O35147 · BAD_RAT
- ProteinBcl2-associated agonist of cell death
- GeneBad
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids205 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Appears to act as a link between growth factor receptor signaling and the apoptotic pathways
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBcl2-associated agonist of cell death
- Short namesBAD
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO35147
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with HIF3A in the cytoplasm. Upon phosphorylation, locates to the cytoplasm.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 113 | No effect on heterodimerization with 14-3-3 proteins. | ||||
Sequence: S → A | ||||||
Mutagenesis | 137 | No heterodimerization with 14-3-3 proteins. No effect on heterodimerization with BCL2 nor with protein P11. | ||||
Sequence: S → A |
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000143105 | 1-205 | Bcl2-associated agonist of cell death | |||
Sequence: MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ | ||||||
Modified residue | 67 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 113 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 129 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 132 | Asymmetric dimethylarginine; by PRMT1 | ||||
Sequence: R | ||||||
Modified residue | 134 | Asymmetric dimethylarginine; by PRMT1 | ||||
Sequence: R | ||||||
Modified residue | 135 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 137 | Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ | ||||
Sequence: S | ||||||
Modified residue | 156 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 171 | Phosphoserine | ||||
Sequence: S |
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
- PTM
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-139 | Disordered | ||||
Sequence: MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAP | ||||||
Compositional bias | 85-112 | Polar residues | ||||
Sequence: IVQQQPGQAANNSHHGGAGTMETRSRHS | ||||||
Motif | 148-162 | BH3 | ||||
Sequence: YGRELRRMSDEFEGS | ||||||
Region | 161-180 | Disordered | ||||
Sequence: GSFKGLPRPKSAGTATQMRQ |
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
- Sequence statusComplete
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.
- NameAlpha
- Length205
- Mass (Da)22,228
- Last updated2001-09-26 v2
- Checksum7AFA71DAE9CF4A81
O35147-2
- NameBeta
- Differences from canonical
- 166-205: LPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ → EELTYSVEFLPVRAIAMEGWPLLWSFQSFPHTLPPTPPEVAMFPLRYWTALRRLC
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AQN1 | A0A8I6AQN1_RAT | Bad | 179 | ||
A0A8L2UKI4 | A0A8L2UKI4_RAT | Bad | 235 |
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 29-34 | in Ref. 1; AAC53374 | ||||
Sequence: SDAGGR → ERRGRK | ||||||
Compositional bias | 85-112 | Polar residues | ||||
Sequence: IVQQQPGQAANNSHHGGAGTMETRSRHS | ||||||
Alternative sequence | VSP_000534 | 166-205 | in isoform Beta | |||
Sequence: LPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ → EELTYSVEFLPVRAIAMEGWPLLWSFQSFPHTLPPTPPEVAMFPLRYWTALRRLC |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |