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Q61337

- BAD_MOUSE

UniProt

Q61337 - BAD_MOUSE

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Protein
Bcl2-associated agonist of cell death
Gene
Bad, Bbc6
Organism
Mus musculus (Mouse)
Status
Reviewed - 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. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.

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: UniProtKB
  5. protein heterodimerization activity Source: MGI
  6. protein phosphatase binding Source: MGI

GO - Biological processi

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

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_209641. NRAGE signals death through JNK.
REACT_220918. AKT phosphorylates targets in the cytosol.
REACT_223399. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1096330. Bad.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: MGI
  3. mitochondrial outer membrane Source: UniProtKB
  4. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121S → A: Enhances pro-apoptotic activity; no phosphorylation. 3 Publications
Mutagenesisi136 – 1361S → A: No phosphorylation. 2 Publications
Mutagenesisi155 – 1551S → A: Enhances pro-apoptotic activity; no phosphorylation; interacts with Bcl-X(L). 2 Publications
Mutagenesisi155 – 1551S → D: No pro-apoptotic activity, no interaction with Bcl-X(L). 2 Publications
Mutagenesisi170 – 1701S → A: Enhances pro-apoptotic activity. 2 Publications
Mutagenesisi170 – 1701S → D: No pro-apoptotic activity; even when associated with A-112. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Bcl2-associated agonist of cell death
PRO_0000143104Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121Phosphoserine; by PKA, PKB, PIM2, PIM3, PAK1, PAK2, PAK4, PAK7/PAK5, RPS6KA1 AND RAF16 Publications
Modified residuei128 – 1281Phosphoserine By similarity
Modified residuei131 – 1311Asymmetric dimethylarginine; by PRMT1 By similarity
Modified residuei133 – 1331Asymmetric dimethylarginine; by PRMT1 By similarity
Modified residuei136 – 1361Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ5 Publications
Modified residuei155 – 1551Phosphoserine; by PKA and PKB Inferred
Modified residuei170 – 1701Phosphoserine1 Publication

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.

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ61337.
PRIDEiQ61337.

PTM databases

PhosphoSiteiQ61337.

Miscellaneous databases

PMAP-CutDBQ61337.

Expressioni

Gene expression databases

ArrayExpressiQ61337.
BgeeiQ61337.
CleanExiMM_BAD.
GenevestigatoriQ61337.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL2P104156EBI-400328,EBI-77694From a different organism.
BCL2L1Q07817-12EBI-400328,EBI-287195From a different organism.
Bcl2l1Q64373-12EBI-400328,EBI-526380
YWHAZP631043EBI-400328,EBI-347088From a different organism.

Protein-protein interaction databases

BioGridi198296. 4 interactions.
DIPiDIP-273N.
IntActiQ61337. 16 interactions.
MINTiMINT-202237.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi139 – 1413
Helixi142 – 16019

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZWX-ray2.30B137-163[»]
DisProtiDP00563.
ProteinModelPortaliQ61337.
SMRiQ61337. Positions 137-163.

Miscellaneous databases

EvolutionaryTraceiQ61337.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi147 – 16115BH3
Add
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.

Phylogenomic databases

eggNOGiNOG43412.
GeneTreeiENSGT00390000010740.
HOGENOMiHOG000095169.
HOVERGENiHBG001653.
InParanoidiQ61337.
KOiK02158.
OMAiGEAGHQQ.
OrthoDBiEOG7MD4RF.
PhylomeDBiQ61337.
TreeFamiTF102001.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q61337-1 [UniParc]FASTAAdd to Basket

« Hide

MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE    50
PSEQEDASAT DRGLGPSLTE DQPGPYLAPG LLGSNIHQQG RAATNSHHGG 100
AGAMETRSRH SSYPAGTEED EGMEEELSPF RGRSRSAPPN LWAAQRYGRE 150
LRRMSDEFEG SFKGLPRPKS AGTATQMRQS AGWTRIIQSW WDRNLGKGGS 200
TPSQ 204
Length:204
Mass (Da):22,080
Last modified:November 1, 1996 - v1
Checksum:i6C2BA910205053F7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L37296 mRNA. Translation: AAA64465.1 .
BC006762 mRNA. Translation: AAH06762.1 .
CCDSi CCDS29513.1.
PIRi A55671.
RefSeqi NP_031548.1. NM_007522.3.
UniGenei Mm.4387.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BZW X-ray 2.30 B 137-163 [» ]
DisProti DP00563.
ProteinModelPortali Q61337.
SMRi Q61337. Positions 137-163.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198296. 4 interactions.
DIPi DIP-273N.
IntActi Q61337. 16 interactions.
MINTi MINT-202237.

Chemistry

BindingDBi Q61337.
ChEMBLi CHEMBL5385.

PTM databases

PhosphoSitei Q61337.

Proteomic databases

PaxDbi Q61337.
PRIDEi Q61337.

Protocols and materials databases

DNASUi 12015.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025910 ; ENSMUSP00000025910 ; ENSMUSG00000024959 .
GeneIDi 12015.
KEGGi mmu:12015.
UCSCi uc008gjn.1. mouse.

Organism-specific databases

CTDi 572.
MGIi MGI:1096330. Bad.

Phylogenomic databases

eggNOGi NOG43412.
GeneTreei ENSGT00390000010740.
HOGENOMi HOG000095169.
HOVERGENi HBG001653.
InParanoidi Q61337.
KOi K02158.
OMAi GEAGHQQ.
OrthoDBi EOG7MD4RF.
PhylomeDBi Q61337.
TreeFami TF102001.

Enzyme and pathway databases

Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_209641. NRAGE signals death through JNK.
REACT_220918. AKT phosphorylates targets in the cytosol.
REACT_223399. BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.

Miscellaneous databases

EvolutionaryTracei Q61337.
NextBioi 280229.
PMAP-CutDB Q61337.
PROi Q61337.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q61337.
Bgeei Q61337.
CleanExi MM_BAD.
Genevestigatori Q61337.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death."
    Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., Korsmeyer S.J.
    Cell 80:285-291(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NMRI.
    Tissue: Mammary gland.
  3. "Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt."
    Del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G.
    Science 278:687-689(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-112 AND SER-136, MUTAGENESIS OF SER-112 AND SER-136.
  4. "Rsk1 mediates a MEK-MAP kinase cell survival signal."
    Shimamura A., Ballif B.A., Richards S.A., Blenis J.
    Curr. Biol. 10:127-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-112 AND SER-136.
  5. "14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation."
    Datta S.R., Katsov A., Hu L., Petros A., Fesik S.W., Yaffe M.B., Greenberg M.E.
    Mol. Cell 6:41-51(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SERINE RESIDUES.
  6. "p21-activated kinase 1 phosphorylates the death agonist bad and protects cells from apoptosis."
    Schurmann A., Mooney A.F., Sanders L.C., Sells M.A., Wang H.G., Reed J.C., Bokoch G.M.
    Mol. Cell. Biol. 20:453-461(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-112 AND SER-136.
  7. "p21-activated protein kinase gamma-PAK suppresses programmed cell death of BALB3T3 fibroblasts."
    Jakobi R., Moertl E., Koeppel M.A.
    J. Biol. Chem. 276:16624-16634(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-112.
  8. "Protein kinase C-theta mediates a selective T cell survival signal via phosphorylation of BAD."
    Villalba M., Bushway P., Altman A.
    J. Immunol. 166:5955-5963(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-136.
  9. "p70S6 kinase signals cell survival as well as growth, inactivating the pro-apoptotic molecule BAD."
    Harada H., Andersen J.S., Mann M., Terada N., Korsmeyer S.J.
    Proc. Natl. Acad. Sci. U.S.A. 98:9666-9670(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-136.
  10. "Identification of a novel phosphorylation site, Ser-170, as a regulator of bad pro-apoptotic activity."
    Dramsi S., Scheid M.P., Maiti A., Hojabrpour P., Chen X., Schubert K., Goodlett D.R., Aebersold R., Duronio V.
    J. Biol. Chem. 277:6399-6405(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-155 AND SER-170, MUTAGENESIS OF SER-112; SER-155 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-induced cell death."
    Yan B., Zemskova M., Holder S., Chin V., Kraft A., Koskinen P.J., Lilly M.
    J. Biol. Chem. 278:45358-45367(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-112 BY PIM2.
  12. "p21-activated Kinase 1 (Pak1)-dependent phosphorylation of Raf-1 regulates its mitochondrial localization, phosphorylation of BAD, and Bcl-2 association."
    Jin S., Zhuo Y., Guo W., Field J.
    J. Biol. Chem. 280:24698-24705(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-112 BY RAF1.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiBAD_MOUSE
AccessioniPrimary (citable) accession number: Q61337
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 121 of the entry and version 1 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.

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

External Data

Dasty 3

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