about
sameAs
P688
Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondriaMCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domaintBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome cBAK multimerization for apoptosis, but not bid binding, is inhibited by negatively charged residue in the BAK hydrophobic grooveApoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or BakInteraction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosisProapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1BH3 domains other than Bim and Bid can directly activate Bax/BakPlasminogen kringle 5 induces endothelial cell apoptosis by triggering a voltage-dependent anion channel 1 (VDAC1) positive feedback loopDifferential contribution of Puma and Noxa in dual regulation of p53-mediated apoptotic pathwaysA common binding site mediates heterodimerization and homodimerization of Bcl-2 family membersA pathway sensor for genome-wide screens of intracellular proteolytic cleavageProapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alphaMAP-1 is a mitochondrial effector of Bax.Modulation of apoptosis by the widely distributed Bcl-2 homologue BakThe identification of a novel gene, MAPO2, that is involved in the induction of apoptosis triggered by O⁶-methylguaninePLEKHN1 promotes apoptosis by enhancing Bax-Bak hetro-oligomerization through interaction with Bid in human colon cancer.
P921
Q22008484-416110B0-F4CD-4154-85E4-20D28D810028Q22254196-DEB385F4-A2E0-480E-BF72-38D52C0C5938Q24290118-3315B7C1-1DDD-4122-8A1A-8C483D610166Q24295530-6F91F194-1997-46B0-915D-05028D3B7889Q24296478-F5D9F20A-707F-46CD-B699-305A525ABB09Q24302248-9B26E62D-B943-49A6-AC23-F963160D8867Q24302494-BC75E0D2-BB33-40E3-B316-51AEF35162A3Q24303558-5A97C51F-BF14-4523-93E9-4CCF56AD13FBQ24305138-CEADA5B4-9DD4-4515-81AC-08E0741FE91BQ24305329-8EE9BDF7-DE9C-48C9-A142-8DBB527C1C61Q24306130-8DCBE3FF-4E6A-4723-BE7E-5FA00D4A22A6Q24314405-0FF70C55-D2BB-4C02-91AA-FBE3E9D6E0C5Q24316457-9358212E-A3CD-4D22-AA4D-33DC2B347C6BQ24322072-2D2AD605-8779-4B57-BFBA-D3648F9E075BQ24337383-8AAB071A-BB9E-4660-B672-B331205B501EQ28299882-0CB26828-1782-4B83-9D46-4BA72376BF6BQ32884511-9215C055-F842-4A34-808B-1262EC140B03Q55438828-467B9010-1806-43CE-9EB2-315CD108E26F
P921
description
Protein in Homo sapiens
@de
mammalian protein found in Homo sapiens
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in BCL2 antagonist/killer 1
@nl
protèin
@ace
protéine
@fr
بروتين في الإنسان العاقل
@ar
name
BCL2 antagonist/killer 1
@en
BCL2 antagonist/killer 1
@nl
type
label
BCL2 antagonist/killer 1
@en
BCL2 antagonist/killer 1
@nl
altLabel
BAK1
@en
BCL2-like 7 protein
@en
apoptosis regulator BAK
@en
bcl-2 homologous antagonist/killer
@en
bcl-2-like protein 7
@en
bcl2-L-7
@en
pro-apoptotic protein BAK
@en
prefLabel
BCL2 antagonist/killer 1
@en
BCL2 antagonist/killer 1
@nl
P361
P527
P637
P638
P680
P681
P682
P705
P352
P2888
P31
P352
P527
P637
XP_011513081
XP_011513082
P638
P680
P681
P682
P702
P703
P705
ENSP00000353878
ENSP00000363591
ENSP00000391258
P7260
1.A.21.1.3