Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A novel adenovirus E1B19K-binding protein B5 inhibits apoptosis induced by Nip3 by forming a heterodimer through the C-terminal hydrophobic region.
MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain.
tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c.
Tumor necrosis factor-alpha induces Bax-Bak interaction and apoptosis, which is inhibited by adenovirus E1B 19K.
Inhibition of Bid-induced apoptosis by Bcl-2. tBid insertion, Bax translocation, and Bax/Bak oligomerization suppressed.
Bax and Bak can localize to the endoplasmic reticulum to initiate apoptosis.
UniProt entry Q16611 (BAK_HUMAN)
High-throughput methods to detect dimerization of Bcl-2 family proteins.
Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.
Towards a proteome-scale map of the human protein-protein interaction network.
MAP-1 is a mitochondrial effector of Bax.
Interaction of F1L with the BH3 domain of Bak is responsible for inhibiting vaccinia-induced apoptosis.
Differential contribution of Puma and Noxa in dual regulation of p53-mediated apoptotic pathways.
Mechanisms of apoptosis sensitivity and resistance to the BH3 mimetic ABT-737 in acute myeloid leukemia.
Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak.
Functional and physical interaction between Bcl-X(L) and a BH3-like domain in Beclin-1.
Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins.
Small molecule obatoclax (GX15-070) antagonizes MCL-1 and overcomes MCL-1-mediated resistance to apoptosis.
No death without life: vital functions of apoptotic effectors.
A pathway sensor for genome-wide screens of intracellular proteolytic cleavage.
An empirical framework for binary interactome mapping.
Expression of the Bcl-2 protein BAD promotes prostate cancer growth.
Mcl-1(128-350) fragment induces apoptosis through direct interaction with Bax.
Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival.
Heterodimerization of BAK and MCL-1 activated by detergent micelles.
BH3 domains other than Bim and Bid can directly activate Bax/Bak.
Mcl-1 is critical for survival in a subgroup of non-small-cell lung cancer cell lines.
Active Bax and Bak are functional holins.
The unfolded protein response: integrating stress signals through the stress sensor IRE1α.
NMR solution structure of a photoswitchable apoptosis activating Bak peptide bound to Bcl-xL.
Chemical genomics identifies small-molecule MCL1 repressors and BCL-xL as a predictor of MCL1 dependency.
The endoplasmic reticulum stress response in aging and age-related diseases.
The identification of a novel gene, MAPO2, that is involved in the induction of apoptosis triggered by O⁶-methylguanine.
Human Bop is a novel BH3-only member of the Bcl-2 protein family.
BID-induced structural changes in BAK promote apoptosis.
The novel BH3 α-helix mimetic JY-1-106 induces apoptosis in a subset of cancer cells (lung cancer, colon cancer and mesothelioma) by disrupting Bcl-xL and Mcl-1 protein-protein interactions with Bak.
BAK multimerization for apoptosis, but not bid binding, is inhibited by negatively charged residue in the BAK hydrophobic groove.
Plasminogen kringle 5 induces endothelial cell apoptosis by triggering a voltage-dependent anion channel 1 (VDAC1) positive feedback loop.
A proteome-scale map of the human interactome network.
Small-Molecule Bcl2 BH4 Antagonist for Lung Cancer Therapy.
Architecture of the human interactome defines protein communities and disease networks.
PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetro-oligomerization through interaction with Bid in human colon cancer.
LuTHy: a double-readout bioluminescence-based two-hybrid technology for quantitative mapping of protein-protein interactions in mammalian cells.
Maximizing binary interactome mapping with a minimal number of assays.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
BAK core dimers bind lipids and can be bridged by them.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
AI-guided pipeline for protein-protein interaction drug discovery identifies a SARS-CoV-2 inhibitor.
Multimodal cell maps as a foundation for structural and functional genomics.
Modulation of apoptosis by the widely distributed Bcl-2 homologue Bak.
Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death.
A common binding site mediates heterodimerization and homodimerization of Bcl-2 family members.
The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4.
Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria.
Oligomerization of BAK at the mitochondrial membrane
tBID activates BAK protein
tBID binds to inactive BAK protein
Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members.
Malignant transformation of normal enterocytes following downregulation of Bak expression.