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Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-2-like protein 8) (Bcl2-L-8) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)

 BAD_HUMAN               Reviewed;         168 AA.
Q92934; O14803; Q6FH21;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 3.
22-NOV-2017, entry version 184.
RecName: Full=Bcl2-associated agonist of cell death;
Short=BAD;
AltName: Full=Bcl-2-binding component 6;
AltName: Full=Bcl-2-like protein 8;
Short=Bcl2-L-8;
AltName: Full=Bcl-xL/Bcl-2-associated death promoter;
AltName: Full=Bcl2 antagonist of cell death;
Name=BAD; Synonyms=BBC6, BCL2L8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Yin D.X., Li Z., Huang B., Chen S., Zhou H.;
"A human protein that interacts with Bcl-2 and have homology to mouse
BAD.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION BY RAF-1.
PubMed=8929532; DOI=10.1016/S0092-8674(00)81383-5;
Wang H.-G., Rapp U.R., Reed J.C.;
"Bcl-2 targets the protein kinase Raf-1 to mitochondria.";
Cell 87:629-638(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Takayama S., Reed J.C.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND DIMERIZATION.
TISSUE=Bone marrow;
PubMed=9388232; DOI=10.1074/jbc.272.49.30866;
Ottilie S., Diaz J.-L., Horne W., Chang J., Wang Y., Wilson G.,
Chang S., Weeks S., Fritz L.C., Oltersdorf T.;
"Dimerization properties of human BAD. Identification of a BH-3 domain
and analysis of its binding to mutant BCL-2 and BCL-XL proteins.";
J. Biol. Chem. 272:30866-30872(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[11]
INTERACTION WITH AKT1, AND PHOSPHORYLATION AT SER-99.
PubMed=10926925; DOI=10.1074/jbc.M001753200;
Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.;
"Inhibition of Akt and its anti-apoptotic activities by tumor necrosis
factor-induced protein kinase C-related kinase 2 (PRK2) cleavage.";
J. Biol. Chem. 275:34451-34458(2000).
[12]
PHOSPHORYLATION AT SER-75.
PubMed=11278822; DOI=10.1074/jbc.M011046200;
Gnesutta N., Qu J., Minden A.;
"The serine/threonine kinase PAK4 prevents caspase activation and
protects cells from apoptosis.";
J. Biol. Chem. 276:14414-14419(2001).
[13]
PHOSPHORYLATION AT SER-75.
PubMed=12897128; DOI=10.1128/MCB.23.16.5526-5539.2003;
Cotteret S., Jaffer Z.M., Beeser A., Chernoff J.;
"p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits
apoptosis by phosphorylating BAD.";
Mol. Cell. Biol. 23:5526-5539(2003).
[14]
PHOSPHORYLATION AT SER-75.
PubMed=16818649; DOI=10.1158/0008-5472.CAN-05-4272;
Li Y.Y., Popivanova B.K., Nagai Y., Ishikura H., Fujii C., Mukaida N.;
"Pim-3, a proto-oncogene with serine/threonine kinase activity, is
aberrantly expressed in human pancreatic cancer and phosphorylates bad
to block bad-mediated apoptosis in human pancreatic cancer cell
lines.";
Cancer Res. 66:6741-6747(2006).
[15]
INTERACTION WITH PIM3.
PubMed=17270021; DOI=10.1111/j.1349-7006.2007.00390.x;
Popivanova B.K., Li Y.Y., Zheng H., Omura K., Fujii C., Tsuneyama K.,
Mukaida N.;
"Proto-oncogene, Pim-3 with serine/threonine kinase activity, is
aberrantly expressed in human colon cancer cells and can prevent Bad-
mediated apoptosis.";
Cancer Sci. 98:321-328(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-118, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
METHYLATION AT ARG-94 AND ARG-96 BY PRMT1, AND MUTAGENESIS OF ARG-94
AND ARG-96.
PubMed=21444773; DOI=10.1073/pnas.1015328108;
Sakamaki J., Daitoku H., Ueno K., Hagiwara A., Yamagata K.,
Fukamizu A.;
"Arginine methylation of BCL-2 antagonist of cell death (BAD)
counteracts its phosphorylation and inactivation by Akt.";
Proc. Natl. Acad. Sci. U.S.A. 108:6085-6090(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-75; SER-99 AND
SER-118, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-118 AND SER-134,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-161, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[23]
STRUCTURE BY NMR OF 103-127.
PubMed=11206074; DOI=10.1110/ps.9.12.2528;
Petros A.M., Nettesheim D.G., Wang Y., Olejniczak E.T., Meadows R.P.,
Mack J., Swift K., Matayoshi E.D., Zhang H., Thompson C.B.,
Fesik S.W.;
"Rationale for Bcl-xL/Bad peptide complex formation from structure,
mutagenesis, and biophysical studies.";
Protein Sci. 9:2528-2534(2000).
-!- 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 (By
similarity). Appears to act as a link between growth factor
receptor signaling and the apoptotic pathways. {ECO:0000250}.
-!- SUBUNIT: Forms heterodimers with the anti-apoptotic proteins, Bcl-
X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity).
The Ser-75/Ser-99 phosphorylated form binds 14-3-3 proteins (By
similarity). Interacts with AKT1 and PIM3. Interacts (via BH3
domain) with NOL3 (via CARD domain); preventing the association of
BAD with BCL2 (By similarity). Interacts with HIF3A (via C-
terminus domain); the interaction reduces the binding between BAD
and BAX (By similarity). {ECO:0000250|UniProtKB:O35147,
ECO:0000250|UniProtKB:Q61337, ECO:0000269|PubMed:10926925,
ECO:0000269|PubMed:17270021}.
-!- INTERACTION:
P10415:BCL2; NbExp=5; IntAct=EBI-700771, EBI-77694;
Q07817:BCL2L1; NbExp=9; IntAct=EBI-700771, EBI-78035;
Q07817-1:BCL2L1; NbExp=6; IntAct=EBI-700771, EBI-287195;
O43521:BCL2L11; NbExp=2; IntAct=EBI-700771, EBI-526406;
Q92843:BCL2L2; NbExp=4; IntAct=EBI-700771, EBI-707714;
O60238:BNIP3L; NbExp=2; IntAct=EBI-700771, EBI-849893;
P45983:MAPK8; NbExp=2; IntAct=EBI-700771, EBI-286483;
P03495:NS (xeno); NbExp=2; IntAct=EBI-700771, EBI-2548993;
P04049:RAF1; NbExp=2; IntAct=EBI-700771, EBI-365996;
P31947:SFN; NbExp=4; IntAct=EBI-700771, EBI-476295;
P17361:VACWR028 (xeno); NbExp=2; IntAct=EBI-700771, EBI-7115640;
P63104:YWHAZ; NbExp=5; IntAct=EBI-700771, EBI-347088;
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm
{ECO:0000250|UniProtKB:Q61337}. Note=Colocalizes with HIF3A in the
cytoplasm (By similarity). Upon phosphorylation, locates to the
cytoplasm. {ECO:0000250|UniProtKB:Q61337}.
-!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
-!- 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-75, Ser-99, Ser-118 and
Ser-134 in response to survival stimuli, which blocks its pro-
apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes
heterodimerization with 14-3-3 proteins. This interaction then
facilitates the phosphorylation at Ser-118, a site within the BH3
motif, leading to the release of Bcl-X(L) and the promotion of
cell survival. Ser-99 is the major site of AKT/PKB
phosphorylation, Ser-118 the major site of protein kinase A (CAPK)
phosphorylation. Phosphorylation at Ser-99 by PKB/AKT1 is almost
completely blocked by the apoptotic C-terminus cleavage product of
PKN2 generated by caspases-3 activity during apoptosis.
{ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:11278822,
ECO:0000269|PubMed:12897128, ECO:0000269|PubMed:16818649}.
-!- PTM: Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-
mediated phosphorylation at Ser-99. {ECO:0000269|PubMed:10926925,
ECO:0000269|PubMed:21444773}.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAB36516.1; Type=Frameshift; Positions=64, 91; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BADID130ch11q13.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Bcl 2-associated death promoter
entry;
URL="https://en.wikipedia.org/wiki/Bcl-2-associated_death_promoter";
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EMBL; U66879; AAB36516.1; ALT_FRAME; mRNA.
EMBL; AF021792; AAB72092.1; -; mRNA.
EMBL; AF031523; AAB88124.1; -; mRNA.
EMBL; AK291863; BAF84552.1; -; mRNA.
EMBL; BT006678; AAP35324.1; -; mRNA.
EMBL; CR541935; CAG46733.1; -; mRNA.
EMBL; CR541959; CAG46757.1; -; mRNA.
EMBL; AB451254; BAG70068.1; -; mRNA.
EMBL; AB451378; BAG70192.1; -; mRNA.
EMBL; CH471076; EAW74235.1; -; Genomic_DNA.
EMBL; BC001901; AAH01901.1; -; mRNA.
EMBL; BC095431; AAH95431.1; -; mRNA.
CCDS; CCDS8065.1; -.
RefSeq; NP_004313.1; NM_004322.3.
RefSeq; NP_116784.1; NM_032989.2.
UniGene; Hs.370254; -.
PDB; 1G5J; NMR; -; B=103-127.
PDBsum; 1G5J; -.
ProteinModelPortal; Q92934; -.
SMR; Q92934; -.
BioGrid; 107048; 45.
DIP; DIP-29184N; -.
ELM; Q92934; -.
IntAct; Q92934; 39.
MINT; MINT-216253; -.
STRING; 9606.ENSP00000309103; -.
BindingDB; Q92934; -.
ChEMBL; CHEMBL3817; -.
DrugBank; DB05764; ABT-263.
iPTMnet; Q92934; -.
PhosphoSitePlus; Q92934; -.
BioMuta; BAD; -.
DMDM; 17371773; -.
EPD; Q92934; -.
MaxQB; Q92934; -.
PaxDb; Q92934; -.
PeptideAtlas; Q92934; -.
PRIDE; Q92934; -.
DNASU; 572; -.
Ensembl; ENST00000309032; ENSP00000309103; ENSG00000002330.
Ensembl; ENST00000394532; ENSP00000378040; ENSG00000002330.
GeneID; 572; -.
KEGG; hsa:572; -.
UCSC; uc001nzc.4; human.
CTD; 572; -.
DisGeNET; 572; -.
EuPathDB; HostDB:ENSG00000002330.13; -.
GeneCards; BAD; -.
HGNC; HGNC:936; BAD.
HPA; CAB004205; -.
HPA; HPA028185; -.
HPA; HPA062105; -.
MIM; 603167; gene.
neXtProt; NX_Q92934; -.
OpenTargets; ENSG00000002330; -.
PharmGKB; PA25236; -.
eggNOG; ENOG410IXUQ; Eukaryota.
eggNOG; ENOG410Y2J3; LUCA.
GeneTree; ENSGT00390000010740; -.
HOGENOM; HOG000095169; -.
HOVERGEN; HBG001653; -.
InParanoid; Q92934; -.
KO; K02158; -.
OMA; IQSWWDR; -.
OrthoDB; EOG091G0Z5T; -.
PhylomeDB; Q92934; -.
TreeFam; TF102001; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
SIGNOR; Q92934; -.
ChiTaRS; BAD; human.
EvolutionaryTrace; Q92934; -.
GeneWiki; Bcl-2-associated_death_promoter; -.
GenomeRNAi; 572; -.
PMAP-CutDB; Q92934; -.
PRO; PR:Q92934; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000002330; -.
CleanEx; HS_BAD; -.
ExpressionAtlas; Q92934; baseline and differential.
Genevisible; Q92934; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; IMP:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0043422; F:protein kinase B binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0046031; P:ADP metabolic process; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IEA:Ensembl.
GO; GO:0071247; P:cellular response to chromate; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
GO; GO:0071396; P:cellular response to lipid; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0071316; P:cellular response to nicotine; IDA:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0006007; P:glucose catabolic process; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0045918; P:negative regulation of cytolysis; IMP:CACAO.
GO; GO:0046931; P:pore complex assembly; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; IEA:Ensembl.
GO; GO:0010508; P:positive regulation of autophagy; TAS:UniProtKB.
GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:UniProtKB.
GO; GO:0033133; P:positive regulation of glucokinase activity; ISS:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; TAS:Reactome.
GO; GO:1902220; P:positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISS:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
GO; GO:2000078; P:positive regulation of type B pancreatic cell development; ISS:UniProtKB.
GO; GO:0001844; P:protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; 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; IEA:Ensembl.
GO; GO:0044342; P:type B pancreatic cell proliferation; ISS:UniProtKB.
InterPro; IPR018868; BAD.
PANTHER; PTHR28540; PTHR28540; 1.
Pfam; PF10514; Bcl-2_BAD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Complete proteome; Cytoplasm;
Membrane; Methylation; Mitochondrion; Mitochondrion outer membrane;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 168 Bcl2-associated agonist of cell death.
/FTId=PRO_0000143103.
MOTIF 110 124 BH3.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 94 94 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:21444773}.
MOD_RES 96 96 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000269|PubMed:21444773}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:O35147}.
MOD_RES 99 99 Phosphoserine; by PKA, PKB, PAK1,
RPS6KA1, RPS6KB1 and PKC/PRKCQ.
{ECO:0000250|UniProtKB:Q61337}.
MOD_RES 99 99 Phosphoserine; by PKB/AKT1.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:10926925}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 161 161 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VARIANT 107 107 A -> S (in dbSNP:rs3729933).
/FTId=VAR_015380.
MUTAGEN 94 94 R->K: Decreased methylation; when
associated with K-96.
{ECO:0000269|PubMed:21444773}.
MUTAGEN 96 96 R->K: Decreased methylation; when
associated with K-94.
{ECO:0000269|PubMed:21444773}.
HELIX 106 121 {ECO:0000244|PDB:1G5J}.
STRAND 123 125 {ECO:0000244|PDB:1G5J}.
SEQUENCE 168 AA; 18392 MW; 69FD8D27DDEE3241 CRC64;
MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH QQEQPTSSSH
HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA PPNLWAAQRY GRELRRMSDE
FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV FQSWWDRNLG RGSSAPSQ


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