Q07812 (BAX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apoptosis regulator BAX

Alternative name(s):
Bcl-2-like protein 4
Short name=Bcl2-L-4

Gene names

Name:	BAX
Synonyms:	BCL2L4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Protein existence	Evidence 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.18 Ref.25 Ref.26
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. Interacts with FAIM2/LFG2. Interacts with human cytomegalovirus/HHV-5 protein vMIA/UL37. Interacts with BOP/C22orf29. Ref.1 Ref.4 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.25 Ref.26
Subcellular location	Isoform Alpha: Mitochondrion membrane; Single-pass membrane protein. Cytoplasm Ref.1 Ref.13 Ref.16 Ref.18 Ref.23. 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.18 Ref.23 Isoform Beta: Cytoplasm Ref.1 Ref.13 Ref.16 Ref.18 Ref.23. Isoform Gamma: Cytoplasm Ref.1 Ref.13 Ref.16 Ref.18 Ref.23. Isoform Delta: Cytoplasm Potential Ref.1 Ref.13 Ref.16 Ref.18 Ref.23.
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 process	Apoptosis Host-virus interaction
Cellular component	Cytoplasm Membrane Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Tumor suppressor
Domain	Transmembrane Transmembrane helix
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell apoptotic process Inferred from direct assay PubMed 15214043PubMed 16424160. Source: HGNC B cell homeostasis Inferred from electronic annotation. Source: Compara B cell homeostatic proliferation Inferred from electronic annotation. Source: Compara B cell negative selection Inferred from electronic annotation. Source: Compara Sertoli cell proliferation Inferred from electronic annotation. Source: Compara T cell homeostatic proliferation Inferred from electronic annotation. Source: Compara activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c Inferred from direct assay PubMed 15214043. Source: HGNC apoptotic DNA fragmentation Inferred from mutant phenotype PubMed 11350920. Source: HGNC blood vessel remodeling Inferred from electronic annotation. Source: Compara cellular response to UV Inferred from electronic annotation. Source: Compara cellular response to organic substance Inferred from electronic annotation. Source: Compara cerebral cortex development Inferred from electronic annotation. Source: Compara cleavage of lamin involved in execution phase of apoptosis Inferred from mutant phenotype PubMed 11350920. Source: HGNC development of secondary sexual characteristics Inferred from electronic annotation. Source: Compara establishment or maintenance of transmembrane electrochemical gradient Inferred from direct assay PubMed 9843949. Source: HGNC fertilization Inferred from electronic annotation. Source: Compara germ cell development Inferred from electronic annotation. Source: Compara germ cell programmed cell death Inferred from electronic annotation. Source: Compara glycosphingolipid metabolic process Inferred from electronic annotation. Source: Compara homeostasis of number of cells within a tissue Inferred from electronic annotation. Source: Compara hypothalamus development Inferred from electronic annotation. Source: Compara induction of apoptosis Non-traceable author statement Ref.3. Source: UniProtKB intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Inferred from mutant phenotype PubMed 16645094. Source: UniProtKB kidney development Inferred from electronic annotation. Source: Compara limb morphogenesis Inferred from electronic annotation. Source: Compara mitochondrial fragmentation involved in apoptotic process Inferred from direct assay PubMed 12499352. Source: HGNC mitochondrial fusion Inferred from direct assay PubMed 14769861. Source: HGNC myeloid cell homeostasis Inferred from electronic annotation. Source: Compara negative regulation of fibroblast proliferation Inferred from electronic annotation. Source: Compara negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara negative regulation of protein binding Inferred from direct assay PubMed 9388232. Source: UniProtKB neuron apoptotic process Inferred from electronic annotation. Source: Compara neuron migration Inferred from electronic annotation. Source: Compara nuclear fragmentation involved in apoptotic nuclear change Inferred from mutant phenotype PubMed 11350920. Source: HGNC odontogenesis of dentin-containing tooth Inferred from electronic annotation. Source: Compara ovarian follicle development Inferred from electronic annotation. Source: Compara positive regulation of B cell apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process involved in mammary gland involution Inferred from electronic annotation. Source: Compara positive regulation of developmental pigmentation Inferred from electronic annotation. Source: Compara positive regulation of endoplasmic reticulum unfolded protein response Inferred from mutant phenotype PubMed 16645094. Source: UniProtKB positive regulation of intrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 14963330Ref.26. Source: UniProtKB positive regulation of mitochondrial outer membrane permeabilization Traceable author statement. Source: Reactome positive regulation of neuron apoptotic process Inferred from direct assay PubMed 15637643. Source: HGNC positive regulation of protein oligomerization Inferred from direct assay PubMed 19805544. Source: UniProtKB positive regulation of release of cytochrome c from mitochondria Inferred from direct assay PubMed 14963330. Source: UniProtKB positive regulation of release of sequestered calcium ion into cytosol Inferred from electronic annotation. Source: Compara post-embryonic camera-type eye morphogenesis Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from direct assay PubMed 14522999. Source: HGNC protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Inferred from electronic annotation. Source: Compara reduction of endoplasmic reticulum calcium ion concentration Inferred from electronic annotation. Source: Compara regulation of cell cycle Inferred from electronic annotation. Source: Compara regulation of mammary gland epithelial cell proliferation Inferred from electronic annotation. Source: Compara regulation of mitochondrial membrane potential Inferred from direct assay PubMed 9843949. Source: HGNC regulation of nitrogen utilization Inferred from electronic annotation. Source: Compara regulation of protein heterodimerization activity Inferred from physical interaction PubMed 9111042. Source: HGNC regulation of protein homodimerization activity Inferred from direct assay PubMed 9111042. Source: HGNC release of cytochrome c from mitochondria Inferred from direct assay PubMed 17052454PubMed 9843949. Source: HGNC release of matrix enzymes from mitochondria Inferred from direct assay PubMed 9843949. Source: HGNC response to DNA damage stimulus Inferred from electronic annotation. Source: Compara response to acid Inferred from electronic annotation. Source: Compara response to axon injury Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from electronic annotation. Source: Compara response to salt stress Inferred from electronic annotation. Source: Compara response to toxic substance Inferred from direct assay PubMed 16307838. Source: HGNC retina development in camera-type eye Inferred from electronic annotation. Source: Compara retinal cell apoptotic process Inferred from mutant phenotype PubMed 10702418. Source: HGNC retinal cell programmed cell death Inferred from electronic annotation. Source: Compara spermatid differentiation Inferred from electronic annotation. Source: Compara transformed cell apoptotic process Inferred from mutant phenotype PubMed 10739008. Source: HGNC vagina development Inferred from electronic annotation. Source: Compara virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Bcl-2 family protein complex Inferred from direct assay Ref.26. Source: UniProtKB cytosol Inferred from direct assay PubMed 15102863. Source: UniProtKB cytosolic part Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Inferred from direct assay PubMed 16424160. Source: HGNC mitochondrial outer membrane Traceable author statement. Source: Reactome mitochondrial permeability transition pore complex Inferred from direct assay PubMed 9843949. Source: HGNC nucleus Inferred from mutant phenotype PubMed 15102863. Source: UniProtKB
Molecular_function	BH3 domain binding Inferred from direct assay Ref.26. Source: UniProtKB channel activity Inferred from direct assay PubMed 9219694. Source: BHF-UCL lipid binding Inferred from direct assay PubMed 14522999. Source: HGNC protein homodimerization activity Inferred from direct assay PubMed 16608847. Source: HGNC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		19	EBI-516580,EBI-516580
BAK1	Q16611	3	EBI-516580,EBI-519866
BCL2	P10415	8	EBI-516580,EBI-77694
BCL2L1	Q07817-1	13	EBI-516580,EBI-287195
BCL2L11	O43521	11	EBI-516580,EBI-526406
BCL2L2	Q92843	3	EBI-516580,EBI-707714
BID	P55957	14	EBI-516580,EBI-519672
Bid	P70444	2	EBI-516580,EBI-2128640	From a different organism.
ERN1	O75460	2	EBI-516580,EBI-371750
MCL1	Q07820	3	EBI-516580,EBI-1003422
Mcl1	P97287	2	EBI-516580,EBI-707292	From a different organism.
PYCARD	Q9ULZ3	7	EBI-516580,EBI-751215
SH3GLB1	Q9Y371-1	2	EBI-516580,EBI-5291808
tom-40	P24391	2	EBI-516580,EBI-1791540	From a different organism.
XRCC6	P12956	2	EBI-516580,EBI-353208

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 192

192

Apoptosis regulator BAX

PRO_0000143053

Regions

Transmembrane

172 – 192

21

Helical; Potential

Motif

59 – 73

15

BH3

Motif

98 – 118

21

BH1

Motif

150 – 165

16

BH2

Natural variations

Alternative sequence

1 – 78

78

Missing in isoform Zeta.

VSP_031239

Alternative sequence

1 – 19

19

Missing in isoform Psi.

VSP_031238

Alternative sequence

12 – 41

30

GPTSS…RMGGE → VSSRIEQGEWGGRHPSWPWT RCLRMRPPRS in isoform Gamma.

VSP_031234

Alternative sequence

30 – 78

49

Missing in isoform Delta.

VSP_031235

Alternative sequence

42 – 192

151

Missing in isoform Gamma.

VSP_031236

Alternative sequence

125 – 192

68

LCTKV…WKKMG → GVKWRDLGSLQPLPPGFKRF TCLSIPRSWDYRPCAPRCRN in isoform Epsilon.

VSP_031240

Alternative sequence

159 – 192

34

DGLLS…WKKMG → VRLLKPPHPHHRALTTAPAP PSLPPATPLGPWAFWSRSQW CPLPIFRSSDVVYNAFSLRV in isoform Beta.

VSP_031237

Alternative sequence

159 – 171

13

Missing in isoform Sigma.

VSP_037475

Natural variant

11

1

G → E in a plasmacytoma cell line. Ref.27

VAR_013575

Natural variant

39

1

G → R.
Corresponds to variant rs36017265 [ dbSNP | Ensembl ].

VAR_047053

Natural variant

67

1

G → R in a T-cell acute lymphoblastic leukemia cell line; loss of heterodimerization with Bcl-2 or Bcl-X(L). Ref.11 Ref.27

VAR_007809

Natural variant

108

1

G → V in a Burkitt lymphoma; loss of homodimerization. Ref.11 Ref.27

VAR_013576

Experimental info

Mutagenesis

21

1

K → E: Reduces interaction with BCL2L11, homooligomerization and triggering of apoptosis. Ref.25

Mutagenesis

74

1

M → 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.26

Mutagenesis

184

1

S → D, E, H or K: Constitutive cytoplasmic location. Ref.13

Mutagenesis

184

1

S → V: Constitutive mitochondrial location. Ref.13

Secondary structure

1

.

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192

Helix Strand Turn

Details...

Turn

2 – 4

3

Beta strand

10 – 14

5

Helix

16 – 36

21

Beta strand

43 – 45

3

Helix

54 – 72

19

Helix

74 – 82

9

Helix

88 – 99

12

Turn

100 – 102

3

Helix

107 – 147

41

Helix

149 – 154

6

Turn

155 – 158

4

Helix

159 – 164

6

Helix

171 – 188

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 6C0CDB0A7DEE4994	FASTA	192	21,184
	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
	Isoform Beta [UniParc] [UniParc]. Checksum: F69DCD70F960192F	FASTA	218	24,220
	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 WIQDQGGWVR LLKPPHPHHR ALTTAPAPPS 190 200 210 LPPATPLGPW AFWSRSQWCP LPIFRSSDVV YNAFSLRV
	Isoform Gamma [UniParc] [UniParc]. Checksum: D94639AABB927859	FASTA	41	4,678
	10 20 30 40 MDGSGEQPRG GVSSRIEQGE WGGRHPSWPW TRCLRMRPPR S
	Isoform Delta [UniParc] [UniParc]. Checksum: BADE4D71D06A75AB	FASTA	143	15,772
	10 20 30 40 50 60 MDGSGEQPRG GGPTSSEQIM KTGALLLQGM IAAVDTDSPR EVFFRVAADM FSDGNFNWGR 70 80 90 100 110 120 VVALFYFASK LVLKALCTKV PELIRTIMGW TLDFLRERLL GWIQDQGGWD GLLSYFGTPT 130 140 WQTVTIFVAG VLTASLTIWK KMG
	Isoform Epsilon [UniParc]. Checksum: 12CCDB8073EF4C9E	FASTA	164	18,129
	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 VLKAGVKWRD LGSLQPLPPG FKRFTCLSIP RSWDYRPCAP RCRN
	Isoform Zeta [UniParc]. Checksum: A9DAFC5C06E36F4A	FASTA	114	12,887
	10 20 30 40 50 60 MIAAVDTDSP REVFFRVAAD MFSDGNFNWG RVVALFYFAS KLVLKALCTK VPELIRTIMG 70 80 90 100 110 WTLDFLRERL LGWIQDQGGW DGLLSYFGTP TWQTVTIFVA GVLTASLTIW KKMG
	Isoform Psi [UniParc]. Checksum: 266F3151438B6201	FASTA	173	19,312
	10 20 30 40 50 60 MKTGALLLQG FIQDRAGRMG GEAPELALDP VPQDASTKKL SECLKRIGDE LDSNMELQRM 70 80 90 100 110 120 IAAVDTDSPR EVFFRVAADM FSDGNFNWGR VVALFYFASK LVLKALCTKV PELIRTIMGW 130 140 150 160 170 TLDFLRERLL GWIQDQGGWD GLLSYFGTPT WQTVTIFVAG VLTASLTIWK KMG
	Isoform Sigma [UniParc]. Checksum: 5802B0AC73B2E4CE	FASTA	179	19,718
	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 VLKALCTKVP ELIRTIMGWT LDFLRERLLG WIQDQGGWTV TIFVAGVLTA SLTIWKKMG

References

	« Hide 'large scale' referencesShow '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] [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]	"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] [Europe PMC] [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] [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]	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. , 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] [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]	"An anti-apoptotic viral protein that recruits Bax to mitochondria." Poncet D., Larochette N., Pauleau A.L., Boya P., Jalil A.A., Cartron P.F., Vallette F., Schnebelen C., Bartle L.M., Skaletskaya A., Boutolleau D., Martinou J.C., Goldmacher V.S., Kroemer G., Zamzami N. J. Biol. Chem. 279:22605-22614(2004) [PubMed] [Europe PMC] [Abstract] 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]	"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.
[21]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH BCL2L11, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-21, INTERACTION WITH BCL2L11.
[26]	"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.
[27]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00071059.
IPI00439209.
IPI00443773.
IPI00444945.
IPI00445503.
IPI00845474.
IPI00885178.
IPI00885203.

PIR

A47538.
B47538.
C47538.
I38921.
JC7255.

RefSeq

NP_004315.1. NM_004324.3.
NP_620116.1. NM_138761.3.
NP_620118.1. NM_138763.3.
NP_620119.2. NM_138764.4.

UniGene

Hs.624291.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q07812.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-232N.

IntAct

Q07812. 19 interactions.

MINT

MINT-134330.

Protein family/group databases

TCDB

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

PTM databases

PhosphoSite

Q07812.

Polymorphism databases

DMDM

728945.

Proteomic databases

PaxDb

Q07812.

PRIDE

Q07812.

Protocols and materials databases

DNASU

581.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000293288; ENSP00000293288; ENSG00000087088.
ENST00000345358; ENSP00000263262; ENSG00000087088.
ENST00000354470; ENSP00000346461; ENSG00000087088.
ENST00000356483; ENSP00000348871; ENSG00000087088.
ENST00000391871; ENSP00000375744; ENSG00000087088.
ENST00000415969; ENSP00000389971; ENSG00000087088.
ENST00000515540; ENSP00000426328; ENSG00000087088.
ENST00000539787; ENSP00000441413; ENSG00000087088.

GeneID

581.

KEGG

hsa:581.

UCSC

uc002plf.1. human.
uc002plj.3. human.
uc002plk.3. human.
uc002pll.3. human.

Organism-specific databases

CTD

581.

GeneCards

GC19P049458.

HGNC

HGNC:959. BAX.

HPA

CAB004206.
HPA027878.

MIM

600040. gene.

neXtProt

NX_Q07812.

PharmGKB

PA25269.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG46695.

HOVERGEN

HBG003606.

KO

K02159.

OMA

GWIQEQG.

OrthoDB

EOG49CQ8P.

Enzyme and pathway databases

Pathway_Interaction_DB

caspase_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.

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q07812.

Bgee

Q07812.

CleanEx

HS_BAX.

Genevestigator

Q07812.

GermOnline

ENSG00000087088. Homo sapiens.

Family and domain databases

InterPro

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]

PANTHER

PTHR11256. PTHR11256. 1 hit.
PTHR11256:SF9. PTHR11256:SF9. 1 hit.

Pfam

PF00452. Bcl-2. 1 hit.
[Graphical view]

PRINTS

PR01862. BCL2FAMILY.

PROSITE

PS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q07812.

ChEMBL

CHEMBL5318.

ChiTaRS

BAX. human.

EvolutionaryTrace

Q07812.

GenomeRNAi

581.

NextBio

2371.

PMAP-CutDB

Q07812.

SOURCE

Search...

Entry information

Entry name

BAX_HUMAN

Accession

Primary (citable) accession number: Q07812
Secondary accession number(s): A8K4W1 , 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:	May 29, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.