HUMAN:B2CL1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	BCL2L1 (synonyms: BCL2L, BCLX)
Protein Name(s)	Bcl-2-like protein 1 Bcl2-L-1 Apoptosis regulator Bcl-X
External Links
UniProt	Q07817
EMBL	Z23115 Z23116 U72398 CR936637 BT007208 AL160175 AL117381 AL117381 AL160175 CH471077 CH471077 CH471077 BC019307
CCDS	CCDS13188.1 CCDS13189.1
PIR	B47537 JE0203
RefSeq	NP_001182.1 NP_612815.1 XP_005260543.1 XP_005260544.1
UniGene	Hs.516966
PDB	1BXL 1G5J 1LXL 1MAZ 1R2D 1R2E 1R2G 1R2H 1R2I 1YSG 1YSI 1YSN 2B48 2LP8 2LPC 2M03 2M04 2ME8 2ME9 2MEJ 2O1Y 2O2M 2O2N 2P1L 2PON 2YJ1 2YQ6 2YQ7 2YXJ 3CVA 3FDL 3FDM 3INQ 3IO8 3PL7 3QKD 3R85 3SP7 3SPF 3WIZ 3ZK6 3ZLN 3ZLO 3ZLR 4A1U 4A1W 4AQ3 4BPK 4C52 4C5D 4CIN 4EHR 4HNJ 4IEH 4TUH
PDBsum	1BXL 1G5J 1LXL 1MAZ 1R2D 1R2E 1R2G 1R2H 1R2I 1YSG 1YSI 1YSN 2B48 2LP8 2LPC 2M03 2M04 2ME8 2ME9 2MEJ 2O1Y 2O2M 2O2N 2P1L 2PON 2YJ1 2YQ6 2YQ7 2YXJ 3CVA 3FDL 3FDM 3INQ 3IO8 3PL7 3QKD 3R85 3SP7 3SPF 3WIZ 3ZK6 3ZLN 3ZLO 3ZLR 4A1U 4A1W 4AQ3 4BPK 4C52 4C5D 4CIN 4EHR 4HNJ 4IEH 4TUH
DisProt	DP00298
ProteinModelPortal	Q07817
SMR	Q07817
BioGrid	107070
DIP	DIP-30916N
IntAct	Q07817
MINT	MINT-89538
STRING	9606.ENSP00000302564
BindingDB	Q07817
ChEMBL	CHEMBL3137283
TCDB	1.A.21.1.1
PhosphoSite	Q07817
DMDM	728955
MaxQB	Q07817
PaxDb	Q07817
PRIDE	Q07817
DNASU	598
Ensembl	ENST00000307677 ENST00000376055 ENST00000376062
GeneID	598
KEGG	hsa:598
UCSC	uc002wwl.3
CTD	598
GeneCards	GC20M030252
HGNC	HGNC:992
HPA	CAB000105 HPA035734
MIM	600039
neXtProt	NX_Q07817
PharmGKB	PA76
eggNOG	NOG300479
GeneTree	ENSGT00530000062935
HOGENOM	HOG000056452
InParanoid	Q07817
KO	K04570
OMA	NGSPSWH
OrthoDB	EOG70GMGD
PhylomeDB	Q07817
TreeFam	TF315834
Reactome	REACT_330 REACT_75927
ChiTaRS	BCL2L1
EvolutionaryTrace	Q07817
GeneWiki	BCL2-like_1_(gene)
GenomeRNAi	598
NextBio	2433
PMAP-CutDB	Q07817
PRO	PR:Q07817
Proteomes	UP000005640
Bgee	Q07817
CleanEx	HS_BCL2L1
ExpressionAtlas	Q07817
Genevestigator	Q07817
GO	GO:0097136 GO:0030054 GO:0005813 GO:0005737 GO:0005829 GO:0016021 GO:0005743 GO:0005759 GO:0005741 GO:0005739 GO:0031965 GO:0005730 GO:0005634 GO:0030672 GO:0051434 GO:0042802 GO:0046982 GO:0042803 GO:0019901 GO:0008637 GO:0006915 GO:0071839 GO:0008283 GO:0060154 GO:0071312 GO:0071230 GO:0071480 GO:0000910 GO:0006897 GO:0097192 GO:0009566 GO:0007281 GO:0040007 GO:0097284 GO:0001701 GO:0045087 GO:0097193 GO:0008630 GO:0008584 GO:0070584 GO:0007093 GO:2000811 GO:0043066 GO:0010507 GO:0090005 GO:1900118 GO:2001240 GO:2001243 GO:1902230 GO:0043524 GO:0090201 GO:0051402 GO:0035872 GO:0001541 GO:0008284 GO:2001244 GO:0046902 GO:0051881 GO:0001836 GO:0046898 GO:0034097 GO:0007283 GO:0019050
InterPro	IPR013279 IPR002475 IPR004725 IPR020717 IPR020726 IPR020728 IPR003093 IPR020731 IPR026298
PANTHER	PTHR11256 PTHR11256:SF12
Pfam	PF00452 PF02180
PRINTS	PR01864 PR01862
SMART	SM00265
TIGRFAMs	TIGR00865
PROSITE	PS50062 PS01080 PS01258 PS01259 PS01260 PS50063

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:1902236	negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway	PMID:29507230^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051434	BH3 domain binding	PMID:21639858^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9Y5Z4	F		Seeded From UniProt	complete
involved_in	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	PMID:12011449^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902230	negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage	PMID:16608847^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090201	negative regulation of release of cytochrome c from mitochondria	PMID:21041309^[5]	ECO:0000305	curator inference used in manual assertion	GO:1903077	P		Seeded From UniProt	complete
involved_in	GO:1903077	negative regulation of protein localization to plasma membrane	PMID:21041309^[5]	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^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046902	regulation of mitochondrial membrane permeability	PMID:9843949^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:12011449^[3]	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^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900118	negative regulation of execution phase of apoptosis	PMID:20673843^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0097136	Bcl-2 family protein complex	PMID:21199865^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:9388232^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:21840391^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9H4B4	F		Seeded From UniProt	complete
involved_in	GO:0007093	mitotic cell cycle checkpoint	PMID:21840391^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005813	centrosome	PMID:21840391^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	PMID:12667443^[11]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:20673843^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0032465	regulation of cytokinesis	PMID:21840391^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000135647 UniProtKB:P10415 UniProtKB:Q07817 ZFIN:ZDB-GENE-010730-1	P		Seeded From UniProt	complete
involved_in	GO:0097192	extrinsic apoptotic signaling pathway in absence of ligand	PMID:21873635^[12]	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^[12]	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:0043066	negative regulation of apoptotic process	PMID:21873635^[12]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:101769 MGI:MGI:102687 MGI:MGI:88138 MGI:MGI:88139 PANTHER:PTN000135647 RGD:2199 RGD:2200 RGD:620525 UniProtKB:P10415 UniProtKB:Q07817 UniProtKB:Q07820 UniProtKB:Q92843 WB:WBGene00000423 ZFIN:ZDB-GENE-000511-7 ZFIN:ZDB-GENE-010730-1	P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:21873635^[12]	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
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	PMID:21873635^[12]	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
part_of	GO:0005741	mitochondrial outer membrane	PMID:21873635^[12]	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:1902042	negative regulation of extrinsic apoptotic signaling pathway via death domain receptors	PMID:26582200^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:7650367^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034097	response to cytokine	PMID:9184696^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019050	suppression by virus of host apoptotic process	PMID:15231831^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21856303^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07817	F		Seeded From UniProt	complete
involved_in	GO:0097284	hepatocyte apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0071839	apoptotic process in bone marrow cell	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0071480	cellular response to gamma radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0071312	cellular response to alkaloid	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0071230	cellular response to amino acid stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0070584	mitochondrion morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0060154	cellular process regulating host cell cycle in response to virus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	F		Seeded From UniProt	complete
involved_in	GO:0046898	response to cycloheximide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0040008	regulation of growth	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
part_of	GO:0031966	mitochondrial membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	C		Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0009566	fertilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0007283	spermatogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	C		Seeded From UniProt	complete
part_of	GO:0005783	endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	C		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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
involved_in	GO:0001701	in utero embryonic development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q64373 ensembl:ENSMUSP00000105445	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:Q64373 ensembl:ENSMUSP00000105445	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004725	C		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:IPR003093 InterPro:IPR004725 InterPro:IPR013279 InterPro:IPR020717 InterPro:IPR020726 InterPro:IPR020728 InterPro:IPR020731 InterPro:IPR026298 InterPro:IPR036834	P		Seeded From UniProt	complete
involved_in	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	PMID:21567405^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000811	negative regulation of anoikis	PMID:15006356^[19]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q08117)	Seeded From UniProt	complete
involved_in	GO:0090201	negative regulation of release of cytochrome c from mitochondria	PMID:12667443^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051434	BH3 domain binding	PMID:15901672^[20]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q16611	F		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:17289999^[21]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q16611)\|has_regulation_target:(UniProtKB:Q07812)	Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:21567405^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	PMID:19767770^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15131699^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q07817-1	F		Seeded From UniProt	complete
involved_in	GO:0008637	apoptotic mitochondrial changes	PMID:9393856^[24]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:10365962^[25]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2001240	negative regulation of extrinsic apoptotic signaling pathway in absence of ligand	PMID:8358789^[26]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001244	positive regulation of intrinsic apoptotic signaling pathway	Reactome:R-HSA-111453	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0019221	cytokine-mediated signaling pathway	Reactome:R-HSA-6785807	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	Reactome:R-HSA-879201 Reactome:R-HSA-6790025 Reactome:R-HSA-508162	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0254	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
part_of	GO:0005856	cytoskeleton	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206	C		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: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: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
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
part_of	GO:0005634	nucleus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0968	C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0999 UniProtKB-SubCell:SL-0168	C		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0770	C		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
part_of	GO:0030672	synaptic vesicle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0260	C		Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0182	C		Seeded From UniProt	complete
part_of	GO:0005815	microtubule organizing center	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0048	C		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0170	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0091	C		Seeded From UniProt	complete
involved_in	GO:0010507	negative regulation of autophagy	PMID:18309324^[27]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:Q14457)	Seeded From UniProt	complete
edit table

Notes

References

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

↑ Wu, Y et al. (2018) Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by degrading Bcl-xL. Proc. Natl. Acad. Sci. U.S.A. 115 E2762-E2771 PubMed GONUTS page
↑ Ambrosi, E et al. (2011) Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL. Biochem. J. 438 291-301 PubMed GONUTS page
↑ ^3.0 ^3.1 Xue, L et al. (2002) Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis. Proc. Natl. Acad. Sci. U.S.A. 99 6925-30 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
↑ ^5.0 ^5.1 Du, H et al. (2011) BH3 domains other than Bim and Bid can directly activate Bax/Bak. J. Biol. Chem. 286 491-501 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 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
↑ ^7.0 ^7.1 Jääskeläinen, M et al. (2010) Regulation of cell death in human fetal and adult ovaries--role of Bok and Bcl-X(L). Mol. Cell. Endocrinol. 330 17-24 PubMed GONUTS page
↑ 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
↑ 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
↑ ^10.0 ^10.1 ^10.2 ^10.3 Wang, J et al. (2011) Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle progression and checkpoints. Cell. Signal. 23 2030-8 PubMed GONUTS page
↑ ^11.0 ^11.1 Mihara, M et al. (2003) p53 has a direct apoptogenic role at the mitochondria. Mol. Cell 11 577-90 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 ^12.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Urresti, J et al. (2016) Lifeguard Inhibits Fas Ligand-mediated Endoplasmic Reticulum-Calcium Release Mandatory for Apoptosis in Type II Apoptotic Cells. J. Biol. Chem. 291 1221-34 PubMed GONUTS page
↑ Broome, HE et al. (1995) Expression of Bcl-2, Bcl-x, and Bax after T cell activation and IL-2 withdrawal. J. Immunol. 155 2311-7 PubMed GONUTS page
↑ Li, L et al. (1997) The apoptosis and proliferation of SAC-activated B cells by IL-10 are associated with changes in Bcl-2, Bcl-xL, and Mcl-1 expression. Cell. Immunol. 178 33-41 PubMed GONUTS page
↑ Seo, SY et al. (2004) BAD is a pro-survival factor prior to activation of its pro-apoptotic function. J. Biol. Chem. 279 42240-9 PubMed GONUTS page
↑ Ospina, A et al. (2011) Protein oligomerization mediated by the transmembrane carboxyl terminal domain of Bcl-XL. FEBS Lett. 585 2935-42 PubMed GONUTS page
↑ ^18.0 ^18.1 Kim, N et al. (2012) Human nuclear clusterin mediates apoptosis by interacting with Bcl-XL through C-terminal coiled coil domain. J. Cell. Physiol. 227 1157-67 PubMed GONUTS page
↑ Jan, Y et al. (2004) A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell 116 751-62 PubMed GONUTS page
↑ Willis, SN et al. (2005) Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 19 1294-305 PubMed GONUTS page
↑ 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
↑ 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
↑ Jeong, SY et al. (2004) Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers. EMBO J. 23 2146-55 PubMed GONUTS page
↑ Vander Heiden, MG et al. (1997) Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria. Cell 91 627-37 PubMed GONUTS page
↑ Shimizu, S et al. (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399 483-7 PubMed GONUTS page
↑ Boise, LH et al. (1993) bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell 74 597-608 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:29507230-1] Wu, Y et al. (2018) Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by degrading Bcl-xL. Proc. Natl. Acad. Sci. U.S.A. 115 E2762-E2771 PubMed GONUTS page

[PMID:21639858-2] Ambrosi, E et al. (2011) Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL. Biochem. J. 438 291-301 PubMed GONUTS page

[PMID:12011449-3] 3.0 ^3.1 Xue, L et al. (2002) Siva-1 binds to and inhibits BCL-X(L)-mediated protection against UV radiation-induced apoptosis. Proc. Natl. Acad. Sci. U.S.A. 99 6925-30 PubMed GONUTS page

[PMID:16608847-4] 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:21041309-5] 5.0 ^5.1 Du, H et al. (2011) BH3 domains other than Bim and Bid can directly activate Bax/Bak. J. Biol. Chem. 286 491-501 PubMed GONUTS page

[PMID:9843949-6] 6.0 ^6.1 ^6.2 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:20673843-7] 7.0 ^7.1 Jääskeläinen, M et al. (2010) Regulation of cell death in human fetal and adult ovaries--role of Bok and Bcl-X(L). Mol. Cell. Endocrinol. 330 17-24 PubMed GONUTS page

[PMID:21199865-8] 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:9388232-9] 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:21840391-10] 10.0 ^10.1 ^10.2 ^10.3 Wang, J et al. (2011) Bcl-xL phosphorylation at Ser49 by polo kinase 3 during cell cycle progression and checkpoints. Cell. Signal. 23 2030-8 PubMed GONUTS page

[PMID:12667443-11] 11.0 ^11.1 Mihara, M et al. (2003) p53 has a direct apoptogenic role at the mitochondria. Mol. Cell 11 577-90 PubMed GONUTS page

[PMID:21873635-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 ^12.5 ^12.6 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:26582200-13] Urresti, J et al. (2016) Lifeguard Inhibits Fas Ligand-mediated Endoplasmic Reticulum-Calcium Release Mandatory for Apoptosis in Type II Apoptotic Cells. J. Biol. Chem. 291 1221-34 PubMed GONUTS page

[PMID:7650367-14] Broome, HE et al. (1995) Expression of Bcl-2, Bcl-x, and Bax after T cell activation and IL-2 withdrawal. J. Immunol. 155 2311-7 PubMed GONUTS page

[PMID:9184696-15] Li, L et al. (1997) The apoptosis and proliferation of SAC-activated B cells by IL-10 are associated with changes in Bcl-2, Bcl-xL, and Mcl-1 expression. Cell. Immunol. 178 33-41 PubMed GONUTS page

[PMID:15231831-16] Seo, SY et al. (2004) BAD is a pro-survival factor prior to activation of its pro-apoptotic function. J. Biol. Chem. 279 42240-9 PubMed GONUTS page

[PMID:21856303-17] Ospina, A et al. (2011) Protein oligomerization mediated by the transmembrane carboxyl terminal domain of Bcl-XL. FEBS Lett. 585 2935-42 PubMed GONUTS page

[PMID:21567405-18] 18.0 ^18.1 Kim, N et al. (2012) Human nuclear clusterin mediates apoptosis by interacting with Bcl-XL through C-terminal coiled coil domain. J. Cell. Physiol. 227 1157-67 PubMed GONUTS page

[PMID:15006356-19] Jan, Y et al. (2004) A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell 116 751-62 PubMed GONUTS page

[PMID:15901672-20] Willis, SN et al. (2005) Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. Genes Dev. 19 1294-305 PubMed GONUTS page

[PMID:17289999-21] 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:19767770-22] 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:15131699-23] Jeong, SY et al. (2004) Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers. EMBO J. 23 2146-55 PubMed GONUTS page

[PMID:9393856-24] Vander Heiden, MG et al. (1997) Bcl-xL regulates the membrane potential and volume homeostasis of mitochondria. Cell 91 627-37 PubMed GONUTS page

[PMID:10365962-25] Shimizu, S et al. (1999) Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399 483-7 PubMed GONUTS page

[PMID:8358789-26] Boise, LH et al. (1993) bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell 74 597-608 PubMed GONUTS page

[PMID:18309324-27] 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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HUMAN:B2CL1

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