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Protein

Apoptosis regulator BAX

Gene

Bax

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis. BAX deficiency leads to lymphoid hyperplasia and male sterility, because of the cessation of sperm production.2 Publications

GO - Molecular functioni

  • BH3 domain binding Source: MGI
  • channel activity Source: UniProtKB
  • identical protein binding Source: MGI
  • lipid binding Source: UniProtKB
  • protein heterodimerization activity Source: MGI
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: MGI
  • activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: MGI
  • apoptotic mitochondrial changes Source: MGI
  • apoptotic process Source: MGI
  • apoptotic process involved in embryonic digit morphogenesis Source: MGI
  • apoptotic process involved in patterning of blood vessels Source: MGI
  • apoptotic signaling pathway Source: MGI
  • B cell apoptotic process Source: MGI
  • B cell homeostasis Source: MGI
  • B cell homeostatic proliferation Source: MGI
  • B cell negative selection Source: MGI
  • B cell receptor apoptotic signaling pathway Source: MGI
  • blood vessel remodeling Source: MGI
  • cell proliferation Source: MGI
  • cellular respiration Source: Ensembl
  • cellular response to DNA damage stimulus Source: MGI
  • cellular response to organic substance Source: MGI
  • cellular response to UV Source: MGI
  • cerebral cortex development Source: MGI
  • development of secondary sexual characteristics Source: MGI
  • ectopic germ cell programmed cell death Source: MGI
  • establishment or maintenance of transmembrane electrochemical gradient Source: UniProtKB
  • extrinsic apoptotic signaling pathway Source: MGI
  • extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • fertilization Source: MGI
  • germ cell development Source: MGI
  • glial cell apoptotic process Source: Ensembl
  • glycosphingolipid metabolic process Source: MGI
  • homeostasis of number of cells Source: MGI
  • homeostasis of number of cells within a tissue Source: MGI
  • hypothalamus development Source: MGI
  • inner mitochondrial membrane organization Source: Ensembl
  • intrinsic apoptotic signaling pathway Source: MGI
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: MGI
  • kidney development Source: MGI
  • leukocyte homeostasis Source: MGI
  • limb morphogenesis Source: MGI
  • male gonad development Source: MGI
  • mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
  • mitochondrial fusion Source: UniProtKB
  • mitochondrion morphogenesis Source: MGI
  • myeloid cell homeostasis Source: MGI
  • negative regulation of apoptotic signaling pathway Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of endoplasmic reticulum calcium ion concentration Source: MGI
  • negative regulation of fibroblast proliferation Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • negative regulation of peptidyl-serine phosphorylation Source: MGI
  • negative regulation of protein binding Source: UniProtKB
  • nervous system development Source: MGI
  • neuron apoptotic process Source: MGI
  • neuron migration Source: MGI
  • odontogenesis of dentin-containing tooth Source: MGI
  • outer mitochondrial membrane organization Source: Ensembl
  • ovarian follicle development Source: MGI
  • positive regulation of apoptotic DNA fragmentation Source: MGI
  • positive regulation of apoptotic process Source: MGI
  • positive regulation of apoptotic process involved in mammary gland involution Source: MGI
  • positive regulation of B cell apoptotic process Source: MGI
  • positive regulation of calcium ion transport into cytosol Source: MGI
  • positive regulation of developmental pigmentation Source: MGI
  • positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • positive regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
  • positive regulation of neuron apoptotic process Source: MGI
  • positive regulation of protein oligomerization Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  • positive regulation of release of sequestered calcium ion into cytosol Source: MGI
  • post-embryonic camera-type eye morphogenesis Source: MGI
  • post-embryonic development Source: MGI
  • protein homooligomerization Source: MGI
  • protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: MGI
  • protein oligomerization Source: MGI
  • regulation of cell cycle Source: MGI
  • regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • regulation of mammary gland epithelial cell proliferation Source: MGI
  • regulation of mitochondrial membrane permeability involved in apoptotic process Source: MGI
  • regulation of mitochondrial membrane permeability involved in programmed necrotic cell death Source: MGI
  • regulation of neuron apoptotic process Source: MGI
  • regulation of nitrogen utilization Source: MGI
  • regulation of protein heterodimerization activity Source: MGI
  • regulation of protein homodimerization activity Source: UniProtKB
  • release of cytochrome c from mitochondria Source: MGI
  • release of matrix enzymes from mitochondria Source: UniProtKB
  • response to axon injury Source: MGI
  • response to cocaine Source: Ensembl
  • response to copper ion Source: Ensembl
  • response to corticosterone Source: Ensembl
  • response to drug Source: Ensembl
  • response to gamma radiation Source: MGI
  • response to ionizing radiation Source: MGI
  • response to salt stress Source: MGI
  • response to toxic substance Source: MGI
  • response to wounding Source: MGI
  • retina development in camera-type eye Source: MGI
  • retinal cell apoptotic process Source: UniProtKB
  • retinal cell programmed cell death Source: MGI
  • Sertoli cell proliferation Source: MGI
  • sex differentiation Source: MGI
  • spermatid differentiation Source: MGI
  • spermatogenesis Source: MGI
  • T cell homeostatic proliferation Source: MGI
  • thymocyte apoptotic process Source: MGI
  • transformed cell apoptotic process Source: UniProtKB
  • vagina development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiREACT_340204. Activation, translocation and oligomerization of BAX.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis regulator BAX
Gene namesi
Name:Bax
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:99702. Bax.

Subcellular locationi

Isoform Alpha :
  • Mitochondrion outer membrane By similarity; Single-pass membrane protein By similarity
  • Cytoplasm By similarity

  • Note: Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane (By similarity).By similarity
Isoform Beta :
Isoform Gamma :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei172 – 19221HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • BAX complex Source: UniProtKB
  • Bcl-2 family protein complex Source: UniProtKB
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • endoplasmic reticulum Source: MGI
  • endoplasmic reticulum membrane Source: UniProtKB
  • extracellular exosome Source: MGI
  • integral component of membrane Source: MGI
  • intracellular Source: MGI
  • membrane Source: MGI
  • mitochondrial membrane Source: MGI
  • mitochondrial outer membrane Source: MGI
  • mitochondrial permeability transition pore complex Source: UniProtKB
  • mitochondrion Source: ParkinsonsUK-UCL
  • nuclear envelope Source: MGI
  • nucleus Source: UniProtKB
  • pore complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Apoptosis regulator BAXPRO_0000143057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ07813.
PaxDbiQ07813.
PRIDEiQ07813.

PTM databases

PhosphoSiteiQ07813.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues.

Gene expression databases

BgeeiQ07813.
CleanExiMM_BAX.
ExpressionAtlasiQ07813. baseline and differential.
GenevisibleiQ07813. MM.

Interactioni

Subunit structurei

Homodimer. Forms higher oligomers under stress conditions. Interacts with BCL2L11. Interaction with BCL2L11 promotes BAX oligomerization and association with mitochondrial membranes, with subsequent release of cytochrome c. Forms heterodimers with BCL2, E1B 19K protein, BCL2L1 isoform Bcl-X(L), BCL2L2, MCL1 and A1. Interacts with SH3GLB1 and HN. Interacts with SFN and YWHAZ; the interaction occurs in the cytoplasm. Under stress conditions, JNK-mediated phosphorylation of SFN and YWHAZ, releases BAX to mitochondria. Interacts with RNF144B, which regulates the ubiquitin-dependent stability of BAX. Interacts with CLU under stress conditions that cause a conformation change leading to BAX oligomerization and association with mitochondria. Does not interact with CLU in unstressed cells (By similarity). Interacts with FAIM2/LFG2 (By similarity). Interacts with BOP (By similarity). Interacts (via a C-terminal 33 residues) with NOL3 (via CARD domain); inhibits BAX activation and translocationand consequently cytochrome c release from mitochondria.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Bcl2P104172EBI-700711,EBI-526314
ERN1O754602EBI-700711,EBI-371750From a different organism.

Protein-protein interaction databases

BioGridi198304. 21 interactions.
DIPiDIP-29541N.
IntActiQ07813. 9 interactions.
MINTiMINT-1517262.
STRINGi10090.ENSMUSP00000033093.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 8022Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XA0X-ray2.70C/D52-82[»]
ProteinModelPortaliQ07813.
SMRiQ07813. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi59 – 7315BH3Add
BLAST
Motifi98 – 11821BH1Add
BLAST
Motifi150 – 16516BH2Add
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.By similarity

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46695.
GeneTreeiENSGT00730000111112.
HOGENOMiHOG000095178.
HOVERGENiHBG003606.
InParanoidiQ07813.
KOiK02159.
OMAiADMFADG.
OrthoDBiEOG70GMGD.
PhylomeDBiQ07813.
TreeFamiTF315834.

Family and domain databases

InterProiIPR026304. BAX.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF8. PTHR11256:SF8. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
[Graphical view]
PRINTSiPR01862. BCL2FAMILY.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: Q07813-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDGSGEQLGS GGPTSSEQIM KTGAFLLQGF IQDRAGRMAG ETPELTLEQP
60 70 80 90 100
PQDASTKKLS ECLRRIGDEL DSNMELQRMI ADVDTDSPRE VFFRVAADMF
110 120 130 140 150
ADGNFNWGRV VALFYFASKL VLKALCTKVP ELIRTIMGWT LDFLRERLLV
160 170 180 190
WIQDQGGWEG LLSYFGTPTW QTVTIFVAGV LTASLTIWKK MG
Length:192
Mass (Da):21,395
Last modified:February 1, 1995 - v1
Checksum:iD2E0B3566579FAFF
GO
Isoform Beta (identifier: Q07813-2)

Sequence is not available
Length:
Mass (Da):
Isoform Gamma (identifier: Q07813-3)

Sequence is not available
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22472 mRNA. Translation: AAA03622.1.
BC018228 mRNA. Translation: AAH18228.1.
BC053380 mRNA. Translation: AAH53380.1.
CCDSiCCDS21246.1. [Q07813-1]
PIRiD47538.
RefSeqiNP_031553.1. NM_007527.3. [Q07813-1]
UniGeneiMm.19904.

Genome annotation databases

EnsembliENSMUST00000033093; ENSMUSP00000033093; ENSMUSG00000003873. [Q07813-1]
GeneIDi12028.
KEGGimmu:12028.
UCSCiuc009gvh.1. mouse. [Q07813-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22472 mRNA. Translation: AAA03622.1.
BC018228 mRNA. Translation: AAH18228.1.
BC053380 mRNA. Translation: AAH53380.1.
CCDSiCCDS21246.1. [Q07813-1]
PIRiD47538.
RefSeqiNP_031553.1. NM_007527.3. [Q07813-1]
UniGeneiMm.19904.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XA0X-ray2.70C/D52-82[»]
ProteinModelPortaliQ07813.
SMRiQ07813. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198304. 21 interactions.
DIPiDIP-29541N.
IntActiQ07813. 9 interactions.
MINTiMINT-1517262.
STRINGi10090.ENSMUSP00000033093.

PTM databases

PhosphoSiteiQ07813.

Proteomic databases

MaxQBiQ07813.
PaxDbiQ07813.
PRIDEiQ07813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033093; ENSMUSP00000033093; ENSMUSG00000003873. [Q07813-1]
GeneIDi12028.
KEGGimmu:12028.
UCSCiuc009gvh.1. mouse. [Q07813-1]

Organism-specific databases

CTDi581.
MGIiMGI:99702. Bax.

Phylogenomic databases

eggNOGiNOG46695.
GeneTreeiENSGT00730000111112.
HOGENOMiHOG000095178.
HOVERGENiHBG003606.
InParanoidiQ07813.
KOiK02159.
OMAiADMFADG.
OrthoDBiEOG70GMGD.
PhylomeDBiQ07813.
TreeFamiTF315834.

Enzyme and pathway databases

ReactomeiREACT_340204. Activation, translocation and oligomerization of BAX.

Miscellaneous databases

ChiTaRSiBax. mouse.
NextBioi280259.
PROiQ07813.
SOURCEiSearch...

Gene expression databases

BgeeiQ07813.
CleanExiMM_BAX.
ExpressionAtlasiQ07813. baseline and differential.
GenevisibleiQ07813. MM.

Family and domain databases

InterProiIPR026304. BAX.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR026298. Blc2_fam.
[Graphical view]
PANTHERiPTHR11256. PTHR11256. 1 hit.
PTHR11256:SF8. PTHR11256:SF8. 1 hit.
PfamiPF00452. Bcl-2. 1 hit.
[Graphical view]
PRINTSiPR01862. BCL2FAMILY.
PROSITEiPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death."
    Oltvai Z.N., Milliman C.L., Korsmeyer S.J.
    Cell 74:609-619(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BCL2, FUNCTION.
    Strain: C57BL/6 X DBA/2.
  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: FVB/N-3.
    Tissue: Mammary tumor.
  3. "Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions."
    Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B., Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.
    Mol. Cell 15:901-912(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL3.
  4. "Evidence that inhibition of BAX activation by BCL-2 involves its tight and preferential interaction with the BH3 domain of BAX."
    Ku B., Liang C., Jung J.U., Oh B.H.
    Cell Res. 21:627-641(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 52-82 IN COMPLEX WITH BCL2, FUNCTION, INTERACTION WITH BCL2 AND BCL2L2.

Entry informationi

Entry nameiBAX_MOUSE
AccessioniPrimary (citable) accession number: Q07813
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 22, 2015
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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

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 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.