BCL2L11 encodes BIM, a BH3-only BCL2-family apoptosis regulator that is held on cytoskeletal or endomembrane sites in unstressed cells and is induced, released, or stabilized after death signals. BH3-containing BIM isoforms promote intrinsic apoptosis at mitochondria by engaging and neutralizing pro-survival BCL2 relatives such as BCL2, BCL2L1/Bcl-xL, MCL1, BCL2A1, BCL2L2/Bcl-w, and BCL2L10/Bcl-B, and by directly activating BAX and BAK so they oligomerize, permeabilize the mitochondrial outer membrane, and release cytochrome c. BIM is a major effector downstream of stresses such as growth-factor withdrawal, ER stress, cytoskeletal damage, glucocorticoids, and anoikis, while splice variation and phosphorylation tune the potency, localization, and degradation of particular isoforms.
Definition: Binding to a pro-survival BCL2-family protein through a BH3-mediated interaction to inhibit that protein from sequestering pro-apoptotic BCL2-family effectors or activators.
Justification: BIM, BID, PUMA, BAD, NOXA, and related BH3-only proteins donate BH3 helices to the grooves of pro-survival BCL2 proteins and inhibit their anti-apoptotic activity. GO:0051434 BH3 domain binding annotates the groove-side receptor and is directionally wrong for the BH3-only ligand.
Parent term: molecular function inhibitor activity
Supporting Evidence:
Definition: Binding to a pro-apoptotic BCL2-family effector such as BAX or BAK to promote the conformational activation and oligomerization that drives apoptotic mitochondrial outer-membrane permeabilization.
Justification: Direct-activator BH3-only proteins donate a BH3 helix that activates BAX/BAK, but GO:0051434 BH3 domain binding annotates the groove-containing protein that recognizes a BH3 helix. A BIM/BID-side molecular-function term would prevent these central interactions from collapsing to GO:0005515 protein binding.
Parent term: molecular function activator activity
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:14596824 High-throughput methods to detect dimerization of Bcl-2 fami... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:15694340 Differential targeting of prosurvival Bcl-2 proteins by thei... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:15694340 Differential targeting of prosurvival Bcl-2 proteins by thei... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:15694340 Differential targeting of prosurvival Bcl-2 proteins by thei... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:15694340 Differential targeting of prosurvival Bcl-2 proteins by thei... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:15694340 Differential targeting of prosurvival Bcl-2 proteins by thei... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:16697956 Mitochondria primed by death signals determine cellular addi... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:16697956 Mitochondria primed by death signals determine cellular addi... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:16697956 Mitochondria primed by death signals determine cellular addi... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:16697956 Mitochondria primed by death signals determine cellular addi... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:16697956 Mitochondria primed by death signals determine cellular addi... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:17074758 The vaccinia virus protein F1L interacts with Bim and inhibi... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17074758 The vaccinia virus protein F1L interacts with Bim and inhibi... | REMOVE | Summary: This row captures sequestration of BIM by vaccinia virus F1L. Reason: The viral anti-apoptotic protein uses BCL2-like mimicry to bind BIM; this exogenous countermeasure is not a normal human BCL2L11 molecular function, and GO:0005515 adds no mechanistic specificity. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17525735 ERK1/2-dependent phosphorylation of BimEL promotes its rapid... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17525735 ERK1/2-dependent phosphorylation of BimEL promotes its rapid... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:17525735 ERK1/2-dependent phosphorylation of BimEL promotes its rapid... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:18420585 RACK1 and CIS mediate the degradation of BimEL in cancer cel... | REMOVE | Summary: RACK1 can associate with BimEL during paclitaxel-induced BIM turnover. Reason: RACK1/DLC1/CIS-mediated degradation is a non-core regulatory context for BimEL, and the generic interaction row should not be kept as a BCL2L11 molecular-function annotation. |
| GO:0005515 protein binding | IPI PMID:18551131 Vaccinia virus anti-apoptotic F1L is a novel Bcl-2-like doma... | REMOVE | Summary: This row captures sequestration of BIM by vaccinia virus F1L. Reason: The viral anti-apoptotic protein uses BCL2-like mimicry to bind BIM; this exogenous countermeasure is not a normal human BCL2L11 molecular function, and GO:0005515 adds no mechanistic specificity. |
| GO:0005515 protein binding | IPI PMID:18948948 BAX activation is initiated at a novel interaction site. | MODIFY | Summary: BIM BH3 directly activates BAX rather than merely binding an inert partner. Reason: BIM supplies an activator BH3 helix that triggers BAX conformational activation and downstream oligomerization. GO lacks a directionally correct MF for this direct-activator role, so the row should be replaced by a BCL2-family effector-activator term rather than BH3 domain binding. Proposed replacements: pro-apoptotic BCL2 family effector activator activity |
| GO:0005515 protein binding | IPI PMID:19427863 BimL directly neutralizes Bcl-xL to promote Bax activation d... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:19427863 BimL directly neutralizes Bcl-xL to promote Bax activation d... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:20085765 Noxa is necessary for hydrogen peroxide-induced caspase-depe... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:20627101 The fast-mobility isoform of mouse Mcl-1 is a mitochondrial ... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:21132008 Mcl-1 is critical for survival in a subgroup of non-small-ce... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:21199865 Mutation to Bax beyond the BH3 domain disrupts interactions ... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:21507240 Role of bile salt in regulating Mcl-1 phosphorylation and ch... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:21671007 Role of Bim in apoptosis induced in H460 lung tumor cells by... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:22498477 The anti-apoptotic Bcl-B protein inhibits BECN1-dependent au... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:22516262 Chemical genomics identifies small-molecule MCL1 repressors ... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:22516262 Chemical genomics identifies small-molecule MCL1 repressors ... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:23235460 The restricted binding repertoire of Bcl-B leaves Bim as the... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:23235460 The restricted binding repertoire of Bcl-B leaves Bim as the... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:23245996 Synthetic lethal interaction of combined BCL-XL and MEK inhi... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:23245996 Synthetic lethal interaction of combined BCL-XL and MEK inhi... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:23374347 Bax crystal structures reveal how BH3 domains activate Bax a... | MODIFY | Summary: BIM BH3 directly activates BAX rather than merely binding an inert partner. Reason: BIM supplies an activator BH3 helix that triggers BAX conformational activation and downstream oligomerization. GO lacks a directionally correct MF for this direct-activator role, so the row should be replaced by a BCL2-family effector-activator term rather than BH3 domain binding. Proposed replacements: pro-apoptotic BCL2 family effector activator activity |
| GO:0005515 protein binding | IPI PMID:23563182 Polyubiquitination and proteasomal turnover controls the ant... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:23845444 Targeting BCL-2 with the BH3 mimetic ABT-199 in estrogen rec... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:24008843 Structure homology and interaction redundancy for discoverin... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:25497728 BAX-induced apoptosis can be initiated through a conformatio... | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:26004684 Small-Molecule Bcl2 BH4 Antagonist for Lung Cancer Therapy. | UNDECIDED | Summary: The imported IPI row is not recoverable as a precise BIM molecular function from the cached evidence. Reason: Do not reject a manually curated experimental interaction from an abstract-only or indirect cache, but GO:0005515 is too generic to describe BIM-side BH3 activity and the available local evidence is insufficient to assign a specific replacement term safely. |
| GO:0005515 protein binding | IPI PMID:26859456 Exploitation of the Apoptosis-Primed State of MYCN-Amplified... | MODIFY | Summary: BIM uses its BH3 helix to engage and neutralize a pro-survival BCL2-family groove protein. Reason: The interaction is core BCL2-family apoptosis regulation, but GO:0051434 BH3 domain binding describes the groove-side pro-survival partner. A BIM-side inhibitor MF is needed instead of generic GO:0005515. Proposed replacements: pro-survival BCL2 family protein inhibitor activity |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: This large-scale interactome import asserts only generic BIM protein binding. Reason: The row is a high-throughput or computationally expanded protein-interaction edge that does not define an informative BCL2L11 molecular function and should not be retained as GO:0005515. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005739 mitochondrion | IEA GO_REF:0000120 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-139919 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-508162 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-508163 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005741 mitochondrial outer membrane | TAS Reactome:R-HSA-8870686 | ACCEPT | Summary: BIM protein is an outer-mitochondrial-membrane BCL2-family apoptosis regulator after induction or release. Reason: Although this Reactome pathway is a transcriptional context, the expressed BIM protein feeds the same mitochondrial outer-membrane BCL2-family apoptosis module captured by the other OMM rows. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-139918 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-139919 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-205075 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8952232 | ACCEPT | Summary: This Reactome event models transcriptional regulation of the BCL2L11 gene, not cytosolic BIM protein. Reason: Cytosol is accepted for BIM on the other Reactome rows for this term, and the claim is the same here. The Reactome event behind this row describes transcriptional regulation of the BCL2L11 gene; its product, newly made BIM protein, is placed by Reactome in the cytosol. 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-9699574 | ACCEPT | Summary: This Reactome event models transcriptional regulation of the BCL2L11 gene, not cytosolic BIM protein. Reason: Cytosol is accepted for BIM on the other Reactome rows for this term, and the claim is the same here. The Reactome event behind this row describes transcriptional regulation of the BCL2L11 gene; its product, newly made BIM protein, is placed by Reactome in the cytosol. The event is not itself a localization experiment, which limits this row's evidence but not the claim. |
| GO:0006915 apoptotic process | TAS PMID:10381623 A novel adenovirus E1B19K-binding protein B5 inhibits apopto... | UNDECIDED | Summary: The old UniProt TAS source does not expose enough cached evidence to tighten this broad BIM apoptosis assertion. Reason: PMID:10381623 is abstract-only and foregrounds a 219-amino-acid BNIP3-like B5 protein. Keep the broad GO:0006915 row unresolved until the original UniProt TAS context or full text can be checked. |
| GO:0006915 apoptotic process | TAS PMID:9731710 BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 dom... | UNDECIDED | Summary: The old UniProt TAS source does not expose enough cached evidence to tighten this broad BIM apoptosis assertion. Reason: PMID:9731710 is abstract-only and uses the old BOD nomenclature without enough local detail to map its isoforms onto current BIM isoforms. Keep the broad GO:0006915 row unresolved until the original UniProt TAS context or full text can be checked. |
| GO:0008017 microtubule binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: BimEL is sequestered to a microtubule-associated motor complex through dynein light chain proteins. Reason: The row is transferred from mouse Bcl2l11, which carries microtubule binding from a direct assay (IDA, PMID:16832056), so the association of BIM with microtubules is an experimental observation in the ortholog. The association is, however, indirect: BIM is held on the microtubule-associated dynein motor complex through dynein light chain (DYNLL1), and nothing shows that BIM itself binds tubulin polymers. A microtubule-binding molecular function therefore over-reads the sequestration mechanism rather than being a wrong transfer. |
| GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The BCL2L11/BIM PAINT node supports a stress-specific intrinsic-apoptosis role. Reason: BIM is a direct BH3-only regulator of mitochondrial apoptosis; the DNA-damage response is one stimulus context for that activity rather than a separate core molecular function. |
| GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage | IDA PMID:11546872 Bmf: a proapoptotic BH3-only protein regulated by interactio... | KEEP AS NON CORE | Summary: BIM is a BH3-only effector in DNA-damage-associated intrinsic apoptosis. Reason: The full BMF paper is not cached, but this experimental row is plausible for BIM and is best kept as a stimulus-specific instance of the same BCL2-family mitochondrial activity rather than rejected from abstract-only evidence. |
| GO:0012505 endomembrane system | IEA GO_REF:0000044 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0016020 membrane | IEA GO_REF:0000107 | ACCEPT | Summary: BIM is a cytosolic, endomembrane-associated, and mitochondrial BCL2-family protein. Reason: BIM isoforms are sequestered outside mitochondria in unstressed cells and act at mitochondrial membranes after release or induction, so these broad localization rows are consistent with the established activation and translocation cycle. |
| GO:0019901 protein kinase binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: BIM is regulated by phosphorylation, but protein kinase binding is not an established core BIM activity. Reason: The BCL2-family function of BIM is BH3-mediated regulation of pro-survival proteins and BAX/BAK. Kinase contact with BIM as a substrate or regulatory target is too indirect to keep as a core molecular function without a partner-specific assay. |
| GO:0031334 positive regulation of protein-containing complex assembly | IDA PMID:21041309 BH3 domains other than Bim and Bid can directly activate Bax... | MODIFY | Summary: Direct activator BH3 domains promote BAX/BAK oligomerization leading to MOMP. Reason: GO:0031334 is overly generic; the relevant assembly is the BAX/BAK apoptotic pore that drives mitochondrial outer-membrane permeabilization. |
| GO:0031334 positive regulation of protein-containing complex assembly | IMP PMID:19767770 A novel pro-apoptotic function of RACK1: suppression of Src ... | MODIFY | Summary: The complex-assembly row is too broad for BIM-dependent apoptotic pore assembly. Reason: The relevant outcome of RACK1/BIM signaling is promotion of BIM-dependent mitochondrial apoptosis, not a generic positive effect on protein-containing complex assembly. |
| GO:0034976 response to endoplasmic reticulum stress | IBA GO_REF:0000033 | MODIFY | Summary: BIM acts in ER-stress-triggered intrinsic apoptosis rather than as a generic ER-stress response factor. Reason: BIM is induced or activated downstream of prolonged ER stress and then feeds the mitochondrial apoptotic branch; positive regulation of ER-stress-induced intrinsic apoptosis is more specific than response to ER stress. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN001738902 · PTN001738902 SUPPORTS TRANSFER The BCL2L11/BIM ancestral node supports ER-stress-associated apoptosis; the GOA term is merely broader than the mitochondrial apoptosis role. |
| GO:0034976 response to endoplasmic reticulum stress | IDA PMID:22761832 CHOP potentially co-operates with FOXO3a in neuronal cells t... | MODIFY | Summary: BIM acts in ER-stress-triggered intrinsic apoptosis rather than as a generic ER-stress response factor. Reason: BIM is induced or activated downstream of prolonged ER stress and then feeds the mitochondrial apoptotic branch; positive regulation of ER-stress-induced intrinsic apoptosis is more specific than response to ER stress. |
| GO:0034976 response to endoplasmic reticulum stress | IEA GO_REF:0000107 | MODIFY | Summary: BIM acts in ER-stress-triggered intrinsic apoptosis rather than as a generic ER-stress response factor. Reason: BIM is induced or activated downstream of prolonged ER stress and then feeds the mitochondrial apoptotic branch; positive regulation of ER-stress-induced intrinsic apoptosis is more specific than response to ER stress. |
| GO:0042981 regulation of apoptotic process | IDA PMID:18209102 A novel BH3 ligand that selectively targets Mcl-1 reveals th... | MODIFY | Summary: The apoptosis-regulation row is correct but too broad for BIM. Reason: BIM promotes intrinsic apoptosis by neutralizing anti-apoptotic BCL2 proteins and activating BAX/BAK-dependent MOMP, so a positive intrinsic-apoptosis term captures the sign and branch more accurately. Proposed replacements: positive regulation of intrinsic apoptotic signaling pathway |
| GO:0042981 regulation of apoptotic process | TAS PMID:20371704 Glycogen synthase kinase-3 plays a central role in mediating... | MODIFY | Summary: The apoptosis-regulation row is correct but too broad for BIM. Reason: BIM promotes intrinsic apoptosis by neutralizing anti-apoptotic BCL2 proteins and activating BAX/BAK-dependent MOMP, so a positive intrinsic-apoptosis term captures the sign and branch more accurately. Proposed replacements: positive regulation of intrinsic apoptotic signaling pathway |
| GO:0043065 positive regulation of apoptotic process | IBA GO_REF:0000033 | MODIFY | Summary: BIM is a positive BCL2-family regulator of mitochondrial apoptosis. Reason: The positive-regulation sign is correct but the row should be tightened to BIM-dependent mitochondrial outer-membrane permeabilization. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN001738902 · PTN001738902 SUPPORTS TRANSFER The BCL2L11/BIM ancestral node supports a positive pro-apoptotic role; the generic parent should be tightened to BAX/BAK-dependent MOMP. |
| GO:0043065 positive regulation of apoptotic process | IMP PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | MODIFY | Summary: BIM is a positive BCL2-family regulator of mitochondrial apoptosis. Reason: The positive-regulation sign is correct but the row should be tightened to BIM-dependent mitochondrial outer-membrane permeabilization. |
| GO:0071385 cellular response to glucocorticoid stimulus | TAS PMID:20371704 Glycogen synthase kinase-3 plays a central role in mediating... | MARK AS OVER ANNOTATED | Summary: BIM acts downstream in glucocorticoid-triggered apoptosis. Reason: The cached source identifies BIM as an essential mediator of glucocorticoid-induced apoptosis, but BIM does not execute the glucocorticoid stimulus-response machinery itself. |
| GO:0090200 positive regulation of release of cytochrome c from mitochondria | IGI PMID:21041309 BH3 domains other than Bim and Bid can directly activate Bax... | ACCEPT | Summary: The row captures core BIM-dependent mitochondrial apoptosis control. Reason: BIM is a BH3-only member of BCL2-family complexes and promotes cytochrome-c release by activating or derepressing BAX/BAK at mitochondria. |
| GO:0090200 positive regulation of release of cytochrome c from mitochondria | IMP PMID:17289999 Apoptosis initiated when BH3 ligands engage multiple Bcl-2 h... | ACCEPT | Summary: The row captures core BIM-dependent mitochondrial apoptosis control. Reason: BIM is a BH3-only member of BCL2-family complexes and promotes cytochrome-c release by activating or derepressing BAX/BAK at mitochondria. |
| GO:0097136 Bcl-2 family protein complex | IEA GO_REF:0000107 | ACCEPT | Summary: The row captures core BIM-dependent mitochondrial apoptosis control. Reason: BIM is a BH3-only member of BCL2-family complexes and promotes cytochrome-c release by activating or derepressing BAX/BAK at mitochondria. |
| GO:0097136 Bcl-2 family protein complex | IPI PMID:20066663 Mcl-1-Bim complexes accommodate surprising point mutations v... | ACCEPT | Summary: The row captures core BIM-dependent mitochondrial apoptosis control. Reason: BIM is a BH3-only member of BCL2-family complexes and promotes cytochrome-c release by activating or derepressing BAX/BAK at mitochondria. |
| GO:0097141 BIM-BCL-2 complex | IBA GO_REF:0000033 | ACCEPT | Summary: The row captures core BIM-dependent mitochondrial apoptosis control. Reason: BIM is a BH3-only member of BCL2-family complexes and promotes cytochrome-c release by activating or derepressing BAX/BAK at mitochondria. |
| GO:1902237 positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway | TAS PMID:22013210 The unfolded protein response: integrating stress signals th... | KEEP AS NON CORE | Summary: BIM links unresolved ER stress to the mitochondrial apoptosis machinery. Reason: The ER-stress context is stimulus-specific, but it acts through the same direct BH3-only activity that drives BAX/BAK-dependent intrinsic apoptosis. |
| GO:1903896 positive regulation of IRE1-mediated unfolded protein response | TAS PMID:22013210 The unfolded protein response: integrating stress signals th... | UNDECIDED | Summary: TAS annotation from a review of IRE1-alpha signalling. BIM acts downstream of ER stress to promote mitochondrial apoptosis; whether it also modulates IRE1-alpha, as the annotation states, cannot be checked without the review's full text. Reason: The term is a traceable author statement from a review of signalling through the stress sensor IRE1-alpha; only its abstract is available, so what the review says about BIM cannot be checked. The same review is the source of the same term on BAX and BAK1, where it is kept as a non-core role, and BH3-only proteins have been reported to modulate IRE1-alpha signalling, so the claim cannot be dismissed as a simple confusion of downstream induction with upstream regulation. It is left undecided until the review can be read. |
| GO:2000271 positive regulation of fibroblast apoptotic process | IDA PMID:11997495 Identification of novel isoforms of the BH3 domain protein B... | MODIFY | Summary: The fibroblast qualifier reflects the assay cell type rather than a BIM-specific process. Reason: Human BIM isoforms promoted intrinsic apoptosis in transfected cells; the fibroblast-specific child term is too narrow for this BCL2-family function. Proposed replacements: positive regulation of intrinsic apoptotic signaling pathway |
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Download this section (compressed HTML)Q: Should GO add paired BIM-side molecular-function terms for BH3-only inhibition of pro-survival BCL2 proteins and direct activation of BAX/BAK, so these interactions are not forced into GO:0005515 or the directionally wrong GO:0051434 BH3 domain binding term?
Q: Should BIM splice isoforms that lack the canonical BH3 or C-terminal mitochondrial targeting regions be separated in GOA once source papers specify exactly which human isoform was assayed?
Experiment: For candidate BIM interactions outside the BCL2-family core, map whether the partner changes BIM release from dynein, mitochondrial targeting, BH3-groove occupancy, or BAX/BAK activation before curating the edge as more than generic protein binding.
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