O35147 · BAD_RAT

  • Protein
    Bcl2-associated agonist of cell death
  • Gene
    Bad
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentBAD-BCL-2 complex
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componentmitochondrial outer membrane
Cellular Componentmitochondrion
Molecular Function14-3-3 protein binding
Molecular Functioncysteine-type endopeptidase activator activity involved in apoptotic process
Molecular Functionlipid binding
Molecular Functionphospholipid binding
Molecular Functionprotein kinase B binding
Molecular Functionprotein kinase binding
Molecular Functionprotein phosphatase 2B binding
Molecular Functionprotein phosphatase binding
Biological Processactivation of cysteine-type endopeptidase activity involved in apoptotic process
Biological ProcessADP metabolic process
Biological Processapoptotic process
Biological Processapoptotic signaling pathway
Biological ProcessATP metabolic process
Biological Processcellular response to chromate
Biological Processcellular response to hypoxia
Biological Processcellular response to lipid
Biological Processcellular response to mechanical stimulus
Biological Processcellular response to nicotine
Biological Processcerebral cortex development
Biological Processcytokine-mediated signaling pathway
Biological Processepithelial cell proliferation
Biological Processextrinsic apoptotic signaling pathway
Biological Processextrinsic apoptotic signaling pathway in absence of ligand
Biological Processextrinsic apoptotic signaling pathway via death domain receptors
Biological Processglucose catabolic process
Biological Processglucose homeostasis
Biological Processintrinsic apoptotic signaling pathway
Biological Processintrinsic apoptotic signaling pathway in response to DNA damage
Biological Processnegative regulation of apoptotic process
Biological Processpore complex assembly
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of B cell differentiation
Biological Processpositive regulation of epithelial cell proliferation
Biological Processpositive regulation of granulosa cell apoptotic process
Biological Processpositive regulation of insulin secretion
Biological Processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
Biological Processpositive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
Biological Processpositive regulation of mitochondrial membrane potential
Biological Processpositive regulation of proteolysis
Biological Processpositive regulation of release of cytochrome c from mitochondria
Biological Processpositive regulation of T cell differentiation
Biological Processpositive regulation of type B pancreatic cell development
Biological Processregulation of apoptotic process
Biological Processregulation of mitochondrial membrane permeability
Biological Processrelease of cytochrome c from mitochondria
Biological Processresponse to amino acid
Biological Processresponse to benzene
Biological Processresponse to calcium ion
Biological Processresponse to estradiol
Biological Processresponse to ethanol
Biological Processresponse to glucocorticoid
Biological Processresponse to glucose
Biological Processresponse to hormone
Biological Processresponse to hydrogen peroxide
Biological Processresponse to hypoxia
Biological Processresponse to oleic acid
Biological Processresponse to organic cyclic compound
Biological Processresponse to progesterone
Biological Processresponse to testosterone
Biological Processresponse to xenobiotic stimulus
Biological Processspermatogenesis
Biological Processtype B pancreatic cell proliferation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Bcl2-associated agonist of cell death
  • Short names
    BAD
  • Alternative names
    • Bcl-2-binding component 6
    • Bcl-xL/Bcl-2-associated death promoter
    • Bcl2 antagonist of cell death

Gene names

    • Name
      Bad

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    O35147
  • Secondary accessions
    • O70256
    • Q9JHX1

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Note: Colocalizes with HIF3A in the cytoplasm. Upon phosphorylation, locates to the cytoplasm.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis113No effect on heterodimerization with 14-3-3 proteins.
Mutagenesis137No heterodimerization with 14-3-3 proteins. No effect on heterodimerization with BCL2 nor with protein P11.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001431051-205Bcl2-associated agonist of cell death
Modified residue67Phosphoserine
Modified residue113Phosphoserine
Modified residue129Phosphoserine
Modified residue132Asymmetric dimethylarginine; by PRMT1
Modified residue134Asymmetric dimethylarginine; by PRMT1
Modified residue135Phosphoserine
Modified residue137Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ
Modified residue156Phosphoserine
Modified residue171Phosphoserine

Post-translational modification

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.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

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

Interaction

Subunit

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).
Interacts with HIF3A (via C-terminus domain); the interaction reduces the binding between BAD and BAX (By similarity).
Interacts (via BH3 domain) with NOL3 (via CARD domain); preventing the association of BAD with BCL2 (PubMed:17998337).
Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 (By similarity).

Complex viewer

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region1-139Disordered
Compositional bias85-112Polar residues
Motif148-162BH3
Region161-180Disordered

Domain

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 similarities

Belongs to the Bcl-2 family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

O35147-1

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.

  • Name
    Alpha
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    205
  • Mass (Da)
    22,228
  • Last updated
    2001-09-26 v2
  • Checksum
    7AFA71DAE9CF4A81
MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ

O35147-2

  • Name
    Beta
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 166-205: LPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ → EELTYSVEFLPVRAIAMEGWPLLWSFQSFPHTLPPTPPEVAMFPLRYWTALRRLC

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6AQN1A0A8I6AQN1_RATBad179
A0A8L2UKI4A0A8L2UKI4_RATBad235

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict29-34in Ref. 1; AAC53374
Compositional bias85-112Polar residues
Alternative sequenceVSP_000534166-205in isoform Beta

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF003523
EMBL· GenBank· DDBJ
AAC53374.1
EMBL· GenBank· DDBJ
mRNA
AF031227
EMBL· GenBank· DDBJ
AAC15100.1
EMBL· GenBank· DDBJ
mRNA
AF279910
EMBL· GenBank· DDBJ
AAF91427.1
EMBL· GenBank· DDBJ
mRNA
AF279911
EMBL· GenBank· DDBJ
AAF91428.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp