Apoptosis regulator BAX - Homo sapiens (Human)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Induces the release of cytochrome c, activation of CASP3, and thereby apoptosis. Ref.1 Ref.4 Ref.12
Subunit structure	Homodimer. Forms heterodimers with BCL2, E1B 19K protein, BCL2L1 isoform Bcl-X(L), 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). Ref.1 Ref.4 Ref.14 Ref.15 Ref.16 Ref.19
Subcellular location	Isoform Alpha: Mitochondrion membrane; Single-pass membrane protein. Cytoplasm. Note: Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, redistributes to the mitochondrion membrane through the release from JNK-phosphorylated 14-3-3 proteins. Ref.1 Ref.16 Ref.19 Ref.13 Isoform Beta: Cytoplasm Ref.1 Ref.16 Ref.19 Ref.13. Isoform Gamma: Cytoplasm Ref.1 Ref.16 Ref.19 Ref.13. Isoform Delta: Cytoplasm Potential Ref.1 Ref.16 Ref.19 Ref.13.
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, histyocytic 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.

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Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Membrane Mitochondrion
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Tumor suppressor
Domain	Transmembrane
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	B cell apoptosis Inferred from direct assay. Source: HGNC DNA fragmentation involved in apoptosis Inferred from mutant phenotype. Source: HGNC activation of caspase activity by cytochrome c Inferred from direct assay. Source: HGNC 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 during apoptosis Inferred from direct assay. Source: HGNC mitochondrial fusion Inferred from direct assay. Source: HGNC negative regulation of survival gene product expression Inferred from direct assay. Source: HGNC nuclear fragmentation during apoptosis 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 component	cytosol Ref.5 Inferred from direct assay. Source: UniProtKB endoplasmic reticulum membrane Inferred from direct assay. Source: HGNC mitochondrial outer membrane Inferred from Experiment. Source: Reactome mitochondrial permeability transition pore complex Inferred from direct assay. Source: HGNC
Molecular function	BH3 domain binding Inferred from physical interaction. Source: HGNC 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...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-516580,EBI-516580
BAK1	Q16611	1	EBI-516580,EBI-519866
BCL2	P10415	2	EBI-516580,EBI-77694
BCL2L1	Q07817	1	EBI-516580,EBI-78035
BCL2L1	Q07817-1	2	EBI-516580,EBI-287195
PRKCE	Q02156	1	EBI-516580,EBI-706254
tom-40	P24391	1	EBI-516580,EBI-1791540	From a different organism.

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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.
Note: Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, redistributes to the mitochondrion membrane through the release from JNK-phosphorylated 14-3-3 proteins. Ref.1 Ref.16 Ref.19 Ref.13

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.

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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

Potential

Motif

59 – 73

15

BH3

Motif

98 – 118

21

BH1

Motif

150 – 165

16

BH2

Amino acid modifications

Modified residue

1

N-acetylmethionine Ref.18

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.

VAR_013575

Natural variant

39

1

G → R: dbSNP rs36017265.

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).

VAR_007809

Natural variant

108

1

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

VAR_013576

Experimental info

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

.

192

Helix Strand Turn

Details...

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Sequences

Sequence		Length	Mass (Da)
Isoform Alpha [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 6C0CDB0A7DEE4994 Show »	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 « Hide
Isoform Beta [UniParc] [UniParc]. Checksum: F69DCD70F960192F Show »	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 « Hide
Isoform Gamma [UniParc] [UniParc]. Checksum: D94639AABB927859 Show »	FASTA	41	4,678
10 20 30 40 MDGSGEQPRG GVSSRIEQGE WGGRHPSWPW TRCLRMRPPR S « Hide
Isoform Delta [UniParc] [UniParc]. Checksum: BADE4D71D06A75AB Show »	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 « Hide
Isoform Epsilon. Checksum: 12CCDB8073EF4C9E Show »	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 « Hide
Isoform Zeta. Checksum: A9DAFC5C06E36F4A Show »	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 « Hide
Isoform Psi. Checksum: 266F3151438B6201 Show »	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 « Hide
Isoform Sigma. Checksum: 5802B0AC73B2E4CE Show »	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 « Hide

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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: 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. 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. 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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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.
[19]	"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.
[20]	"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.
[21]	"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.

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Web resources

NIEHS-SNPs

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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.
NP_620116.1.
NP_620118.1.
NP_620119.2.

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-232N.

IntAct

Q07812. 10 interactions.

STRING

Q07812.

Protein family/group databases

TCDB

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

PTM databases

PhosphoSite

Q07812.

Proteomic databases

PRIDE

Q07812.

Genome annotation databases

Ensembl

ENST00000345358; ENSP00000263262; ENSG00000087088; Homo sapiens. [Genome view]

GeneID

581.

KEGG

hsa:581.

UCSC

uc002plf.1. human.
uc002pli.1. human.
uc002plk.1. human.
uc002pll.1. human.

Organism-specific databases

CTD

581.

GeneCards

GC19P054149.

HGNC

HGNC:959. BAX.

HPA

CAB004206.

MIM

600040. gene.

PharmGKB

PA25269.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q07812.

OMA

FATKLVL.

OrthoDB

EOG9WDGX1.

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

IPR002475. BCL2_apoptsis.
IPR000712. Bcl2_BH.
IPR020717. Bcl2_BH1_motif_CS.
IPR020726. Bcl2_BH2_motif_CS.
IPR020728. Bcl2_BH3_motif_CS.
[Graphical view]

Pfam

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

PRINTS

PR01862. BCL2FAMILY.

SMART

SM00337. BCL. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

2371.

PMAP-CutDB

Q07812.

SOURCE

Search...

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Entry information

Entry name

BAX_HUMAN

Accession

Primary (citable) accession number: Q07812
Secondary accession number(s): A8K4W1

Q9UQD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 19, 2010
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents