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Protein

Bcl2-associated agonist of cell death

Gene

BAD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity). Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.By similarity

GO - Molecular functioni

  • cysteine-type endopeptidase activator activity involved in apoptotic process Source: UniProtKB
  • lipid binding Source: UniProtKB
  • phospholipid binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000002330-MONOMER.
ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
R-HSA-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-HSA-193648. NRAGE signals death through JNK.
R-HSA-198323. AKT phosphorylates targets in the cytosol.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
SIGNORiQ92934.

Names & Taxonomyi

Protein namesi
Recommended name:
Bcl2-associated agonist of cell death
Short name:
BAD
Alternative name(s):
Bcl-2-binding component 6
Bcl-2-like protein 8
Short name:
Bcl2-L-8
Bcl-xL/Bcl-2-associated death promoter
Bcl2 antagonist of cell death
Gene namesi
Name:BAD
Synonyms:BBC6, BCL2L8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:936. BAD.

Subcellular locationi

  • Mitochondrion outer membrane
  • Cytoplasm By similarity

  • Note: Colocalizes with HIF3A in the cytoplasm (By similarity). Upon phosphorylation, locates to the cytoplasm.By similarity

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • mitochondrial outer membrane Source: UniProtKB
  • mitochondrion Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi94R → K: Decreased methylation; when associated with K-96. 1 Publication1
Mutagenesisi96R → K: Decreased methylation; when associated with K-94. 1 Publication1

Organism-specific databases

DisGeNETi572.
OpenTargetsiENSG00000002330.
PharmGKBiPA25236.

Chemistry databases

ChEMBLiCHEMBL3817.

Polymorphism and mutation databases

BioMutaiBAD.
DMDMi17371773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001431031 – 168Bcl2-associated agonist of cell deathAdd BLAST168

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei25PhosphoserineCombined sources1
Modified residuei75PhosphoserineCombined sources1
Modified residuei91PhosphoserineCombined sources1
Modified residuei94Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei96Asymmetric dimethylarginine; by PRMT11 Publication1
Modified residuei97PhosphoserineBy similarity1
Modified residuei99Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQBy similarity1
Modified residuei99Phosphoserine; by PKB/AKT1Combined sources1 Publication1
Modified residuei118PhosphoserineCombined sources1
Modified residuei134PhosphoserineCombined sources1
Modified residuei161Omega-N-methylarginineCombined sources1

Post-translational modificationi

Phosphorylated on one or more of Ser-75, Ser-99, Ser-118 and Ser-134 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-99 or Ser-75 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-118, a site within the BH3 motif, leading to the release of Bcl-X(L) and the promotion of cell survival. Ser-99 is the major site of AKT/PKB phosphorylation, Ser-118 the major site of protein kinase A (CAPK) phosphorylation. Phosphorylation at Ser-99 by PKB/AKT1 is almost completely blocked by the apoptotic C-terminus cleavage product of PKN2 generated by caspases-3 activity during apoptosis.4 Publications
Methylation at Arg-94 and Arg-96 by PRMT1 inhibits Akt-mediated phosphorylation at Ser-99.2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ92934.
MaxQBiQ92934.
PaxDbiQ92934.
PeptideAtlasiQ92934.
PRIDEiQ92934.

PTM databases

iPTMnetiQ92934.
PhosphoSitePlusiQ92934.

Miscellaneous databases

PMAP-CutDBQ92934.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues.

Gene expression databases

BgeeiENSG00000002330.
CleanExiHS_BAD.
ExpressionAtlasiQ92934. baseline and differential.
GenevisibleiQ92934. HS.

Organism-specific databases

HPAiCAB004205.
HPA028185.
HPA062105.

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-75/Ser-99 phosphorylated form binds 14-3-3 proteins (By similarity). Interacts with AKT1 and PIM3. Interacts (via BH3 domain) with NOL3 (via CARD domain); preventing the association of BAD with BCL2 (By similarity). Interacts with HIF3A (via C-terminus domain); the interaction reduces the binding between BAD and BAX (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2P104155EBI-700771,EBI-77694
BCL2L1Q078177EBI-700771,EBI-78035
BCL2L1Q07817-16EBI-700771,EBI-287195
BCL2L11O435212EBI-700771,EBI-526406
BNIP3LO602382EBI-700771,EBI-849893
MAPK8P459832EBI-700771,EBI-286483
NSP034952EBI-700771,EBI-2548993From a different organism.
RAF1P040492EBI-700771,EBI-365996
SFNP319474EBI-700771,EBI-476295
VACWR028P173612EBI-700771,EBI-7115640From a different organism.
YWHAZP631045EBI-700771,EBI-347088

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107048. 44 interactors.
DIPiDIP-29184N.
IntActiQ92934. 37 interactors.
MINTiMINT-216253.
STRINGi9606.ENSP00000309103.

Chemistry databases

BindingDBiQ92934.

Structurei

Secondary structure

1168
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi106 – 121Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G5JNMR-B103-127[»]
ProteinModelPortaliQ92934.
SMRiQ92934.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92934.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi110 – 124BH3Add 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.
InParanoidiQ92934.
KOiK02158.
OMAiSMFQIPE.
OrthoDBiEOG091G0Z5T.
PhylomeDBiQ92934.
TreeFamiTF102001.

Family and domain databases

InterProiIPR018868. BAD.
[Graphical view]
PANTHERiPTHR28540:SF1. PTHR28540:SF1. 1 hit.
PfamiPF10514. Bcl-2_BAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92934-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQIPEFEPS EQEDSSSAER GLGPSPAGDG PSGSGKHHRQ APGLLWDASH
60 70 80 90 100
QQEQPTSSSH HGGAGAVEIR SRHSSYPAGT EDDEGMGEEP SPFRGRSRSA
110 120 130 140 150
PPNLWAAQRY GRELRRMSDE FVDSFKKGLP RPKSAGTATQ MRQSSSWTRV
160
FQSWWDRNLG RGSSAPSQ
Length:168
Mass (Da):18,392
Last modified:September 26, 2001 - v3
Checksum:i69FD8D27DDEE3241
GO

Sequence cautioni

The sequence AAB36516 differs from that shown. Reason: Frameshift at positions 64 and 91.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015380107A → S.Corresponds to variant rs3729933dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66879 mRNA. Translation: AAB36516.1. Frameshift.
AF021792 mRNA. Translation: AAB72092.1.
AF031523 mRNA. Translation: AAB88124.1.
AK291863 mRNA. Translation: BAF84552.1.
BT006678 mRNA. Translation: AAP35324.1.
CR541935 mRNA. Translation: CAG46733.1.
CR541959 mRNA. Translation: CAG46757.1.
AB451254 mRNA. Translation: BAG70068.1.
AB451378 mRNA. Translation: BAG70192.1.
CH471076 Genomic DNA. Translation: EAW74235.1.
BC001901 mRNA. Translation: AAH01901.1.
BC095431 mRNA. Translation: AAH95431.1.
CCDSiCCDS8065.1.
RefSeqiNP_004313.1. NM_004322.3.
NP_116784.1. NM_032989.2.
UniGeneiHs.370254.

Genome annotation databases

EnsembliENST00000309032; ENSP00000309103; ENSG00000002330.
ENST00000394532; ENSP00000378040; ENSG00000002330.
GeneIDi572.
KEGGihsa:572.
UCSCiuc001nzc.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

Bcl 2-associated death promoter entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66879 mRNA. Translation: AAB36516.1. Frameshift.
AF021792 mRNA. Translation: AAB72092.1.
AF031523 mRNA. Translation: AAB88124.1.
AK291863 mRNA. Translation: BAF84552.1.
BT006678 mRNA. Translation: AAP35324.1.
CR541935 mRNA. Translation: CAG46733.1.
CR541959 mRNA. Translation: CAG46757.1.
AB451254 mRNA. Translation: BAG70068.1.
AB451378 mRNA. Translation: BAG70192.1.
CH471076 Genomic DNA. Translation: EAW74235.1.
BC001901 mRNA. Translation: AAH01901.1.
BC095431 mRNA. Translation: AAH95431.1.
CCDSiCCDS8065.1.
RefSeqiNP_004313.1. NM_004322.3.
NP_116784.1. NM_032989.2.
UniGeneiHs.370254.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G5JNMR-B103-127[»]
ProteinModelPortaliQ92934.
SMRiQ92934.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107048. 44 interactors.
DIPiDIP-29184N.
IntActiQ92934. 37 interactors.
MINTiMINT-216253.
STRINGi9606.ENSP00000309103.

Chemistry databases

BindingDBiQ92934.
ChEMBLiCHEMBL3817.

PTM databases

iPTMnetiQ92934.
PhosphoSitePlusiQ92934.

Polymorphism and mutation databases

BioMutaiBAD.
DMDMi17371773.

Proteomic databases

EPDiQ92934.
MaxQBiQ92934.
PaxDbiQ92934.
PeptideAtlasiQ92934.
PRIDEiQ92934.

Protocols and materials databases

DNASUi572.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309032; ENSP00000309103; ENSG00000002330.
ENST00000394532; ENSP00000378040; ENSG00000002330.
GeneIDi572.
KEGGihsa:572.
UCSCiuc001nzc.4. human.

Organism-specific databases

CTDi572.
DisGeNETi572.
GeneCardsiBAD.
HGNCiHGNC:936. BAD.
HPAiCAB004205.
HPA028185.
HPA062105.
MIMi603167. gene.
neXtProtiNX_Q92934.
OpenTargetsiENSG00000002330.
PharmGKBiPA25236.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXUQ. Eukaryota.
ENOG410Y2J3. LUCA.
GeneTreeiENSGT00390000010740.
HOGENOMiHOG000095169.
HOVERGENiHBG001653.
InParanoidiQ92934.
KOiK02158.
OMAiSMFQIPE.
OrthoDBiEOG091G0Z5T.
PhylomeDBiQ92934.
TreeFamiTF102001.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000002330-MONOMER.
ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
R-HSA-111453. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
R-HSA-193648. NRAGE signals death through JNK.
R-HSA-198323. AKT phosphorylates targets in the cytosol.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
SIGNORiQ92934.

Miscellaneous databases

ChiTaRSiBAD. human.
EvolutionaryTraceiQ92934.
GeneWikiiBcl-2-associated_death_promoter.
GenomeRNAii572.
PMAP-CutDBQ92934.
PROiQ92934.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000002330.
CleanExiHS_BAD.
ExpressionAtlasiQ92934. baseline and differential.
GenevisibleiQ92934. HS.

Family and domain databases

InterProiIPR018868. BAD.
[Graphical view]
PANTHERiPTHR28540:SF1. PTHR28540:SF1. 1 hit.
PfamiPF10514. Bcl-2_BAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBAD_HUMAN
AccessioniPrimary (citable) accession number: Q92934
Secondary accession number(s): O14803, Q6FH21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 26, 2001
Last modified: November 30, 2016
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

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. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.