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Q61337

- BAD_MOUSE

UniProt

Q61337 - BAD_MOUSE

Protein

Bcl2-associated agonist of cell death

Gene

Bad

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.

    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 heterodimerization activity Source: MGI
    6. protein phosphatase binding Source: MGI

    GO - Biological processi

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

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_209641. NRAGE signals death through JNK.
    REACT_220918. AKT phosphorylates targets in the cytosol.
    REACT_223399. 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-xL/Bcl-2-associated death promoter
    Bcl2 antagonist of cell death
    Gene namesi
    Name:Bad
    Synonyms:Bbc6
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1096330. Bad.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: MGI
    3. mitochondrial outer membrane Source: UniProtKB
    4. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi112 – 1121S → A: Enhances pro-apoptotic activity; no phosphorylation. 3 Publications
    Mutagenesisi136 – 1361S → A: No phosphorylation. 2 Publications
    Mutagenesisi155 – 1551S → A: Enhances pro-apoptotic activity; no phosphorylation; interacts with Bcl-X(L). 2 Publications
    Mutagenesisi155 – 1551S → D: No pro-apoptotic activity, no interaction with Bcl-X(L). 2 Publications
    Mutagenesisi170 – 1701S → A: Enhances pro-apoptotic activity. 2 Publications
    Mutagenesisi170 – 1701S → D: No pro-apoptotic activity; even when associated with A-112. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 204204Bcl2-associated agonist of cell deathPRO_0000143104Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei112 – 1121Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK7/PAK5, RPS6KA1 AND RAF16 Publications
    Modified residuei128 – 1281PhosphoserineBy similarity
    Modified residuei131 – 1311Asymmetric dimethylarginine; by PRMT1By similarity
    Modified residuei133 – 1331Asymmetric dimethylarginine; by PRMT1By similarity
    Modified residuei136 – 1361Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ5 Publications
    Modified residuei155 – 1551Phosphoserine; by PKA and PKB1 Publication
    Modified residuei170 – 1701Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylated on one or more of Ser-112, Ser-136, Ser-155 and Ser-170 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-136 or Ser-112 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-155, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-136 is the major site of AKT/PKB phosphorylation, Ser-155 the major site of protein kinase A (CAPK) phosphorylation.9 Publications
    Methylation at Arg-131 and Arg-133 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-136.5 Publications

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ61337.
    PRIDEiQ61337.

    PTM databases

    PhosphoSiteiQ61337.

    Miscellaneous databases

    PMAP-CutDBQ61337.

    Expressioni

    Gene expression databases

    ArrayExpressiQ61337.
    BgeeiQ61337.
    CleanExiMM_BAD.
    GenevestigatoriQ61337.

    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-112/Ser-136 phosphorylated form binds 14-3-3 proteins. Interacts with AKT1 and PIM3 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2P104156EBI-400328,EBI-77694From a different organism.
    BCL2L1Q07817-12EBI-400328,EBI-287195From a different organism.
    Bcl2l1Q64373-12EBI-400328,EBI-526380
    YWHAZP631043EBI-400328,EBI-347088From a different organism.

    Protein-protein interaction databases

    BioGridi198296. 4 interactions.
    DIPiDIP-273N.
    IntActiQ61337. 16 interactions.
    MINTiMINT-202237.

    Structurei

    Secondary structure

    1
    204
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi139 – 1413
    Helixi142 – 16019

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BZWX-ray2.30B137-163[»]
    DisProtiDP00563.
    ProteinModelPortaliQ61337.
    SMRiQ61337. Positions 137-163.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ61337.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi147 – 16115BH3Add
    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.
    GeneTreeiENSGT00390000010740.
    HOGENOMiHOG000095169.
    HOVERGENiHBG001653.
    InParanoidiQ61337.
    KOiK02158.
    OMAiGEAGHQQ.
    OrthoDBiEOG7MD4RF.
    PhylomeDBiQ61337.
    TreeFamiTF102001.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    Q61337-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE    50
    PSEQEDASAT DRGLGPSLTE DQPGPYLAPG LLGSNIHQQG RAATNSHHGG 100
    AGAMETRSRH SSYPAGTEED EGMEEELSPF RGRSRSAPPN LWAAQRYGRE 150
    LRRMSDEFEG SFKGLPRPKS AGTATQMRQS AGWTRIIQSW WDRNLGKGGS 200
    TPSQ 204
    Length:204
    Mass (Da):22,080
    Last modified:November 1, 1996 - v1
    Checksum:i6C2BA910205053F7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37296 mRNA. Translation: AAA64465.1.
    BC006762 mRNA. Translation: AAH06762.1.
    CCDSiCCDS29513.1.
    PIRiA55671.
    RefSeqiNP_031548.1. NM_007522.3.
    UniGeneiMm.4387.

    Genome annotation databases

    EnsembliENSMUST00000025910; ENSMUSP00000025910; ENSMUSG00000024959.
    GeneIDi12015.
    KEGGimmu:12015.
    UCSCiuc008gjn.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L37296 mRNA. Translation: AAA64465.1 .
    BC006762 mRNA. Translation: AAH06762.1 .
    CCDSi CCDS29513.1.
    PIRi A55671.
    RefSeqi NP_031548.1. NM_007522.3.
    UniGenei Mm.4387.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BZW X-ray 2.30 B 137-163 [» ]
    DisProti DP00563.
    ProteinModelPortali Q61337.
    SMRi Q61337. Positions 137-163.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198296. 4 interactions.
    DIPi DIP-273N.
    IntActi Q61337. 16 interactions.
    MINTi MINT-202237.

    Chemistry

    BindingDBi Q61337.
    ChEMBLi CHEMBL5385.

    PTM databases

    PhosphoSitei Q61337.

    Proteomic databases

    PaxDbi Q61337.
    PRIDEi Q61337.

    Protocols and materials databases

    DNASUi 12015.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025910 ; ENSMUSP00000025910 ; ENSMUSG00000024959 .
    GeneIDi 12015.
    KEGGi mmu:12015.
    UCSCi uc008gjn.1. mouse.

    Organism-specific databases

    CTDi 572.
    MGIi MGI:1096330. Bad.

    Phylogenomic databases

    eggNOGi NOG43412.
    GeneTreei ENSGT00390000010740.
    HOGENOMi HOG000095169.
    HOVERGENi HBG001653.
    InParanoidi Q61337.
    KOi K02158.
    OMAi GEAGHQQ.
    OrthoDBi EOG7MD4RF.
    PhylomeDBi Q61337.
    TreeFami TF102001.

    Enzyme and pathway databases

    Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_209641. NRAGE signals death through JNK.
    REACT_220918. AKT phosphorylates targets in the cytosol.
    REACT_223399. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

    Miscellaneous databases

    EvolutionaryTracei Q61337.
    NextBioi 280229.
    PMAP-CutDB Q61337.
    PROi Q61337.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61337.
    Bgeei Q61337.
    CleanExi MM_BAD.
    Genevestigatori Q61337.

    Family and domain databases

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

    Publicationsi

    1. "Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death."
      Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., Korsmeyer S.J.
      Cell 80:285-291(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain and Thymus.
    2. "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].
      Strain: NMRI.
      Tissue: Mammary gland.
    3. "Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt."
      Del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G.
      Science 278:687-689(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-112 AND SER-136, MUTAGENESIS OF SER-112 AND SER-136.
    4. "Rsk1 mediates a MEK-MAP kinase cell survival signal."
      Shimamura A., Ballif B.A., Richards S.A., Blenis J.
      Curr. Biol. 10:127-135(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-112 AND SER-136.
    5. "14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation."
      Datta S.R., Katsov A., Hu L., Petros A., Fesik S.W., Yaffe M.B., Greenberg M.E.
      Mol. Cell 6:41-51(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SERINE RESIDUES.
    6. "p21-activated kinase 1 phosphorylates the death agonist bad and protects cells from apoptosis."
      Schurmann A., Mooney A.F., Sanders L.C., Sells M.A., Wang H.G., Reed J.C., Bokoch G.M.
      Mol. Cell. Biol. 20:453-461(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-112 AND SER-136.
    7. "p21-activated protein kinase gamma-PAK suppresses programmed cell death of BALB3T3 fibroblasts."
      Jakobi R., Moertl E., Koeppel M.A.
      J. Biol. Chem. 276:16624-16634(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-112.
    8. "Protein kinase C-theta mediates a selective T cell survival signal via phosphorylation of BAD."
      Villalba M., Bushway P., Altman A.
      J. Immunol. 166:5955-5963(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-136.
    9. "p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD."
      Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.
      Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-136.
    10. "Identification of a novel phosphorylation site, Ser-170, as a regulator of bad pro-apoptotic activity."
      Dramsi S., Scheid M.P., Maiti A., Hojabrpour P., Chen X., Schubert K., Goodlett D.R., Aebersold R., Duronio V.
      J. Biol. Chem. 277:6399-6405(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-155 AND SER-170, MUTAGENESIS OF SER-112; SER-155 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY.
    11. "The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death."
      Yan B., Zemskova M., Holder S., Chin V., Kraft A., Koskinen P.J., Lilly M.
      J. Biol. Chem. 278:45358-45367(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-112 BY PIM2.
    12. "p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1 regulates its mitochondrial localization, phosphorylation of BAD, and Bcl-2 association."
      Jin S., Zhuo Y., Guo W., Field J.
      J. Biol. Chem. 280:24698-24705(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-112 BY RAF1.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiBAD_MOUSE
    AccessioniPrimary (citable) accession number: Q61337
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3