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Protein

Bcl2-associated agonist of cell death

Gene

Bad

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

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

GO - Molecular functioni

GO - Biological processi

  • activation of cysteine-type endopeptidase activity Source: MGI
  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • ADP metabolic process Source: UniProtKB
  • apoptotic process Source: MGI
  • apoptotic signaling pathway Source: MGI
  • ATP metabolic process Source: UniProtKB
  • cell proliferation Source: MGI
  • cellular process regulating host cell cycle in response to virus Source: MGI
  • cellular response to chromate Source: Ensembl
  • cellular response to hypoxia Source: Ensembl
  • cellular response to lipid Source: UniProtKB
  • cellular response to mechanical stimulus Source: Ensembl
  • cellular response to nicotine Source: UniProtKB
  • cellular response to organic substance Source: MGI
  • cerebral cortex development Source: Ensembl
  • cytokine-mediated signaling pathway Source: MGI
  • extrinsic apoptotic signaling pathway Source: MGI
  • extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • glucose catabolic process Source: MGI
  • glucose homeostasis Source: UniProtKB
  • intrinsic apoptotic signaling pathway Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • pore complex assembly Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of apoptotic process by virus Source: MGI
  • positive regulation of B cell differentiation Source: MGI
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: UniProtKB
  • positive regulation of glucokinase activity Source: UniProtKB
  • positive regulation of insulin secretion Source: UniProtKB
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  • positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress Source: CAFA
  • positive regulation of mitochondrial membrane potential Source: UniProtKB
  • positive regulation of neuron death Source: MGI
  • positive regulation of proteolysis Source: MGI
  • positive regulation of release of cytochrome c from mitochondria Source: MGI
  • positive regulation of T cell differentiation Source: MGI
  • positive regulation of type B pancreatic cell development Source: UniProtKB
  • regulation of apoptotic process Source: MGI
  • regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • regulation of mitochondrial membrane permeability Source: UniProtKB
  • release of cytochrome c from mitochondria Source: MGI
  • response to amino acid Source: Ensembl
  • response to calcium ion Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to glucose Source: Ensembl
  • response to hydrogen peroxide Source: Ensembl
  • response to oleic acid Source: Ensembl
  • response to progesterone Source: Ensembl
  • response to testosterone Source: Ensembl
  • spermatogenesis Source: Ensembl
  • suppression by virus of host apoptotic process Source: MGI
  • type B pancreatic cell proliferation Source: UniProtKB

Keywordsi

Biological processApoptosis

Enzyme and pathway databases

ReactomeiR-MMU-111447 Activation of BAD and translocation to mitochondria
R-MMU-111453 BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members
R-MMU-193648 NRAGE signals death through JNK

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1096330 Bad

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112S → A: Enhances pro-apoptotic activity; no phosphorylation. 2 Publications1
Mutagenesisi136S → A: No phosphorylation. 1 Publication1
Mutagenesisi155S → A: Enhances pro-apoptotic activity; no phosphorylation; interacts with Bcl-X(L). 1 Publication1
Mutagenesisi155S → D: No pro-apoptotic activity, no interaction with Bcl-X(L). 1 Publication1
Mutagenesisi170S → A: Enhances pro-apoptotic activity. 1 Publication1
Mutagenesisi170S → D: No pro-apoptotic activity; even when associated with A-112. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5385

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001431041 – 204Bcl2-associated agonist of cell deathAdd BLAST204

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67PhosphoserineBy similarity1
Modified residuei112Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK5, RPS6KA1 AND RAF16 Publications1
Modified residuei128PhosphoserineBy similarity1
Modified residuei131Asymmetric dimethylarginine; by PRMT1By similarity1
Modified residuei133Asymmetric dimethylarginine; by PRMT1By similarity1
Modified residuei134PhosphoserineBy similarity1
Modified residuei136Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQCombined sources5 Publications1
Modified residuei155PhosphoserineCombined sources1
Modified residuei155Phosphoserine; by PKA and PKBCombined sources1 Publication1
Modified residuei170PhosphoserineCombined sources1 Publication1

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

EPDiQ61337
MaxQBiQ61337
PaxDbiQ61337
PRIDEiQ61337

PTM databases

iPTMnetiQ61337
PhosphoSitePlusiQ61337

Miscellaneous databases

PMAP-CutDBiQ61337

Expressioni

Gene expression databases

BgeeiENSMUSG00000024959
CleanExiMM_BAD
ExpressionAtlasiQ61337 baseline and differential
GenevisibleiQ61337 MM

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). Interacts (via BH3 domain) with NOL3 (via CARD domain); preventing the association of BAD with BCL2 (By similarity). Interacts with HIF3A isoform 2 (via C-terminus domain); the interaction reduces the binding between BAD and BAX (PubMed:21546903).By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • 14-3-3 protein binding Source: MGI
  • protein heterodimerization activity Source: MGI
  • protein kinase B binding Source: MGI
  • protein kinase binding Source: MGI
  • protein phosphatase 2B binding Source: MGI
  • protein phosphatase binding Source: MGI

Protein-protein interaction databases

BioGridi198296, 7 interactors
ComplexPortaliCPX-2019 BAD:BCL-2 complex
CPX-2021 BAD:BCL-XL complex
CORUMiQ61337
DIPiDIP-273N
ELMiQ61337
IntActiQ61337, 17 interactors
MINTiQ61337
STRINGi10090.ENSMUSP00000025910

Chemistry databases

BindingDBiQ61337

Structurei

Secondary structure

1204
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi139 – 141Combined sources3
Helixi142 – 160Combined sources19

3D structure databases

DisProtiDP00563
ProteinModelPortaliQ61337
SMRiQ61337
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61337

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi147 – 161BH3Add BLAST15

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

eggNOGiENOG410IXUQ Eukaryota
ENOG410Y2J3 LUCA
GeneTreeiENSGT00390000010740
HOGENOMiHOG000095169
HOVERGENiHBG001653
InParanoidiQ61337
KOiK02158
OMAiIQSWWDR
OrthoDBiEOG091G0Z5T
PhylomeDBiQ61337
TreeFamiTF102001

Family and domain databases

InterProiView protein in InterPro
IPR018868 BAD
PANTHERiPTHR28540 PTHR28540, 1 hit
PfamiView protein in Pfam
PF10514 Bcl-2_BAD, 1 hit

Sequencei

Sequence statusi: Complete.

Q61337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE
60 70 80 90 100
PSEQEDASAT DRGLGPSLTE DQPGPYLAPG LLGSNIHQQG RAATNSHHGG
110 120 130 140 150
AGAMETRSRH SSYPAGTEED EGMEEELSPF RGRSRSAPPN LWAAQRYGRE
160 170 180 190 200
LRRMSDEFEG SFKGLPRPKS AGTATQMRQS AGWTRIIQSW WDRNLGKGGS

TPSQ
Length:204
Mass (Da):22,080
Last modified:November 1, 1996 - v1
Checksum:i6C2BA910205053F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.2 mouse

Similar proteinsi

Entry informationi

Entry nameiBAD_MOUSE
AccessioniPrimary (citable) accession number: Q61337
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 18, 2018
This is version 156 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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