HUMAN:BAX

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	BAX (synonyms: BCL2L4)
Protein Name(s)	Apoptosis regulator BAX Bcl-2-like protein 4 Bcl2-L-4
External Links
UniProt	Q07812
EMBL	L22473 L22474 L22475 U19599 AF007826 AF247393 AJ417988 AF250190 AK291076 AY217036 CH471177 CH471177 BC014175
CCDS	CCDS12742.1 CCDS12743.1 CCDS12744.1 CCDS12745.2
PIR	A47538 B47538 C47538 I38921 JC7255
RefSeq	NP_001278357.1 NP_001278360.1 NP_004315.1 NP_620116.1 NP_620118.1 NP_620119.2
UniGene	Hs.624291
PDB	1F16 2G5B 2K7W 2LR1 3PK1 3PL7 4BD2 4BD6 4BD7 4BD8 4BDU
PDBsum	1F16 2G5B 2K7W 2LR1 3PK1 3PL7 4BD2 4BD6 4BD7 4BD8 4BDU
ProteinModelPortal	Q07812
SMR	Q07812
BioGrid	107057
DIP	DIP-232N
IntAct	Q07812
MINT	MINT-134330
ChEMBL	CHEMBL5318
TCDB	1.A.21.1.2
PhosphoSite	Q07812
DMDM	728945
MaxQB	Q07812
PaxDb	Q07812
PRIDE	Q07812
DNASU	581
Ensembl	ENST00000293288 ENST00000345358 ENST00000354470 ENST00000356483 ENST00000415969 ENST00000515540
GeneID	581
KEGG	hsa:581
UCSC	uc002plf.1 uc002plj.3 uc002plk.3 uc002pll.3
CTD	581
GeneCards	GC19P049458
HGNC	HGNC:959
HPA	CAB004206 HPA027878
MIM	600040
neXtProt	NX_Q07812
PharmGKB	PA25269
eggNOG	NOG46695
GeneTree	ENSGT00730000111112
HOVERGEN	HBG003606
InParanoid	Q07812
KO	K02159
OMA	ADMFADG
PhylomeDB	Q07812
TreeFam	TF315834
Reactome	REACT_584
ChiTaRS	BAX
EvolutionaryTrace	Q07812
GeneWiki	Bcl-2-associated_X_protein
GenomeRNAi	581
NextBio	2371
PMAP-CutDB	Q07812
PRO	PR:Q07812
Proteomes	UP000005640
Bgee	Q07812
CleanEx	HS_BAX
ExpressionAtlas	Q07812
Genevestigator	Q07812
GO	GO:0097144 GO:0097136 GO:0005829 GO:0005783 GO:0005789 GO:0070062 GO:0016020 GO:0005741 GO:0005757 GO:0005739 GO:0005634 GO:0046930 GO:0051434 GO:0015267 GO:0042802 GO:0008289 GO:0046982 GO:0042803 GO:0006919 GO:0008635 GO:0097296 GO:0008637 GO:0006915 GO:1902263 GO:1902262 GO:0097190 GO:0001783 GO:0001782 GO:0002358 GO:0002352 GO:1990117 GO:0001974 GO:0071310 GO:0034644 GO:0021987 GO:0045136 GO:0035234 GO:0032469 GO:0010248 GO:0097191 GO:0097192 GO:0008625 GO:0009566 GO:0007281 GO:0006687 GO:0048873 GO:0021854 GO:0097193 GO:0072332 GO:0008630 GO:0070059 GO:0001822 GO:0043653 GO:0008053 GO:0070584 GO:0002262 GO:2001234 GO:0032471 GO:0048147 GO:0043524 GO:0033137 GO:0032091 GO:0051402 GO:0001764 GO:0042475 GO:0001541 GO:1902512 GO:0043065 GO:0060058 GO:0002904 GO:0048087 GO:1900103 GO:2001241 GO:2001244 GO:1901030 GO:0043525 GO:0032461 GO:0090200 GO:0051281 GO:0048597 GO:0051260 GO:0001844 GO:0051259 GO:0051726 GO:0033599 GO:1902445 GO:0051881 GO:0006808 GO:0043497 GO:0043496 GO:0001836 GO:0032976 GO:0048678 GO:0010332 GO:0009651 GO:0009636 GO:0060041 GO:1990009 GO:0046666 GO:0060011 GO:0048515 GO:0001777 GO:0070242 GO:0006927 GO:0060068 GO:0016032
InterPro	IPR026304 IPR002475 IPR020717 IPR020726 IPR020728 IPR026298
PANTHER	PTHR11256 PTHR11256:SF8
Pfam	PF00452
PRINTS	PR01862
PROSITE	PS50062 PS01080 PS01258 PS01259

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006915	apoptosis	PMID:9531611^[1]	ECO:0000315			P		Figures 2 and 3.	complete CACAO 3542
part_of	GO:0005737	cytoplasm	PMID:29531808^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	PMID:29531808^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090200	positive regulation of release of cytochrome c from mitochondria	PMID:21262771^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001244	positive regulation of intrinsic apoptotic signaling pathway	PMID:21262771^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010917	negative regulation of mitochondrial membrane potential	PMID:16751333^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:16751333^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:17464193^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0071944	cell periphery	PMID:21803450^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(GO:0042981)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16302269^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:15102863^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:9660918^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:9531611^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
involved_in	GO:1990117	B cell receptor apoptotic signaling pathway	PMID:15214043^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902512	positive regulation of apoptotic DNA fragmentation	PMID:11350920^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097193	intrinsic apoptotic signaling pathway	PMID:9219694^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097191	extrinsic apoptotic signaling pathway	PMID:15214043^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0046930	pore complex	PMID:9219694^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16113678^[15]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F		Seeded From UniProt	complete
enables	GO:0015267	channel activity	PMID:9219694^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008625	extrinsic apoptotic signaling pathway via death domain receptors	PMID:16199525^[16]	ECO:0000305	curator inference used in manual assertion	GO:0001836 GO:0005739	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15705586^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:17823127^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16199525^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:15705586^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:17823127^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001836	release of cytochrome c from mitochondria	PMID:16199525^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097193	intrinsic apoptotic signaling pathway	PMID:16462759^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097190	apoptotic signaling pathway	PMID:16424160^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051881	regulation of mitochondrial membrane potential	PMID:9843949^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051434	BH3 domain binding	PMID:17052454^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P55957	F		Seeded From UniProt	complete
enables	GO:0051434	BH3 domain binding	PMID:15705586^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13794	F		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:14522999^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9111042^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10415	F		Seeded From UniProt	complete
involved_in	GO:0043653	mitochondrial fragmentation involved in apoptotic process	PMID:12499352^[25]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043525	positive regulation of neuron apoptotic process	PMID:15637643^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043497	regulation of protein heterodimerization activity	PMID:9111042^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	P		Seeded From UniProt	complete
involved_in	GO:0043496	regulation of protein homodimerization activity	PMID:9111042^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:9111042^[24]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:16608847^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032976	release of matrix enzymes from mitochondria	PMID:9843949^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010248	establishment or maintenance of transmembrane electrochemical gradient	PMID:9843949^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	PMID:16307838^[28]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008637	apoptotic mitochondrial changes	PMID:9843949^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008635	activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c	PMID:15214043^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008289	lipid binding	PMID:14522999^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0008053	mitochondrial fusion	PMID:14769861^[29]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	PMID:11350920^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	PMID:11912183^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:11912183^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	PMID:16424160^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	PMID:16424160^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005757	mitochondrial permeability transition pore complex	PMID:9843949^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:11912183^[30]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001836	release of cytochrome c from mitochondria	PMID:9843949^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001836	release of cytochrome c from mitochondria	PMID:17052454^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001783	B cell apoptotic process	PMID:16424160^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001783	B cell apoptotic process	PMID:15214043^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:12925958^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005635	nuclear envelope	PMID:12925958^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12925958^[31]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2001244	positive regulation of intrinsic apoptotic signaling pathway	PMID:14963330^[32]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001244	positive regulation of intrinsic apoptotic signaling pathway	PMID:21199865^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900103	positive regulation of endoplasmic reticulum unfolded protein response	PMID:16645094^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_input:(UniProtKB:P17861)\|has_direct_input(UniProtKB:O75460)	Seeded From UniProt	complete
part_of	GO:0097144	BAX complex	PMID:19767770^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0097136	Bcl-2 family protein complex	PMID:21199865^[33]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0090200	positive regulation of release of cytochrome c from mitochondria	PMID:14963330^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070059	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	PMID:16645094^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051434	BH3 domain binding	PMID:21199865^[33]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	PMID:19767770^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051259	protein complex oligomerization	PMID:19074440^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:17289999^[37]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032461	positive regulation of protein oligomerization	PMID:19805544^[38]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q9Y371)	Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	PMID:9388232^[39]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:9920818^[40]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:19767770^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15102863^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:19767770^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15102863^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0097192	extrinsic apoptotic signaling pathway in absence of ligand	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:101769 MGI:MGI:108052 MGI:MGI:1097161 MGI:MGI:88138 MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648 UniProtKB:Q07820	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88138 MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648 RGD:2192 RGD:2199 RGD:2200 RGD:620525 RGD:620621 RGD:620717 RGD:621635 RGD:70984 UniProtKB:P10415 UniProtKB:Q07812 UniProtKB:Q07820 UniProtKB:Q16611 UniProtKB:Q92843 ZFIN:ZDB-GENE-000511-7 ZFIN:ZDB-GENE-030825-1 ZFIN:ZDB-GENE-051012-1	F		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99702 PANTHER:PTN000883418 RGD:2192 UniProtKB:Q07812 ZFIN:ZDB-GENE-000511-6	P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1330841 MGI:MGI:1858494 MGI:MGI:99702 PANTHER:PTN000135648 RGD:621635 UniProtKB:P10415 UniProtKB:Q07812 UniProtKB:Q16611	F		Seeded From UniProt	complete
enables	GO:0015267	channel activity	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000883418 UniProtKB:Q07812	F		Seeded From UniProt	complete
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029131 MGI:MGI:101769 MGI:MGI:1097161 MGI:MGI:88138 MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648	P		Seeded From UniProt	complete
involved_in	GO:0008053	mitochondrial fusion	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99702 PANTHER:PTN000883418 UniProtKB:Q07812	P		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648 RGD:2192 RGD:2200 UniProtKB:P10415 UniProtKB:Q07817 WB:WBGene00000423	C		Seeded From UniProt	complete
involved_in	GO:0001836	release of cytochrome c from mitochondria	PMID:21873635^[41]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99702 PANTHER:PTN000883418 UniProtKB:Q07812	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23374347^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22198199^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20850011^[44]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20360684^[45]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19767770^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19074440^[36]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19062087^[46]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18835031^[47]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18547146^[48]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17668322^[49]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17289999^[37]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:14963330^[32]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:10620504^[50]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07812	F	occurs_in:(GO:0005739)\|occurs_in:(GO:0005829)	Seeded From UniProt	complete
involved_in	GO:2001244	positive regulation of intrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:2001234	negative regulation of apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:1902445	regulation of mitochondrial membrane permeability involved in programmed necrotic cell death	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:1902263	apoptotic process involved in embryonic digit morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:1902262	apoptotic process involved in blood vessel morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:1902110	positive regulation of mitochondrial membrane permeability involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:1902108	regulation of mitochondrial membrane permeability involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0097296	activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0097192	extrinsic apoptotic signaling pathway in absence of ligand	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0097190	apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
part_of	GO:0097144	BAX complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	C		Seeded From UniProt	complete
involved_in	GO:0072332	intrinsic apoptotic signaling pathway by p53 class mediator	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0071310	cellular response to organic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0070584	mitochondrion morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0070242	thymocyte apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0070059	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0060068	vagina development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0060058	positive regulation of apoptotic process involved in mammary gland involution	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0060041	retina development in camera-type eye	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0060011	Sertoli cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0051726	regulation of cell cycle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0051402	neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0051281	positive regulation of release of sequestered calcium ion into cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0051260	protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	F		Seeded From UniProt	complete
involved_in	GO:0048873	homeostasis of number of cells within a tissue	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0048872	homeostasis of number of cells	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0048678	response to axon injury	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0048597	post-embryonic camera-type eye morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0048515	spermatid differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0048147	negative regulation of fibroblast proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0048087	positive regulation of developmental pigmentation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	F		Seeded From UniProt	complete
involved_in	GO:0046666	retinal cell programmed cell death	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0045136	development of secondary sexual characteristics	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0043525	positive regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0043523	regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0043281	regulation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	F		Seeded From UniProt	complete
involved_in	GO:0042475	odontogenesis of dentin-containing tooth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0035234	ectopic germ cell programmed cell death	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0035108	limb morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0034644	cellular response to UV	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0033599	regulation of mammary gland epithelial cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0033137	negative regulation of peptidyl-serine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0032471	negative regulation of endoplasmic reticulum calcium ion concentration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
part_of	GO:0031966	mitochondrial membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	C		Seeded From UniProt	complete
enables	GO:0030544	Hsp70 protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	F		Seeded From UniProt	complete
involved_in	GO:0021987	cerebral cortex development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0021854	hypothalamus development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0010524	positive regulation of calcium ion transport into cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0010332	response to gamma radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0010212	response to ionizing radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0009791	post-embryonic development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0009651	response to salt stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0009611	response to wounding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0009566	fertilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008637	apoptotic mitochondrial changes	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008635	activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008625	extrinsic apoptotic signaling pathway via death domain receptors	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008584	male gonad development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008283	cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0008053	mitochondrial fusion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0007548	sex differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0007399	nervous system development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0007281	germ cell development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0006808	regulation of nitrogen utilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0006687	glycosphingolipid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	C		Seeded From UniProt	complete
involved_in	GO:0002904	positive regulation of B cell apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0002358	B cell homeostatic proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0002352	B cell negative selection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0002262	myeloid cell homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001974	blood vessel remodeling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001844	protein insertion into mitochondrial membrane involved in apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001836	release of cytochrome c from mitochondria	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001822	kidney development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001783	B cell apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001782	B cell homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001777	T cell homeostatic proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001776	leukocyte homeostasis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001764	neuron migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0001541	ovarian follicle development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q07813 ensembl:ENSMUSP00000033093	P		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020717 InterPro:IPR020726 InterPro:IPR020728 InterPro:IPR026298 InterPro:IPR036834	P		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR026304	P		Seeded From UniProt	complete
involved_in	GO:0070059	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	PMID:22934019^[51]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034620	cellular response to unfolded protein	PMID:22013210^[52]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903896	positive regulation of IRE1-mediated unfolded protein response	PMID:22013210^[52]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032469	endoplasmic reticulum calcium ion homeostasis	PMID:18309324^[53]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901030	positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway	Reactome:R-HSA-114294	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	Reactome:R-HSA-5633008	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006977	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest	Reactome:R-HSA-6791312	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006367	transcription initiation from RNA polymerase II promoter	Reactome:R-HSA-212436	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-9008839 Reactome:R-HSA-6803892 Reactome:R-HSA-3700984 Reactome:R-HSA-168849 Reactome:R-HSA-139917 Reactome:R-HSA-114264	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	Reactome:R-HSA-114275 Reactome:R-HSA-114264	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001844	protein insertion into mitochondrial membrane involved in apoptotic signaling pathway	Reactome:R-HSA-114264	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1000 UniProtKB-SubCell:SL-0172	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 Meijerink, JP et al. (1998) Hematopoietic malignancies demonstrate loss-of-function mutations of BAX. Blood 91 2991-7 PubMed GONUTS page
↑ ^2.0 ^2.1 Kuriyama, S et al. (2018) PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetro-oligomerization through interaction with Bid in human colon cancer. Cell Death Discov 4 11 PubMed GONUTS page
↑ ^3.0 ^3.1 Niemi, NM et al. (2011) MK-STYX, a catalytically inactive phosphatase regulating mitochondrially dependent apoptosis. Mol. Cell. Biol. 31 1357-68 PubMed GONUTS page
↑ ^4.0 ^4.1 Wang, L et al. (2006) Cell-based screening and validation of human novel genes associated with cell viability. J Biomol Screen 11 369-76 PubMed GONUTS page
↑ Park, KM et al. (2007) Identification of novel regulators of apoptosis using a high-throughput cell-based screen. Mol. Cells 23 170-4 PubMed GONUTS page
↑ Kögel, D et al. (2012) The APP intracellular domain (AICD) potentiates ER stress-induced apoptosis. Neurobiol. Aging 33 2200-9 PubMed GONUTS page
↑ Bartholomeusz, G et al. (2006) Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces apoptosis. Mol. Carcinog. 45 73-83 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Yakovlev, AG et al. (2004) BOK and NOXA are essential mediators of p53-dependent apoptosis. J. Biol. Chem. 279 28367-74 PubMed GONUTS page
↑ Xu, Q & Reed, JC (1998) Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Mol. Cell 1 337-46 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 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
↑ ^13.0 ^13.1 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
↑ ^14.0 ^14.1 ^14.2 Antonsson, B et al. (1997) Inhibition of Bax channel-forming activity by Bcl-2. Science 277 370-2 PubMed GONUTS page
↑ Zhang, H et al. (2005) Clusterin inhibits apoptosis by interacting with activated Bax. Nat. Cell Biol. 7 909-15 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Tan, KO et al. (2005) MAP-1 is a mitochondrial effector of Bax. Proc. Natl. Acad. Sci. U.S.A. 102 14623-8 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 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
↑ ^18.0 ^18.1 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
↑ 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
↑ ^20.0 ^20.1 ^20.2 ^20.3 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
↑ ^21.0 ^21.1 ^21.2 ^21.3 ^21.4 ^21.5 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
↑ ^22.0 ^22.1 Walensky, LD et al. (2006) A stapled BID BH3 helix directly binds and activates BAX. Mol. Cell 24 199-210 PubMed GONUTS page
↑ ^23.0 ^23.1 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
↑ ^24.0 ^24.1 ^24.2 ^24.3 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ ^30.0 ^30.1 ^30.2 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
↑ ^31.0 ^31.1 ^31.2 Chung, YL et al. (2003) Hepatitis C virus NS5A as a potential viral Bcl-2 homologue interacts with Bax and inhibits apoptosis in hepatocellular carcinoma. Int. J. Cancer 107 65-73 PubMed GONUTS page
↑ ^32.0 ^32.1 ^32.2 Chipuk, JE et al. (2004) Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 303 1010-4 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 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
↑ ^34.0 ^34.1 Hetz, C et al. (2006) Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha. Science 312 572-6 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 ^35.3 ^35.4 Mamidipudi, V & Cartwright, CA (2009) A novel pro-apoptotic function of RACK1: suppression of Src activity in the intrinsic and Akt pathways. Oncogene 28 4421-33 PubMed GONUTS page
↑ ^36.0 ^36.1 Etxebarria, A et al. (2009) Endophilin B1/Bif-1 stimulates BAX activation independently from its capacity to produce large scale membrane morphological rearrangements. J. Biol. Chem. 284 4200-12 PubMed GONUTS page
↑ ^37.0 ^37.1 Willis, SN et al. (2007) Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 315 856-9 PubMed GONUTS page
↑ Rostovtseva, TK et al. (2009) Bax activates endophilin B1 oligomerization and lipid membrane vesiculation. J. Biol. Chem. 284 34390-9 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
↑ 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
↑ ^41.0 ^41.1 ^41.2 ^41.3 ^41.4 ^41.5 ^41.6 ^41.7 ^41.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Czabotar, PE et al. (2013) Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis. Cell 152 519-31 PubMed GONUTS page
↑ Renault, TT et al. (2012) The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast. FEBS Lett. 586 116-21 PubMed GONUTS page
↑ Montessuit, S et al. (2010) Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization. Cell 142 889-901 PubMed GONUTS page
↑ Chattopadhyay, S et al. (2010) Viral apoptosis is induced by IRF-3-mediated activation of Bax. EMBO J. 29 1762-73 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
↑ Kolluri, SK et al. (2008) A short Nur77-derived peptide converts Bcl-2 from a protector to a killer. Cancer Cell 14 285-98 PubMed GONUTS page
↑ Billen, LP et al. (2008) Bcl-XL inhibits membrane permeabilization by competing with Bax. PLoS Biol. 6 e147 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
↑ Antonsson, B et al. (2000) Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345 Pt 2 271-8 PubMed GONUTS page
↑ Brown, MK & Naidoo, N (2012) The endoplasmic reticulum stress response in aging and age-related diseases. Front Physiol 3 263 PubMed GONUTS page
↑ ^52.0 ^52.1 Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page
↑ Galluzzi, L et al. (2008) No death without life: vital functions of apoptotic effectors. Cell Death Differ. 15 1113-23 PubMed GONUTS page

[PMID:9531611-1] 1.0 ^1.1 Meijerink, JP et al. (1998) Hematopoietic malignancies demonstrate loss-of-function mutations of BAX. Blood 91 2991-7 PubMed GONUTS page

[PMID:29531808-2] 2.0 ^2.1 Kuriyama, S et al. (2018) PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetro-oligomerization through interaction with Bid in human colon cancer. Cell Death Discov 4 11 PubMed GONUTS page

[PMID:21262771-3] 3.0 ^3.1 Niemi, NM et al. (2011) MK-STYX, a catalytically inactive phosphatase regulating mitochondrially dependent apoptosis. Mol. Cell. Biol. 31 1357-68 PubMed GONUTS page

[PMID:16751333-4] 4.0 ^4.1 Wang, L et al. (2006) Cell-based screening and validation of human novel genes associated with cell viability. J Biomol Screen 11 369-76 PubMed GONUTS page

[PMID:17464193-5] Park, KM et al. (2007) Identification of novel regulators of apoptosis using a high-throughput cell-based screen. Mol. Cells 23 170-4 PubMed GONUTS page

[PMID:21803450-6] Kögel, D et al. (2012) The APP intracellular domain (AICD) potentiates ER stress-induced apoptosis. Neurobiol. Aging 33 2200-9 PubMed GONUTS page

[PMID:16302269-7] Bartholomeusz, G et al. (2006) Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces apoptosis. Mol. Carcinog. 45 73-83 PubMed GONUTS page

[PMID:15102863-8] 8.0 ^8.1 ^8.2 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:9660918-9] Xu, Q & Reed, JC (1998) Bax inhibitor-1, a mammalian apoptosis suppressor identified by functional screening in yeast. Mol. Cell 1 337-46 PubMed GONUTS page

[PMID:19946888-10] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:20458337-11] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:15214043-12] 12.0 ^12.1 ^12.2 ^12.3 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:11350920-13] 13.0 ^13.1 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:9219694-14] 14.0 ^14.1 ^14.2 Antonsson, B et al. (1997) Inhibition of Bax channel-forming activity by Bcl-2. Science 277 370-2 PubMed GONUTS page

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

[PMID:16199525-16] 16.0 ^16.1 ^16.2 Tan, KO et al. (2005) MAP-1 is a mitochondrial effector of Bax. Proc. Natl. Acad. Sci. U.S.A. 102 14623-8 PubMed GONUTS page

[PMID:15705586-17] 17.0 ^17.1 ^17.2 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:17823127-18] 18.0 ^18.1 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:16462759-19] 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:16424160-20] 20.0 ^20.1 ^20.2 ^20.3 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:9843949-21] 21.0 ^21.1 ^21.2 ^21.3 ^21.4 ^21.5 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:17052454-22] 22.0 ^22.1 Walensky, LD et al. (2006) A stapled BID BH3 helix directly binds and activates BAX. Mol. Cell 24 199-210 PubMed GONUTS page

[PMID:14522999-23] 23.0 ^23.1 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:9111042-24] 24.0 ^24.1 ^24.2 ^24.3 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:12499352-25] 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:15637643-26] 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:16608847-27] 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:16307838-28] 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:14769861-29] 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:11912183-30] 30.0 ^30.1 ^30.2 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:12925958-31] 31.0 ^31.1 ^31.2 Chung, YL et al. (2003) Hepatitis C virus NS5A as a potential viral Bcl-2 homologue interacts with Bax and inhibits apoptosis in hepatocellular carcinoma. Int. J. Cancer 107 65-73 PubMed GONUTS page

[PMID:14963330-32] 32.0 ^32.1 ^32.2 Chipuk, JE et al. (2004) Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science 303 1010-4 PubMed GONUTS page

[PMID:21199865-33] 33.0 ^33.1 ^33.2 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:16645094-34] 34.0 ^34.1 Hetz, C et al. (2006) Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha. Science 312 572-6 PubMed GONUTS page

[PMID:19767770-35] 35.0 ^35.1 ^35.2 ^35.3 ^35.4 Mamidipudi, V & Cartwright, CA (2009) A novel pro-apoptotic function of RACK1: suppression of Src activity in the intrinsic and Akt pathways. Oncogene 28 4421-33 PubMed GONUTS page

[PMID:19074440-36] 36.0 ^36.1 Etxebarria, A et al. (2009) Endophilin B1/Bif-1 stimulates BAX activation independently from its capacity to produce large scale membrane morphological rearrangements. J. Biol. Chem. 284 4200-12 PubMed GONUTS page

[PMID:17289999-37] 37.0 ^37.1 Willis, SN et al. (2007) Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science 315 856-9 PubMed GONUTS page

[PMID:19805544-38] Rostovtseva, TK et al. (2009) Bax activates endophilin B1 oligomerization and lipid membrane vesiculation. J. Biol. Chem. 284 34390-9 PubMed GONUTS page

[PMID:9388232-39] 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:9920818-40] 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:21873635-41] 41.0 ^41.1 ^41.2 ^41.3 ^41.4 ^41.5 ^41.6 ^41.7 ^41.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:23374347-42] Czabotar, PE et al. (2013) Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis. Cell 152 519-31 PubMed GONUTS page

[PMID:22198199-43] Renault, TT et al. (2012) The cytosolic domain of human Tom22 modulates human Bax mitochondrial translocation and conformation in yeast. FEBS Lett. 586 116-21 PubMed GONUTS page

[PMID:20850011-44] Montessuit, S et al. (2010) Membrane remodeling induced by the dynamin-related protein Drp1 stimulates Bax oligomerization. Cell 142 889-901 PubMed GONUTS page

[PMID:20360684-45] Chattopadhyay, S et al. (2010) Viral apoptosis is induced by IRF-3-mediated activation of Bax. EMBO J. 29 1762-73 PubMed GONUTS page

[PMID:19062087-46] 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:18835031-47] Kolluri, SK et al. (2008) A short Nur77-derived peptide converts Bcl-2 from a protector to a killer. Cancer Cell 14 285-98 PubMed GONUTS page

[PMID:18547146-48] Billen, LP et al. (2008) Bcl-XL inhibits membrane permeabilization by competing with Bax. PLoS Biol. 6 e147 PubMed GONUTS page

[PMID:17668322-49] 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:10620504-50] Antonsson, B et al. (2000) Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345 Pt 2 271-8 PubMed GONUTS page

[PMID:22934019-51] Brown, MK & Naidoo, N (2012) The endoplasmic reticulum stress response in aging and age-related diseases. Front Physiol 3 263 PubMed GONUTS page

[PMID:22013210-52] 52.0 ^52.1 Hetz, C et al. (2011) The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91 1219-43 PubMed GONUTS page

[PMID:18309324-53] Galluzzi, L et al. (2008) No death without life: vital functions of apoptotic effectors. Cell Death Differ. 15 1113-23 PubMed GONUTS page

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