HUMAN:BAX

From GONUTS

Jump to: navigation, search

Species (Taxon ID)	Homo sapiens (Human). ([1])
Gene Name(s)	BAX (synonyms: BCL2L4)
Protein Name(s)	Apoptosis regulator BAX Bcl-2-like protein 4 Bcl2-L-4
External Links
EMBL	L22473 L22474 L22475 U19599 AF007826 AF247393 AJ417988 AF250190 AK291076 AY217036 CH471177 CH471177 BC014175
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
PDB	1F16 2G5B 2K7W 3PK1 3PL7
PDBsum	1F16 2G5B 2K7W 3PK1 3PL7
ProteinModelPortal	Q07812
SMR	Q07812
DIP	DIP-232N
IntAct	Q07812
MINT	MINT-134330
STRING	Q07812
TCDB	1.A.21.1.2
PhosphoSite	Q07812
PRIDE	Q07812
Ensembl	ENST00000345358
GeneID	581
KEGG	hsa:581
UCSC	uc002plf.1 uc002pli.1 uc002plk.1 uc002pll.1
CTD	581
GeneCards	GC19P045835
H-InvDB	HIX0015309
HGNC	HGNC:959
HPA	CAB004206 HPA027878
MIM	600040
neXtProt	NX_Q07812
PharmGKB	PA25269
HOVERGEN	HBG003606
OMA	FYFATKL
OrthoDB	EOG49CQ8P
Pathway_Interaction_DB	caspase_pathway ceramidepathway hdac_classiii_pathway syndecan_2_pathway
Reactome	REACT_578
NextBio	2371
PMAP-CutDB	Q07812
ArrayExpress	Q07812
Bgee	Q07812
CleanEx	HS_BAX
Genevestigator	Q07812
GermOnline	ENSG00000087088
GO	GO:0097136 GO:0005829 GO:0005789 GO:0005741 GO:0005757 GO:0005634 GO:0051434 GO:0015267 GO:0008289 GO:0046982 GO:0042803 GO:0008635 GO:0008633 GO:0001783 GO:0006922 GO:0006309 GO:0010248 GO:0008624 GO:0008629 GO:0046674 GO:0043653 GO:0008053 GO:0032091 GO:0008634 GO:0030264 GO:0043525 GO:0051260 GO:0051881 GO:0043497 GO:0043496 GO:0001836 GO:0032976 GO:0009636 GO:0006927
InterPro	IPR002475 IPR000712 IPR020717 IPR020726 IPR020728
KO	K02159
Pfam	PF00452
PRINTS	PR01862
SMART	SM00337
PROSITE	PS50062 PS01080 PS01258 PS01259

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0001783	B cell apoptosis	PMID:15214043^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0001783	B cell apoptosis	PMID:16424160^[2]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0001836	release of cytochrome c from mitochondria	PMID:17052454^[3]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0001836	release of cytochrome c from mitochondria	PMID:9843949^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0005515	protein binding	PMID:10753914^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q16548	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11161816^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y371	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11278245^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q9HD36	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11571294^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q16611	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11574543^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P06493	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11574543^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P31947	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:14752512^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P02489	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:14752512^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P02511	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16113678^[11]	IPI: Inferred from Physical Interaction	UniProtKB:P10909	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16608847^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q07817	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17635912^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P24391	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19062087^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P70444	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20300062^[15]	IPI: Inferred from Physical Interaction	UniProtKB:Q7Z419	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20541605^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P63244	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21458670^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q07820	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21671007^[18]	IPI: Inferred from Physical Interaction	UniProtKB:P10415	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21671007^[18]	IPI: Inferred from Physical Interaction	UniProtKB:Q07817-1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9111042^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P10415	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9843949^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Z2L0	F	Seeded From UniProt
	GO:0005634	nucleus	PMID:15102863^[20]	IMP: Inferred from Mutant Phenotype		C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C	Seeded From UniProt
	GO:0005737	cytoplasm	PMID:18029348^[21]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005739	mitochondrion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0496	C	Seeded From UniProt
	GO:0005739	mitochondrion	PMID:11912183^[22]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005739	mitochondrion	PMID:17823127^[23]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005739	mitochondrion	PMID:18029348^[21]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005741	mitochondrial outer membrane	Reactome:REACT_1286	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005741	mitochondrial outer membrane	Reactome:REACT_341	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005757	mitochondrial permeability transition pore complex	PMID:9843949^[4]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005783	endoplasmic reticulum	PMID:16424160^[2]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005789	endoplasmic reticulum membrane	PMID:16424160^[2]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005829	cytosol	PMID:11912183^[22]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005829	cytosol	PMID:15102863^[20]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005829	cytosol	PMID:17823127^[23]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_1286	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_1506	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_6160	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0006309	DNA fragmentation involved in apoptotic nuclear change	PMID:11350920^[24]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P	Seeded From UniProt
	GO:0006915	apoptosis	PMID:9219694^[25]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006915	apoptosis	Reactome:REACT_578	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006917	induction of apoptosis	PMID:11350920^[24]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006917	induction of apoptosis	PMID:11912183^[22]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006917	induction of apoptosis	PMID:9920818^[26]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0006919	activation of caspase activity	PMID:11350920^[24]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006919	activation of caspase activity	PMID:11912183^[22]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006922	cleavage of lamin	PMID:11350920^[24]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0006927	transformed cell apoptosis	PMID:10739008^[27]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0008053	mitochondrial fusion	PMID:14769861^[28]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008289	lipid binding	PMID:14522999^[29]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008624	induction of apoptosis by extracellular signals	PMID:16424160^[2]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008629	induction of apoptosis by intracellular signals	PMID:16462759^[30]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008629	induction of apoptosis by intracellular signals	Reactome:REACT_964	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0008633	activation of pro-apoptotic gene products	Reactome:REACT_584	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0008634	negative regulation of survival gene product expression	PMID:9111042^[19]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008635	activation of caspase activity by cytochrome c	PMID:15214043^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0008637	apoptotic mitochondrial changes	PMID:9843949^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0009636	response to toxin	PMID:16307838^[31]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0010248	establishment or maintenance of transmembrane electrochemical gradient	PMID:9843949^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0015267	channel activity	PMID:9219694^[25]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016021	integral to membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0812	C	Seeded From UniProt
	GO:0030264	nuclear fragmentation involved in apoptotic nuclear change	PMID:11350920^[24]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0031966	mitochondrial membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0171	C	Seeded From UniProt
	GO:0032091	negative regulation of protein binding	PMID:9388232^[32]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0032976	release of matrix enzymes from mitochondria	PMID:9843949^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0042802	identical protein binding	PMID:16113678^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q07812	F	Seeded From UniProt
	GO:0042802	identical protein binding	PMID:17668322^[33]	IPI: Inferred from Physical Interaction	UniProtKB:Q07812	F	Seeded From UniProt
	GO:0042803	protein homodimerization activity	PMID:16608847^[12]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0042803	protein homodimerization activity	PMID:9111042^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q07812	F	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000712	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002475	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020717	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020726	P	Seeded From UniProt
	GO:0042981	regulation of apoptosis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020728	P	Seeded From UniProt
	GO:0043496	regulation of protein homodimerization activity	PMID:9111042^[19]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043497	regulation of protein heterodimerization activity	PMID:9111042^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q07812	P	Seeded From UniProt
	GO:0043525	positive regulation of neuron apoptosis	PMID:15637643^[34]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0043653	mitochondrial fragmentation involved in apoptosis	PMID:12499352^[35]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0046674	induction of retinal programmed cell death	PMID:10702418^[36]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0046930	pore complex	PMID:9219694^[25]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0046982	protein heterodimerization activity	PMID:9111042^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P10415	F	Seeded From UniProt
	GO:0051260	protein homooligomerization	PMID:14522999^[29]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0051434	BH3 domain binding	PMID:15705586^[37]	IPI: Inferred from Physical Interaction	UniProtKB:Q13794	F	Seeded From UniProt
	GO:0051434	BH3 domain binding	PMID:17052454^[3]	IPI: Inferred from Physical Interaction	UniProtKB:P55957	F	Seeded From UniProt
	GO:0051434	BH3 domain binding	PMID:21199865^[38]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0051881	regulation of mitochondrial membrane potential	PMID:9843949^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0097136	Bcl-2 family protein complex	PMID:21199865^[38]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0019835	cytolysis	PMID:22006182^[39]	IMP: Inferred from Mutant Phenotype		P	Fig. 4(D-G), Fig. 5B, and Fig. 6	complete
	GO:0005829	cytosol	PMID:22006182^[39]	IMP: Inferred from Mutant Phenotype		C	Supplemental Figure S1	complete
	GO:0005624	membrane fraction	PMID:22006182^[39]	IMP: Inferred from Mutant Phenotype		C	Supplemental Figure S1	complete
	GO:0034290	holin activity	PMID:22006182^[39]	IMP: Inferred from Mutant Phenotype		F	Fig. 1B and Fig. 2BDF	complete
	GO:0006915	apoptosis	PMID:9531611^[40]	IMP: Inferred from Mutant Phenotype		P	Figures 2 and 3.	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Eldering E et al. (2004) Apoptosis via the B cell antigen receptor requires Bax translocation and involves mitochondrial depolarization, cytochrome C release, and caspase-9 activation. Eur J Immunol 34: 1950-60 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Pelletier N et al. (2006) The endoplasmic reticulum is a key component of the plasma cell death pathway. J Immunol 176: 1340-7 PubMed GONUTS page
↑ ^3.0 ^3.1 Walensky LD et al. (2006) A stapled BID BH3 helix directly binds and activates BAX. Mol Cell 24: 199-210 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Narita M et al. (1998) Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci U S A 95: 14681-6 PubMed GONUTS page
↑ Zhang H et al. (2000) Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells. J Biol Chem 275: 11092-9 PubMed GONUTS page
↑ Pierrat B et al. (2001) SH3GLB, a new endophilin-related protein family featuring an SH3 domain. Genomics 71: 222-34 PubMed GONUTS page
↑ Ke N et al. (2001) Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak. J Biol Chem 276: 12481-4 PubMed GONUTS page
↑ Sundararajan R et al. (2001) Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K. J Biol Chem 276: 45120-7 PubMed GONUTS page
↑ ^9.0 ^9.1 Samuel T et al. (2001) The G2/M regulator 14-3-3sigma prevents apoptosis through sequestration of Bax. J Biol Chem 276: 45201-6 PubMed GONUTS page
↑ ^10.0 ^10.1 Mao YW et al. (2004) Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ 11: 512-26 PubMed GONUTS page
↑ ^11.0 ^11.1 Zhang H et al. (2005) Clusterin inhibits apoptosis by interacting with activated Bax. Nat Cell Biol 7: 909-15 PubMed GONUTS page
↑ ^12.0 ^12.1 Ming L et al. (2006) PUMA Dissociates Bax and Bcl-X(L) to induce apoptosis in colon cancer cells. J Biol Chem 281: 16034-42 PubMed GONUTS page
↑ Ott M et al. (2007) The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release. J Biol Chem 282: 27633-9 PubMed GONUTS page
↑ Lovell JF et al. (2008) Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 135: 1074-84 PubMed GONUTS page
↑ Benard G et al. (2010) IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation. EMBO J 29: 1458-71 PubMed GONUTS page
↑ Wu Y et al. (2010) RACK1 promotes Bax oligomerization and dissociates the interaction of Bax and Bcl-XL. Cell Signal 22: 1495-501 PubMed GONUTS page
↑ Edlich F et al. (2011) Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol. Cell 145: 104-16 PubMed GONUTS page
↑ ^18.0 ^18.1 Mendez G et al. (2011) Role of Bim in apoptosis induced in H460 lung tumor cells by the spindle poison Combretastatin-A4. Apoptosis 16: 940-9 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 Diaz JL et al. (1997) A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members. J Biol Chem 272: 11350-5 PubMed GONUTS page
↑ ^20.0 ^20.1 Yakovlev AG et al. (2004) BOK and NOXA are essential mediators of p53-dependent apoptosis. J Biol Chem 279: 28367-74 PubMed GONUTS page
↑ ^21.0 ^21.1 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 ^22.3 Cartron PF et al. (2002) The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patients. Hum Mol Genet 11: 675-87 PubMed GONUTS page
↑ ^23.0 ^23.1 Chandra D et al. (2007) Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J Biol Chem 282: 31289-301 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 ^24.4 Kagawa S et al. (2001) Deficiency of caspase-3 in MCF7 cells blocks Bax-mediated nuclear fragmentation but not cell death. Clin Cancer Res 7: 1474-80 PubMed GONUTS page
↑ ^25.0 ^25.1 ^25.2 Antonsson B et al. (1997) Inhibition of Bax channel-forming activity by Bcl-2. Science 277: 370-2 PubMed GONUTS page
↑ Shi B et al. (1999) Identification and characterization of baxepsilon, a novel bax variant missing the BH2 and the transmembrane domains. Biochem Biophys Res Commun 254: 779-85 PubMed GONUTS page
↑ Inoue K et al. (2000) Frequent microsatellite instability and BAX mutations in T cell acute lymphoblastic leukemia cell lines. Leuk Res 24: 255-62 PubMed GONUTS page
↑ Karbowski M et al. (2004) Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J Cell Biol 164: 493-9 PubMed GONUTS page
↑ ^29.0 ^29.1 Yethon JA et al. (2003) Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis. J Biol Chem 278: 48935-41 PubMed GONUTS page
↑ Vogt M et al. (2006) Inhibition of Bax activity is crucial for the antiapoptotic function of the human papillomavirus E6 oncoprotein. Oncogene 25: 4009-15 PubMed GONUTS page
↑ Chen J et al. (2006) T-2 toxin induces apoptosis, and selenium partly blocks, T-2 toxin induced apoptosis in chondrocytes through modulation of the Bax/Bcl-2 ratio. Food Chem Toxicol 44: 567-73 PubMed GONUTS page
↑ Ottilie S et al. (1997) Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins. J Biol Chem 272: 30866-72 PubMed GONUTS page
↑ Lu D et al. (2007) Protein kinase C-epsilon protects MCF-7 cells from TNF-mediated cell death by inhibiting Bax translocation. Apoptosis 12: 1893-900 PubMed GONUTS page
↑ Precht TA et al. (2005) The permeability transition pore triggers Bax translocation to mitochondria during neuronal apoptosis. Cell Death Differ 12: 255-65 PubMed GONUTS page
↑ Karbowski M et al. (2002) Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. J Cell Biol 159: 931-8 PubMed GONUTS page
↑ Podestà F et al. (2000) Bax is increased in the retina of diabetic subjects and is associated with pericyte apoptosis in vivo and in vitro. Am J Pathol 156: 1025-32 PubMed GONUTS page
↑ Sun Y & Leaman DW (2005) Involvement of Noxa in cellular apoptotic responses to interferon, double-stranded RNA, and virus infection. J Biol Chem 280: 15561-8 PubMed GONUTS page
↑ ^38.0 ^38.1 Czabotar PE et al. (2011) Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis. J Biol Chem 286: 7123-31 PubMed GONUTS page
↑ ^39.0 ^39.1 ^39.2 ^39.3 Pang X et al. (2011) Active Bax and Bak are functional holins. Genes Dev 25: 2278-90 PubMed GONUTS page
↑ Meijerink JP et al. (1998) Hematopoietic malignancies demonstrate loss-of-function mutations of BAX. Blood 91: 2991-7 PubMed GONUTS page

[PMID:15214043-0] 1.0 ^1.1 Eldering E et al. (2004) Apoptosis via the B cell antigen receptor requires Bax translocation and involves mitochondrial depolarization, cytochrome C release, and caspase-9 activation. Eur J Immunol 34: 1950-60 PubMed GONUTS page

[PMID:16424160-1] 2.0 ^2.1 ^2.2 ^2.3 Pelletier N et al. (2006) The endoplasmic reticulum is a key component of the plasma cell death pathway. J Immunol 176: 1340-7 PubMed GONUTS page

[PMID:17052454-2] 3.0 ^3.1 Walensky LD et al. (2006) A stapled BID BH3 helix directly binds and activates BAX. Mol Cell 24: 199-210 PubMed GONUTS page

[PMID:9843949-3] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Narita M et al. (1998) Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci U S A 95: 14681-6 PubMed GONUTS page

[PMID:10753914-4] Zhang H et al. (2000) Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells. J Biol Chem 275: 11092-9 PubMed GONUTS page

[PMID:11161816-5] Pierrat B et al. (2001) SH3GLB, a new endophilin-related protein family featuring an SH3 domain. Genomics 71: 222-34 PubMed GONUTS page

[PMID:11278245-6] Ke N et al. (2001) Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak. J Biol Chem 276: 12481-4 PubMed GONUTS page

[PMID:11571294-7] Sundararajan R et al. (2001) Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K. J Biol Chem 276: 45120-7 PubMed GONUTS page

[PMID:11574543-8] 9.0 ^9.1 Samuel T et al. (2001) The G2/M regulator 14-3-3sigma prevents apoptosis through sequestration of Bax. J Biol Chem 276: 45201-6 PubMed GONUTS page

[PMID:14752512-9] 10.0 ^10.1 Mao YW et al. (2004) Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S) to sequester their translocation during staurosporine-induced apoptosis. Cell Death Differ 11: 512-26 PubMed GONUTS page

[PMID:16113678-10] 11.0 ^11.1 Zhang H et al. (2005) Clusterin inhibits apoptosis by interacting with activated Bax. Nat Cell Biol 7: 909-15 PubMed GONUTS page

[PMID:16608847-11] 12.0 ^12.1 Ming L et al. (2006) PUMA Dissociates Bax and Bcl-X(L) to induce apoptosis in colon cancer cells. J Biol Chem 281: 16034-42 PubMed GONUTS page

[PMID:17635912-12] Ott M et al. (2007) The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release. J Biol Chem 282: 27633-9 PubMed GONUTS page

[PMID:19062087-13] Lovell JF et al. (2008) Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. Cell 135: 1074-84 PubMed GONUTS page

[PMID:20300062-14] Benard G et al. (2010) IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation. EMBO J 29: 1458-71 PubMed GONUTS page

[PMID:20541605-15] Wu Y et al. (2010) RACK1 promotes Bax oligomerization and dissociates the interaction of Bax and Bcl-XL. Cell Signal 22: 1495-501 PubMed GONUTS page

[PMID:21458670-16] Edlich F et al. (2011) Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol. Cell 145: 104-16 PubMed GONUTS page

[PMID:21671007-17] 18.0 ^18.1 Mendez G et al. (2011) Role of Bim in apoptosis induced in H460 lung tumor cells by the spindle poison Combretastatin-A4. Apoptosis 16: 940-9 PubMed GONUTS page

[PMID:9111042-18] 19.0 ^19.1 ^19.2 ^19.3 ^19.4 ^19.5 Diaz JL et al. (1997) A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members. J Biol Chem 272: 11350-5 PubMed GONUTS page

[PMID:15102863-19] 20.0 ^20.1 Yakovlev AG et al. (2004) BOK and NOXA are essential mediators of p53-dependent apoptosis. J Biol Chem 279: 28367-74 PubMed GONUTS page

[PMID:18029348-20] 21.0 ^21.1 Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page

[PMID:11912183-21] 22.0 ^22.1 ^22.2 ^22.3 Cartron PF et al. (2002) The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patients. Hum Mol Genet 11: 675-87 PubMed GONUTS page

[PMID:17823127-22] 23.0 ^23.1 Chandra D et al. (2007) Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase-3. J Biol Chem 282: 31289-301 PubMed GONUTS page

[PMID:11350920-23] 24.0 ^24.1 ^24.2 ^24.3 ^24.4 Kagawa S et al. (2001) Deficiency of caspase-3 in MCF7 cells blocks Bax-mediated nuclear fragmentation but not cell death. Clin Cancer Res 7: 1474-80 PubMed GONUTS page

[PMID:9219694-24] 25.0 ^25.1 ^25.2 Antonsson B et al. (1997) Inhibition of Bax channel-forming activity by Bcl-2. Science 277: 370-2 PubMed GONUTS page

[PMID:9920818-25] Shi B et al. (1999) Identification and characterization of baxepsilon, a novel bax variant missing the BH2 and the transmembrane domains. Biochem Biophys Res Commun 254: 779-85 PubMed GONUTS page

[PMID:10739008-26] Inoue K et al. (2000) Frequent microsatellite instability and BAX mutations in T cell acute lymphoblastic leukemia cell lines. Leuk Res 24: 255-62 PubMed GONUTS page

[PMID:14769861-27] Karbowski M et al. (2004) Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis. J Cell Biol 164: 493-9 PubMed GONUTS page

[PMID:14522999-28] 29.0 ^29.1 Yethon JA et al. (2003) Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis. J Biol Chem 278: 48935-41 PubMed GONUTS page

[PMID:16462759-29] Vogt M et al. (2006) Inhibition of Bax activity is crucial for the antiapoptotic function of the human papillomavirus E6 oncoprotein. Oncogene 25: 4009-15 PubMed GONUTS page

[PMID:16307838-30] Chen J et al. (2006) T-2 toxin induces apoptosis, and selenium partly blocks, T-2 toxin induced apoptosis in chondrocytes through modulation of the Bax/Bcl-2 ratio. Food Chem Toxicol 44: 567-73 PubMed GONUTS page

[PMID:9388232-31] Ottilie S et al. (1997) Dimerization properties of human BAD. Identification of a BH-3 domain and analysis of its binding to mutant BCL-2 and BCL-XL proteins. J Biol Chem 272: 30866-72 PubMed GONUTS page

[PMID:17668322-32] Lu D et al. (2007) Protein kinase C-epsilon protects MCF-7 cells from TNF-mediated cell death by inhibiting Bax translocation. Apoptosis 12: 1893-900 PubMed GONUTS page

[PMID:15637643-33] Precht TA et al. (2005) The permeability transition pore triggers Bax translocation to mitochondria during neuronal apoptosis. Cell Death Differ 12: 255-65 PubMed GONUTS page

[PMID:12499352-34] Karbowski M et al. (2002) Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. J Cell Biol 159: 931-8 PubMed GONUTS page

[PMID:10702418-35] Podestà F et al. (2000) Bax is increased in the retina of diabetic subjects and is associated with pericyte apoptosis in vivo and in vitro. Am J Pathol 156: 1025-32 PubMed GONUTS page

[PMID:15705586-36] Sun Y & Leaman DW (2005) Involvement of Noxa in cellular apoptotic responses to interferon, double-stranded RNA, and virus infection. J Biol Chem 280: 15561-8 PubMed GONUTS page

[PMID:21199865-37] 38.0 ^38.1 Czabotar PE et al. (2011) Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis. J Biol Chem 286: 7123-31 PubMed GONUTS page

[PMID:22006182-38] 39.0 ^39.1 ^39.2 ^39.3 Pang X et al. (2011) Active Bax and Bak are functional holins. Genes Dev 25: 2278-90 PubMed GONUTS page

[PMID:9531611-39] Meijerink JP et al. (1998) Hematopoietic malignancies demonstrate loss-of-function mutations of BAX. Blood 91: 2991-7 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

[26]

[27]

[28]

[29]

[30]

[31]

[32]

[33]

[34]

[35]

[36]

[37]

[38]

[39]

[40]

HUMAN:BAX

Contents

Annotations

Notes

References

a

b

c

d

e

h

i

l

m

n

n cont.

p

r

t

Personal tools

Namespaces

Variants

Views

Actions

Search

Navigation

Cacao

Journal Clubs

page contributors

Toolbox