BAD_HUMAN
ID BAD_HUMAN Reviewed; 168 AA.
AC Q92934; O14803; Q6FH21;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Bcl2-associated agonist of cell death;
DE Short=BAD;
DE AltName: Full=Bcl-2-binding component 6;
DE AltName: Full=Bcl-2-like protein 8;
DE Short=Bcl2-L-8;
DE AltName: Full=Bcl-xL/Bcl-2-associated death promoter;
DE AltName: Full=Bcl2 antagonist of cell death;
GN Name=BAD; Synonyms=BBC6, BCL2L8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yin D.X., Li Z., Huang B., Chen S., Zhou H.;
RT "A human protein that interacts with Bcl-2 and have homology to mouse
RT BAD.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION BY RAF-1.
RX PubMed=8929532; DOI=10.1016/s0092-8674(00)81383-5;
RA Wang H.-G., Rapp U.R., Reed J.C.;
RT "Bcl-2 targets the protein kinase Raf-1 to mitochondria.";
RL Cell 87:629-638(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Takayama S., Reed J.C.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DIMERIZATION.
RC TISSUE=Bone marrow;
RX PubMed=9388232; DOI=10.1074/jbc.272.49.30866;
RA Ottilie S., Diaz J.-L., Horne W., Chang J., Wang Y., Wilson G., Chang S.,
RA Weeks S., Fritz L.C., Oltersdorf T.;
RT "Dimerization properties of human BAD. Identification of a BH-3 domain and
RT analysis of its binding to mutant BCL-2 and BCL-XL proteins.";
RL J. Biol. Chem. 272:30866-30872(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [11]
RP INTERACTION WITH AKT1, AND PHOSPHORYLATION AT SER-99.
RX PubMed=10926925; DOI=10.1074/jbc.m001753200;
RA Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.;
RT "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis
RT factor-induced protein kinase C-related kinase 2 (PRK2) cleavage.";
RL J. Biol. Chem. 275:34451-34458(2000).
RN [12]
RP PHOSPHORYLATION AT SER-75.
RX PubMed=11278822; DOI=10.1074/jbc.m011046200;
RA Gnesutta N., Qu J., Minden A.;
RT "The serine/threonine kinase PAK4 prevents caspase activation and protects
RT cells from apoptosis.";
RL J. Biol. Chem. 276:14414-14419(2001).
RN [13]
RP PHOSPHORYLATION AT SER-75.
RX PubMed=12897128; DOI=10.1128/mcb.23.16.5526-5539.2003;
RA Cotteret S., Jaffer Z.M., Beeser A., Chernoff J.;
RT "p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits
RT apoptosis by phosphorylating BAD.";
RL Mol. Cell. Biol. 23:5526-5539(2003).
RN [14]
RP PHOSPHORYLATION AT SER-75.
RX PubMed=16818649; DOI=10.1158/0008-5472.can-05-4272;
RA Li Y.Y., Popivanova B.K., Nagai Y., Ishikura H., Fujii C., Mukaida N.;
RT "Pim-3, a proto-oncogene with serine/threonine kinase activity, is
RT aberrantly expressed in human pancreatic cancer and phosphorylates bad to
RT block bad-mediated apoptosis in human pancreatic cancer cell lines.";
RL Cancer Res. 66:6741-6747(2006).
RN [15]
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 [16]
RP INTERACTION WITH PIM3.
RX PubMed=17270021; DOI=10.1111/j.1349-7006.2007.00390.x;
RA Popivanova B.K., Li Y.Y., Zheng H., Omura K., Fujii C., Tsuneyama K.,
RA Mukaida N.;
RT "Proto-oncogene, Pim-3 with serine/threonine kinase activity, is aberrantly
RT expressed in human colon cancer cells and can prevent Bad-mediated
RT apoptosis.";
RL Cancer Sci. 98:321-328(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-118, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP METHYLATION AT ARG-94 AND ARG-96 BY PRMT1, AND MUTAGENESIS OF ARG-94 AND
RP ARG-96.
RX PubMed=21444773; DOI=10.1073/pnas.1015328108;
RA Sakamaki J., Daitoku H., Ueno K., Hagiwara A., Yamagata K., Fukamizu A.;
RT "Arginine methylation of BCL-2 antagonist of cell death (BAD) counteracts
RT its phosphorylation and inactivation by Akt.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6085-6090(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-75; SER-99 AND
RP SER-118, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-118 AND SER-134, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-161, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [24]
RP STRUCTURE BY NMR OF 103-127.
RX PubMed=11206074; DOI=10.1110/ps.9.12.2528;
RA Petros A.M., Nettesheim D.G., Wang Y., Olejniczak E.T., Meadows R.P.,
RA Mack J., Swift K., Matayoshi E.D., Zhang H., Thompson C.B., Fesik S.W.;
RT "Rationale for Bcl-xL/Bad peptide complex formation from structure,
RT mutagenesis, and biophysical studies.";
RL Protein Sci. 9:2528-2534(2000).
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 (By similarity).
CC Appears to act as a link between growth factor receptor signaling and
CC the apoptotic pathways. {ECO:0000250}.
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 75/Ser-99 phosphorylated form binds 14-3-3 proteins (By similarity).
CC Interacts with AKT1 and PIM3. Interacts (via BH3 domain) with NOL3 (via
CC CARD domain); preventing the association of BAD with BCL2 (By
CC similarity). Interacts with HIF3A (via C-terminus domain); the
CC interaction reduces the binding between BAD and BAX (By similarity).
CC Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 (PubMed:16509771).
CC {ECO:0000250|UniProtKB:O35147, ECO:0000250|UniProtKB:Q61337,
CC ECO:0000269|PubMed:10926925, ECO:0000269|PubMed:16509771,
CC ECO:0000269|PubMed:17270021}.
CC -!- INTERACTION:
CC Q92934; P35609: ACTN2; NbExp=3; IntAct=EBI-700771, EBI-77797;
CC Q92934; P05067: APP; NbExp=3; IntAct=EBI-700771, EBI-77613;
CC Q92934; P10415: BCL2; NbExp=5; IntAct=EBI-700771, EBI-77694;
CC Q92934; Q07817: BCL2L1; NbExp=31; IntAct=EBI-700771, EBI-78035;
CC Q92934; Q07817-1: BCL2L1; NbExp=6; IntAct=EBI-700771, EBI-287195;
CC Q92934; O43521: BCL2L11; NbExp=2; IntAct=EBI-700771, EBI-526406;
CC Q92934; Q92843: BCL2L2; NbExp=7; IntAct=EBI-700771, EBI-707714;
CC Q92934; O60238: BNIP3L; NbExp=2; IntAct=EBI-700771, EBI-849893;
CC Q92934; P07384: CAPN1; NbExp=3; IntAct=EBI-700771, EBI-1542113;
CC Q92934; Q15323: KRT31; NbExp=3; IntAct=EBI-700771, EBI-948001;
CC Q92934; P31947: SFN; NbExp=6; IntAct=EBI-700771, EBI-476295;
CC Q92934; P31946: YWHAB; NbExp=4; IntAct=EBI-700771, EBI-359815;
CC Q92934; P62258: YWHAE; NbExp=4; IntAct=EBI-700771, EBI-356498;
CC Q92934; P61981: YWHAG; NbExp=4; IntAct=EBI-700771, EBI-359832;
CC Q92934; Q04917: YWHAH; NbExp=5; IntAct=EBI-700771, EBI-306940;
CC Q92934; P27348: YWHAQ; NbExp=5; IntAct=EBI-700771, EBI-359854;
CC Q92934; P63104: YWHAZ; NbExp=8; IntAct=EBI-700771, EBI-347088;
CC Q92934; P03495: NS; Xeno; NbExp=2; IntAct=EBI-700771, EBI-2548993;
CC Q92934; P17361: VACWR028; Xeno; NbExp=2; IntAct=EBI-700771, EBI-7115640;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm
CC {ECO:0000250|UniProtKB:Q61337}. Note=Colocalizes with HIF3A in the
CC cytoplasm (By similarity). Upon phosphorylation, locates to the
CC cytoplasm. {ECO:0000250|UniProtKB:Q61337}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
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-75, Ser-99, Ser-118 and Ser-
CC 134 in response to survival stimuli, which blocks its pro-apoptotic
CC activity. Phosphorylation on Ser-99 or Ser-75 promotes
CC heterodimerization with 14-3-3 proteins. This interaction then
CC facilitates the phosphorylation at Ser-118, a site within the BH3
CC motif, leading to the release of Bcl-X(L) and the promotion of cell
CC survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118
CC the major site of protein kinase A (CAPK) phosphorylation.
CC Phosphorylation at Ser-99 by PKB/AKT1 is almost completely blocked by
CC the apoptotic C-terminus cleavage product of PKN2 generated by
CC caspases-3 activity during apoptosis. {ECO:0000269|PubMed:10926925,
CC ECO:0000269|PubMed:11278822, ECO:0000269|PubMed:12897128,
CC ECO:0000269|PubMed:16818649}.
CC -!- PTM: Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated
CC phosphorylation at Ser-99. {ECO:0000269|PubMed:10926925,
CC ECO:0000269|PubMed:21444773}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB36516.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/130/bad-(bcl2-antagonist-of-cell-death)";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Bcl 2-associated death promoter
CC entry;
CC URL="https://en.wikipedia.org/wiki/Bcl-2-associated_death_promoter";
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DR EMBL; U66879; AAB36516.1; ALT_FRAME; mRNA.
DR EMBL; AF021792; AAB72092.1; -; mRNA.
DR EMBL; AF031523; AAB88124.1; -; mRNA.
DR EMBL; AK291863; BAF84552.1; -; mRNA.
DR EMBL; BT006678; AAP35324.1; -; mRNA.
DR EMBL; CR541935; CAG46733.1; -; mRNA.
DR EMBL; CR541959; CAG46757.1; -; mRNA.
DR EMBL; AB451254; BAG70068.1; -; mRNA.
DR EMBL; AB451378; BAG70192.1; -; mRNA.
DR EMBL; CH471076; EAW74235.1; -; Genomic_DNA.
DR EMBL; BC001901; AAH01901.1; -; mRNA.
DR EMBL; BC095431; AAH95431.1; -; mRNA.
DR CCDS; CCDS8065.1; -.
DR RefSeq; NP_004313.1; NM_004322.3.
DR RefSeq; NP_116784.1; NM_032989.2.
DR PDB; 1G5J; NMR; -; B=103-127.
DR PDB; 7Q16; X-ray; 2.36 A; A=71-81.
DR PDBsum; 1G5J; -.
DR PDBsum; 7Q16; -.
DR AlphaFoldDB; Q92934; -.
DR BMRB; Q92934; -.
DR SMR; Q92934; -.
DR BioGRID; 107048; 106.
DR ComplexPortal; CPX-1982; BAD:BCL-2 complex.
DR ComplexPortal; CPX-1983; BAD:BCL-XL complex.
DR DIP; DIP-29184N; -.
DR ELM; Q92934; -.
DR IntAct; Q92934; 89.
DR MINT; Q92934; -.
DR STRING; 9606.ENSP00000378040; -.
DR BindingDB; Q92934; -.
DR ChEMBL; CHEMBL3817; -.
DR DrugBank; DB12340; Navitoclax.
DR iPTMnet; Q92934; -.
DR PhosphoSitePlus; Q92934; -.
DR BioMuta; BAD; -.
DR DMDM; 17371773; -.
DR EPD; Q92934; -.
DR jPOST; Q92934; -.
DR MassIVE; Q92934; -.
DR MaxQB; Q92934; -.
DR PaxDb; Q92934; -.
DR PeptideAtlas; Q92934; -.
DR PRIDE; Q92934; -.
DR ProteomicsDB; 75614; -.
DR Antibodypedia; 3776; 3220 antibodies from 49 providers.
DR CPTC; Q92934; 1 antibody.
DR DNASU; 572; -.
DR Ensembl; ENST00000309032.8; ENSP00000309103.3; ENSG00000002330.14.
DR Ensembl; ENST00000394532.7; ENSP00000378040.3; ENSG00000002330.14.
DR GeneID; 572; -.
DR KEGG; hsa:572; -.
DR MANE-Select; ENST00000309032.8; ENSP00000309103.3; NM_032989.3; NP_116784.1.
DR UCSC; uc001nzc.4; human.
DR CTD; 572; -.
DR DisGeNET; 572; -.
DR GeneCards; BAD; -.
DR HGNC; HGNC:936; BAD.
DR HPA; ENSG00000002330; Low tissue specificity.
DR MIM; 603167; gene.
DR neXtProt; NX_Q92934; -.
DR OpenTargets; ENSG00000002330; -.
DR PharmGKB; PA25236; -.
DR VEuPathDB; HostDB:ENSG00000002330; -.
DR eggNOG; ENOG502S71H; Eukaryota.
DR GeneTree; ENSGT00390000010740; -.
DR HOGENOM; CLU_129052_0_0_1; -.
DR InParanoid; Q92934; -.
DR OMA; SSWTRIF; -.
DR OrthoDB; 1454876at2759; -.
DR PhylomeDB; Q92934; -.
DR TreeFam; TF102001; -.
DR PathwayCommons; Q92934; -.
DR Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-HSA-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR SignaLink; Q92934; -.
DR SIGNOR; Q92934; -.
DR BioGRID-ORCS; 572; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; BAD; human.
DR EvolutionaryTrace; Q92934; -.
DR GeneWiki; Bcl-2-associated_death_promoter; -.
DR GenomeRNAi; 572; -.
DR Pharos; Q92934; Tchem.
DR PRO; PR:Q92934; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q92934; protein.
DR Bgee; ENSG00000002330; Expressed in mucosa of transverse colon and 133 other tissues.
DR ExpressionAtlas; Q92934; baseline and differential.
DR Genevisible; Q92934; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IMP:UniProtKB.
DR GO; GO:0043422; F:protein kinase B binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IBA:GO_Central.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IDA:BHF-UCL.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0046031; P:ADP metabolic process; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
DR GO; GO:0071247; P:cellular response to chromate; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
DR GO; GO:0071396; P:cellular response to lipid; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
DR GO; GO:0071316; P:cellular response to nicotine; IDA:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0006007; P:glucose catabolic process; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0046931; P:pore complex assembly; IDA:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; TAS:UniProtKB.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0033133; P:positive regulation of glucokinase activity; ISS:UniProtKB.
DR GO; GO:1904710; P:positive regulation of granulosa cell apoptotic process; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:1902220; P:positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
DR GO; GO:2000078; P:positive regulation of type B pancreatic cell development; ISS:UniProtKB.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IBA:GO_Central.
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:0044342; P:type B pancreatic cell proliferation; ISS:UniProtKB.
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; Acetylation; Apoptosis; Cytoplasm; Membrane; Methylation;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..168
FT /note="Bcl2-associated agonist of cell death"
FT /id="PRO_0000143103"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 110..124
FT /note="BH3"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 94
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:21444773"
FT MOD_RES 96
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000269|PubMed:21444773"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35147"
FT MOD_RES 99
FT /note="Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1
FT and PKC/PRKCQ"
FT /evidence="ECO:0000250|UniProtKB:Q61337"
FT MOD_RES 99
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000269|PubMed:10926925,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 161
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VARIANT 107
FT /note="A -> S (in dbSNP:rs3729933)"
FT /id="VAR_015380"
FT MUTAGEN 94
FT /note="R->K: Decreased methylation; when associated with K-
FT 96."
FT /evidence="ECO:0000269|PubMed:21444773"
FT MUTAGEN 96
FT /note="R->K: Decreased methylation; when associated with K-
FT 94."
FT /evidence="ECO:0000269|PubMed:21444773"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:1G5J"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1G5J"
SQ SEQUENCE 168 AA; 18392 MW; 69FD8D27DDEE3241 CRC64;
MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH QQEQPTSSSH
HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA PPNLWAAQRY GRELRRMSDE
FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV FQSWWDRNLG RGSSAPSQ
