Bcl2-associated agonist of cell death

Details

Name
Bcl2-associated agonist of cell death
Synonyms
  • BAD
  • BBC6
  • Bcl-2-binding component 6
  • Bcl-2-like protein 8
  • Bcl-xL/Bcl-2-associated death promoter
  • Bcl2 antagonist of cell death
  • Bcl2-L-8
  • BCL2L8
Gene Name
BAD
Organism
Humans
Amino acid sequence
>lcl|BSEQ0006675|Bcl2-associated agonist of cell death
MFQIPEFEPSEQEDSSSAERGLGPSPAGDGPSGSGKHHRQAPGLLWDASHQQEQPTSSSH
HGGAGAVEIRSRHSSYPAGTEDDEGMGEEPSPFRGRSRSAPPNLWAAQRYGRELRRMSDE
FVDSFKKGLPRPKSAGTATQMRQSSSWTRVFQSWWDRNLGRGSSAPSQ
Number of residues
168
Molecular Weight
18391.765
Theoretical pI
7.19
GO Classification
Functions
cysteine-type endopeptidase activator activity involved in apoptotic process / lipid binding / phospholipid binding / protein kinase binding
Processes
activation of cysteine-type endopeptidase activity / activation of cysteine-type endopeptidase activity involved in apoptotic process / ADP metabolic process / apoptotic process / apoptotic signaling pathway / ATP metabolic process / cellular process regulating host cell cycle in response to virus / cellular response to chromate / cellular response to hypoxia / cellular response to lipid / cellular response to mechanical stimulus / cellular response to nicotine / cytokine-mediated signaling pathway / epidermal growth factor receptor signaling pathway / extrinsic apoptotic signaling pathway / extrinsic apoptotic signaling pathway in absence of ligand / extrinsic apoptotic signaling pathway via death domain receptors / Fc-epsilon receptor signaling pathway / fibroblast growth factor receptor signaling pathway / glucose catabolic process / glucose homeostasis / innate immune response / intrinsic apoptotic signaling pathway / intrinsic apoptotic signaling pathway in response to DNA damage / negative regulation of cytolysis / neurotrophin TRK receptor signaling pathway / phosphatidylinositol-mediated signaling / pore complex assembly / positive regulation of apoptotic process / positive regulation of apoptotic process by virus / positive regulation of autophagy / positive regulation of B cell differentiation / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of epithelial cell proliferation / positive regulation of glucokinase activity / positive regulation of insulin secretion / positive regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of intrinsic apoptotic signaling pathway / positive regulation of mitochondrial membrane potential / positive regulation of neuron death / positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway / positive regulation of proteolysis / positive regulation of release of cytochrome c from mitochondria / positive regulation of T cell differentiation / positive regulation of type B pancreatic cell development / programmed cell death / regulation of mitochondrial membrane permeability / release of cytochrome c from mitochondria / response to amino acid / response to calcium ion / response to drug / response to estradiol / response to ethanol / response to glucocorticoid / response to glucose / response to hydrogen peroxide / response to oleic acid / response to progesterone / response to testosterone / suppression by virus of host apoptotic process / type B pancreatic cell proliferation
Components
cytosol / mitochondrial outer membrane / mitochondrion
General Function
Protein kinase binding
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Mitochondrion outer membrane
Gene sequence
>lcl|BSEQ0021355|Bcl2-associated agonist of cell death (BAD)
ATGTTCCAGATCCCAGAGTTTGAGCCGAGTGAGCAGGAAGACTCCAGCTCTGCAGAGAGG
GGCCTGGGCCCCAGCCCCGCAGGGGACGGGCCCTCAGGCTCCGGCAAGCATCATCGCCAG
GCCCCAGGCCTCCTGTGGGACGCCAGTCACCAGCAGGAGCAGCCAACCAGCAGCAGCCAT
CATGGAGGCGCTGGGGCTGTGGAGATCCGGAGTCGCCACAGCTCCTACCCCGCGGGGACG
GAGGACGACGAAGGGATGGGGGAGGAGCCCAGCCCCTTTCGGGGCCGCTCGCGCTCGGCG
CCCCCCAACCTCTGGGCAGCACAGCGCTATGGCCGCGAGCTCCGGAGGATGAGTGACGAG
TTTGTGGACTCCTTTAAGAAGGGACTTCCTCGCCCGAAGAGCGCGGGCACAGCAACGCAG
ATGCGGCAAAGCTCCAGCTGGACGCGAGTCTTCCAGTCCTGGTGGGATCGGAACTTGGGC
AGGGGAAGCTCCGCCCCCTCCCAGTGA
Chromosome Location
11
Locus
11q13.1
External Identifiers
ResourceLink
UniProtKB IDQ92934
UniProtKB Entry NameBAD_HUMAN
GenBank Gene IDU66879
GenAtlas IDBAD
HGNC IDHGNC:936
General References
  1. Wang HG, Rapp UR, Reed JC: Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell. 1996 Nov 15;87(4):629-38. [Article]
  2. Ottilie S, Diaz JL, Horne W, Chang J, Wang Y, Wilson G, Chang S, Weeks S, Fritz LC, 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. 1997 Dec 5;272(49):30866-72. [Article]
  3. 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [Article]
  4. 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. 2008 Dec;5(12):1011-7. [Article]
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  6. Koh H, Lee KH, Kim D, Kim S, Kim JW, 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. 2000 Nov 3;275(44):34451-8. [Article]
  7. Gnesutta N, Qu J, Minden A: The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis. J Biol Chem. 2001 Apr 27;276(17):14414-9. Epub 2001 Jan 24. [Article]
  8. Cotteret S, Jaffer ZM, Beeser A, Chernoff J: p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD. Mol Cell Biol. 2003 Aug;23(16):5526-39. [Article]
  9. Li YY, Popivanova BK, 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. 2006 Jul 1;66(13):6741-7. [Article]
  10. Popivanova BK, Li YY, 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. 2007 Mar;98(3):321-8. [Article]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [Article]
  13. 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. 2011 Apr 12;108(15):6085-90. doi: 10.1073/pnas.1015328108. Epub 2011 Mar 28. [Article]
  14. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, 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. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
  15. 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. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  16. Petros AM, Nettesheim DG, Wang Y, Olejniczak ET, Meadows RP, Mack J, Swift K, Matayoshi ED, Zhang H, Thompson CB, Fesik SW: Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies. Protein Sci. 2000 Dec;9(12):2528-34. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB12340NavitoclaxinvestigationalunknownDetails