BAX is a multidomain pro-apoptotic BCL2-family effector that drives mitochondrial outer membrane permeabilization during intrinsic apoptosis. In healthy cells, BAX is largely cytosolic or retrotranslocated away from mitochondria by pro-survival BCL2-family proteins. After apoptotic stimulation, BH3-only activators and release from pro-survival restraints drive BAX conformational activation, mitochondrial outer-membrane insertion, homodimerization, and assembly into higher-order oligomeric pores that release cytochrome c and other intermembrane-space factors. BAX can also act with BAK and is modulated by accessory proteins that tune its localization, conformation, stability, and ER or mitochondrial-dynamics outputs.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001783 B cell apoptotic process | IDA PMID:15214043 Apoptosis via the B cell antigen receptor requires Bax trans... | MODIFY | Summary: The BCR-induced B-cell apoptosis row should be scoped to BCR apoptotic signaling. Reason: PMID:15214043 supports BAX translocation, mitochondrial depolarization, cytochrome c release, and caspase-9 activation downstream of the B-cell receptor, so the seeded generic B-cell apoptotic-process term can be tightened to the existing BCR apoptotic-signaling child. Proposed replacements: B cell receptor apoptotic signaling pathway |
| GO:0001783 B cell apoptotic process | IDA PMID:16424160 The endoplasmic reticulum is a key component of the plasma c... | KEEP AS NON CORE | Summary: The plasma-cell apoptosis row is a context-specific BAX apoptosis assertion. Reason: BAX participates in ER-associated plasma-cell death, but the same effector activity is captured more generally by mitochondrial outer-membrane permeabilization and intrinsic apoptotic signaling. |
| GO:0001836 release of cytochrome c from mitochondria | IBA GO_REF:0000033 | ACCEPT | Summary: BAX directly permeabilizes the outer mitochondrial membrane to drive cytochrome-c release. Reason: Cytochrome-c release is the immediate process-level output of BAX conformational activation and oligomerization at the mitochondrial outer membrane. |
| GO:0001836 release of cytochrome c from mitochondria | IDA PMID:16199525 MAP-1 is a mitochondrial effector of Bax. | ACCEPT | Summary: BAX directly permeabilizes the outer mitochondrial membrane to drive cytochrome-c release. Reason: Cytochrome-c release is the immediate process-level output of BAX conformational activation and oligomerization at the mitochondrial outer membrane. |
| GO:0001836 release of cytochrome c from mitochondria | IDA PMID:17052454 A stapled BID BH3 helix directly binds and activates BAX. | ACCEPT | Summary: BAX directly permeabilizes the outer mitochondrial membrane to drive cytochrome-c release. Reason: Cytochrome-c release is the immediate process-level output of BAX conformational activation and oligomerization at the mitochondrial outer membrane. |
| GO:0001836 release of cytochrome c from mitochondria | IDA PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | ACCEPT | Summary: BAX directly permeabilizes the outer mitochondrial membrane to drive cytochrome-c release. Reason: Cytochrome-c release is the immediate process-level output of BAX conformational activation and oligomerization at the mitochondrial outer membrane. |
| GO:0001836 release of cytochrome c from mitochondria | IDA PMID:9843949 Bax interacts with the permeability transition pore to induc... | ACCEPT | Summary: BAX directly permeabilizes the outer mitochondrial membrane to drive cytochrome-c release. Reason: Cytochrome-c release is the immediate process-level output of BAX conformational activation and oligomerization at the mitochondrial outer membrane. |
| GO:0001836 release of cytochrome c from mitochondria | IEA GO_REF:0000117 | ACCEPT | Summary: BAX directly permeabilizes the outer mitochondrial membrane to drive cytochrome-c release. Reason: Cytochrome-c release is the immediate process-level output of BAX conformational activation and oligomerization at the mitochondrial outer membrane. |
| GO:0005515 protein binding | IPI PMID:10753914 Structural basis of BFL-1 for its interaction with BAX and i... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:11161816 SH3GLB, a new endophilin-related protein family featuring an... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:11278245 Bcl-B, a novel Bcl-2 family member that differentially binds... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:11571294 Tumor necrosis factor-alpha induces Bax-Bak interaction and ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:11574543 The G2/M regulator 14-3-3sigma prevents apoptosis through se... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:11574543 The G2/M regulator 14-3-3sigma prevents apoptosis through se... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:12732850 Humanin peptide suppresses apoptosis by interfering with Bax... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:12925958 Hepatitis C virus NS5A as a potential viral Bcl-2 homologue ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:14730312 ASC is a Bax adaptor and regulates the p53-Bax mitochondrial... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:14752512 Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:14752512 Human alphaA- and alphaB-crystallins bind to Bax and Bcl-X(S... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:14963330 Direct activation of Bax by p53 mediates mitochondrial membr... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:15205477 Calorie restriction promotes mammalian cell survival by indu... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:15901672 Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:16113678 Clusterin inhibits apoptosis by interacting with activated B... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:16151013 PUMA couples the nuclear and cytoplasmic proapoptotic functi... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:16439990 Interaction of F1L with the BH3 domain of Bak is responsible... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:16509771 IAN family critically regulates survival and development of ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:16509771 IAN family critically regulates survival and development of ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:16608847 PUMA Dissociates Bax and Bcl-X(L) to induce apoptosis in col... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17123957 Vaccinia virus N1L protein resembles a B cell lymphoma-2 (Bc... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17485524 Functional and structural studies of the vaccinia virus viru... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17525735 ERK1/2-dependent phosphorylation of BimEL promotes its rapid... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17525735 ERK1/2-dependent phosphorylation of BimEL promotes its rapid... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17525735 ERK1/2-dependent phosphorylation of BimEL promotes its rapid... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17635912 The mitochondrial TOM complex is required for tBid/Bax-induc... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:17635912 The mitochondrial TOM complex is required for tBid/Bax-induc... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:18547146 Bcl-XL inhibits membrane permeabilization by competing with ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:18818304 Mitochondrial potassium channel Kv1.3 mediates Bax-induced a... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:18948948 BAX activation is initiated at a novel interaction site. | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:18981409 Apoptosis is triggered when prosurvival Bcl-2 proteins canno... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:18981409 Apoptosis is triggered when prosurvival Bcl-2 proteins canno... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:18981409 Apoptosis is triggered when prosurvival Bcl-2 proteins canno... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:18981409 Apoptosis is triggered when prosurvival Bcl-2 proteins canno... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:19062087 Membrane binding by tBid initiates an ordered series of even... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:19062087 Membrane binding by tBid initiates an ordered series of even... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:19074440 Endophilin B1/Bif-1 stimulates BAX activation independently ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:19074440 Endophilin B1/Bif-1 stimulates BAX activation independently ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:19427863 BimL directly neutralizes Bcl-xL to promote Bax activation d... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:19968986 Mcl-1(128-350) fragment induces apoptosis through direct int... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:20300062 IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory fac... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:20541605 RACK1 promotes Bax oligomerization and dissociates the inter... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:20541605 RACK1 promotes Bax oligomerization and dissociates the inter... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:20956295 Autophagy protein microtubule-associated protein 1 light cha... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21458670 Bcl-x(L) retrotranslocates Bax from the mitochondria into th... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21458670 Bcl-x(L) retrotranslocates Bax from the mitochondria into th... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21458670 Bcl-x(L) retrotranslocates Bax from the mitochondria into th... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21567405 Human nuclear clusterin mediates apoptosis by interacting wi... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21597469 UV irradiation resistance-associated gene suppresses apoptos... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21671007 Role of Bim in apoptosis induced in H460 lung tumor cells by... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:21671007 Role of Bim in apoptosis induced in H460 lung tumor cells by... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:22198199 The cytosolic domain of human Tom22 modulates human Bax mito... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:22198199 The cytosolic domain of human Tom22 modulates human Bax mito... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:22198199 The cytosolic domain of human Tom22 modulates human Bax mito... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:23055042 Human Bop is a novel BH3-only member of the Bcl-2 protein fa... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:23213219 Structural mechanism of Bax inhibition by cytomegalovirus pr... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:23235460 The restricted binding repertoire of Bcl-B leaves Bim as the... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:23235460 The restricted binding repertoire of Bcl-B leaves Bim as the... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:23374347 Bax crystal structures reveal how BH3 domains activate Bax a... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:23374347 Bax crystal structures reveal how BH3 domains activate Bax a... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:24814347 The DNA-binding domain mediates both nuclear and cytosolic f... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:26004684 Small-Molecule Bcl2 BH4 Antagonist for Lung Cancer Therapy. | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:26344567 An interconnected hierarchical model of cell death regulatio... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:29749471 GSK3Ξ²βmediated Ser156 phosphorylation modulates a BH3βlike d... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:29749471 GSK3Ξ²βmediated Ser156 phosphorylation modulates a BH3βlike d... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:29749471 GSK3Ξ²βmediated Ser156 phosphorylation modulates a BH3βlike d... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: This high-throughput interaction-map edge should not be converted into a BAX molecular function or apoptosis-process assertion without BAX-specific mechanistic evidence. |
| GO:0005515 protein binding | IPI PMID:9027312 Interaction of CED-4 with CED-3 and CED-9: a molecular frame... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:9111042 A common binding site mediates heterodimerization and homodi... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:9388232 Dimerization properties of human BAD. Identification of a BH... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:9388232 Dimerization properties of human BAD. Identification of a BH... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:9463381 The conserved N-terminal BH4 domain of Bcl-2 homologues is e... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005515 protein binding | IPI PMID:9843949 Bax interacts with the permeability transition pore to induc... | REMOVE | Summary: This BAX interaction is imported only as generic protein binding. Reason: GO:0005515 is uninformative for BAX and should not duplicate curated BAX homodimerization, BH3-domain binding, BCL2-family heterodimerization, or BAX-complex rows. |
| GO:0005634 nucleus | EXP PMID:36361894 Deubiquitinating Enzyme USP12 Regulates the Pro-Apoptosis Pr... | KEEP AS NON CORE | Summary: Nuclear or nuclear-envelope BAX localization is secondary to its mitochondrial apoptosis role. Reason: These rows are BAX-specific enough to retain conservatively, but the core active compartments for apoptotic BAX are the cytosol and the mitochondrial outer membrane. |
| GO:0005634 nucleus | IDA PMID:12925958 Hepatitis C virus NS5A as a potential viral Bcl-2 homologue ... | KEEP AS NON CORE | Summary: Nuclear or nuclear-envelope BAX localization is secondary to its mitochondrial apoptosis role. Reason: These rows are BAX-specific enough to retain conservatively, but the core active compartments for apoptotic BAX are the cytosol and the mitochondrial outer membrane. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Nuclear or nuclear-envelope BAX localization is secondary to its mitochondrial apoptosis role. Reason: These rows are BAX-specific enough to retain conservatively, but the core active compartments for apoptotic BAX are the cytosol and the mitochondrial outer membrane. |
| GO:0005634 nucleus | IMP PMID:15102863 BOK and NOXA are essential mediators of p53-dependent apopto... | KEEP AS NON CORE | Summary: Nuclear or nuclear-envelope BAX localization is secondary to its mitochondrial apoptosis role. Reason: These rows are BAX-specific enough to retain conservatively, but the core active compartments for apoptotic BAX are the cytosol and the mitochondrial outer membrane. |
| GO:0005635 nuclear envelope | IDA PMID:12925958 Hepatitis C virus NS5A as a potential viral Bcl-2 homologue ... | KEEP AS NON CORE | Summary: Nuclear or nuclear-envelope BAX localization is secondary to its mitochondrial apoptosis role. Reason: These rows are BAX-specific enough to retain conservatively, but the core active compartments for apoptotic BAX are the cytosol and the mitochondrial outer membrane. |
| GO:0005737 cytoplasm | EXP PMID:27558414 Enterovirus 71 2B Induces Cell Apoptosis by Directly Inducin... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005737 cytoplasm | IDA PMID:16302269 Nuclear translocation of the pro-apoptotic Bcl-2 family memb... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005737 cytoplasm | IDA PMID:29531808 PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetro-oligom... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IDA PMID:11912183 The expression of a new variant of the pro-apoptotic molecul... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IDA PMID:15102863 BOK and NOXA are essential mediators of p53-dependent apopto... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IDA PMID:15705586 Involvement of Noxa in cellular apoptotic responses to inter... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IDA PMID:16199525 MAP-1 is a mitochondrial effector of Bax. | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IDA PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IDA PMID:19767770 A novel pro-apoptotic function of RACK1: suppression of Src ... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IDA PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005739 mitochondrion | IEA GO_REF:0000107 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005741 mitochondrial outer membrane | EXP PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | ACCEPT | Summary: The mitochondrial outer membrane is the active site of apoptotic BAX oligomers. Reason: Activated BAX translocates to and inserts in the mitochondrial outer membrane, where it oligomerizes to permeabilize the membrane. |
| GO:0005741 mitochondrial outer membrane | IBA GO_REF:0000033 | ACCEPT | Summary: The mitochondrial outer membrane is the active site of apoptotic BAX oligomers. Reason: Activated BAX translocates to and inserts in the mitochondrial outer membrane, where it oligomerizes to permeabilize the membrane. |
| GO:0005741 mitochondrial outer membrane | IDA PMID:29531808 PLEKHN1 promotes apoptosis by enhancing Bax-Bak hetro-oligom... | ACCEPT | Summary: The mitochondrial outer membrane is the active site of apoptotic BAX oligomers. Reason: Activated BAX translocates to and inserts in the mitochondrial outer membrane, where it oligomerizes to permeabilize the membrane. |
| GO:0005741 mitochondrial outer membrane | IEA GO_REF:0000120 | ACCEPT | Summary: The mitochondrial outer membrane is the active site of apoptotic BAX oligomers. Reason: Activated BAX translocates to and inserts in the mitochondrial outer membrane, where it oligomerizes to permeabilize the membrane. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-114264 | ACCEPT | Summary: The mitochondrial outer membrane is the active site of apoptotic BAX oligomers. Reason: Activated BAX translocates to and inserts in the mitochondrial outer membrane, where it oligomerizes to permeabilize the membrane. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-114275 | ACCEPT | Summary: The mitochondrial outer membrane is the active site of apoptotic BAX oligomers. Reason: Activated BAX translocates to and inserts in the mitochondrial outer membrane, where it oligomerizes to permeabilize the membrane. |
| GO:0005757 mitochondrial permeability transition pore complex | IDA PMID:9843949 Bax interacts with the permeability transition pore to induc... | REMOVE | Summary: The historical permeability-transition-pore model should not place BAX in the PTP complex. Reason: PMID:9843949 proposed that recombinant BAX acted through permeability-transition-pore components, but current BAX curation should represent the MOM-localized BCL2-family pore rather than a stable mitochondrial permeability-transition-pore complex. |
| GO:0005783 endoplasmic reticulum | IDA PMID:16424160 The endoplasmic reticulum is a key component of the plasma c... | KEEP AS NON CORE | Summary: ER or ER-membrane localization captures a secondary BAX/BAK regulatory context. Reason: BAX and BAK have ER calcium and ER-stress-associated activities, but those are not the main mitochondrial outer-membrane permeabilization role. |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ER or ER-membrane localization captures a secondary BAX/BAK regulatory context. Reason: BAX and BAK have ER calcium and ER-stress-associated activities, but those are not the main mitochondrial outer-membrane permeabilization role. |
| GO:0005789 endoplasmic reticulum membrane | IDA PMID:16424160 The endoplasmic reticulum is a key component of the plasma c... | KEEP AS NON CORE | Summary: ER or ER-membrane localization captures a secondary BAX/BAK regulatory context. Reason: BAX and BAK have ER calcium and ER-stress-associated activities, but those are not the main mitochondrial outer-membrane permeabilization role. |
| GO:0005829 cytosol | IDA PMID:11912183 The expression of a new variant of the pro-apoptotic molecul... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | IDA PMID:12925958 Hepatitis C virus NS5A as a potential viral Bcl-2 homologue ... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | IDA PMID:15102863 BOK and NOXA are essential mediators of p53-dependent apopto... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | IDA PMID:15705586 Involvement of Noxa in cellular apoptotic responses to inter... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | IDA PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | IDA PMID:19767770 A novel pro-apoptotic function of RACK1: suppression of Src ... | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-114264 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-139917 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-168849 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3700984 | ACCEPT | Summary: This Reactome localization projection comes from regulation of BAX gene expression. Reason: Cytosol is the established location of inactive BAX and is accepted on the direct-assay and other rows for this term, so the claim stands here as well. The Reactome event behind this row describes transcriptional induction of the BAX gene; its product, newly made BAX protein, is placed by Reactome in the cytosol, which agrees with the experimental rows. The event is not itself a localization experiment, which limits this row's evidence but not the claim. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6803892 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9008839 | ACCEPT | Summary: This Reactome localization projection comes from regulation of BAX gene expression. Reason: Cytosol is the established location of inactive BAX and is accepted on the direct-assay and other rows for this term, so the claim stands here as well. The Reactome event behind this row describes transcriptional induction of the BAX gene; its product, newly made BAX protein, is placed by Reactome in the cytosol, which agrees with the experimental rows. The event is not itself a localization experiment, which limits this row's evidence but not the claim. |
| GO:0006915 apoptotic process | IDA PMID:17428862 Induction of apoptosis by the severe acute respiratory syndr... | UNDECIDED | Summary: The SARS-CoV 7a paper does not show a direct BAX role in the cached abstract. Reason: The abstract reports 7a binding to BCL-XL and not to BAX, BAK, BAD, or BID; full text would be needed before preserving a BAX apoptotic-process annotation from this source. |
| GO:0006915 apoptotic process | IDA PMID:9660918 Bax inhibitor-1, a mammalian apoptosis suppressor identified... | MARK AS OVER ANNOTATED | Summary: This generic apoptotic-process row is based on an artificial or indirect BAX death readout. Reason: BAX is a mitochondrial permeabilization effector, and yeast-expression, tumor-loss, or isoform cell-death assays should not remain at the top-level apoptotic process term. |
| GO:0006915 apoptotic process | IMP PMID:9531611 Hematopoietic malignancies demonstrate loss-of-function muta... | MARK AS OVER ANNOTATED | Summary: This generic apoptotic-process row is based on an artificial or indirect BAX death readout. Reason: BAX is a mitochondrial permeabilization effector, and yeast-expression, tumor-loss, or isoform cell-death assays should not remain at the top-level apoptotic process term. |
| GO:0006915 apoptotic process | NAS PMID:9920818 Identification and characterization of baxepsilon, a novel b... | MARK AS OVER ANNOTATED | Summary: This generic apoptotic-process row is based on an artificial or indirect BAX death readout. Reason: BAX is a mitochondrial permeabilization effector, and yeast-expression, tumor-loss, or isoform cell-death assays should not remain at the top-level apoptotic process term. |
| GO:0008053 mitochondrial fusion | IBA GO_REF:0000033 | MODIFY | Summary: The inherited mitochondrial-fusion row has the polarity backwards for apoptotic BAX. Reason: BAX activation is associated with blockade of mitochondrial fusion during apoptosis rather than BAX acting as a positive mitochondrial-fusion factor. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: REGULATORY SIGN INVERSION Sources checked: PANTHER:PTN000135648 SUPPORTS SOURCE BUT NOT TARGET The inherited row captures the BAX mitochondrial-dynamics connection, but the more precise direction is negative regulation of mitochondrial fusion. Proposed replacements: negative regulation of mitochondrial fusion |
| GO:0008053 mitochondrial fusion | IDA PMID:14769861 Quantitation of mitochondrial dynamics by photolabeling of i... | MODIFY | Summary: The mitochondrial-fusion row has the polarity backwards for apoptotic BAX. Reason: PMID:14769861 showed that mitochondrial fusion is blocked during the Bax activation phase of apoptosis, so the specific negative-regulation term captures the result better than mitochondrial fusion itself. Proposed replacements: negative regulation of mitochondrial fusion |
| GO:0008289 lipid binding | IDA PMID:14522999 Interaction with a membrane surface triggers a reversible co... | ACCEPT | Summary: BAX membrane binding is part of its conformational activation mechanism. Reason: Purified BAX interacts with liposomes and undergoes a membrane-triggered conformational change that primes tBID-induced oligomerization and pore formation. |
| GO:0008625 extrinsic apoptotic signaling pathway via death domain receptors | IC PMID:16199525 MAP-1 is a mitochondrial effector of Bax. | MODIFY | Summary: MAP-1 support places BAX at mitochondrial cytochrome-c release, not receptor-proximal extrinsic signaling. Reason: PMID:16199525 supports MAP-1 as a mitochondrial BAX effector needed for BAX-mediated cytochrome-c release, so the BAX row should be scoped to that mitochondrial output rather than to the death-domain-receptor pathway. Proposed replacements: release of cytochrome c from mitochondria |
| GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: DNA damage is a valid but context-specific upstream trigger of BAX-dependent intrinsic apoptosis. Reason: BAX is a general mitochondrial effector; the DNA-damage child term can be retained as non-core while MOMP and cytochrome-c release remain the core BAX process annotations. |
| GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage | IDA PMID:11912183 The expression of a new variant of the pro-apoptotic molecul... | KEEP AS NON CORE | Summary: DNA damage is a valid but context-specific upstream trigger of BAX-dependent intrinsic apoptosis. Reason: BAX is a general mitochondrial effector; the DNA-damage child term can be retained as non-core while MOMP and cytochrome-c release remain the core BAX process annotations. |
| GO:0008637 apoptotic mitochondrial changes | IDA PMID:9843949 Bax interacts with the permeability transition pore to induc... | MODIFY | Summary: This early mitochondrial-changes row can be tightened to cytochrome-c release. Reason: PMID:9843949 directly reported recombinant BAX-induced cytochrome-c release from isolated mitochondria, whereas apoptotic mitochondrial changes is a broad grouping term. Proposed replacements: release of cytochrome c from mitochondria |
| GO:0009636 response to toxic substance | IDA PMID:16307838 T-2 toxin induces apoptosis, and selenium partly blocks, T-2... | MARK AS OVER ANNOTATED | Summary: A toxin-induced change in BAX/BCL2 balance is not a direct BAX response-to-toxic-substance function. Reason: The row projects an upstream toxic stimulus or death readout onto BAX rather than the mitochondrial permeabilization step performed by BAX. |
| GO:0010248 establishment or maintenance of transmembrane electrochemical gradient | IDA PMID:9843949 Bax interacts with the permeability transition pore to induc... | MODIFY | Summary: BAX decreases mitochondrial membrane potential rather than maintaining an electrochemical gradient. Reason: PMID:9843949 measured loss of mitochondrial transmembrane potential after recombinant BAX treatment, so the directional mitochondrial-membrane-potential term is the better assertion. Proposed replacements: negative regulation of mitochondrial membrane potential |
| GO:0010917 negative regulation of mitochondrial membrane potential | IDA PMID:16751333 Cell-based screening and validation of human novel genes ass... | UNDECIDED | Summary: The cached source does not expose a direct BAX membrane-potential assay. Reason: PMID:16751333 is an abstract-only high-throughput cell-viability screen that appears to use BAX as a positive death control; full text is needed to verify this exact membrane-potential row. |
| GO:0015267 channel activity | IBA GO_REF:0000033 | ACCEPT | Summary: BAX has channel activity as a pore-forming mitochondrial apoptosis effector. Reason: BAX forms ion-conducting channels in lipid membranes and oligomerizes into mitochondrial membrane pores during MOMP. |
| GO:0015267 channel activity | IDA PMID:9219694 Inhibition of Bax channel-forming activity by Bcl-2. | ACCEPT | Summary: BAX has channel activity as a pore-forming mitochondrial apoptosis effector. Reason: BAX forms ion-conducting channels in lipid membranes and oligomerizes into mitochondrial membrane pores during MOMP. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | TOO GENERAL | Summary: The membrane row is a nonspecific high-throughput localization hit. Reason: A broad NK-cell membrane proteomics result does not place BAX in its established cytosol-to-mitochondrial-outer-membrane apoptotic activation cycle. TOO_GENERAL rather than REMOVE: endoplasmic reticulum membrane, mitochondrial membrane and mitochondrial outer membrane, kept in this review, entail this term, so the claim is true but less informative. |
| GO:0030544 Hsp70 protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The Hsp70/chaperone-binding assertion is specific but peripheral. Reason: Chaperone binding may regulate BAX conformation or stability, but it is not the core BAX pore-forming function in intrinsic apoptosis. |
| GO:0031334 positive regulation of protein-containing complex assembly | IDA PMID:19805544 Bax activates endophilin B1 oligomerization and lipid membra... | KEEP AS NON CORE | Summary: BAX-dependent endophilin B1 oligomerization is peripheral to BAX MOMP. Reason: The Bif-1/SH3GLB1 result is a specific BAX-associated process, but it is a side branch relative to BAX oligomerization and pore formation at the mitochondrial outer membrane. |
| GO:0031334 positive regulation of protein-containing complex assembly | IDA PMID:9111042 A common binding site mediates heterodimerization and homodi... | KEEP AS NON CORE | Summary: This broad complex-assembly row duplicates the direct BAX-BCL2 heterodimer row. Reason: The same term is kept as non-core on another direct-assay row, and the claim is the same here. The cited study of the common binding site for hetero- and homodimerization of BCL2-family proteins used Bax and Bax-derived BH3 peptides; only the abstract is available, so the experimental annotation is not overruled. The term is generic and the specific content (BAX-BCL2 heterodimerization, BAX oligomerization) is carried by other annotations, which is why it is non-core rather than removed. |
| GO:0031966 mitochondrial membrane | IEA GO_REF:0000107 | ACCEPT | Summary: BAX localizes to cytosol and mitochondria as part of its activation cycle. Reason: Inactive BAX is largely cytosolic, and apoptotic activation drives BAX association with mitochondrial membranes en route to insertion and oligomerization at the outer mitochondrial membrane. |
| GO:0032091 negative regulation of protein binding | IDA PMID:9388232 Dimerization properties of human BAD. Identification of a BH... | UNDECIDED | Summary: The cached BAD abstract does not verify a direct BAX negative-regulation-of-binding row. Reason: PMID:9388232 is abstract-only and visibly focused on BAD binding to mutant BCL2 and BCL-XL, so the curator-visible BAX support cannot be checked locally. |
| GO:0032469 endoplasmic reticulum calcium ion homeostasis | TAS PMID:18309324 No death without life: vital functions of apoptotic effector... | KEEP AS NON CORE | Summary: The ER-stress/IRE1 annotation is review-level support for a peripheral BAX context. Reason: BAX and BAK are discussed in ER-stress signaling, but these TAS rows are not direct experimental evidence for BAX mitochondrial pore formation and should remain non-core. |
| GO:0032976 release of matrix enzymes from mitochondria | IDA PMID:9843949 Bax interacts with the permeability transition pore to induc... | MODIFY | Summary: This matrix-enzyme-release row should be scoped to cytochrome-c release. Reason: PMID:9843949 reported BAX-induced cytochrome-c release from isolated mitochondria; release of matrix enzymes from mitochondria is less specific and not the right BAX effector step. Proposed replacements: release of cytochrome c from mitochondria |
| GO:0033554 cellular response to stress | IEA GO_REF:0000117 | TOO GENERAL | Summary: The automated cellular-stress row is too broad for BAX. Reason: Cellular response to stress is entailed by the more specific annotations kept in this review (intrinsic apoptotic signaling in response to DNA damage and to endoplasmic reticulum stress, cellular response to unfolded protein), so the broad term is true of BAX but adds nothing to them. |
| GO:0034620 cellular response to unfolded protein | TAS PMID:22013210 The unfolded protein response: integrating stress signals th... | KEEP AS NON CORE | Summary: The ER-stress/IRE1 annotation is review-level support for a peripheral BAX context. Reason: BAX and BAK are discussed in ER-stress signaling, but these TAS rows are not direct experimental evidence for BAX mitochondrial pore formation and should remain non-core. |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:10620504 Bax oligomerization is required for channel-forming activity... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:14963330 Direct activation of Bax by p53 mediates mitochondrial membr... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:16113678 Clusterin inhibits apoptosis by interacting with activated B... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:17024184 Differential contribution of Puma and Noxa in dual regulatio... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:17668322 Protein kinase C-epsilon protects MCF-7 cells from TNF-media... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:18547146 Bcl-XL inhibits membrane permeabilization by competing with ... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:18835031 A short Nur77-derived peptide converts Bcl-2 from a protecto... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:19062087 Membrane binding by tBid initiates an ordered series of even... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:19074440 Endophilin B1/Bif-1 stimulates BAX activation independently ... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:19767770 A novel pro-apoptotic function of RACK1: suppression of Src ... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:20360684 Viral apoptosis is induced by IRF-3-mediated activation of B... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:20541605 RACK1 promotes Bax oligomerization and dissociates the inter... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:20850011 Membrane remodeling induced by the dynamin-related protein D... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:22198199 The cytosolic domain of human Tom22 modulates human Bax mito... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042802 identical protein binding | IPI PMID:23374347 Bax crystal structures reveal how BH3 domains activate Bax a... | ACCEPT | Summary: BAX self-association is part of BAX oligomer formation. Reason: Identical protein binding captures the direct BAX-BAX contacts that nucleate oligomers at the mitochondrial outer membrane. |
| GO:0042803 protein homodimerization activity | IDA PMID:16608847 PUMA Dissociates Bax and Bcl-X(L) to induce apoptosis in col... | ACCEPT | Summary: BAX homodimerization is part of its oligomeric pore-forming mechanism. Reason: BAX self-association and higher-order oligomerization build the mitochondrial outer-membrane pore. |
| GO:0042981 regulation of apoptotic process | IDA PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | MODIFY | Summary: The broad positive-regulation apoptosis row should be scoped to BAX-mediated MOMP. Reason: BAX is one of the pore-forming effectors that permeabilizes the mitochondrial outer membrane rather than a generic regulator of apoptotic process. Proposed replacements: mitochondrial outer membrane permeabilization |
| GO:0042981 regulation of apoptotic process | IEA GO_REF:0000120 | MODIFY | Summary: The broad positive-regulation apoptosis row should be scoped to BAX-mediated MOMP. Reason: BAX is one of the pore-forming effectors that permeabilizes the mitochondrial outer membrane rather than a generic regulator of apoptotic process. Proposed replacements: mitochondrial outer membrane permeabilization |
| GO:0043065 positive regulation of apoptotic process | IDA PMID:16751333 Cell-based screening and validation of human novel genes ass... | MARK AS OVER ANNOTATED | Summary: This cell-screen row is too broad to support a mechanistic BAX process. Reason: The cached screen abstract does not establish a BAX-specific mitochondrial permeabilization assay, so positive regulation of apoptotic process is an over-annotation from a death-readout context. |
| GO:0043065 positive regulation of apoptotic process | IDA PMID:17464193 Identification of novel regulators of apoptosis using a high... | MARK AS OVER ANNOTATED | Summary: This cell-screen row is too broad to support a mechanistic BAX process. Reason: The cached screen abstract does not establish a BAX-specific mitochondrial permeabilization assay, so positive regulation of apoptotic process is an over-annotation from a death-readout context. |
| GO:0043065 positive regulation of apoptotic process | IEA GO_REF:0000117 | MODIFY | Summary: The broad positive-regulation apoptosis row should be scoped to BAX-mediated MOMP. Reason: BAX is one of the pore-forming effectors that permeabilizes the mitochondrial outer membrane rather than a generic regulator of apoptotic process. Proposed replacements: mitochondrial outer membrane permeabilization |
| GO:0043065 positive regulation of apoptotic process | IMP PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | MODIFY | Summary: The broad positive-regulation apoptosis row should be scoped to BAX-mediated MOMP. Reason: BAX is one of the pore-forming effectors that permeabilizes the mitochondrial outer membrane rather than a generic regulator of apoptotic process. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: GO_REF:0000117 SUPPORTS SOURCE BUT NOT TARGET The imported process is a broad positive-regulation term; BAX itself directly permeabilizes the mitochondrial outer membrane. Proposed replacements: mitochondrial outer membrane permeabilization |
| GO:0043066 negative regulation of apoptotic process | IBA GO_REF:0000033 | REMOVE | Summary: This PAINT row crossed the pro- and anti-apoptotic split in the BCL2 family. Reason: BAX is a pro-apoptotic MOMP effector; negative regulation of apoptotic process is appropriate for pro-survival BCL2-family members, not for BAX. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG Sources checked: PANTHER:PTN000135648 SUPPORTS SOURCE BUT NOT TARGET This BCL2-family node includes anti-apoptotic family members, but BAX is on the pro-apoptotic effector side of the family split. |
| GO:0043523 regulation of neuron apoptotic process | IEA GO_REF:0000117 | MARK AS OVER ANNOTATED | Summary: The automated neuronal-apoptosis regulation row is too context-specific and broad. Reason: BAX can promote neuronal apoptosis through its usual mitochondrial effector function, but a generic ARBA transfer to regulation of neuron apoptotic process overstates this as a separate function. |
| GO:0043525 positive regulation of neuron apoptotic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Neuronal apoptosis is a context-specific outcome of BAX MOMP. Reason: The neuronal-apoptosis rows can be retained as non-core, but the same mitochondrial permeabilization mechanism is already represented by BAX MOMP and cytochrome-c-release annotations. |
| GO:0043525 positive regulation of neuron apoptotic process | IDA PMID:15637643 The permeability transition pore triggers Bax translocation ... | KEEP AS NON CORE | Summary: Neuronal apoptosis is a context-specific outcome of BAX MOMP. Reason: The neuronal-apoptosis rows can be retained as non-core, but the same mitochondrial permeabilization mechanism is already represented by BAX MOMP and cytochrome-c-release annotations. |
| GO:0043653 mitochondrial fragmentation involved in apoptotic process | IDA PMID:12499352 Spatial and temporal association of Bax with mitochondrial f... | KEEP AS NON CORE | Summary: BAX-associated mitochondrial fragmentation is a secondary apoptotic morphology row. Reason: BAX foci associate with mitochondrial fission/scission sites during apoptosis, but mitochondrial fragmentation is not the core BAX pore-forming step. |
| GO:0046930 pore complex | IDA PMID:9219694 Inhibition of Bax channel-forming activity by Bcl-2. | MODIFY | Summary: The generic pore-complex row can be tightened to the BAX complex. Reason: The relevant apoptotic protein-containing complex is the BAX oligomer rather than an unspecified pore complex. Proposed replacements: BAX complex |
| GO:0046982 protein heterodimerization activity | IPI PMID:9111042 A common binding site mediates heterodimerization and homodi... | ACCEPT | Summary: BAX heterodimerization with BCL2-family partners is central to apoptotic control. Reason: BAX forms regulatory heterodimers with other BCL2-family proteins as part of the activation and restraint network around MOMP. |
| GO:0051087 protein-folding chaperone binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The Hsp70/chaperone-binding assertion is specific but peripheral. Reason: Chaperone binding may regulate BAX conformation or stability, but it is not the core BAX pore-forming function in intrinsic apoptosis. |
| GO:0051434 BH3 domain binding | IDA PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | MODIFY | Summary: This BAX BH3-peptide assay should be annotated as heterodimerization rather than BH3-domain binding by BAX. Reason: PMID:21199865 assayed mutant BAX BH3 peptide binding to prosurvival MCL1 and BCL-XL; the supporting partners bind the BAX BH3 domain, so the BAX-side function is better represented by BCL2-family heterodimerization. Proposed replacements: protein heterodimerization activity |
| GO:0051434 BH3 domain binding | IPI PMID:15705586 Involvement of Noxa in cellular apoptotic responses to inter... | ACCEPT | Summary: BAX binds activator BH3 domains from BH3-only proteins. Reason: Direct engagement of BID or BIM BH3 helices is a proximal conformational activation step for BAX. |
| GO:0051434 BH3 domain binding | IPI PMID:17052454 A stapled BID BH3 helix directly binds and activates BAX. | ACCEPT | Summary: BAX binds activator BH3 domains from BH3-only proteins. Reason: Direct engagement of BID or BIM BH3 helices is a proximal conformational activation step for BAX. |
| GO:0051881 regulation of mitochondrial membrane potential | IDA PMID:9843949 Bax interacts with the permeability transition pore to induc... | MODIFY | Summary: The mitochondrial-potential row can be made directional. Reason: BAX activation is associated with loss of mitochondrial membrane potential in the 1998 isolated-mitochondria experiments, so the negative-regulation child is more precise. Proposed replacements: negative regulation of mitochondrial membrane potential |
| GO:0070059 intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress | TAS PMID:22934019 The endoplasmic reticulum stress response in aging and age-r... | KEEP AS NON CORE | Summary: The ER-stress/IRE1 annotation is review-level support for a peripheral BAX context. Reason: BAX and BAK are discussed in ER-stress signaling, but these TAS rows are not direct experimental evidence for BAX mitochondrial pore formation and should remain non-core. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | MARK AS OVER ANNOTATED | Summary: The exosome row is a high-throughput proteomics projection. Reason: BAX was detected in a proteomic survey of B-cell exosomes, so the row records a real observation and is not removed. It is a single proteome hit: no independent study places BAX in exosomes and no mechanism is known that would sort it into them, vesicle preparations contain many abundant cytosolic proteins, and BAX acts at the mitochondrial outer membrane. The location over-reads the proteomic detection and is marked as an over-annotation. |
| GO:0071944 cell periphery | IDA PMID:21803450 The APP intracellular domain (AICD) potentiates ER stress-in... | UNDECIDED | Summary: The cached APP/AICD abstract does not establish this cell-periphery localization. Reason: The abstract does not expose why BAX should colocalize with the cell periphery, so the row needs full-text curator evidence before a confident decision. |
| GO:0090200 positive regulation of release of cytochrome c from mitochondria | IDA PMID:14963330 Direct activation of Bax by p53 mediates mitochondrial membr... | ACCEPT | Summary: BAX promotes cytochrome-c release through mitochondrial outer-membrane permeabilization. Reason: Although phrased as positive regulation, these rows capture the core fact that BAX activation is upstream of cytochrome-c egress during intrinsic apoptosis. |
| GO:0090200 positive regulation of release of cytochrome c from mitochondria | IMP PMID:21262771 MK-STYX, a catalytically inactive phosphatase regulating mit... | ACCEPT | Summary: BAX promotes cytochrome-c release through mitochondrial outer-membrane permeabilization. Reason: Although phrased as positive regulation, these rows capture the core fact that BAX activation is upstream of cytochrome-c egress during intrinsic apoptosis. |
| GO:0097136 Bcl-2 family protein complex | IDA PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097136 Bcl-2 family protein complex | IEA GO_REF:0000117 | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097144 BAX complex | IDA PMID:14522999 Interaction with a membrane surface triggers a reversible co... | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097144 BAX complex | IDA PMID:17024184 Differential contribution of Puma and Noxa in dual regulatio... | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097144 BAX complex | IDA PMID:19074440 Endophilin B1/Bif-1 stimulates BAX activation independently ... | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097144 BAX complex | IDA PMID:19767770 A novel pro-apoptotic function of RACK1: suppression of Src ... | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097144 BAX complex | IDA PMID:20541605 RACK1 promotes Bax oligomerization and dissociates the inter... | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097144 BAX complex | IDA PMID:20850011 Membrane remodeling induced by the dynamin-related protein D... | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097144 BAX complex | IEA GO_REF:0000107 | ACCEPT | Summary: BAX assembles into BAX and broader BCL2-family complexes during MOMP. Reason: BAX oligomerization at the mitochondrial outer membrane is central to apoptotic pore formation and is more specific than individual generic interaction rows. |
| GO:0097145 BAK complex | IDA PMID:16113678 Clusterin inhibits apoptosis by interacting with activated B... | REMOVE | Summary: The Clusterin source should not place BAX in the BAK complex. Reason: PMID:16113678 supports regulation of activated BAX, but a BAK-complex cellular-component row is not the right assertion for BAX oligomers. |
| GO:0097190 apoptotic signaling pathway | IDA PMID:16424160 The endoplasmic reticulum is a key component of the plasma c... | MODIFY | Summary: The apoptotic-signaling parent can be tightened to intrinsic apoptotic signaling. Reason: The plasma-cell death paper places BAX in mitochondrion- and ER-associated apoptosis rather than in apoptotic signaling generically. Proposed replacements: intrinsic apoptotic signaling pathway |
| GO:0097191 extrinsic apoptotic signaling pathway | IDA PMID:15214043 Apoptosis via the B cell antigen receptor requires Bax trans... | MODIFY | Summary: The BCR paper should be scoped to B-cell receptor apoptotic signaling. Reason: PMID:15214043 supports BAX translocation downstream of B-cell receptor signaling, not generic extrinsic death-receptor signaling. Proposed replacements: B cell receptor apoptotic signaling pathway |
| GO:0097192 extrinsic apoptotic signaling pathway in absence of ligand | IBA GO_REF:0000033 | MODIFY | Summary: The inherited ligand-absence extrinsic row should be scoped to BAX-mediated MOMP. Reason: BAX is a mitochondrial permeabilization effector, and the inherited extrinsic ligand-absence subtype overstates the pathway context for that direct activity. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000135648 SUPPORTS SOURCE BUT NOT TARGET The node supports a BCL2-family apoptosis role, but BAX itself directly permeabilizes the mitochondrial outer membrane rather than defining the ligand-absence extrinsic subtype. Proposed replacements: mitochondrial outer membrane permeabilization |
| GO:0097193 intrinsic apoptotic signaling pathway | IDA PMID:16462759 Inhibition of Bax activity is crucial for the antiapoptotic ... | ACCEPT | Summary: BAX is a mitochondrial effector of intrinsic apoptotic signaling. Reason: BAX conformational activation and oligomerization at mitochondria are core intrinsic-pathway steps upstream of apoptosome formation. |
| GO:0097193 intrinsic apoptotic signaling pathway | IDA PMID:9219694 Inhibition of Bax channel-forming activity by Bcl-2. | ACCEPT | Summary: BAX is a mitochondrial effector of intrinsic apoptotic signaling. Reason: BAX conformational activation and oligomerization at mitochondria are core intrinsic-pathway steps upstream of apoptosome formation. |
| GO:0097194 execution phase of apoptosis | IMP PMID:11350920 Deficiency of caspase-3 in MCF7 cells blocks Bax-mediated nu... | MODIFY | Summary: BAX acts before the execution phase of apoptosis. Reason: BAX-mediated MOMP and cytochrome-c release are upstream of apoptosome formation and executioner-caspase activation, so mitochondrial outer membrane permeabilization is the more precise process. Proposed replacements: mitochondrial outer membrane permeabilization |
| GO:0097435 supramolecular fiber organization | IDA PMID:31690630 Humanin induces conformational changes in the apoptosis regu... | MARK AS OVER ANNOTATED | Summary: Humanin sequesters BAX into fibers; BAX is not the fiber-organizing factor. Reason: The cited study shows that humanin and BAX form fibers together in vitro and that BAX undergoes structural rearrangement and is incorporated into the fibers (PMID:31690630). BAX is therefore a constituent of these co-assemblies, and the observation is real. It was made with recombinant proteins, and the fibers are proposed as a way in which humanin sequesters BAX away from mitochondria; nothing shows that organizing supramolecular fibers is a physiological activity of BAX. The process term over-reads the in vitro finding rather than being false. |
| GO:0098586 cellular response to virus | IDA PMID:25609812 Tom70 mediates Sendai virus-induced apoptosis on mitochondri... | MARK AS OVER ANNOTATED | Summary: Sendai-virus-induced apoptosis should not make BAX a generic viral-response protein. Reason: PMID:25609812 places BAX downstream of TOM70 in virus-induced mitochondrial apoptosis, but BAX performs MOMP rather than executing a broad cellular response to virus. |
| GO:1902512 positive regulation of apoptotic DNA fragmentation | IMP PMID:11350920 Deficiency of caspase-3 in MCF7 cells blocks Bax-mediated nu... | MARK AS OVER ANNOTATED | Summary: Apoptotic DNA fragmentation is downstream of BAX MOMP. Reason: DNA fragmentation is carried out after caspase activation; the upstream BAX step should not be annotated to this downstream nuclear endpoint. |
| GO:1902531 regulation of intracellular signal transduction | IEA GO_REF:0000117 | TOO GENERAL | Summary: The automated intracellular-signaling row is too broad for BAX. Reason: Regulation of intracellular signal transduction is entailed by the more specific annotations kept in this review (positive regulation of intrinsic apoptotic signaling pathway, positive regulation of IRE1-mediated unfolded protein response), so the broad term is true of BAX but adds nothing to them. |
| GO:1903896 positive regulation of IRE1-mediated unfolded protein response | TAS PMID:22013210 The unfolded protein response: integrating stress signals th... | KEEP AS NON CORE | Summary: The ER-stress/IRE1 annotation is review-level support for a peripheral BAX context. Reason: BAX and BAK are discussed in ER-stress signaling, but these TAS rows are not direct experimental evidence for BAX mitochondrial pore formation and should remain non-core. |
| GO:1990117 B cell receptor apoptotic signaling pathway | IDA PMID:15214043 Apoptosis via the B cell antigen receptor requires Bax trans... | KEEP AS NON CORE | Summary: B-cell receptor apoptotic signaling is a valid context-specific BAX pathway. Reason: The BCR row is supported by BAX translocation and cytochrome-c release downstream of B-cell receptor signaling, but it is a stimulus-specific use of the core BAX MOMP mechanism. |
| GO:2001233 regulation of apoptotic signaling pathway | IEA GO_REF:0000117 | MODIFY | Summary: The broad apoptotic-signaling-regulation row should be scoped to BAX-mediated MOMP. Reason: BAX directly permeabilizes the mitochondrial outer membrane rather than merely regulating apoptotic signaling generically. Proposed replacements: mitochondrial outer membrane permeabilization |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | IMP PMID:14963330 Direct activation of Bax by p53 mediates mitochondrial membr... | ACCEPT | Summary: BAX promotes intrinsic apoptotic signaling by driving MOMP. Reason: These rows are regulatory in wording but correctly place BAX upstream of cytochrome-c release and apoptosome activation in the intrinsic pathway. |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | IMP PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | ACCEPT | Summary: BAX promotes intrinsic apoptotic signaling by driving MOMP. Reason: These rows are regulatory in wording but correctly place BAX upstream of cytochrome-c release and apoptosome activation in the intrinsic pathway. |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | IMP PMID:21262771 MK-STYX, a catalytically inactive phosphatase regulating mit... | ACCEPT | Summary: BAX promotes intrinsic apoptotic signaling by driving MOMP. Reason: These rows are regulatory in wording but correctly place BAX upstream of cytochrome-c release and apoptosome activation in the intrinsic pathway. |
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Download this section (compressed HTML)Q: Should GO add a BAX/BAK-specific molecular function term for BH3-triggered mitochondrial outer-membrane permeabilizing pore assembly, rather than relying on the broader channel activity term?
Q: Should historical BAX annotations to mitochondrial permeability transition pore complex and related permeability-transition process terms be systematically retired in favor of mitochondrial outer membrane permeabilization?
Experiment: For peripheral regulators such as ER-resident BAX/BAK and mitochondrial-dynamics factors, reconstitute or deplete the candidate proteins in BAX/BAK-defined cells and measure BAX conformational activation, OMM insertion, oligomerization, and cytochrome-c release separately from terminal cell-death readouts.
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