Bcl2 antagonist of cell death - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot Q61337 (BAD_MOUSE)

Last modified January 19, 2010. Version 81. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Bcl2 antagonist of cell death
      Short name=BAD
Alternative name(s):
    Bcl-2-binding component 6
    Bcl-xL/Bcl-2-associated death promoter

Gene names

Name:	Bad
Synonyms:	Bbc6

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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. Appears to act as a link between growth factor receptor signaling and the apoptotic pathways.
Subunit structure	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 PIM3 By similarity.
Subcellular location	Mitochondrion outer membrane. Cytoplasm. Note: Upon phosphorylation, locates to the cytoplasm.
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.
Post-translational modification	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. Ser-112 is phosphorylated by AKT/PKB, protein kinase A and PIM2. Ref.3 Ref.5 Ref.6 Ref.7
Sequence similarities	Belongs to the Bcl-2 family.

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Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Membrane Mitochondrion Mitochondrion outer membrane
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	apoptosis Inferred from direct assay. Source: MGI cell proliferation Inferred from direct assay. Source: MGI cytokine-mediated signaling pathway Inferred from direct assay. Source: MGI glucose catabolic process Inferred from mutant phenotype. Source: MGI glucose homeostasis Inferred from mutant phenotype. Source: MGI induction of apoptosis by extracellular signals Inferred from mutant phenotype. Source: MGI positive regulation of B cell differentiation Inferred from mutant phenotype. Source: MGI positive regulation of T cell differentiation Inferred from mutant phenotype. Source: MGI regulation of caspase activity Inferred from mutant phenotype. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: MGI mitochondrial outer membrane Ref.1 Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL2	P10415	3	EBI-400328,EBI-77694	From a different organism.
BCL2L1	Q07817	1	EBI-400328,EBI-78035	From a different organism.
BCL2L1	Q07817-1	2	EBI-400328,EBI-287195	From a different organism.
BCL2L2	Q92843	1	EBI-400328,EBI-707714	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 204

204

Bcl2 antagonist of cell death

PRO_0000143104

Regions

Motif

147 – 161

BH3

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

112

Phosphoserine; by PKA, PKB and PIM2 Ref.3 Ref.6 Ref.7

Modified residue

128

Phosphoserine By similarity

Modified residue

136

Phosphoserine; by PKA and PKB Ref.3

Modified residue

155

Phosphoserine; by PKA and PKB

Modified residue

170

Phosphoserine Ref.5

Experimental info

Mutagenesis

112

S → A: Enhances pro-apoptotic activity; no phosphorylation. Ref.3 Ref.5 Ref.4

Mutagenesis

136

S → A: No phosphorylation. Ref.3 Ref.4

Mutagenesis

155

S → A: Enhances pro-apoptotic activity; no phosphorylation; interacts with Bcl-X(L). Ref.5 Ref.4

Mutagenesis

155

S → D: No pro-apoptotic activity, no interaction with Bcl-X(L). Ref.5 Ref.4

Mutagenesis

170

S → A: Enhances pro-apoptotic activity. Ref.5 Ref.4

Mutagenesis

170

S → D: No pro-apoptotic activity; even when associated with A-112. Ref.5 Ref.4

Secondary structure

204

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q61337-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 6C2BA910205053F7
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FASTA

204

22,080

        10         20         30         40         50         60 
MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE PSEQEDASAT 

        70         80         90        100        110        120 
DRGLGPSLTE DQPGPYLAPG LLGSNIHQQG RAATNSHHGG AGAMETRSRH SSYPAGTEED 

       130        140        150        160        170        180 
EGMEEELSPF RGRSRSAPPN LWAAQRYGRE LRRMSDEFEG SFKGLPRPKS AGTATQMRQS 

       190        200 
AGWTRIIQSW WDRNLGKGGS TPSQ

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7834748] [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: 15489334] [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: 9381178] [Abstract] Cited for: PHOSPHORYLATION AT SER-112 AND SER-136, MUTAGENESIS OF SER-112 AND SER-136.
[4]	"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: 10949026] [Abstract] Cited for: MUTAGENESIS OF SERINE RESIDUES.
[5]	"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: 11717309] [Abstract] Cited for: PHOSPHORYLATION AT SER-170, MUTAGENESIS OF SER-112; SER-155 AND SER-170, MASS SPECTROMETRY.
[6]	"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: 12954615] [Abstract] Cited for: PHOSPHORYLATION AT SER-112 BY PIM2.
[7]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L37296 mRNA. Translation: AAA64465.1.
BC006762 mRNA. Translation: AAH06762.1.

IPI

IPI00119986.

PIR

A55671.

RefSeq

NP_031548.1.

UniGene

Mm.4387

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BZW	X-ray	2.30	B	137-163	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-273N.

IntAct

Q61337. 15 interactions.

STRING

Q61337.

PTM databases

PhosphoSite

Q61337.

Proteomic databases

PRIDE

Q61337.

Genome annotation databases

Ensembl

ENSMUST00000025910; ENSMUSP00000025910; ENSMUSG00000024959; Mus musculus. [Genome view]

GeneID

12015.

KEGG

mmu:12015.

UCSC

uc008gjn.1. mouse.

Organism-specific databases

CTD

12015.

MGI

MGI:1096330. Bad.

Phylogenomic databases

HOGENOM

HBG125823.

HOVERGEN

Q61337.

InParanoid

Q61337.

OMA

SFKGLPR.

OrthoDB

EOG9FTZKG.

PhylomeDB

Q61337.

Gene expression databases

ArrayExpress

Q61337.

Bgee

Q61337.

CleanEx

MM_BAD.

Genevestigator

Q61337.

GermOnline

ENSMUSG00000024959. Mus musculus.

Family and domain databases

InterPro

IPR018868. Bcl-2_BAD.
[Graphical view]

Pfam

PF10514. Bcl-2_BAD. 1 hit.
[Graphical view]

PROSITE

PS01259. BH3. False negative.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

280229.

PMAP-CutDB

Q61337.

SOURCE

Search...

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Entry information

Entry name

BAD_MOUSE

Accession

Primary (citable) accession number: Q61337

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents