewed; 204 AA.
AC Q61337;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Bcl2-associated agonist of cell death;
DE Short=BAD;
DE AltName: Full=Bcl-2-binding component 6;
DE AltName: Full=Bcl-xL/Bcl-2-associated death promoter;
DE AltName: Full=Bcl2 antagonist of cell death;
GN Name=Bad; Synonyms=Bbc6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain, and Thymus;
RX PubMed=7834748; DOI=10.1016/0092-8674(95)90411-5;
RA Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., Korsmeyer S.J.;
RT "Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and
RT promotes cell death.";
RL Cell 80:285-291(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION AT SER-112 AND SER-136, AND MUTAGENESIS OF SER-112 AND
RP SER-136.
RX PubMed=9381178; DOI=10.1126/science.278.5338.687;
RA Del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G.;
RT "Interleukin-3-induced phosphorylation of BAD through the protein kinase
RT Akt.";
RL Science 278:687-689(1997).
RN [4]
RP PHOSPHORYLATION AT SER-112 AND SER-136.
RX PubMed=10679322; DOI=10.1016/s0960-9822(00)00310-9;
RA Shimamura A., Ballif B.A., Richards S.A., Blenis J.;
RT "Rsk1 mediates a MEK-MAP kinase cell survival signal.";
RL Curr. Biol. 10:127-135(2000).
RN [5]
RP MUTAGENESIS OF SERINE RESIDUES.
RX PubMed=10949026; DOI=10.1016/s1097-2765(05)00012-2;
RA Datta S.R., Katsov A., Hu L., Petros A., Fesik S.W., Yaffe M.B.,
RA Greenberg M.E.;
RT "14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3
RT domain phosphorylation.";
RL Mol. Cell 6:41-51(2000).
RN [6]
RP PHOSPHORYLATION AT SER-112 AND SER-136.
RX PubMed=10611223; DOI=10.1128/mcb.20.2.453-461.2000;
RA Schurmann A., Mooney A.F., Sanders L.C., Sells M.A., Wang H.G., Reed J.C.,
RA Bokoch G.M.;
RT "p21-activated kinase 1 phosphorylates the death agonist bad and protects
RT cells from apoptosis.";
RL Mol. Cell. Biol. 20:453-461(2000).
RN [7]
RP PHOSPHORYLATION AT SER-112.
RX PubMed=11278362; DOI=10.1074/jbc.m007753200;
RA Jakobi R., Moertl E., Koeppel M.A.;
RT "p21-activated protein kinase gamma-PAK suppresses programmed cell death of
RT BALB3T3 fibroblasts.";
RL J. Biol. Chem. 276:16624-16634(2001).
RN [8]
RP PHOSPHORYLATION AT SER-136.
RX PubMed=11342610; DOI=10.4049/jimmunol.166.10.5955;
RA Villalba M., Bushway P., Altman A.;
RT "Protein kinase C-theta mediates a selective T cell survival signal via
RT phosphorylation of BAD.";
RL J. Immunol. 166:5955-5963(2001).
RN [9]
RP PHOSPHORYLATION AT SER-136.
RX PubMed=11493700; DOI=10.1073/pnas.171301998;
RA Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.;
RT "p70S6 kinase signals cell survival as well as growth, inactivating the
RT pro-apoptotic molecule BAD.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001).
RN [10]
RP PHOSPHORYLATION AT SER-155 AND SER-170, MUTAGENESIS OF SER-112; SER-155 AND
RP SER-170, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11717309; DOI=10.1074/jbc.m109990200;
RA Dramsi S., Scheid M.P., Maiti A., Hojabrpour P., Chen X., Schubert K.,
RA Goodlett D.R., Aebersold R., Duronio V.;
RT "Identification of a novel phosphorylation site, Ser-170, as a regulator of
RT bad pro-apoptotic activity.";
RL J. Biol. Chem. 277:6399-6405(2002).
RN [11]
RP PHOSPHORYLATION AT SER-112 BY PIM2.
RX PubMed=12954615; DOI=10.1074/jbc.m307933200;
RA Yan B., Zemskova M., Holder S., Chin V., Kraft A., Koskinen P.J., Lilly M.;
RT "The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced
RT cell death.";
RL J. Biol. Chem. 278:45358-45367(2003).
RN [12]
RP PHOSPHORYLATION AT SER-112 BY RAF1.
RX PubMed=15849194; DOI=10.1074/jbc.m413374200;
RA Jin S., Zhuo Y., Guo W., Field J.;
RT "p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1 regulates
RT its mitochondrial localization, phosphorylation of BAD, and Bcl-2
RT association.";
RL J. Biol. Chem. 280:24698-24705(2005).
RN [13]
RP INTERACTION WITH GIMAP3 AND GIMAP5.
RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103;
RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T.,
RA Kanno M., Takahama Y.;
RT "IAN family critically regulates survival and development of T
RT lymphocytes.";
RL PLoS Biol. 4:593-605(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136; SER-155 AND SER-170, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP INTERACTION WITH HIF3A, AND SUBCELLULAR LOCATION.
RX PubMed=21546903; DOI=10.1038/cdd.2011.47;
RA Torii S., Goto Y., Ishizawa T., Hoshi H., Goryo K., Yasumoto K.,
RA Fukumura H., Sogawa K.;
RT "Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a negative
RT regulator of HIF-1, through binding to pro-survival Bcl-2 family
RT proteins.";
RL Cell Death Differ. 18:1711-1725(2011).
CC -!- FUNCTION: Promotes cell death. Successfully competes for the binding to
CC Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of
CC heterodimerization of these proteins with BAX. Can reverse the death
CC repressor activity of Bcl-X(L), but not that of Bcl-2. Appears to act
CC as a link between growth factor receptor signaling and the apoptotic
CC pathways.
CC -!- SUBUNIT: Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L),
CC Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity). The Ser-
CC 112/Ser-136 phosphorylated form binds 14-3-3 proteins. Interacts with
CC AKT1 and PIM3 (By similarity). Interacts (via BH3 domain) with NOL3
CC (via CARD domain); preventing the association of BAD with BCL2 (By
CC similarity). Interacts with HIF3A isoform 2 (via C-terminus domain);
CC the interaction reduces the binding between BAD and BAX
CC (PubMed:21546903). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5
CC (PubMed:16509771). {ECO:0000250|UniProtKB:O35147,
CC ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:21546903}.
CC -!- INTERACTION:
CC Q61337; Q64373-1: Bcl2l1; NbExp=2; IntAct=EBI-400328, EBI-526380;
CC Q61337; P10415: BCL2; Xeno; NbExp=6; IntAct=EBI-400328, EBI-77694;
CC Q61337; Q07817-1: BCL2L1; Xeno; NbExp=3; IntAct=EBI-400328, EBI-287195;
CC Q61337; P63104: YWHAZ; Xeno; NbExp=3; IntAct=EBI-400328, EBI-347088;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm
CC {ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform 2 in
CC the cytoplasm (PubMed:21546903). Upon phosphorylation, locates to the
CC cytoplasm. {ECO:0000269|PubMed:21546903}.
CC -!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for
CC their pro-apoptotic activity and for their interaction with anti-
CC apoptotic members of the Bcl-2 family.
CC -!- PTM: Phosphorylated on one or more of Ser-112, Ser-136, Ser-155 and
CC Ser-170 in response to survival stimuli, which blocks its pro-apoptotic
CC activity. Phosphorylation on Ser-136 or Ser-112 promotes
CC heterodimerization with 14-3-3 proteins. This interaction then
CC facilitates the phosphorylation at Ser-155, a site within the BH3
CC motif, leading to the release of Bcl-X(L) and the promotion of cell
CC survival. Ser-136 is the major site of AKT/PKB phosphorylation, Ser-155
CC the major site of protein kinase A (CAPK) phosphorylation.
CC {ECO:0000269|PubMed:10611223, ECO:0000269|PubMed:10679322,
CC ECO:0000269|PubMed:11278362, ECO:0000269|PubMed:11342610,
CC ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:11717309,
CC ECO:0000269|PubMed:12954615, ECO:0000269|PubMed:15849194,
CC ECO:0000269|PubMed:9381178}.
CC -!- PTM: Methylation at Arg-131 and Arg-133 by PRMT1 inhibits Akt-mediated
CC phosphorylation at Ser-136. {ECO:0000269|PubMed:10611223,
CC ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11342610,
CC ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:9381178}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
CC -!- CAUTION: The protein name 'Bcl2 antagonist of cell death' may be
CC misleading. The protein antagonises Bcl2-mediated repression of cell
CC death, hence it promotes apoptosis. {ECO:0000305}.
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DR EMBL; L37296; AAA64465.1; -; mRNA.
DR EMBL; BC006762; AAH06762.1; -; mRNA.
DR CCDS; CCDS29513.1; -.
DR PIR; A55671; A55671.
DR RefSeq; NP_031548.1; NM_007522.3.
DR PDB; 2BZW; X-ray; 2.30 A; B=137-163.
DR PDBsum; 2BZW; -.
DR AlphaFoldDB; Q61337; -.
DR SMR; Q61337; -.
DR BioGRID; 198296; 11.
DR ComplexPortal; CPX-2019; BAD:BCL-2 complex.
DR ComplexPortal; CPX-2021; BAD:BCL-XL complex.
DR CORUM; Q61337; -.
DR DIP; DIP-273N; -.
DR ELM; Q61337; -.
DR IntAct; Q61337; 14.
DR MINT; Q61337; -.
DR STRING; 10090.ENSMUSP00000025910; -.
DR BindingDB; Q61337; -.
DR ChEMBL; CHEMBL5385; -.
DR iPTMnet; Q61337; -.
DR PhosphoSitePlus; Q61337; -.
DR EPD; Q61337; -.
DR jPOST; Q61337; -.
DR MaxQB; Q61337; -.
DR PaxDb; Q61337; -.
DR PRIDE; Q61337; -.
DR ProteomicsDB; 273648; -.
DR Antibodypedia; 3776; 3220 antibodies from 49 providers.
DR DNASU; 12015; -.
DR Ensembl; ENSMUST00000025910; ENSMUSP00000025910; ENSMUSG00000024959.
DR GeneID; 12015; -.
DR KEGG; mmu:12015; -.
DR UCSC; uc008gjn.2; mouse.
DR CTD; 572; -.
DR MGI; MGI:1096330; Bad.
DR VEuPathDB; HostDB:ENSMUSG00000024959; -.
DR eggNOG; ENOG502S71H; Eukaryota.
DR GeneTree; ENSGT00390000010740; -.
DR InParanoid; Q61337; -.
DR OMA; SSWTRIF; -.
DR OrthoDB; 1454876at2759; -.
DR PhylomeDB; Q61337; -.
DR TreeFam; TF102001; -.
DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR BioGRID-ORCS; 12015; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Bad; mouse.
DR EvolutionaryTrace; Q61337; -.
DR PRO; PR:Q61337; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q61337; protein.
DR Bgee; ENSMUSG00000024959; Expressed in blastocyst and 251 other tissues.
DR ExpressionAtlas; Q61337; baseline and differential.
DR Genevisible; Q61337; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030346; F:protein phosphatase 2B binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0046031; P:ADP metabolic process; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0046034; P:ATP metabolic process; IMP:UniProtKB.
DR GO; GO:0071247; P:cellular response to chromate; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central.
DR GO; GO:0071396; P:cellular response to lipid; IEP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071316; P:cellular response to nicotine; ISS:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
DR GO; GO:0006007; P:glucose catabolic process; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
DR GO; GO:0046931; P:pore complex assembly; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0060139; P:positive regulation of apoptotic process by virus; IDA:MGI.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0033133; P:positive regulation of glucokinase activity; IMP:UniProtKB.
DR GO; GO:1904710; P:positive regulation of granulosa cell apoptotic process; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB.
DR GO; GO:1902220; P:positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IDA:CAFA.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
DR GO; GO:2000078; P:positive regulation of type B pancreatic cell development; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IMP:MGI.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:1901423; P:response to benzene; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0034201; P:response to oleic acid; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:MGI.
DR GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:UniProtKB.
DR DisProt; DP00563; -.
DR InterPro; IPR018868; BAD.
DR PANTHER; PTHR28540; PTHR28540; 1.
DR Pfam; PF10514; Bcl-2_BAD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Membrane; Methylation; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..204
FT /note="Bcl2-associated agonist of cell death"
FT /id="PRO_0000143104"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 147..161
FT /note="BH3"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92934"
FT MOD_RES 112
FT /note="Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2,
FT PAK4, PAK5, RPS6KA1 AND RAF1"
FT /evidence="ECO:0000269|PubMed:10611223,
FT ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11278362,
FT ECO:0000269|PubMed:12954615, ECO:0000269|PubMed:15849194,
FT ECO:0000269|PubMed:9381178"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92934"
FT MOD_RES 131
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q92934"
FT MOD_RES 133
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q92934"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35147"
FT MOD_RES 136
FT /note="Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1
FT and PKC/PRKCQ"
FT /evidence="ECO:0000269|PubMed:10611223,
FT ECO:0000269|PubMed:10679322, ECO:0000269|PubMed:11342610,
FT ECO:0000269|PubMed:11493700, ECO:0000269|PubMed:9381178,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 155
FT /note="Phosphoserine; by PKA and PKB"
FT /evidence="ECO:0000305|PubMed:11717309,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11717309,
FT ECO:0007744|PubMed:21183079"
FT MUTAGEN 112
FT /note="S->A: Enhances pro-apoptotic activity; no
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:11717309,
FT ECO:0000269|PubMed:9381178"
FT MUTAGEN 136
FT /note="S->A: No phosphorylation."
FT /evidence="ECO:0000269|PubMed:9381178"
FT MUTAGEN 155
FT /note="S->A: Enhances pro-apoptotic activity; no
FT phosphorylation; interacts with Bcl-X(L)."
FT /evidence="ECO:0000269|PubMed:11717309"
FT MUTAGEN 155
FT /note="S->D: No pro-apoptotic activity, no interaction with
FT Bcl-X(L)."
FT /evidence="ECO:0000269|PubMed:11717309"
FT MUTAGEN 170
FT /note="S->A: Enhances pro-apoptotic activity."
FT /evidence="ECO:0000269|PubMed:11717309"
FT MUTAGEN 170
FT /note="S->D: No pro-apoptotic activity; even when
FT associated with A-112."
FT /evidence="ECO:0000269|PubMed:11717309"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2BZW"
FT HELIX 142..160
FT /evidence="ECO:0007829|PDB:2BZW"
SQ 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
