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Q61337

- BAD_MOUSE

UniProt

Q61337 - BAD_MOUSE

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Protein

Bcl2-associated agonist of cell death

Gene

Bad

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

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  2. ADP metabolic process Source: UniProtKB
  3. apoptotic signaling pathway Source: MGI
  4. ATP metabolic process Source: UniProtKB
  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 apoptotic process Source: UniProtKB
  22. positive regulation of apoptotic process by virus Source: MGI
  23. positive regulation of B cell differentiation Source: MGI
  24. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  25. positive regulation of epithelial cell proliferation Source: UniProtKB
  26. positive regulation of glucokinase activity Source: UniProtKB
  27. positive regulation of insulin secretion Source: UniProtKB
  28. positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
  29. positive regulation of mitochondrial membrane potential Source: UniProtKB
  30. positive regulation of neuron death Source: Ensembl
  31. positive regulation of proteolysis Source: Ensembl
  32. positive regulation of release of cytochrome c from mitochondria Source: Ensembl
  33. positive regulation of T cell differentiation Source: MGI
  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. 2 Publications
Mutagenesisi136 – 1361S → A: No phosphorylation. 1 Publication
Mutagenesisi155 – 1551S → A: Enhances pro-apoptotic activity; no phosphorylation; interacts with Bcl-X(L). 1 Publication
Mutagenesisi155 – 1551S → D: No pro-apoptotic activity, no interaction with Bcl-X(L). 1 Publication
Mutagenesisi170 – 1701S → A: Enhances pro-apoptotic activity. 1 Publication
Mutagenesisi170 – 1701S → D: No pro-apoptotic activity; even when associated with A-112. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Bcl2-associated agonist of cell deathPRO_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 – 1281PhosphoserineBy similarity
Modified residuei131 – 1311Asymmetric dimethylarginine; by PRMT1By similarity
Modified residuei133 – 1331Asymmetric dimethylarginine; by PRMT1By similarity
Modified residuei136 – 1361Phosphoserine; by PKA, PKB, PAK1, RPS6KA1, RPS6KB1 and PKC/PRKCQ5 Publications
Modified residuei155 – 1551Phosphoserine; by PKA and PKB1 Publication
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-136.5 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ61337.
PaxDbiQ61337.
PRIDEiQ61337.

PTM databases

PhosphoSiteiQ61337.

Miscellaneous databases

PMAP-CutDBQ61337.

Expressioni

Gene expression databases

BgeeiQ61337.
CleanExiMM_BAD.
ExpressionAtlasiQ61337. baseline and differential.
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).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

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi139 – 1413Combined sources
Helixi142 – 16019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BZWX-ray2.30B137-163[»]
DisProtiDP00563.
ProteinModelPortaliQ61337.
SMRiQ61337. Positions 137-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ61337.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi147 – 16115BH3Add
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.Curated

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

        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.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

MaxQBi Q61337.
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

Bgeei Q61337.
CleanExi MM_BAD.
ExpressionAtlasi Q61337. baseline and differential.
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: November 26, 2014
This is version 124 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.Curated

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