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Q07812 (BAX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apoptosis regulator BAX
Alternative name(s):
Bcl-2-like protein 4
Short name=Bcl2-L-4
Gene names
Name:BAX
Synonyms:BCL2L4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.12 Ref.17 Ref.23 Ref.24

Subunit structure

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. Ref.1 Ref.4 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.23 Ref.24

Subcellular location

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. Ref.1 Ref.13 Ref.16 Ref.17 Ref.21

Isoform Beta: Cytoplasm Ref.1 Ref.13 Ref.16 Ref.17 Ref.21.

Isoform Gamma: Cytoplasm Ref.1 Ref.13 Ref.16 Ref.17 Ref.21.

Isoform Delta: Cytoplasm Potential Ref.1 Ref.13 Ref.16 Ref.17 Ref.21.

Tissue specificity

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. Ref.4 Ref.5

Domain

Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family By similarity.

Sequence similarities

Belongs to the Bcl-2 family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   DomainTransmembrane
Transmembrane helix
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processB cell apoptosis

Inferred from direct assay. Source: HGNC

DNA fragmentation involved in apoptotic nuclear change

Inferred from mutant phenotype. Source: HGNC

activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c

Inferred from direct assay. Source: HGNC

activation of pro-apoptotic gene products

Traceable author statement. Source: Reactome

cleavage of lamin

Inferred from mutant phenotype. Source: HGNC

establishment or maintenance of transmembrane electrochemical gradient

Inferred from direct assay. Source: HGNC

induction of apoptosis by extracellular signals

Inferred from direct assay. Source: HGNC

induction of apoptosis by intracellular signals

Inferred from direct assay. Source: HGNC

induction of retinal programmed cell death

Inferred from mutant phenotype. Source: HGNC

mitochondrial fragmentation involved in apoptosis

Inferred from direct assay. Source: HGNC

mitochondrial fusion

Inferred from direct assay. Source: HGNC

negative regulation of protein binding

Inferred from direct assay. Source: UniProtKB

negative regulation of survival gene product expression

Inferred from direct assay. Source: HGNC

nuclear fragmentation involved in apoptotic nuclear change

Inferred from mutant phenotype. Source: HGNC

positive regulation of neuron apoptosis

Inferred from direct assay. Source: HGNC

protein homooligomerization

Inferred from direct assay. Source: HGNC

regulation of mitochondrial membrane potential

Inferred from direct assay. Source: HGNC

regulation of protein heterodimerization activity

Inferred from physical interaction. Source: HGNC

regulation of protein homodimerization activity

Inferred from direct assay. Source: HGNC

release of cytochrome c from mitochondria

Inferred from direct assay. Source: HGNC

release of matrix enzymes from mitochondria

Inferred from direct assay. Source: HGNC

response to toxin

Inferred from direct assay. Source: HGNC

transformed cell apoptosis

Inferred from mutant phenotype. Source: HGNC

   Cellular componentBcl-2 family protein complex

Inferred from direct assay Ref.24. Source: UniProtKB

cytosol

Inferred from direct assay. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from direct assay. Source: HGNC

mitochondrial outer membrane

Traceable author statement. Source: Reactome

mitochondrial permeability transition pore complex

Inferred from direct assay. Source: HGNC

nucleus

Inferred from mutant phenotype. Source: UniProtKB

   Molecular functionBH3 domain binding

Inferred from direct assay Ref.24. Source: UniProtKB

channel activity

Inferred from direct assay. Source: BHF-UCL

lipid binding

Inferred from direct assay. Source: HGNC

protein heterodimerization activity

Inferred from physical interaction. Source: HGNC

protein homodimerization activity

Inferred from direct assay. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself14EBI-516580,EBI-516580
BCL2P104155EBI-516580,EBI-77694
BCL2L1Q07817-19EBI-516580,EBI-287195
BidP704442EBI-516580,EBI-2128640From a different organism.
MCL1Q078203EBI-516580,EBI-1003422
tom-40P243912EBI-516580,EBI-1791540From a different organism.

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q07812-1)

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.
Isoform Beta (identifier: Q07812-2)

The sequence of this isoform differs from the canonical sequence as follows:
     159-192: DGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG → VRLLKPPHPH...VVYNAFSLRV
Isoform Gamma (identifier: Q07812-3)

The sequence of this isoform differs from the canonical sequence as follows:
     12-41: GPTSSEQIMKTGALLLQGFIQDRAGRMGGE → VSSRIEQGEWGGRHPSWPWTRCLRMRPPRS
     42-192: Missing.
Isoform Delta (identifier: Q07812-4)

The sequence of this isoform differs from the canonical sequence as follows:
     30-78: Missing.
Isoform Epsilon (identifier: Q07812-5)

The sequence of this isoform differs from the canonical sequence as follows:
     125-192: LCTKVPELIR...ASLTIWKKMG → GVKWRDLGSL...YRPCAPRCRN
Isoform Zeta (identifier: Q07812-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
Isoform Psi (identifier: Q07812-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: Missing.
Isoform Sigma (identifier: Q07812-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Apoptosis regulator BAX
PRO_0000143053

Regions

Transmembrane172 – 19221Helical; Potential
Motif59 – 7315BH3
Motif98 – 11821BH1
Motif150 – 16516BH2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.18

Natural variations

Alternative sequence1 – 7878Missing in isoform Zeta.
VSP_031239
Alternative sequence1 – 1919Missing in isoform Psi.
VSP_031238
Alternative sequence12 – 4130GPTSS…RMGGE → VSSRIEQGEWGGRHPSWPWT RCLRMRPPRS in isoform Gamma.
VSP_031234
Alternative sequence30 – 7849Missing in isoform Delta.
VSP_031235
Alternative sequence42 – 192151Missing in isoform Gamma.
VSP_031236
Alternative sequence125 – 19268LCTKV…WKKMG → GVKWRDLGSLQPLPPGFKRF TCLSIPRSWDYRPCAPRCRN in isoform Epsilon.
VSP_031240
Alternative sequence159 – 19234DGLLS…WKKMG → VRLLKPPHPHHRALTTAPAP PSLPPATPLGPWAFWSRSQW CPLPIFRSSDVVYNAFSLRV in isoform Beta.
VSP_031237
Alternative sequence159 – 17113Missing in isoform Sigma.
VSP_037475
Natural variant111G → E in a plasmacytoma cell line. Ref.25
VAR_013575
Natural variant391G → R.
Corresponds to variant rs36017265 [ dbSNP | Ensembl ].
VAR_047053
Natural variant671G → R in a T-cell acute lymphoblastic leukemia cell line; loss of heterodimerization with Bcl-2 or Bcl-X(L). Ref.11 Ref.25
VAR_007809
Natural variant1081G → V in a Burkitt lymphoma; loss of homodimerization. Ref.11 Ref.25
VAR_013576

Experimental info

Mutagenesis211K → E: Reduces interaction with BCL2L11, homooligomerization and triggering of apoptosis. Ref.23
Mutagenesis741M → D or E: Strongly reduced interaction with MCL1, BCL2, BCL2L1 and BCL2L2. No effect on cytochrome c release and subsequent apoptosis triggered by etoposide. Ref.24
Mutagenesis1841S → D, E, H or K: Constitutive cytoplasmic location. Ref.13
Mutagenesis1841S → V: Constitutive mitochondrial location. Ref.13

Secondary structure

1 ......................... 192
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 6C0CDB0A7DEE4994

FASTA19221,184
        10         20         30         40         50         60 
MDGSGEQPRG GGPTSSEQIM KTGALLLQGF IQDRAGRMGG EAPELALDPV PQDASTKKLS 

        70         80         90        100        110        120 
ECLKRIGDEL DSNMELQRMI AAVDTDSPRE VFFRVAADMF SDGNFNWGRV VALFYFASKL 

       130        140        150        160        170        180 
VLKALCTKVP ELIRTIMGWT LDFLRERLLG WIQDQGGWDG LLSYFGTPTW QTVTIFVAGV 

       190 
LTASLTIWKK MG

« Hide

Isoform Beta [UniParc] [UniParc].

Checksum: F69DCD70F960192F
Show »

FASTA21824,220
Isoform Gamma [UniParc] [UniParc].

Checksum: D94639AABB927859
Show »

FASTA414,678
Isoform Delta [UniParc] [UniParc].

Checksum: BADE4D71D06A75AB
Show »

FASTA14315,772
Isoform Epsilon [UniParc].

Checksum: 12CCDB8073EF4C9E
Show »

FASTA16418,129
Isoform Zeta [UniParc].

Checksum: A9DAFC5C06E36F4A
Show »

FASTA11412,887
Isoform Psi [UniParc].

Checksum: 266F3151438B6201
Show »

FASTA17319,312
Isoform Sigma [UniParc].

Checksum: 5802B0AC73B2E4CE
Show »

FASTA17919,718

References

« Hide 'large scale' references
[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: 8358790] [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: 7607685] [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: 9920818] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EPSILON).
Tissue: Brain.
[4]"Characterization of Bax-sigma, a cell death-inducing isoform of Bax."
Schmitt E., Paquet C., Beauchemin M., Dever-Bertrand J., Bertrand R.
Biochem. Biophys. Res. Commun. 270:868-879(2000) [PubMed: 10772918] [Abstract]
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: 11912183] [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. expand/collapse author list , 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: 14702039] [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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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: 7475270] [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: 8521816] [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: 10228148] [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: 11259440] [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: 12732850] [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: 15071501] [Abstract]
Cited for: INTERACTION WITH SFN AND YWHAZ, SUBCELLULAR LOCATION.
[17]"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: 16113678] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLU.
[18]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[19]"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: 20300062] [Abstract]
Cited for: INTERACTION WITH RNF144B.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structure of Bax: coregulation of dimer formation and intracellular localization."
Suzuki M., Youle R.J., Tjandra N.
Cell 103:645-654(2000) [PubMed: 11106734] [Abstract]
Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION, SUBUNIT.
[22]"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: 16946732] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 13-19 IN COMPLEX WITH ANTIBODY FRAGMENT.
[23]"BAX activation is initiated at a novel interaction site."
Gavathiotis E., Suzuki M., Davis M.L., Pitter K., Bird G.H., Katz S.G., Tu H.C., Kim H., Cheng E.H., Tjandra N., Walensky L.D.
Nature 455:1076-1081(2008) [PubMed: 18948948] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH BCL2L11, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-21, INTERACTION WITH BCL2L11.
[24]"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: 21199865] [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.
[25]"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: 9531611] [Abstract]
Cited for: VARIANTS GLU-11; ARG-67 AND VAL-108.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00071059.
IPI00439209.
IPI00443773.
IPI00444945.
IPI00445503.
IPI00845474.
IPI00885178.
IPI00885203.
PIRA47538.
B47538.
C47538.
I38921.
JC7255.
RefSeqNP_004315.1. NM_004324.3.
NP_620116.1. NM_138761.3.
NP_620118.1. NM_138763.3.
NP_620119.2. NM_138764.4.
UniGeneHs.624291.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F16NMR-A1-192[»]
2G5BX-ray2.30I/J/K/L13-19[»]
2K7WNMR-A1-192[»]
3PK1X-ray2.49B/D48-81[»]
3PL7X-ray2.61C48-81[»]
ProteinModelPortalQ07812.
SMRQ07812. Positions 1-192.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-232N.
IntActQ07812. 14 interactions.
MINTMINT-134330.
STRINGQ07812.

Protein family/group databases

TCDB1.A.21.1.2. bcl-2 (Bcl-2) family.

PTM databases

PhosphoSiteQ07812.

Polymorphism databases

DMDM728945.

Proteomic databases

PRIDEQ07812.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345358; ENSP00000263262; ENSG00000087088.
GeneID581.
KEGGhsa:581.
UCSCuc002plf.1. human.
uc002pli.1. human.
uc002plk.1. human.
uc002pll.1. human.

Organism-specific databases

CTD581.
GeneCardsGC19P049458.
H-InvDBHIX0015309.
HGNCHGNC:959. BAX.
HPACAB004206.
HPA027878.
MIM600040. gene.
neXtProtNX_Q07812.
PharmGKBPA25269.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG003606.
OMAFYFATKL.
OrthoDBEOG49CQ8P.

Enzyme and pathway databases

Pathway_Interaction_DBcaspase_pathway. Caspase cascade in apoptosis.
ceramidepathway. Ceramide signaling pathway.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ07812.
BgeeQ07812.
CleanExHS_BAX.
GenevestigatorQ07812.
GermOnlineENSG00000087088. Homo sapiens.

Family and domain databases

InterProIPR002475. Bcl2-like_apoptosis.
IPR000712. Bcl2_BH.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
[Graphical view]
KOK02159.
PfamPF00452. Bcl-2. 1 hit.
[Graphical view]
PRINTSPR01862. BCL2FAMILY.
SMARTSM00337. BCL. 1 hit.
[Graphical view]
PROSITEPS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio2371.
PMAP-CutDBQ07812.
SOURCESearch...

Entry information

Entry nameBAX_HUMAN
AccessionPrimary (citable) accession number: Q07812
Secondary accession number(s): A8K4W1 expand/collapse secondary AC list , P55269, Q07814, Q07815, Q8WZ49, Q9NR76, Q9NYG7, Q9UCZ6, Q9UCZ7, Q9UQD6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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