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Protein

Apoptosis regulator BAX

Gene

BAX

Organism
Homo sapiens (Human)
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.6 Publications

GO - Molecular functioni

  • BH3 domain binding Source: UniProtKB
  • channel activity Source: BHF-UCL
  • identical protein binding Source: IntAct
  • lipid binding Source: HGNC
  • protein heterodimerization activity Source: HGNC
  • protein homodimerization activity Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_584. Activation, translocation and oligomerization of BAX.

Protein family/group databases

TCDBi1.A.21.1.2. the bcl-2 (bcl-2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis regulator BAX
Alternative name(s):
Bcl-2-like protein 4
Short name:
Bcl2-L-4
Gene namesi
Name:BAX
Synonyms:BCL2L4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:959. BAX.

Subcellular locationi

Isoform Alpha :

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
  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: HGNC
  • endoplasmic reticulum membrane Source: HGNC
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrial outer membrane Source: GO_Central
  • mitochondrial permeability transition pore complex Source: HGNC
  • mitochondrion Source: UniProtKB
  • nuclear envelope Source: AgBase
  • nucleus Source: UniProtKB
  • pore complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211K → E: Reduces interaction with BCL2L11, homooligomerization and triggering of apoptosis. 1 Publication
Mutagenesisi74 – 741M → D or E: Strongly reduced interaction with MCL1, BCL2, BCL2L1 and BCL2L2. No effect on cytochrome c release and subsequent apoptosis triggered by etoposide. 1 Publication
Mutagenesisi184 – 1841S → D, E, H or K: Constitutive cytoplasmic location. 1 Publication
Mutagenesisi184 – 1841S → V: Constitutive mitochondrial location. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA25269.

Polymorphism and mutation databases

BioMutaiBAX.
DMDMi728945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Apoptosis regulator BAXPRO_0000143053Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ07812.
PaxDbiQ07812.
PRIDEiQ07812.

PTM databases

PhosphoSiteiQ07812.

Miscellaneous databases

PMAP-CutDBQ07812.

Expressioni

Tissue specificityi

Expressed in a wide variety of tissues. Isoform Psi is found in glial tumors. Isoform Alpha is expressed in spleen, breast, ovary, testis, colon and brain, and at low levels in skin and lung. Isoform Sigma is expressed in spleen, breast, ovary, testis, lung, colon, brain and at low levels in skin. Isoform Alpha and isoform Sigma are expressed in pro-myelocytic leukemia, histiocytic lymphoma, Burkitt's lymphoma, T-cell lymphoma, lymphoblastic leukemia, breast adenocarcinoma, ovary adenocarcinoma, prostate carcinoma, prostate adenocarcinoma, lung carcinoma, epidermoid carcinoma, small cell lung carcinoma and colon adenocarcinoma cell lines.2 Publications

Gene expression databases

BgeeiQ07812.
CleanExiHS_BAX.
ExpressionAtlasiQ07812. baseline and differential.
GenevestigatoriQ07812.

Organism-specific databases

HPAiCAB004206.
HPA027878.

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. Isoform Sigma interacts with BCL2A1 and BCL2L1 isoform Bcl-X(L). 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. Interacts with FAIM2/LFG2. Interacts with human cytomegalovirus/HHV-5 protein vMIA/UL37. Interacts with BOP/C22orf29. Interacts (via a C-terminal 33 residues) with NOL3 (via CARD domain); inhibits BAX activation and translocation and consequently cytochrome c release from mitochondria.15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself27EBI-516580,EBI-516580
P266623EBI-516580,EBI-9099462From a different organism.
BAK1Q166115EBI-516580,EBI-519866
BCL2P104159EBI-516580,EBI-77694
BCL2L1Q078174EBI-516580,EBI-78035
BCL2L1Q07817-113EBI-516580,EBI-287195
BCL2L11O4352119EBI-516580,EBI-526406
BCL2L2Q928433EBI-516580,EBI-707714
BIDP5595716EBI-516580,EBI-519672
BidP704442EBI-516580,EBI-2128640From a different organism.
ERN1O754602EBI-516580,EBI-371750
MCL1Q078206EBI-516580,EBI-1003422
Mcl1P972872EBI-516580,EBI-707292From a different organism.
PYCARDQ9ULZ37EBI-516580,EBI-751215
RNF144BQ7Z4195EBI-516580,EBI-2129982
SH3GLB1Q9Y371-12EBI-516580,EBI-5291808
TOM22P493343EBI-516580,EBI-12527From a different organism.
TOM40P236442EBI-516580,EBI-12539From a different organism.
tom40P243912EBI-516580,EBI-1791540From a different organism.
TOM70P072132EBI-516580,EBI-12551From a different organism.
UVRAGQ9P2Y56EBI-516580,EBI-2952704
VACWR028P173613EBI-516580,EBI-7115640From a different organism.
XRCC6P129562EBI-516580,EBI-353208

Protein-protein interaction databases

BioGridi107057. 51 interactions.
DIPiDIP-232N.
IntActiQ07812. 39 interactions.
MINTiMINT-134330.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 43Combined sources
Beta strandi10 – 145Combined sources
Helixi16 – 3621Combined sources
Beta strandi43 – 453Combined sources
Helixi54 – 7219Combined sources
Helixi74 – 829Combined sources
Helixi88 – 9912Combined sources
Turni100 – 1023Combined sources
Helixi107 – 14741Combined sources
Helixi149 – 1546Combined sources
Turni155 – 1584Combined sources
Helixi159 – 1646Combined sources
Helixi171 – 18818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F16NMR-A1-192[»]
2G5BX-ray2.30I/J/K/L13-19[»]
2K7WNMR-A1-192[»]
2LR1NMR-A1-192[»]
3PK1X-ray2.49B/D48-81[»]
3PL7X-ray2.61C48-81[»]
4BD2X-ray2.21A1-171[»]
4BD6X-ray2.49A1-171[»]
C48-81[»]
4BD7X-ray2.80A/B/C/D1-171[»]
4BD8X-ray2.22A/B/C/D1-171[»]
4BDUX-ray3.00A/B/C/D53-128[»]
ProteinModelPortaliQ07812.
SMRiQ07812. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07812.

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.
HOVERGENiHBG003606.
InParanoidiQ07812.
KOiK02159.
OMAiADMFADG.
PhylomeDBiQ07812.
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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: Q07812-1) [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
MDGSGEQPRG GGPTSSEQIM KTGALLLQGF IQDRAGRMGG EAPELALDPV
60 70 80 90 100
PQDASTKKLS ECLKRIGDEL DSNMELQRMI AAVDTDSPRE VFFRVAADMF
110 120 130 140 150
SDGNFNWGRV VALFYFASKL VLKALCTKVP ELIRTIMGWT LDFLRERLLG
160 170 180 190
WIQDQGGWDG LLSYFGTPTW QTVTIFVAGV LTASLTIWKK MG
Length:192
Mass (Da):21,184
Last modified:February 1, 1995 - v1
Checksum:i6C0CDB0A7DEE4994
GO
Isoform Beta (identifier: Q07812-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-192: DGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG → VRLLKPPHPH...VVYNAFSLRV

Show »
Length:218
Mass (Da):24,220
Checksum:iF69DCD70F960192F
GO
Isoform Gamma (identifier: Q07812-3) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     12-41: GPTSSEQIMKTGALLLQGFIQDRAGRMGGE → VSSRIEQGEWGGRHPSWPWTRCLRMRPPRS
     42-192: Missing.

Show »
Length:41
Mass (Da):4,678
Checksum:iD94639AABB927859
GO
Isoform Delta (identifier: Q07812-4) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     30-78: Missing.

Show »
Length:143
Mass (Da):15,772
Checksum:iBADE4D71D06A75AB
GO
Isoform Epsilon (identifier: Q07812-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     125-192: LCTKVPELIR...ASLTIWKKMG → GVKWRDLGSL...YRPCAPRCRN

Show »
Length:164
Mass (Da):18,129
Checksum:i12CCDB8073EF4C9E
GO
Isoform Zeta (identifier: Q07812-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.

Show »
Length:114
Mass (Da):12,887
Checksum:iA9DAFC5C06E36F4A
GO
Isoform Psi (identifier: Q07812-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.

Show »
Length:173
Mass (Da):19,312
Checksum:i266F3151438B6201
GO
Isoform Sigma (identifier: Q07812-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-171: Missing.

Show »
Length:179
Mass (Da):19,718
Checksum:i5802B0AC73B2E4CE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111G → E in a plasmacytoma cell line. 1 Publication
VAR_013575
Natural varianti39 – 391G → R.
Corresponds to variant rs36017265 [ dbSNP | Ensembl ].
VAR_047053
Natural varianti67 – 671G → R in a T-cell acute lymphoblastic leukemia cell line; loss of heterodimerization with Bcl-2 or Bcl-X(L). 2 Publications
VAR_007809
Natural varianti108 – 1081G → V in a Burkitt lymphoma; loss of homodimerization. 2 Publications
VAR_013576

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7878Missing in isoform Zeta. 1 PublicationVSP_031239Add
BLAST
Alternative sequencei1 – 1919Missing in isoform Psi. 1 PublicationVSP_031238Add
BLAST
Alternative sequencei12 – 4130GPTSS…RMGGE → VSSRIEQGEWGGRHPSWPWT RCLRMRPPRS in isoform Gamma. 1 PublicationVSP_031234Add
BLAST
Alternative sequencei30 – 7849Missing in isoform Delta. 1 PublicationVSP_031235Add
BLAST
Alternative sequencei42 – 192151Missing in isoform Gamma. 1 PublicationVSP_031236Add
BLAST
Alternative sequencei125 – 19268LCTKV…WKKMG → GVKWRDLGSLQPLPPGFKRF TCLSIPRSWDYRPCAPRCRN in isoform Epsilon. 1 PublicationVSP_031240Add
BLAST
Alternative sequencei159 – 19234DGLLS…WKKMG → VRLLKPPHPHHRALTTAPAP PSLPPATPLGPWAFWSRSQW CPLPIFRSSDVVYNAFSLRV in isoform Beta. 1 PublicationVSP_031237Add
BLAST
Alternative sequencei159 – 17113Missing in isoform Sigma. 1 PublicationVSP_037475Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22473 mRNA. Translation: AAA03619.1.
L22474 mRNA. Translation: AAA03620.1.
L22475 mRNA. Translation: AAA03621.1.
U19599 mRNA. Translation: AAC50142.1.
AF007826 mRNA. Translation: AAD22706.1.
AF247393 mRNA. Translation: AAF71267.1.
AJ417988 mRNA. Translation: CAD10744.1.
AF250190 mRNA. Translation: AAF82094.1.
AK291076 mRNA. Translation: BAF83765.1.
AY217036 Genomic DNA. Translation: AAO22992.1.
CH471177 Genomic DNA. Translation: EAW52418.1.
CH471177 Genomic DNA. Translation: EAW52417.1.
BC014175 mRNA. Translation: AAH14175.1.
CCDSiCCDS12742.1. [Q07812-1]
CCDS12743.1. [Q07812-4]
CCDS12744.1. [Q07812-2]
CCDS12745.2. [Q07812-8]
PIRiA47538.
B47538.
C47538.
I38921.
JC7255.
RefSeqiNP_001278357.1. NM_001291428.1.
NP_001278360.1. NM_001291431.1. [Q07812-6]
NP_004315.1. NM_004324.3. [Q07812-2]
NP_620116.1. NM_138761.3. [Q07812-1]
NP_620118.1. NM_138763.3. [Q07812-4]
NP_620119.2. NM_138764.4. [Q07812-8]
UniGeneiHs.624291.

Genome annotation databases

EnsembliENST00000293288; ENSP00000293288; ENSG00000087088. [Q07812-2]
ENST00000345358; ENSP00000263262; ENSG00000087088. [Q07812-1]
ENST00000354470; ENSP00000346461; ENSG00000087088. [Q07812-4]
ENST00000356483; ENSP00000348871; ENSG00000087088. [Q07812-5]
ENST00000415969; ENSP00000389971; ENSG00000087088. [Q07812-8]
ENST00000515540; ENSP00000426328; ENSG00000087088. [Q07812-3]
GeneIDi581.
KEGGihsa:581.
UCSCiuc002plf.1. human. [Q07812-2]
uc002plj.3. human. [Q07812-8]
uc002plk.3. human. [Q07812-1]
uc002pll.3. human. [Q07812-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22473 mRNA. Translation: AAA03619.1.
L22474 mRNA. Translation: AAA03620.1.
L22475 mRNA. Translation: AAA03621.1.
U19599 mRNA. Translation: AAC50142.1.
AF007826 mRNA. Translation: AAD22706.1.
AF247393 mRNA. Translation: AAF71267.1.
AJ417988 mRNA. Translation: CAD10744.1.
AF250190 mRNA. Translation: AAF82094.1.
AK291076 mRNA. Translation: BAF83765.1.
AY217036 Genomic DNA. Translation: AAO22992.1.
CH471177 Genomic DNA. Translation: EAW52418.1.
CH471177 Genomic DNA. Translation: EAW52417.1.
BC014175 mRNA. Translation: AAH14175.1.
CCDSiCCDS12742.1. [Q07812-1]
CCDS12743.1. [Q07812-4]
CCDS12744.1. [Q07812-2]
CCDS12745.2. [Q07812-8]
PIRiA47538.
B47538.
C47538.
I38921.
JC7255.
RefSeqiNP_001278357.1. NM_001291428.1.
NP_001278360.1. NM_001291431.1. [Q07812-6]
NP_004315.1. NM_004324.3. [Q07812-2]
NP_620116.1. NM_138761.3. [Q07812-1]
NP_620118.1. NM_138763.3. [Q07812-4]
NP_620119.2. NM_138764.4. [Q07812-8]
UniGeneiHs.624291.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F16NMR-A1-192[»]
2G5BX-ray2.30I/J/K/L13-19[»]
2K7WNMR-A1-192[»]
2LR1NMR-A1-192[»]
3PK1X-ray2.49B/D48-81[»]
3PL7X-ray2.61C48-81[»]
4BD2X-ray2.21A1-171[»]
4BD6X-ray2.49A1-171[»]
C48-81[»]
4BD7X-ray2.80A/B/C/D1-171[»]
4BD8X-ray2.22A/B/C/D1-171[»]
4BDUX-ray3.00A/B/C/D53-128[»]
ProteinModelPortaliQ07812.
SMRiQ07812. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107057. 51 interactions.
DIPiDIP-232N.
IntActiQ07812. 39 interactions.
MINTiMINT-134330.

Chemistry

ChEMBLiCHEMBL5318.

Protein family/group databases

TCDBi1.A.21.1.2. the bcl-2 (bcl-2) family.

PTM databases

PhosphoSiteiQ07812.

Polymorphism and mutation databases

BioMutaiBAX.
DMDMi728945.

Proteomic databases

MaxQBiQ07812.
PaxDbiQ07812.
PRIDEiQ07812.

Protocols and materials databases

DNASUi581.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000293288; ENSP00000293288; ENSG00000087088. [Q07812-2]
ENST00000345358; ENSP00000263262; ENSG00000087088. [Q07812-1]
ENST00000354470; ENSP00000346461; ENSG00000087088. [Q07812-4]
ENST00000356483; ENSP00000348871; ENSG00000087088. [Q07812-5]
ENST00000415969; ENSP00000389971; ENSG00000087088. [Q07812-8]
ENST00000515540; ENSP00000426328; ENSG00000087088. [Q07812-3]
GeneIDi581.
KEGGihsa:581.
UCSCiuc002plf.1. human. [Q07812-2]
uc002plj.3. human. [Q07812-8]
uc002plk.3. human. [Q07812-1]
uc002pll.3. human. [Q07812-4]

Organism-specific databases

CTDi581.
GeneCardsiGC19P049458.
HGNCiHGNC:959. BAX.
HPAiCAB004206.
HPA027878.
MIMi600040. gene.
neXtProtiNX_Q07812.
PharmGKBiPA25269.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG46695.
GeneTreeiENSGT00730000111112.
HOVERGENiHBG003606.
InParanoidiQ07812.
KOiK02159.
OMAiADMFADG.
PhylomeDBiQ07812.
TreeFamiTF315834.

Enzyme and pathway databases

ReactomeiREACT_584. Activation, translocation and oligomerization of BAX.

Miscellaneous databases

ChiTaRSiBAX. human.
EvolutionaryTraceiQ07812.
GeneWikiiBcl-2-associated_X_protein.
GenomeRNAii581.
NextBioi2371.
PMAP-CutDBQ07812.
PROiQ07812.
SOURCEiSearch...

Gene expression databases

BgeeiQ07812.
CleanExiHS_BAX.
ExpressionAtlasiQ07812. baseline and differential.
GenevestigatoriQ07812.

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] (ISOFORMS ALPHA; BETA AND GAMMA), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    Tissue: B-cell.
  2. "Mapping of the human BAX gene to chromosome 19q13.3-q13.4 and isolation of a novel alternatively spliced transcript, BAX delta."
    Apte S.S., Mattei M.-G., Olsen B.R.
    Genomics 26:592-594(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
  3. "Identification and characterization of baxepsilon, a novel bax variant missing the BH2 and the transmembrane domains."
    Shi B., Triebe D., Kajiji S., Iwata K.K., Bruskin A., Mahajna J.
    Biochem. Biophys. Res. Commun. 254:779-785(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON).
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND SIGMA), FUNCTION, INTERACTION WITH BCL2A1 AND BCL2L1, TISSUE SPECIFICITY.
  5. "The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patients."
    Cartron P.F., Oliver L., Martin S., Moreau C., LeCabellec M.T., Jezequel P., Meflah K., Vallette F.M.
    Hum. Mol. Genet. 11:675-687(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSI), TISSUE SPECIFICITY.
  6. "Bax mRNA splice variant lacking exons 2 and 3."
    Perez R.P., Sanville H.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA).
    Tissue: Ovarian carcinoma.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
  8. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM ALPHA).
    Tissue: Skin.
  11. "Bax mutations in cell lines derived from hematological malignancies."
    Meijerink J.P.P., Smetsers T.F.C.M., Sloetjes A.W., Linders E.H.P., Mensink E.J.B.M.
    Leukemia 9:1828-1832(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-77 AND 98-118, VARIANTS ARG-67 AND VAL-108.
  12. "A conserved domain in Bak, distinct from BH1 and BH2, mediates cell death and protein binding functions."
    Chittenden T., Flemington C., Houghton A.B., Ebb R.G., Gallo G.J., Elangovan B., Chinnadurai G., Lutz R.J.
    EMBO J. 14:5589-5596(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, FUNCTION OF BH3 MOTIF.
  13. "Conformation of the Bax C-terminus regulates subcellular location and cell death."
    Nechushtan A., Smith C.L., Hsu Y.-T., Youle R.J.
    EMBO J. 18:2330-2341(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF SER-184.
  14. "Molecular cloning and characterization of Bif-1. A novel Src homology 3 domain-containing protein that associates with Bax."
    Cuddeback S.M., Yamaguchi H., Komatsu K., Miyashita T., Yamada M., Wu C., Singh S., Wang H.-G.
    J. Biol. Chem. 276:20559-20565(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH3GLB1.
  15. "Humanin peptide suppresses apoptosis by interfering with Bax activation."
    Guo B., Zhai D., Cabezas E., Welsh K., Nouraini S., Satterthwait A.C., Reed J.C.
    Nature 423:456-461(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HN.
  16. "JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins."
    Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S., Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.
    EMBO J. 23:1889-1899(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SFN AND YWHAZ, SUBCELLULAR LOCATION.
  17. "Apoptosis repressor with caspase recruitment domain protects against cell death by interfering with Bax activation."
    Gustafsson A.B., Tsai J.G., Logue S.E., Crow M.T., Gottlieb R.A.
    J. Biol. Chem. 279:21233-21238(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOL3.
  18. Cited for: INTERACTION WITH HHV-5 PROTEIN UL37.
  19. "Clusterin inhibits apoptosis by interacting with activated Bax."
    Zhang H., Kim J.K., Edwards C.A., Xu Z., Taichman R., Wang C.Y.
    Nat. Cell Biol. 7:909-915(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLU.
  20. "Sequence analysis shows that Lifeguard belongs to a new evolutionarily conserved cytoprotective family."
    Reimers K., Choi C.Y., Mau-Thek E., Vogt P.M.
    Int. J. Mol. Med. 18:729-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FAIM2/LFG2.
  21. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation."
    Benard G., Neutzner A., Peng G., Wang C., Livak F., Youle R.J., Karbowski M.
    EMBO J. 29:1458-1471(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF144B.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Human Bop is a novel BH3-only member of the Bcl-2 protein family."
    Zhang X., Weng C., Li Y., Wang X., Jiang C., Li X., Xu Y., Chen Q., Pan L., Tang H.
    Protein Cell 3:790-801(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BOP/C22ORF29.
  25. "Structure of Bax: coregulation of dimer formation and intracellular localization."
    Suzuki M., Youle R.J., Tjandra N.
    Cell 103:645-654(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION, SUBUNIT.
  26. "Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex."
    Peyerl F.W., Dai S., Murphy G.A., Crawford F., White J., Marrack P., Kappler J.W.
    Cell Death Differ. 14:447-452(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-19 IN COMPLEX WITH ANTIBODY FRAGMENT.
  27. Cited for: STRUCTURE BY NMR IN COMPLEX WITH BCL2L11, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-21, INTERACTION WITH BCL2L11.
  28. "Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis."
    Czabotar P.E., Lee E.F., Thompson G.V., Wardak A.Z., Fairlie W.D., Colman P.M.
    J. Biol. Chem. 286:7123-7131(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 48-81 IN COMPLEXES WITH BCL2L1 AND MCL1, INTERACTION WITH MCL1; BCL2; BCL2L1 AND BCL2L2, FUNCTION, MUTAGENESIS OF MET-74.
  29. "Hematopoietic malignancies demonstrate loss-of-function mutations of BAX."
    Meijerink J.P.P., Mensink E.J.B.M., Wang K., Sedlak T.W., Sloetjes A.W., de Witte T., Waksman G., Korsmeyer S.J.
    Blood 91:2991-2997(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GLU-11; ARG-67 AND VAL-108.

Entry informationi

Entry nameiBAX_HUMAN
AccessioniPrimary (citable) accession number: Q07812
Secondary accession number(s): A8K4W1
, P55269, Q07814, Q07815, Q8WZ49, Q9NR76, Q9NYG7, Q9UCZ6, Q9UCZ7, Q9UQD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 27, 2015
This is version 168 of the entry and version 1 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

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.