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Q07812

- BAX_HUMAN

UniProt

Q07812 - BAX_HUMAN

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Protein

Apoptosis regulator BAX

Gene
BAX, BCL2L4
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. BH3 domain binding Source: UniProtKB
  2. channel activity Source: BHF-UCL
  3. identical protein binding Source: IntAct
  4. lipid binding Source: HGNC
  5. protein binding Source: UniProtKB
  6. protein heterodimerization activity Source: HGNC
  7. protein homodimerization activity Source: HGNC

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Source: HGNC
  3. activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: Ensembl
  4. apoptotic mitochondrial changes Source: HGNC
  5. apoptotic process Source: UniProtKB
  6. apoptotic process involved in embryonic digit morphogenesis Source: Ensembl
  7. apoptotic process involved in patterning of blood vessels Source: Ensembl
  8. apoptotic signaling pathway Source: HGNC
  9. B cell apoptotic process Source: HGNC
  10. B cell homeostasis Source: Ensembl
  11. B cell homeostatic proliferation Source: Ensembl
  12. B cell negative selection Source: Ensembl
  13. B cell receptor apoptotic signaling pathway Source: BHF-UCL
  14. blood vessel remodeling Source: Ensembl
  15. cellular response to organic substance Source: Ensembl
  16. cellular response to UV Source: Ensembl
  17. cerebral cortex development Source: Ensembl
  18. development of secondary sexual characteristics Source: Ensembl
  19. ectopic germ cell programmed cell death Source: Ensembl
  20. endoplasmic reticulum calcium ion homeostasis Source: UniProtKB
  21. establishment or maintenance of transmembrane electrochemical gradient Source: HGNC
  22. extrinsic apoptotic signaling pathway Source: BHF-UCL
  23. extrinsic apoptotic signaling pathway in absence of ligand Source: RefGenome
  24. extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  25. fertilization Source: Ensembl
  26. germ cell development Source: Ensembl
  27. glycosphingolipid metabolic process Source: Ensembl
  28. homeostasis of number of cells within a tissue Source: Ensembl
  29. hypothalamus development Source: Ensembl
  30. intrinsic apoptotic signaling pathway Source: BHF-UCL
  31. intrinsic apoptotic signaling pathway by p53 class mediator Source: Ensembl
  32. intrinsic apoptotic signaling pathway in response to DNA damage Source: RefGenome
  33. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  34. kidney development Source: Ensembl
  35. mitochondrial fragmentation involved in apoptotic process Source: HGNC
  36. mitochondrial fusion Source: HGNC
  37. myeloid cell homeostasis Source: Ensembl
  38. negative regulation of apoptotic signaling pathway Source: Ensembl
  39. negative regulation of endoplasmic reticulum calcium ion concentration Source: Ensembl
  40. negative regulation of fibroblast proliferation Source: Ensembl
  41. negative regulation of neuron apoptotic process Source: Ensembl
  42. negative regulation of peptidyl-serine phosphorylation Source: Ensembl
  43. negative regulation of protein binding Source: UniProtKB
  44. neuron apoptotic process Source: Ensembl
  45. neuron migration Source: Ensembl
  46. nuclear fragmentation involved in apoptotic nuclear change Source: Ensembl
  47. odontogenesis of dentin-containing tooth Source: Ensembl
  48. ovarian follicle development Source: Ensembl
  49. positive regulation of apoptotic DNA fragmentation Source: BHF-UCL
  50. positive regulation of apoptotic process Source: UniProtKB
  51. positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
  52. positive regulation of B cell apoptotic process Source: Ensembl
  53. positive regulation of developmental pigmentation Source: Ensembl
  54. positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  55. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  56. positive regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  57. positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway Source: Reactome
  58. positive regulation of neuron apoptotic process Source: HGNC
  59. positive regulation of protein oligomerization Source: UniProtKB
  60. positive regulation of release of cytochrome c from mitochondria Source: UniProtKB
  61. positive regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  62. post-embryonic camera-type eye morphogenesis Source: Ensembl
  63. protein homooligomerization Source: UniProtKB
  64. protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Ensembl
  65. protein oligomerization Source: UniProtKB
  66. regulation of cell cycle Source: Ensembl
  67. regulation of mammary gland epithelial cell proliferation Source: Ensembl
  68. regulation of mitochondrial membrane potential Source: HGNC
  69. regulation of nitrogen utilization Source: Ensembl
  70. regulation of protein heterodimerization activity Source: HGNC
  71. regulation of protein homodimerization activity Source: HGNC
  72. release of cytochrome c from mitochondria Source: BHF-UCL
  73. release of matrix enzymes from mitochondria Source: HGNC
  74. response to acid Source: Ensembl
  75. response to axon injury Source: Ensembl
  76. response to gamma radiation Source: Ensembl
  77. response to salt stress Source: Ensembl
  78. response to toxic substance Source: HGNC
  79. retina development in camera-type eye Source: Ensembl
  80. retinal cell apoptotic process Source: HGNC
  81. retinal cell programmed cell death Source: Ensembl
  82. Sertoli cell proliferation Source: Ensembl
  83. spermatid differentiation Source: Ensembl
  84. T cell homeostatic proliferation Source: Ensembl
  85. thymocyte apoptotic process Source: Ensembl
  86. transformed cell apoptotic process Source: HGNC
  87. vagina development Source: Ensembl
  88. viral process Source: UniProtKB-KW
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: Chromosome 19

Organism-specific databases

HGNCiHGNC:959. BAX.

Subcellular locationi

Isoform Alpha : Mitochondrion membrane; Single-pass membrane protein. Cytoplasm
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.5 Publications
Isoform Beta : Cytoplasm 5 Publications
Isoform Gamma : Cytoplasm 5 Publications
Isoform Delta : Cytoplasm Reviewed prediction 5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei172 – 19221Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. BAX complex Source: UniProtKB
  2. Bcl-2 family protein complex Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. endoplasmic reticulum Source: HGNC
  5. endoplasmic reticulum membrane Source: HGNC
  6. extracellular vesicular exosome Source: UniProt
  7. mitochondrial outer membrane Source: RefGenome
  8. mitochondrial permeability transition pore complex Source: HGNC
  9. mitochondrion Source: UniProtKB
  10. nucleus Source: UniProtKB
  11. 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.

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

ArrayExpressiQ07812.
BgeeiQ07812.
CleanExiHS_BAX.
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/C22orf29.13 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
BCL2L1Q078173EBI-516580,EBI-78035
BCL2L1Q07817-113EBI-516580,EBI-287195
BCL2L11O4352119EBI-516580,EBI-526406
BCL2L2Q928433EBI-516580,EBI-707714
BIDP5595715EBI-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. 48 interactions.
DIPiDIP-232N.
IntActiQ07812. 34 interactions.
MINTiMINT-134330.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46695.
HOVERGENiHBG003606.
KOiK02159.
OMAiCWINNIC.
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. Align

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

MDGSGEQPRG GGPTSSEQIM KTGALLLQGF IQDRAGRMGG EAPELALDPV    50
PQDASTKKLS ECLKRIGDEL DSNMELQRMI AAVDTDSPRE VFFRVAADMF 100
SDGNFNWGRV VALFYFASKL VLKALCTKVP ELIRTIMGWT LDFLRERLLG 150
WIQDQGGWDG LLSYFGTPTW QTVTIFVAGV LTASLTIWKK MG 192
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. VSP_031239Add
BLAST
Alternative sequencei1 – 1919Missing in isoform Psi. VSP_031238Add
BLAST
Alternative sequencei12 – 4130GPTSS…RMGGE → VSSRIEQGEWGGRHPSWPWT RCLRMRPPRS in isoform Gamma. VSP_031234Add
BLAST
Alternative sequencei30 – 7849Missing in isoform Delta. VSP_031235Add
BLAST
Alternative sequencei42 – 192151Missing in isoform Gamma. VSP_031236Add
BLAST
Alternative sequencei125 – 19268LCTKV…WKKMG → GVKWRDLGSLQPLPPGFKRF TCLSIPRSWDYRPCAPRCRN in isoform Epsilon. VSP_031240Add
BLAST
Alternative sequencei159 – 19234DGLLS…WKKMG → VRLLKPPHPHHRALTTAPAP PSLPPATPLGPWAFWSRSQW CPLPIFRSSDVVYNAFSLRV in isoform Beta. VSP_031237Add
BLAST
Alternative sequencei159 – 17113Missing in isoform Sigma. VSP_037475Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
ENST00000391871; ENSP00000375744; ENSG00000087088. [Q07812-3]
ENST00000415969; ENSP00000389971; ENSG00000087088. [Q07812-8]
ENST00000515540; ENSP00000426328; ENSG00000087088. [Q07812-3]
ENST00000539787; ENSP00000441413; ENSG00000087088. [Q07812-5]
GeneIDi581.
KEGGihsa:581.
UCSCiuc002plf.1. human. [Q07812-2]
uc002plj.3. human. [Q07812-8]
uc002plk.3. human. [Q07812-1]
uc002pll.3. human. [Q07812-4]

Polymorphism databases

DMDMi728945.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS12742.1. [Q07812-1 ]
CCDS12743.1. [Q07812-4 ]
CCDS12744.1. [Q07812-2 ]
CCDS12745.2. [Q07812-8 ]
PIRi A47538.
B47538.
C47538.
I38921.
JC7255.
RefSeqi NP_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 ]
UniGenei Hs.624291.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F16 NMR - A 1-192 [» ]
2G5B X-ray 2.30 I/J/K/L 13-19 [» ]
2K7W NMR - A 1-192 [» ]
2LR1 NMR - A 1-192 [» ]
3PK1 X-ray 2.49 B/D 48-81 [» ]
3PL7 X-ray 2.61 C 48-81 [» ]
4BD2 X-ray 2.21 A 1-171 [» ]
4BD6 X-ray 2.49 A 1-171 [» ]
C 48-81 [» ]
4BD7 X-ray 2.80 A/B/C/D 1-171 [» ]
4BD8 X-ray 2.22 A/B/C/D 1-171 [» ]
4BDU X-ray 3.00 A/B/C/D 53-128 [» ]
ProteinModelPortali Q07812.
SMRi Q07812. Positions 1-192.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107057. 48 interactions.
DIPi DIP-232N.
IntActi Q07812. 34 interactions.
MINTi MINT-134330.

Chemistry

BindingDBi Q07812.
ChEMBLi CHEMBL5318.

Protein family/group databases

TCDBi 1.A.21.1.2. the bcl-2 (bcl-2) family.

PTM databases

PhosphoSitei Q07812.

Polymorphism databases

DMDMi 728945.

Proteomic databases

MaxQBi Q07812.
PaxDbi Q07812.
PRIDEi Q07812.

Protocols and materials databases

DNASUi 581.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293288 ; ENSP00000293288 ; ENSG00000087088 . [Q07812-2 ]
ENST00000345358 ; ENSP00000263262 ; ENSG00000087088 . [Q07812-1 ]
ENST00000354470 ; ENSP00000346461 ; ENSG00000087088 . [Q07812-4 ]
ENST00000356483 ; ENSP00000348871 ; ENSG00000087088 . [Q07812-5 ]
ENST00000391871 ; ENSP00000375744 ; ENSG00000087088 . [Q07812-3 ]
ENST00000415969 ; ENSP00000389971 ; ENSG00000087088 . [Q07812-8 ]
ENST00000515540 ; ENSP00000426328 ; ENSG00000087088 . [Q07812-3 ]
ENST00000539787 ; ENSP00000441413 ; ENSG00000087088 . [Q07812-5 ]
GeneIDi 581.
KEGGi hsa:581.
UCSCi uc002plf.1. human. [Q07812-2 ]
uc002plj.3. human. [Q07812-8 ]
uc002plk.3. human. [Q07812-1 ]
uc002pll.3. human. [Q07812-4 ]

Organism-specific databases

CTDi 581.
GeneCardsi GC19P049458.
HGNCi HGNC:959. BAX.
HPAi CAB004206.
HPA027878.
MIMi 600040. gene.
neXtProti NX_Q07812.
PharmGKBi PA25269.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46695.
HOVERGENi HBG003606.
KOi K02159.
OMAi CWINNIC.
PhylomeDBi Q07812.
TreeFami TF315834.

Enzyme and pathway databases

Reactomei REACT_584. Activation, translocation and oligomerization of BAX.

Miscellaneous databases

ChiTaRSi BAX. human.
EvolutionaryTracei Q07812.
GeneWikii Bcl-2-associated_X_protein.
GenomeRNAii 581.
NextBioi 2371.
PMAP-CutDB Q07812.
PROi Q07812.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q07812.
Bgeei Q07812.
CleanExi HS_BAX.
Genevestigatori Q07812.

Family and domain databases

InterProi IPR026304. BAX.
IPR002475. Bcl2-like.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
IPR026298. Blc2_fam.
[Graphical view ]
PANTHERi PTHR11256. PTHR11256. 1 hit.
PTHR11256:SF8. PTHR11256:SF8. 1 hit.
Pfami PF00452. Bcl-2. 1 hit.
[Graphical view ]
PRINTSi PR01862. BCL2FAMILY.
PROSITEi PS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. Cited for: INTERACTION WITH HHV-5 PROTEIN UL37.
  18. "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.
  19. "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.
  20. "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].
  21. "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.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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.
  24. "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.
  25. "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.
  26. Cited for: STRUCTURE BY NMR IN COMPLEX WITH BCL2L11, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-21, INTERACTION WITH BCL2L11.
  27. "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.
  28. "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: September 3, 2014
This is version 159 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

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