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O35147

- BAD_RAT

UniProt

O35147 - BAD_RAT

Protein

Bcl2-associated agonist of cell death

Gene

Bad

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (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: RGD
    5. protein kinase B binding Source: RGD
    6. protein phosphatase 2B binding Source: RGD

    GO - Biological processi

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

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    ReactomeiREACT_198729. Constitutive PI3K/AKT Signaling in Cancer.

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi620103. Bad.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi113 – 1131S → A: No effect on heterodimerization with 14-3-3 proteins. 1 Publication
    Mutagenesisi137 – 1371S → A: No heterodimerization with 14-3-3 proteins. No effect on heterodimerization with BCL2 nor with protein P11. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205Bcl2-associated agonist of cell deathPRO_0000143105Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei113 – 1131Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK7/PAK5, RPS6KA1 and RAF1By similarity
    Modified residuei129 – 1291PhosphoserineBy similarity
    Modified residuei132 – 1321Asymmetric dimethylarginine; by PRMT1By similarity
    Modified residuei134 – 1341Asymmetric dimethylarginine; by PRMT1By similarity
    Modified residuei137 – 1371Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQBy similarity
    Modified residuei156 – 1561Phosphoserine; by PKA and PKBBy similarity
    Modified residuei171 – 1711PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated at one or more of Ser-113, Ser-137, Ser-156 and Ser-171 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-137 or Ser-113 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-156, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-137 is the major site of AKT/PKB phosphorylation, Ser-156 the major site of protein kinase A (CAPK) phosphorylation.
    Methylation at Arg-132 and Arg-134 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-137.By similarity

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiO35147.

    PTM databases

    PhosphoSiteiO35147.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested, including brain, liver, spleen and heart. In the brain, restricted to epithelial cells of the choroid plexus. Isoform alpha is the more abundant form.

    Gene expression databases

    GenevestigatoriO35147.

    Interactioni

    Subunit structurei

    Forms heterodimers with the anti-apoptotic proteins, Bcl-X(L), Bcl-2 and Bcl-W. Also binds protein S100A10. The Ser-113/Ser-137 phosphorylated form binds 14-3-3 proteins. Interacts with AKT1 and PIM3 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi249177. 2 interactions.
    DIPiDIP-29862N.
    MINTiMINT-206504.

    Structurei

    3D structure databases

    ProteinModelPortaliO35147.
    SMRiO35147. Positions 138-164.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi148 – 16215BH3Add
    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.
    InParanoidiO35147.
    KOiK02158.
    OMAiWVARNAT.
    OrthoDBiEOG7MD4RF.
    PhylomeDBiO35147.
    TreeFamiTF102001.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: O35147-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE    50
    PSEQEDASTT DRGLGPSLTE DQPGPYLAPG LLGSIVQQQP GQAANNSHHG 100
    GAGTMETRSR HSSYPAGTEE DEGMEEELSP FRGRSRSAPP NLWAAQRYGR 150
    ELRRMSDEFE GSFKGLPRPK SAGTATQMRQ SASWTRIIQS WWDRNLGKGG 200
    STPSQ 205
    Length:205
    Mass (Da):22,228
    Last modified:September 26, 2001 - v2
    Checksum:i7AFA71DAE9CF4A81
    GO
    Isoform Beta (identifier: O35147-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         166-205: LPRPKSAGTA...LGKGGSTPSQ → EELTYSVEFL...RYWTALRRLC

    Show »
    Length:220
    Mass (Da):24,278
    Checksum:iE27BCCD7C969E90F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 346SDAGGR → ERRGRK in AAC53374. (PubMed:9369453)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei166 – 20540LPRPK…STPSQ → EELTYSVEFLPVRAIAMEGW PLLWSFQSFPHTLPPTPPEV AMFPLRYWTALRRLC in isoform Beta. 1 PublicationVSP_000534Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003523 mRNA. Translation: AAC53374.1.
    AF031227 mRNA. Translation: AAC15100.1.
    AF279910 mRNA. Translation: AAF91427.1.
    AF279911 mRNA. Translation: AAF91428.1.
    RefSeqiNP_073189.1. NM_022698.1. [O35147-1]
    XP_006230958.1. XM_006230896.1. [O35147-2]
    UniGeneiRn.36696.

    Genome annotation databases

    EnsembliENSRNOT00000028712; ENSRNOP00000028712; ENSRNOG00000021147. [O35147-1]
    ENSRNOT00000067068; ENSRNOP00000061855; ENSRNOG00000021147. [O35147-2]
    GeneIDi64639.
    KEGGirno:64639.
    UCSCiRGD:620103. rat. [O35147-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003523 mRNA. Translation: AAC53374.1 .
    AF031227 mRNA. Translation: AAC15100.1 .
    AF279910 mRNA. Translation: AAF91427.1 .
    AF279911 mRNA. Translation: AAF91428.1 .
    RefSeqi NP_073189.1. NM_022698.1. [O35147-1 ]
    XP_006230958.1. XM_006230896.1. [O35147-2 ]
    UniGenei Rn.36696.

    3D structure databases

    ProteinModelPortali O35147.
    SMRi O35147. Positions 138-164.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249177. 2 interactions.
    DIPi DIP-29862N.
    MINTi MINT-206504.

    PTM databases

    PhosphoSitei O35147.

    Proteomic databases

    PaxDbi O35147.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000028712 ; ENSRNOP00000028712 ; ENSRNOG00000021147 . [O35147-1 ]
    ENSRNOT00000067068 ; ENSRNOP00000061855 ; ENSRNOG00000021147 . [O35147-2 ]
    GeneIDi 64639.
    KEGGi rno:64639.
    UCSCi RGD:620103. rat. [O35147-1 ]

    Organism-specific databases

    CTDi 572.
    RGDi 620103. Bad.

    Phylogenomic databases

    eggNOGi NOG43412.
    GeneTreei ENSGT00390000010740.
    HOGENOMi HOG000095169.
    HOVERGENi HBG001653.
    InParanoidi O35147.
    KOi K02158.
    OMAi WVARNAT.
    OrthoDBi EOG7MD4RF.
    PhylomeDBi O35147.
    TreeFami TF102001.

    Enzyme and pathway databases

    Reactomei REACT_198729. Constitutive PI3K/AKT Signaling in Cancer.

    Miscellaneous databases

    NextBioi 613624.
    PROi O35147.

    Gene expression databases

    Genevestigatori O35147.

    Family and domain databases

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

    Publicationsi

    1. "Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11."
      Hsu S.Y., Kaipia A., Zhu L., Hsueh A.J.W.
      Mol. Endocrinol. 11:1858-1867(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF SER-113 AND SER-137.
      Tissue: Ovary.
    2. "Cloning and expression of the programmed cell death regulator BAD in the rat brain."
      D'Agata V., Magro G., Travali S., Musco S., Cavallaro S.
      Neurosci. Lett. 243:137-140(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Functional characterization of two splice variants of rat BAD and their interaction with Bcl-w in sympathetic neurons."
      Hamner S., Arumae U., Yu L.-Y., Sun Y.-F., Saarma M., Lindholm D.
      Mol. Cell. Neurosci. 17:97-106(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
      Tissue: Brain.

    Entry informationi

    Entry nameiBAD_RAT
    AccessioniPrimary (citable) accession number: O35147
    Secondary accession number(s): O70256, Q9JHX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3