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Q92934

- BAD_HUMAN

UniProt

Q92934 - BAD_HUMAN

Protein

Bcl2-associated agonist of cell death

Gene

BAD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
    2. lipid binding Source: UniProtKB
    3. phospholipid binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity Source: BHF-UCL
    2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    3. ADP metabolic process Source: UniProtKB
    4. apoptotic process Source: UniProtKB
    5. apoptotic signaling pathway Source: Reactome
    6. ATP metabolic process Source: UniProtKB
    7. cellular process regulating host cell cycle in response to virus Source: Ensembl
    8. cellular response to chromate Source: Ensembl
    9. cellular response to hypoxia Source: UniProtKB
    10. cellular response to lipid Source: Ensembl
    11. cellular response to mechanical stimulus Source: UniProtKB
    12. cellular response to nicotine Source: UniProtKB
    13. cytokine-mediated signaling pathway Source: Ensembl
    14. epidermal growth factor receptor signaling pathway Source: Reactome
    15. extrinsic apoptotic signaling pathway Source: UniProtKB
    16. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    17. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    18. Fc-epsilon receptor signaling pathway Source: Reactome
    19. fibroblast growth factor receptor signaling pathway Source: Reactome
    20. glucose catabolic process Source: Ensembl
    21. glucose homeostasis Source: UniProtKB
    22. innate immune response Source: Reactome
    23. intrinsic apoptotic signaling pathway Source: UniProtKB
    24. intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    25. neurotrophin TRK receptor signaling pathway Source: Reactome
    26. phosphatidylinositol-mediated signaling Source: Reactome
    27. pore complex assembly Source: UniProtKB
    28. positive regulation of apoptotic process Source: UniProtKB
    29. positive regulation of apoptotic process by virus Source: Ensembl
    30. positive regulation of autophagy Source: UniProtKB
    31. positive regulation of B cell differentiation Source: Ensembl
    32. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    33. positive regulation of epithelial cell proliferation Source: UniProtKB
    34. positive regulation of glucokinase activity Source: UniProtKB
    35. positive regulation of insulin secretion Source: UniProtKB
    36. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
    37. positive regulation of intrinsic apoptotic signaling pathway Source: Reactome
    38. positive regulation of mitochondrial membrane potential Source: UniProtKB
    39. positive regulation of neuron death Source: Ensembl
    40. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    41. positive regulation of proteolysis Source: BHF-UCL
    42. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
    43. positive regulation of T cell differentiation Source: Ensembl
    44. positive regulation of type B pancreatic cell development Source: UniProtKB
    45. regulation of mitochondrial membrane permeability Source: UniProtKB
    46. release of cytochrome c from mitochondria Source: Ensembl
    47. response to amino acid Source: Ensembl
    48. response to calcium ion Source: Ensembl
    49. response to drug Source: Ensembl
    50. response to estradiol Source: Ensembl
    51. response to ethanol Source: Ensembl
    52. response to glucocorticoid Source: Ensembl
    53. response to glucose Source: Ensembl
    54. response to hydrogen peroxide Source: Ensembl
    55. response to oleic acid Source: Ensembl
    56. response to progesterone Source: Ensembl
    57. response to testosterone Source: Ensembl
    58. suppression by virus of host apoptotic process Source: Ensembl
    59. type B pancreatic cell proliferation Source: UniProtKB

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_13638. NRAGE signals death through JNK.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bcl2-associated agonist of cell death
    Short name:
    BAD
    Alternative name(s):
    Bcl-2-binding component 6
    Bcl-2-like protein 8
    Short name:
    Bcl2-L-8
    Bcl-xL/Bcl-2-associated death promoter
    Bcl2 antagonist of cell death
    Gene namesi
    Name:BAD
    Synonyms:BBC6, BCL2L8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:936. BAD.

    Subcellular locationi

    Mitochondrion outer membrane. Cytoplasm
    Note: Upon phosphorylation, locates to the cytoplasm.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. mitochondrial outer membrane Source: UniProtKB
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi94 – 941R → K: Decreased methylation; when associated with K-96. 1 Publication
    Mutagenesisi96 – 961R → K: Decreased methylation; when associated with K-94. 1 Publication

    Organism-specific databases

    PharmGKBiPA25236.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 168168Bcl2-associated agonist of cell deathPRO_0000143103Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei75 – 751Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK7/PAK5, RPS6KA1 and RAF1By similarity
    Modified residuei91 – 911Phosphoserine1 Publication
    Modified residuei94 – 941Asymmetric dimethylarginine; by PRMT11 Publication
    Modified residuei96 – 961Asymmetric dimethylarginine; by PRMT11 Publication
    Modified residuei99 – 991Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ; alternateBy similarity
    Modified residuei99 – 991Phosphoserine; by PKB/AKT1; alternate1 Publication
    Modified residuei118 – 1181Phosphoserine2 Publications
    Modified residuei134 – 1341PhosphoserineBy similarity

    Post-translational modificationi

    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.6 Publications
    Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.2 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92934.
    PaxDbiQ92934.
    PeptideAtlasiQ92934.
    PRIDEiQ92934.

    PTM databases

    PhosphoSiteiQ92934.

    Miscellaneous databases

    PMAP-CutDBQ92934.

    Expressioni

    Tissue specificityi

    Expressed in a wide variety of tissues.

    Gene expression databases

    ArrayExpressiQ92934.
    BgeeiQ92934.
    CleanExiHS_BAD.
    GenevestigatoriQ92934.

    Organism-specific databases

    HPAiCAB004205.
    HPA028185.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2P104155EBI-700771,EBI-77694
    BCL2L1Q078174EBI-700771,EBI-78035
    BCL2L1Q07817-16EBI-700771,EBI-287195
    BCL2L11O435212EBI-700771,EBI-526406
    BNIP3LO602382EBI-700771,EBI-849893
    MAPK8P459832EBI-700771,EBI-286483
    NSP034952EBI-700771,EBI-2548993From a different organism.
    RAF1P040492EBI-700771,EBI-365996
    SFNP319474EBI-700771,EBI-476295
    VACWR028P173612EBI-700771,EBI-7115640From a different organism.
    YWHAZP631045EBI-700771,EBI-347088

    Protein-protein interaction databases

    BioGridi107048. 35 interactions.
    DIPiDIP-29184N.
    IntActiQ92934. 30 interactions.
    MINTiMINT-216253.
    STRINGi9606.ENSP00000309103.

    Structurei

    Secondary structure

    1
    168
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi106 – 12116

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G5JNMR-B103-127[»]
    ProteinModelPortaliQ92934.
    SMRiQ92934. Positions 100-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92934.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi110 – 12415BH3Add
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Belongs to the Bcl-2 family.Curated

    Phylogenomic databases

    eggNOGiNOG43412.
    HOGENOMiHOG000095169.
    HOVERGENiHBG001653.
    InParanoidiQ92934.
    KOiK02158.
    OMAiGEAGHQQ.
    OrthoDBiEOG7MD4RF.
    PhylomeDBiQ92934.
    TreeFamiTF102001.

    Family and domain databases

    InterProiIPR018868. Bcl-2_BAD.
    [Graphical view]
    PfamiPF10514. Bcl-2_BAD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q92934-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH    50
    QQEQPTSSSH HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA 100
    PPNLWAAQRY GRELRRMSDE FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV 150
    FQSWWDRNLG RGSSAPSQ 168
    Length:168
    Mass (Da):18,392
    Last modified:September 26, 2001 - v3
    Checksum:i69FD8D27DDEE3241
    GO

    Sequence cautioni

    The sequence AAB36516.1 differs from that shown. Reason: Frameshift at positions 64 and 91.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071A → S.
    Corresponds to variant rs3729933 [ dbSNP | Ensembl ].
    VAR_015380

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66879 mRNA. Translation: AAB36516.1. Frameshift.
    AF021792 mRNA. Translation: AAB72092.1.
    AF031523 mRNA. Translation: AAB88124.1.
    AK291863 mRNA. Translation: BAF84552.1.
    BT006678 mRNA. Translation: AAP35324.1.
    CR541935 mRNA. Translation: CAG46733.1.
    CR541959 mRNA. Translation: CAG46757.1.
    AB451254 mRNA. Translation: BAG70068.1.
    AB451378 mRNA. Translation: BAG70192.1.
    CH471076 Genomic DNA. Translation: EAW74235.1.
    BC001901 mRNA. Translation: AAH01901.1.
    BC095431 mRNA. Translation: AAH95431.1.
    CCDSiCCDS8065.1.
    RefSeqiNP_004313.1. NM_004322.3.
    NP_116784.1. NM_032989.2.
    UniGeneiHs.370254.

    Genome annotation databases

    EnsembliENST00000309032; ENSP00000309103; ENSG00000002330.
    ENST00000394532; ENSP00000378040; ENSG00000002330.
    GeneIDi572.
    KEGGihsa:572.
    UCSCiuc001nzc.3. human.

    Polymorphism databases

    DMDMi17371773.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    Bcl 2-associated death promoter entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U66879 mRNA. Translation: AAB36516.1 . Frameshift.
    AF021792 mRNA. Translation: AAB72092.1 .
    AF031523 mRNA. Translation: AAB88124.1 .
    AK291863 mRNA. Translation: BAF84552.1 .
    BT006678 mRNA. Translation: AAP35324.1 .
    CR541935 mRNA. Translation: CAG46733.1 .
    CR541959 mRNA. Translation: CAG46757.1 .
    AB451254 mRNA. Translation: BAG70068.1 .
    AB451378 mRNA. Translation: BAG70192.1 .
    CH471076 Genomic DNA. Translation: EAW74235.1 .
    BC001901 mRNA. Translation: AAH01901.1 .
    BC095431 mRNA. Translation: AAH95431.1 .
    CCDSi CCDS8065.1.
    RefSeqi NP_004313.1. NM_004322.3.
    NP_116784.1. NM_032989.2.
    UniGenei Hs.370254.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G5J NMR - B 103-127 [» ]
    ProteinModelPortali Q92934.
    SMRi Q92934. Positions 100-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107048. 35 interactions.
    DIPi DIP-29184N.
    IntActi Q92934. 30 interactions.
    MINTi MINT-216253.
    STRINGi 9606.ENSP00000309103.

    Chemistry

    BindingDBi Q92934.
    ChEMBLi CHEMBL3817.

    PTM databases

    PhosphoSitei Q92934.

    Polymorphism databases

    DMDMi 17371773.

    Proteomic databases

    MaxQBi Q92934.
    PaxDbi Q92934.
    PeptideAtlasi Q92934.
    PRIDEi Q92934.

    Protocols and materials databases

    DNASUi 572.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309032 ; ENSP00000309103 ; ENSG00000002330 .
    ENST00000394532 ; ENSP00000378040 ; ENSG00000002330 .
    GeneIDi 572.
    KEGGi hsa:572.
    UCSCi uc001nzc.3. human.

    Organism-specific databases

    CTDi 572.
    GeneCardsi GC11M064037.
    HGNCi HGNC:936. BAD.
    HPAi CAB004205.
    HPA028185.
    MIMi 603167. gene.
    neXtProti NX_Q92934.
    PharmGKBi PA25236.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43412.
    HOGENOMi HOG000095169.
    HOVERGENi HBG001653.
    InParanoidi Q92934.
    KOi K02158.
    OMAi GEAGHQQ.
    OrthoDBi EOG7MD4RF.
    PhylomeDBi Q92934.
    TreeFami TF102001.

    Enzyme and pathway databases

    Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_13638. NRAGE signals death through JNK.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_330. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

    Miscellaneous databases

    ChiTaRSi BAD. human.
    EvolutionaryTracei Q92934.
    GeneWikii Bcl-2-associated_death_promoter.
    GenomeRNAii 572.
    NextBioi 2331.
    PMAP-CutDB Q92934.
    PROi Q92934.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92934.
    Bgeei Q92934.
    CleanExi HS_BAD.
    Genevestigatori Q92934.

    Family and domain databases

    InterProi IPR018868. Bcl-2_BAD.
    [Graphical view ]
    Pfami PF10514. Bcl-2_BAD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human protein that interacts with Bcl-2 and have homology to mouse BAD."
      Yin D.X., Li Z., Huang B., Chen S., Zhou H.
      Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Bcl-2 targets the protein kinase Raf-1 to mitochondria."
      Wang H.-G., Rapp U.R., Reed J.C.
      Cell 87:629-638(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION BY RAF-1.
    3. Takayama S., Reed J.C.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins."
      Ottilie S., Diaz J.-L., Horne W., Chang J., Wang Y., Wilson G., Chang S., Weeks S., Fritz L.C., Oltersdorf T.
      J. Biol. Chem. 272:30866-30872(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DIMERIZATION.
      Tissue: Bone marrow.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Skeletal muscle.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    8. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      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.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    11. "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage."
      Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.
      J. Biol. Chem. 275:34451-34458(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKT1, PHOSPHORYLATION AT SER-99.
    12. "The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis."
      Gnesutta N., Qu J., Minden A.
      J. Biol. Chem. 276:14414-14419(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-75.
    13. "p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD."
      Cotteret S., Jaffer Z.M., Beeser A., Chernoff J.
      Mol. Cell. Biol. 23:5526-5539(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-75.
    14. "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."
      Li Y.Y., Popivanova B.K., Nagai Y., Ishikura H., Fujii C., Mukaida N.
      Cancer Res. 66:6741-6747(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-75.
    15. "Proto-oncogene, Pim-3 with serine/threonine kinase activity, is aberrantly expressed in human colon cancer cells and can prevent Bad-mediated apoptosis."
      Popivanova B.K., Li Y.Y., Zheng H., Omura K., Fujii C., Tsuneyama K., Mukaida N.
      Cancer Sci. 98:321-328(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIM3.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Arginine methylation of BCL-2 antagonist of cell death (BAD) counteracts its phosphorylation and inactivation by Akt."
      Sakamaki J., Daitoku H., Ueno K., Hagiwara A., Yamagata K., Fukamizu A.
      Proc. Natl. Acad. Sci. U.S.A. 108:6085-6090(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-94 AND ARG-96 BY PRMT1, MUTAGENESIS OF ARG-94 AND ARG-96.
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies."
      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.
      Protein Sci. 9:2528-2534(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 103-127.

    Entry informationi

    Entry nameiBAD_HUMAN
    AccessioniPrimary (citable) accession number: Q92934
    Secondary accession number(s): O14803, Q6FH21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3