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Q07812

- BAX_HUMAN

UniProt

Q07812 - BAX_HUMAN

Protein

Apoptosis regulator BAX

Gene

BAX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    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 chemical 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

    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.

    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. membrane Source: UniProtKB
    8. mitochondrial outer membrane Source: RefGenome
    9. mitochondrial permeability transition pore complex Source: HGNC
    10. mitochondrion Source: UniProtKB
    11. nucleus Source: UniProtKB
    12. pore complex Source: BHF-UCL

    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. 2 Publications
    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. 2 Publications
    Mutagenesisi184 – 1841S → D, E, H or K: Constitutive cytoplasmic location. 2 Publications
    Mutagenesisi184 – 1841S → V: Constitutive mitochondrial location. 2 Publications

    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/C22orf29.14 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. 48 interactions.
    DIPiDIP-232N.
    IntActiQ07812. 36 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07812.

    Transmembrane

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

    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.
    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. 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:
    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. 36 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

    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: October 1, 2014
    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
    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