BABAM2 (BRISC and BRCA1-A complex member 2; BRE/BRCC45) is an adaptor subunit, built from two ubiquitin E2 variant-like domains, of two BRCC3/BRCC36 K63-linked deubiquitinase complexes. In the nuclear BRCA1-A complex (RAP80, ABRAXAS1, BRCC3, BABAM2, BABAM1) it bridges BABAM1 to the rest of the complex, maintains complex integrity, and supports BRCA1 targeting to K63-ubiquitinated chromatin at DNA double-strand breaks, the G2/M checkpoint and resistance to ionizing radiation. In the cytoplasmic and nuclear BRISC complex (ABRAXAS2, BRCC3, BABAM2, BABAM1, with SHMT2) it has the same bridging role; BRISC deubiquitinates IFNAR1 and NUMA1. After DNA damage, BRE also recruits the deubiquitinase USP7 to stabilize CDC25A (a role identified in a mouse ES-cell screen), and BRE-null mouse fibroblasts repair DSBs more slowly and senesce early. As BRE, it was originally identified as a TNF-R1/Fas-binding protein that inhibits death-receptor apoptosis; in a mouse carcinoma line it maintains XIAP levels.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000152 nuclear ubiquitin ligase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Nuclear ubiquitin ligase complex (IBA). BABAM2 (BRCC45) is part of the BRCA1-BARD1-containing BRCC/BRCA1-A assembly. With BRCC36 it enhances the BRCA1/BARD1 E3 ligase activity, so it is part of a nuclear ubiquitin ligase complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000390309 SUPPORTS TRANSFER BRE/BRCC45 family node. Human BABAM2's own experimental annotations are the descendant evidence, which is why the target appears in the WITH/FROM. UniProtKB:Q9NXR7 SUPPORTS TRANSFER The target itself, with IDA/IMP support for this term. Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically |
| GO:0000152 nuclear ubiquitin ligase complex | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: Nuclear ubiquitin ligase complex (IDA). BABAM2 (BRCC45) is part of the BRCA1-BARD1-containing BRCC/BRCA1-A assembly. With BRCC36 it enhances the BRCA1/BARD1 E3 ligase activity, so it is part of a nuclear ubiquitin ligase complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:14636569 "Reconstitution of a recombinant four-subunit complex containing BRCA1/BARD1/BRCC45/BRCC36 revealed an enhanced E3 ligase activity compared to that of BRCA1/BARD1 heterodimer."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:14636569 Reconstitution of a recombinant four-subunit complex containing BRCA1/BARD1/BRCC45/BRCC36 revealed an enhanced E3 ligase activity compared to that of BRCA1/BARD1 heterodimer. |
| GO:0000268 peroxisome signal sequence receptor activity | TAS PMID:11676476 Expression of human BRE in multiple isoforms. | REMOVE | Summary: Peroxisome signal sequence receptor activity (TAS). The source paper notes that the canonical BRE isoform carries a C-terminal peroxisomal targeting sequence and proposes that BRE regulates peroxisomal activities. Carrying a targeting signal is not acting as a receptor for one, which is the PEX5/PEX7 role. The source shows no peroxisomal function for BRE. Removed. Reason: [PMID:11676476 "We propose that the function of BRE and its isoforms is to regulate peroxisomal activities."] Supporting Evidence: PMID:11676476 We propose that the function of BRE and its isoforms is to regulate peroxisomal activities. |
| GO:0005164 tumor necrosis factor receptor binding | IDA PMID:15465831 A death receptor-associated anti-apoptotic protein, BRE, inh... | KEEP AS NON CORE | Summary: Tumor necrosis factor receptor binding (IDA). BRE was first isolated as a binder of the TNF-R1 juxtamembrane domain and down-regulates TNF-induced NF-kappaB activation. UniProt notes these effects may be indirect. A context-specific function outside BRCA1-A/BRISC; kept as non-core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831)."] [PMID:15465831 "BRE, brain and reproductive organ-expressed protein, was found previously to bind the intracellular juxtamembrane domain of a ubiquitous death receptor, tumor necrosis factor receptor 1 (TNF-R1), and to down-regulate TNF-alpha-induced activation of NF-kappaB."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831). PMID:15465831 BRE, brain and reproductive organ-expressed protein, was found previously to bind the intracellular juxtamembrane domain of a ubiquitous death receptor, tumor necrosis factor receptor 1 (TNF-R1), and to down-regulate TNF-alpha-induced activation of NF-kappaB. |
| GO:0005164 tumor necrosis factor receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Tumor necrosis factor receptor binding (IEA). BRE was first isolated as a binder of the TNF-R1 juxtamembrane domain and down-regulates TNF-induced NF-kappaB activation. UniProt notes these effects may be indirect. A context-specific function outside BRCA1-A/BRISC; kept as non-core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831). |
| GO:0005515 protein binding | IPI PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | REMOVE | Summary: Protein binding (IPI) with BRCC3. BRCC3 is the catalytic subunit of BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:14636569 BRCC36 and BRCC45 are novel components of the complex with sequence homology to a subunit of the signalosome and proteasome complexes. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:15465831 A death receptor-associated anti-apoptotic protein, BRE, inh... | MODIFY | Summary: Protein binding (IPI) with TNFRSF1A (TNF-R1). BRE binds the juxtamembrane domain of TNF-R1. Tumor necrosis factor receptor binding is the informative term, kept as non-core like the existing GO:0005164 row. Reason: [PMID:15465831 "BRE, brain and reproductive organ-expressed protein, was found previously to bind the intracellular juxtamembrane domain of a ubiquitous death receptor, tumor necrosis factor receptor 1 (TNF-R1), and to down-regulate TNF-alpha-induced activation of NF-kappaB."] Proposed replacements: tumor necrosis factor receptor binding Supporting Evidence: PMID:15465831 BRE, brain and reproductive organ-expressed protein, was found previously to bind the intracellular juxtamembrane domain of a ubiquitous death receptor, tumor necrosis factor receptor 1 (TNF-R1), and to down-regulate TNF-alpha-induced activation of NF-kappaB. |
| GO:0005515 protein binding | IPI PMID:15465831 A death receptor-associated anti-apoptotic protein, BRE, inh... | MODIFY | Summary: Protein binding (IPI) with FAS. The 2004 study reports that BRE binds the death receptor Fas. An earlier yeast two-hybrid study found no Fas interaction (only with the p55 TNF receptor). The later binding data come from a different assay with native or mammalian proteins, and the curator annotated them. Death receptor binding is the informative term; the discrepancy is noted, with the later direct evidence taken as current. Reason: [PMID:15465831 "Here we show that BRE also binds to another death receptor, Fas, and upon overexpression conferred resistance to apoptosis induced by TNF-alpha, anti-Fas agonist antibody, cycloheximide, and a variety of stress-related stimuli."] [PMID:9737713 "In the yeast two-hybrid assay, BRE specifically interacted with p55 TNF receptor but not with other TNF family members such as the Fas receptor, the p75 TNF receptor, and p75 neurotrophin receptor."] Proposed replacements: death receptor binding Supporting Evidence: PMID:15465831 Here we show that BRE also binds to another death receptor, Fas, and upon overexpression conferred resistance to apoptosis induced by TNF-alpha, anti-Fas agonist antibody, cycloheximide, and a variety of stress-related stimuli. PMID:9737713 In the yeast two-hybrid assay, BRE specifically interacted with p55 TNF receptor but not with other TNF family members such as the Fas receptor, the p75 TNF receptor, and p75 neurotrophin receptor. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: Protein binding (IPI) with BABAM1. BABAM1 (MERIT40) binds BABAM2 directly in both BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | REMOVE | Summary: Protein binding (IPI) with BRCC3. BRCC3 is the catalytic subunit of BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:14636569 BRCC36 and BRCC45 are novel components of the complex with sequence homology to a subunit of the signalosome and proteasome complexes. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | REMOVE | Summary: Protein binding (IPI) with ABRAXAS1. ABRAXAS1 is a BRCA1-A subunit; this is captured by GO:0070531. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:20656689 Abraxas and BRCC45 were essential for BRCC36 DUB activity within the RAP80 complex, whereas KIAA0157/Abro was the only interaction required for DUB activity within the BRISC. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | REMOVE | Summary: Protein binding (IPI) with BABAM1. BABAM1 (MERIT40) binds BABAM2 directly in both BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:19261749 NBA1, a new player in the Brca1 A complex, is required for D... | REMOVE | Summary: Protein binding (IPI) with ABRAXAS1. ABRAXAS1 is a BRCA1-A subunit; this is captured by GO:0070531. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:20656689 Abraxas and BRCC45 were essential for BRCC36 DUB activity within the RAP80 complex, whereas KIAA0157/Abro was the only interaction required for DUB activity within the BRISC. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:19615732 Defining the human deubiquitinating enzyme interaction lands... | REMOVE | Summary: Protein binding (IPI) with BABAM1. BABAM1 (MERIT40) binds BABAM2 directly in both BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Protein binding (IPI) with BABAM1. BABAM1 (MERIT40) binds BABAM2 directly in both BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Protein binding (IPI) with BABAM1. BABAM1 (MERIT40) binds BABAM2 directly in both BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding (IPI) with BABAM1. BABAM1 (MERIT40) binds BABAM2 directly in both BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | REMOVE | Summary: Protein binding (IPI) with SMAD4. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. |
| GO:0005515 protein binding | IPI PMID:37398436 AI-guided pipeline for protein-protein interaction drug disc... | REMOVE | Summary: Protein binding (IPI) with BABAM1. BABAM1 (MERIT40) binds BABAM2 directly in both BRCA1-A and BRISC; this is captured by the complex rows. Generic protein binding is uninformative; removed under policy. Removal does not mean the interaction is false. Reason: Removed under the generic protein-binding policy: GO:0005515 is uninformative on its own. Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0005634 nucleus | IDA PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: Nucleus (IDA). BABAM2 is nuclear and accumulates at DNA damage sites in the BRCA1-A complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005634 nucleus | IDA PMID:15465831 A death receptor-associated anti-apoptotic protein, BRE, inh... | ACCEPT | Summary: Nucleus (IDA). BABAM2 is nuclear and accumulates at DNA damage sites in the BRCA1-A complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005634 nucleus | IDA PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | ACCEPT | Summary: Nucleus (IDA). BABAM2 is nuclear and accumulates at DNA damage sites in the BRCA1-A complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] [PMID:19261748 "Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). PMID:19261748 Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage. |
| GO:0005634 nucleus | IDA PMID:24075985 A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates in... | ACCEPT | Summary: Nucleus (IDA). BABAM2 is nuclear and accumulates at DNA damage sites in the BRCA1-A complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] [PMID:24075985 "The deubiquitinating enzyme (DUB) BRCC36 segregates into distinct nuclear and cytoplasmic complexes that are specific for K63-Ub hydrolysis."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). PMID:24075985 The deubiquitinating enzyme (DUB) BRCC36 segregates into distinct nuclear and cytoplasmic complexes that are specific for K63-Ub hydrolysis. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: Nucleus (IEA). BABAM2 is nuclear and accumulates at DNA damage sites in the BRCA1-A complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005634 nucleus | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: Nucleus (NAS). BABAM2 is nuclear and accumulates at DNA damage sites in the BRCA1-A complex. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] [PMID:20656689 "BRCC36 is a JAMM (JAB1/MPN/Mov34 metalloenzyme) domain, lysine 63-ubiquitin (K63-Ub)-specific deubiquitinating enzyme (DUB) and a member of two protein complexes: the DNA damage-responsive BRCA1-RAP80 complex, and the cytoplasmic BRCC36 isopeptidase complex (BRISC)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). PMID:20656689 BRCC36 is a JAMM (JAB1/MPN/Mov34 metalloenzyme) domain, lysine 63-ubiquitin (K63-Ub)-specific deubiquitinating enzyme (DUB) and a member of two protein complexes: the DNA damage-responsive BRCA1-RAP80 complex, and the cytoplasmic BRCC36 isopeptidase complex (BRISC). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5683385 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'Formation of BRCA1-A complex at DNA DSBs'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5683735 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'CHEK2 is recruited to DNA DSBs'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5683801 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'CHEK2 phosphorylates BRCA1'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684052 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'PIAS4 SUMOylates MDC1'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684071 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'RNF4 ubiquitinates MDC1'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686685 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'RIF1 and PAX1IP bind TP53BP1 at DNA DSBs'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5691411 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'BRCA1-A complex deubiquitinates K63polyUb-histone H2A'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693551 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'Phosphorylation of BRCA1-A complex at multiple sites by ATM'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-69891 | ACCEPT | Summary: Nucleoplasm (TAS). Nucleoplasmic DNA-damage-response protein. Accepted. Reactome event: 'Phosphorylation and activation of CHEK2 by ATM'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC ECO:0000269|PubMed:24075985}. Nucleus {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). |
| GO:0005737 cytoplasm | IDA PMID:15465831 A death receptor-associated anti-apoptotic protein, BRE, inh... | ACCEPT | Summary: Cytoplasm (IDA). As a BRISC subunit, BABAM2 is also cytoplasmic, where BRISC deubiquitinates IFNAR1 and other substrates. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that |
| GO:0005737 cytoplasm | IDA PMID:24075985 A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates in... | ACCEPT | Summary: Cytoplasm (IDA). As a BRISC subunit, BABAM2 is also cytoplasmic, where BRISC deubiquitinates IFNAR1 and other substrates. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:24075985 "The deubiquitinating enzyme (DUB) BRCC36 segregates into distinct nuclear and cytoplasmic complexes that are specific for K63-Ub hydrolysis."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:24075985 The deubiquitinating enzyme (DUB) BRCC36 segregates into distinct nuclear and cytoplasmic complexes that are specific for K63-Ub hydrolysis. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Cytoplasm (IEA). As a BRISC subunit, BABAM2 is also cytoplasmic, where BRISC deubiquitinates IFNAR1 and other substrates. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that |
| GO:0005737 cytoplasm | IPI PMID:31253574 Structural Basis of BRCC36 Function in DNA Repair and Immune... | ACCEPT | Summary: Cytoplasm (IPI). As a BRISC subunit, BABAM2 is also cytoplasmic, where BRISC deubiquitinates IFNAR1 and other substrates. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:31253574 "While BRCA1-A is predominantly confined to the nucleus, BRISC localizes to the nucleus and the cytoplasm, where its wide range of reported substrates includes ATF4, THAP5, NLRP3, and the cytosolic domain of IFNAR1, an interferon receptor (Ambivero et al., 2012, Cilenti et al., 2011, Py et al., 2013, Zheng et al., 2013)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:31253574 While BRCA1-A is predominantly confined to the nucleus, BRISC localizes to the nucleus and the cytoplasm, where its wide range of reported substrates includes ATF4, THAP5, NLRP3, and the cytosolic domain of IFNAR1, an interferon receptor (Ambivero et al., 2012, Cilenti et al., 2011, Py et al., 2013, Zheng et al., 2013). |
| GO:0005737 cytoplasm | NAS PMID:31253574 Structural Basis of BRCC36 Function in DNA Repair and Immune... | ACCEPT | Summary: Cytoplasm (NAS). As a BRISC subunit, BABAM2 is also cytoplasmic, where BRISC deubiquitinates IFNAR1 and other substrates. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:31253574 "While BRCA1-A is predominantly confined to the nucleus, BRISC localizes to the nucleus and the cytoplasm, where its wide range of reported substrates includes ATF4, THAP5, NLRP3, and the cytosolic domain of IFNAR1, an interferon receptor (Ambivero et al., 2012, Cilenti et al., 2011, Py et al., 2013, Zheng et al., 2013)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:31253574 While BRCA1-A is predominantly confined to the nucleus, BRISC localizes to the nucleus and the cytoplasm, where its wide range of reported substrates includes ATF4, THAP5, NLRP3, and the cytosolic domain of IFNAR1, an interferon receptor (Ambivero et al., 2012, Cilenti et al., 2011, Py et al., 2013, Zheng et al., 2013). |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Cytosol (IDA). Human Protein Atlas immunofluorescence. Cytosolic pool, as part of BRISC. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5691439 | ACCEPT | Summary: Cytosol (TAS). Cytosolic pool, as part of BRISC. Accepted. Reactome event: 'BRISC complex deubiquitinates NLRP3'. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831,"] [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15465831, file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that |
| GO:0006282 regulation of DNA repair | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: Regulation of DNA repair (NAS). A correct parent of the positive-regulation row. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:20656689 "Abraxas and BRCC45 were essential for BRCC36 DUB activity within the RAP80 complex, whereas KIAA0157/Abro was the only interaction required for DUB activity within the BRISC."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:20656689 Abraxas and BRCC45 were essential for BRCC36 DUB activity within the RAP80 complex, whereas KIAA0157/Abro was the only interaction required for DUB activity within the BRISC. |
| GO:0006302 double-strand break repair | IBA GO_REF:0000033 | ACCEPT | Summary: Double-strand break repair (IBA). BABAM2 is required for BRCA1-A complex stability and BRCA1 recruitment to DSBs. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000390309 SUPPORTS TRANSFER BRE/BRCC45 family node. Human BABAM2's own experimental annotations are the descendant evidence, which is why the target appears in the WITH/FROM. UniProtKB:Q9NXR7 SUPPORTS TRANSFER The target itself, with IDA/IMP support for this term. Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically |
| GO:0006302 double-strand break repair | IMP PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | ACCEPT | Summary: Double-strand break repair (IMP). BABAM2 is required for BRCA1-A complex stability and BRCA1 recruitment to DSBs. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:19261748 "Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:19261748 Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage. |
| GO:0006974 DNA damage response | IEP PMID:7826398 Identification of a brain- and reproductive-organs-specific ... | KEEP AS NON CORE | Summary: DNA damage response (IEP). BRE mRNA falls after UV and 4-nitroquinoline-1-oxide treatment. This is an expression response; BABAM2's functional DNA-damage roles are captured by the BRCA1-A rows. Kept as non-core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:7826398 "Treatment of fibroblast cell with UV and 4-nitroquinoline-1-oxide caused more than 90% and 50% decreases in BRE mRNA, respectively."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:7826398 Treatment of fibroblast cell with UV and 4-nitroquinoline-1-oxide caused more than 90% and 50% decreases in BRE mRNA, respectively. |
| GO:0007095 mitotic G2 DNA damage checkpoint signaling | IMP PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | ACCEPT | Summary: Mitotic G2 DNA damage checkpoint signaling (IMP). BABAM2 is required for the BRCA1-dependent G2/M DNA damage checkpoint. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:19261748 "Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:19261748 Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage. |
| GO:0007165 signal transduction | TAS PMID:9737713 BRE: a modulator of TNF-alpha action. | MARK AS OVER ANNOTATED | Summary: Signal transduction (TAS). Too broad to be informative. It rests on the TNF-receptor yeast two-hybrid identification, and UniProt notes the TNF effects may be indirect. The specific BRE functions are captured elsewhere. Over-annotation. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831)."] [PMID:9737713 "Here we report that BRE was identified multiple times in a yeast two-hybrid screen of a murine cerebellar cDNA library, using the juxtamembrane domain of the p55 tumor necrosis factor alpha (TNF) receptor."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831). PMID:9737713 Here we report that BRE was identified multiple times in a yeast two-hybrid screen of a murine cerebellar cDNA library, using the juxtamembrane domain of the p55 tumor necrosis factor alpha (TNF) receptor. |
| GO:0010212 response to ionizing radiation | IMP PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | ACCEPT | Summary: Response to ionizing radiation (IMP). Loss of BRE/BABAM2 sensitizes cells to ionizing radiation. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:19261748 "Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:19261748 Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage. |
| GO:0010212 response to ionizing radiation | IMP PMID:19261749 NBA1, a new player in the Brca1 A complex, is required for D... | ACCEPT | Summary: Response to ionizing radiation (IMP). Loss of BRE/BABAM2 sensitizes cells to ionizing radiation. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:19261749 "In this study, we employed a genetic screen to identify a gene, NBA1 (new component of the BRCA1 A complex), that is required for resistance to ionizing radiation."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:19261749 In this study, we employed a genetic screen to identify a gene, NBA1 (new component of the BRCA1 A complex), that is required for resistance to ionizing radiation. |
| GO:0031593 polyubiquitin modification-dependent protein binding | IDA PMID:19261749 NBA1, a new player in the Brca1 A complex, is required for D... | ACCEPT | Summary: Polyubiquitin modification-dependent protein binding (IDA). Four BRCA1-A members, including BRE, bind polyubiquitin chains. This fits the complex's recognition of K63-ubiquitinated chromatin at DSBs. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:19261749 "Furthermore, we show that four members of the BRCA1-A complex possess a polyubiquitin chain-binding capability, thus forming a complex that might facilitate the deubiquitinating activity of the deubiquitination enzyme BRCC36 or the E3 ligase activity of the BRCA1/BARD1 ligase."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:19261749 Furthermore, we show that four members of the BRCA1-A complex possess a polyubiquitin chain-binding capability, thus forming a complex that might facilitate the deubiquitinating activity of the deubiquitination enzyme BRCC36 or the E3 ligase activity of the BRCA1/BARD1 ligase. |
| GO:0034516 response to vitamin B6 | NAS PMID:31142841 Metabolic control of BRISC-SHMT2 assembly regulates immune s... | MARK AS OVER ANNOTATED | Summary: Response to vitamin B6 (NAS). PLP is sensed by SHMT2, which binds and inhibits BRISC only as a PLP-free dimer. BABAM2 is a structural BRISC subunit downstream of that sensing. Over-annotation. Reason: [PMID:31142841 "Only the inactive SHMT2 dimer-and not the active PLP-bound tetramer-binds and inhibits BRISC."] [PMID:31142841 "Intracellular levels of PLP regulate the interaction between BRISC and SHMT2, as well as inflammatory cytokine responses."] Supporting Evidence: PMID:31142841 Only the inactive SHMT2 dimer-and not the active PLP-bound tetramer-binds and inhibits BRISC. PMID:31142841 Intracellular levels of PLP regulate the interaction between BRISC and SHMT2, as well as inflammatory cytokine responses. |
| GO:0043066 negative regulation of apoptotic process | IDA PMID:15465831 A death receptor-associated anti-apoptotic protein, BRE, inh... | KEEP AS NON CORE | Summary: Negative regulation of apoptotic process (IDA). BRE overexpression protects against death-receptor apoptosis, and endogenous BRE knockdown increases TNF-induced apoptosis. Kept as non-core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831)."] [PMID:15465831 "However, down-regulation of the endogenous BRE by small interfering RNA increased apoptosis to TNF-alpha, but nottoetoposide, indicating that the physiological antiapoptotic role of this protein is specific to death receptor-mediated apoptosis."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC with TNFRSF1A; however these effects may be indirect (PubMed:15465831). PMID:15465831 However, down-regulation of the endogenous BRE by small interfering RNA increased apoptosis to TNF-alpha, but nottoetoposide, indicating that the physiological antiapoptotic role of this protein is specific to death receptor-mediated apoptosis. |
| GO:0044818 mitotic G2/M transition checkpoint | NAS PMID:22369660 BRCA1 tumor suppressor network: focusing on its tail. | ACCEPT | Summary: Mitotic G2/M transition checkpoint (NAS). A parent of the accepted core term GO:0007095 (mitotic G2 DNA damage checkpoint signaling), so it is accepted at the same altitude. Depletion of individual BRCA1-A subunits, including BRE, gives a milder G2-M defect than BRCA1 loss. Reason: [PMID:22369660 "Interestingly knocking down any components of the A complex such as Rap80, Abraxas, NBA1, BRE, BRCC36 or the C complex component CtIP, the phenotype of G2-M checkpoint deficiency is much milder compared to cells depleted of BRCA1 indicating that only partial function of BRCA1 in G2-M checkpoint control is defective when individual complex was deficient [32,35,36,38,40,69,70,76]."] [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] Supporting Evidence: PMID:22369660 Interestingly knocking down any components of the A complex such as Rap80, Abraxas, NBA1, BRE, BRCC36 or the C complex component CtIP, the phenotype of G2-M checkpoint deficiency is much milder compared to cells depleted of BRCA1 indicating that only partial function of BRCA1 in G2-M checkpoint control is defective when individual complex was deficient [32,35,36,38,40,69,70,76]. file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically |
| GO:0045739 positive regulation of DNA repair | IMP PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | ACCEPT | Summary: Positive regulation of DNA repair (IMP). BABAM2 sustains BRCA1-A integrity and BRCA1 localization at DSBs. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:19261748 "Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:19261748 Importantly, MERIT40 regulates BRCA1 retention at DNA breaks and checkpoint function primarily via a role in maintaining the stability of BRE and this five-subunit protein complex at sites of DNA damage. |
| GO:0070531 BRCA1-A complex | IBA GO_REF:0000033 | ACCEPT | Summary: BRCA1-A complex (IBA). BABAM2 (BRE/BRCC45) is a core subunit of the nuclear BRCA1-A complex. Its UEV-like domains bridge BABAM1 (MERIT40) to the rest of the complex, and it is required for complex integrity. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002689529 SUPPORTS TRANSFER BRE/BRCC45 family node. Human BABAM2's own experimental annotations are the descendant evidence, which is why the target appears in the WITH/FROM. UniProtKB:Q9NXR7 SUPPORTS TRANSFER The target itself, with IDA/IMP support for this term. Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between |
| GO:0070531 BRCA1-A complex | IDA PMID:17525341 RAP80 targets BRCA1 to specific ubiquitin structures at DNA ... | ACCEPT | Summary: BRCA1-A complex (IDA). BABAM2 (BRE/BRCC45) is a core subunit of the nuclear BRCA1-A complex. Its UEV-like domains bridge BABAM1 (MERIT40) to the rest of the complex, and it is required for complex integrity. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] [PMID:17525341 "RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-gammaH2AX-dependent lysine(6)- and lysine(63)-linked ubiquitin polymers at DSBs."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between PMID:17525341 RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-gammaH2AX-dependent lysine(6)- and lysine(63)-linked ubiquitin polymers at DSBs. |
| GO:0070531 BRCA1-A complex | IDA PMID:19261746 MERIT40 controls BRCA1-Rap80 complex integrity and recruitme... | ACCEPT | Summary: BRCA1-A complex (IDA). BABAM2 (BRE/BRCC45) is a core subunit of the nuclear BRCA1-A complex. Its UEV-like domains bridge BABAM1 (MERIT40) to the rest of the complex, and it is required for complex integrity. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] [PMID:19261746 "Here, we identify MERIT40 (Mediator of Rap80 Interactions and Targeting 40 kD)/(C19orf62) as a Rap80-associated protein that is essential for BRCA1-Rap80 complex protein interactions, stability, and DSB targeting."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between PMID:19261746 Here, we identify MERIT40 (Mediator of Rap80 Interactions and Targeting 40 kD)/(C19orf62) as a Rap80-associated protein that is essential for BRCA1-Rap80 complex protein interactions, stability, and DSB targeting. |
| GO:0070531 BRCA1-A complex | IDA PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | ACCEPT | Summary: BRCA1-A complex (IDA). BABAM2 (BRE/BRCC45) is a core subunit of the nuclear BRCA1-A complex. Its UEV-like domains bridge BABAM1 (MERIT40) to the rest of the complex, and it is required for complex integrity. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] [PMID:19261748 "MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. |
| GO:0070531 BRCA1-A complex | IDA PMID:19261749 NBA1, a new player in the Brca1 A complex, is required for D... | ACCEPT | Summary: BRCA1-A complex (IDA). BABAM2 (BRE/BRCC45) is a core subunit of the nuclear BRCA1-A complex. Its UEV-like domains bridge BABAM1 (MERIT40) to the rest of the complex, and it is required for complex integrity. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] [PMID:19261749 "Proteomic analysis revealed that NBA1 is a component of the BRCA1 A complex, which also contains Brca1/Bard1, Abra1, RAP80, BRCC36, and BRE."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between PMID:19261749 Proteomic analysis revealed that NBA1 is a component of the BRCA1 A complex, which also contains Brca1/Bard1, Abra1, RAP80, BRCC36, and BRE. |
| GO:0070531 BRCA1-A complex | IEA GO_REF:0000002 | ACCEPT | Summary: BRCA1-A complex (IEA). BABAM2 (BRE/BRCC45) is a core subunit of the nuclear BRCA1-A complex. Its UEV-like domains bridge BABAM1 (MERIT40) to the rest of the complex, and it is required for complex integrity. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between |
| GO:0070531 BRCA1-A complex | NAS PMID:20656689 Differential regulation of JAMM domain deubiquitinating enzy... | ACCEPT | Summary: BRCA1-A complex (NAS). BABAM2 (BRE/BRCC45) is a core subunit of the nuclear BRCA1-A complex. Its UEV-like domains bridge BABAM1 (MERIT40) to the rest of the complex, and it is required for complex integrity. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] [PMID:20656689 "BRCC36 is a JAMM (JAB1/MPN/Mov34 metalloenzyme) domain, lysine 63-ubiquitin (K63-Ub)-specific deubiquitinating enzyme (DUB) and a member of two protein complexes: the DNA damage-responsive BRCA1-RAP80 complex, and the cytoplasmic BRCC36 isopeptidase complex (BRISC)."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between PMID:20656689 BRCC36 is a JAMM (JAB1/MPN/Mov34 metalloenzyme) domain, lysine 63-ubiquitin (K63-Ub)-specific deubiquitinating enzyme (DUB) and a member of two protein complexes: the DNA damage-responsive BRCA1-RAP80 complex, and the cytoplasmic BRCC36 isopeptidase complex (BRISC). |
| GO:0070536 protein K63-linked deubiquitination | IC PMID:24075985 A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates in... | ACCEPT | Summary: Protein K63-linked deubiquitination (IC). BABAM2 is a structural subunit required for BRCC3-dependent K63 deubiquitination in BRISC and BRCA1-A. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:24075985 "BRISC-SHMT2 complexes localize to and deubiquitinate actively engaged IFNAR1, thus limiting its K63-Ub-mediated internalization and lysosomal degradation."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:24075985 BRISC-SHMT2 complexes localize to and deubiquitinate actively engaged IFNAR1, thus limiting its K63-Ub-mediated internalization and lysosomal degradation. |
| GO:0070552 BRISC complex | IDA PMID:19214193 K63-specific deubiquitination by two JAMM/MPN+ complexes: BR... | ACCEPT | Summary: BRISC complex (IDA). BABAM2 is a core subunit of the BRISC K63-specific deubiquitinase complex, where it likewise bridges BABAM1 to BRCC3 and ABRAXAS2. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:21282113 "Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes."] [PMID:19214193 "When we analysed the individual complexes, we found that the activity was intrinsic to PA700 and the Brcc36 isopeptidase complex (BRISC), but that the CSN-associated activity was due entirely to an interaction with Brcc36."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. PMID:19214193 When we analysed the individual complexes, we found that the activity was intrinsic to PA700 and the Brcc36 isopeptidase complex (BRISC), but that the CSN-associated activity was due entirely to an interaction with Brcc36. |
| GO:0070552 BRISC complex | IDA PMID:24075985 A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates in... | ACCEPT | Summary: BRISC complex (IDA). BABAM2 is a core subunit of the BRISC K63-specific deubiquitinase complex, where it likewise bridges BABAM1 to BRCC3 and ABRAXAS2. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:21282113 "Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes."] [PMID:24075985 "BRISC-SHMT2 complexes localize to and deubiquitinate actively engaged IFNAR1, thus limiting its K63-Ub-mediated internalization and lysosomal degradation."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. PMID:24075985 BRISC-SHMT2 complexes localize to and deubiquitinate actively engaged IFNAR1, thus limiting its K63-Ub-mediated internalization and lysosomal degradation. |
| GO:0070552 BRISC complex | IEA GO_REF:0000002 | ACCEPT | Summary: BRISC complex (IEA). BABAM2 is a core subunit of the BRISC K63-specific deubiquitinase complex, where it likewise bridges BABAM1 to BRCC3 and ABRAXAS2. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:21282113 "Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. |
| GO:0070552 BRISC complex | IPI PMID:31253574 Structural Basis of BRCC36 Function in DNA Repair and Immune... | ACCEPT | Summary: BRISC complex (IPI). BABAM2 is a core subunit of the BRISC K63-specific deubiquitinase complex, where it likewise bridges BABAM1 to BRCC3 and ABRAXAS2. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:21282113 "Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes."] [PMID:31253574 "BRCA1-A and BRISC also contain proteins MERIT40 (Feng et al., 2009, Shao et al., 2009, Wang et al., 2009) and BRE (Feng et al., 2009, Hu et al., 2011a) as core components."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. PMID:31253574 BRCA1-A and BRISC also contain proteins MERIT40 (Feng et al., 2009, Shao et al., 2009, Wang et al., 2009) and BRE (Feng et al., 2009, Hu et al., 2011a) as core components. |
| GO:0070552 BRISC complex | NAS PMID:31253574 Structural Basis of BRCC36 Function in DNA Repair and Immune... | ACCEPT | Summary: BRISC complex (NAS). BABAM2 is a core subunit of the BRISC K63-specific deubiquitinase complex, where it likewise bridges BABAM1 to BRCC3 and ABRAXAS2. Core. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC Component of the BRISC complex, a multiprotein complex that"] [PMID:21282113 "Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes."] [PMID:31253574 "BRCA1-A and BRISC also contain proteins MERIT40 (Feng et al., 2009, Shao et al., 2009, Wang et al., 2009) and BRE (Feng et al., 2009, Hu et al., 2011a) as core components."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC Component of the BRISC complex, a multiprotein complex that PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. PMID:31253574 BRCA1-A and BRISC also contain proteins MERIT40 (Feng et al., 2009, Shao et al., 2009, Wang et al., 2009) and BRE (Feng et al., 2009, Hu et al., 2011a) as core components. |
| GO:0071479 cellular response to ionizing radiation | IMP PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: Cellular response to ionizing radiation (IMP). Depleting BRCC45 increases sensitivity to ionizing radiation and causes G2/M checkpoint defects. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:14636569 "In vivo, depletion of BRCC36 and BRCC45 by the small interfering RNAs (siRNAs) resulted in increased sensitivity to ionizing radiation and defects in G2/M checkpoint."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:14636569 In vivo, depletion of BRCC36 and BRCC45 by the small interfering RNAs (siRNAs) resulted in increased sensitivity to ionizing radiation and defects in G2/M checkpoint. |
| GO:2000001 regulation of DNA damage checkpoint | NAS PMID:14636569 Regulation of BRCC, a holoenzyme complex containing BRCA1 an... | ACCEPT | Summary: Regulation of DNA damage checkpoint (NAS). BRCC45 is needed for the G2/M checkpoint after IR. Accepted. Reason: [file:human/BABAM2/BABAM2-uniprot.txt "CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically"] [PMID:14636569 "In vivo, depletion of BRCC36 and BRCC45 by the small interfering RNAs (siRNAs) resulted in increased sensitivity to ionizing radiation and defects in G2/M checkpoint."] Supporting Evidence: file:human/BABAM2/BABAM2-uniprot.txt CC -!- FUNCTION: Component of the BRCA1-A complex, a complex that specifically PMID:14636569 In vivo, depletion of BRCC36 and BRCC45 by the small interfering RNAs (siRNAs) resulted in increased sensitivity to ionizing radiation and defects in G2/M checkpoint. |
| GO:0030674 protein-macromolecule adaptor activity | IDA PMID:19261748 MERIT40 facilitates BRCA1 localization and DNA damage repair... | NEW | Summary: Protein-macromolecule adaptor activity (NEW, IDA). BRE/BRCC45 is the bridging subunit of both BRCC3 complexes: MERIT40 (BABAM1) assembles into the BRCA1-A complex through its direct interaction with BRE, and the BABAM1-BRE interaction holds both complexes together. BRE is also required for BRCC36 DUB activity in the RAP80 complex. It recruits USP7 to deubiquitylate CDC25A after DNA damage. UniProt describes it as an adapter bridging BABAM1 to the rest of the complex. These are adaptor activities. Reason: [PMID:19261748 "MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45."] [PMID:21282113 "Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes."] [PMID:20656689 "Abraxas and BRCC45 were essential for BRCC36 DUB activity within the RAP80 complex, whereas KIAA0157/Abro was the only interaction required for DUB activity within the BRISC."] [PMID:29416040 "We show that BRE facilitates deubiquitylation of CDC25A by recruiting ubiquitin-specific-processing protease 7 (USP7) in the presence of DNA damage."] [file:human/BABAM2/BABAM2-uniprot.txt "CC complex, it acts as an adapter that bridges the interaction between"] Supporting Evidence: PMID:19261748 MERIT40 is assembled into this RAP80/CCDC98-containing complex via its direct interaction with BRE/BRCC45. PMID:21282113 Here, we found that the two complexes are assembled in a similar manner and NBA1 and BRE interaction is critical for maintaining the integrity of both of the complexes. PMID:20656689 Abraxas and BRCC45 were essential for BRCC36 DUB activity within the RAP80 complex, whereas KIAA0157/Abro was the only interaction required for DUB activity within the BRISC. PMID:29416040 We show that BRE facilitates deubiquitylation of CDC25A by recruiting ubiquitin-specific-processing protease 7 (USP7) in the presence of DNA damage. file:human/BABAM2/BABAM2-uniprot.txt CC complex, it acts as an adapter that bridges the interaction between |
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Download this section (compressed HTML)Q: Within BRCA1-A, BABAM2 supports BRCA1 recruitment yet the complex restrains end resection. Is BABAM2's net effect on DSB repair positive (as annotated) or pathway-specific (limiting HR while supporting checkpoint)?
Q: Is BRE's TNF-R1/Fas binding and anti-apoptotic activity independent of its BRCA1-A/BRISC membership, or a consequence of BRISC deubiquitinating death-receptor-pathway substrates?
Experiment: Compare BABAM2 mutants that cannot bind BABAM1 or BRCC3 (complex-null) with wild type for TNF-R1/Fas binding and death-receptor apoptosis protection.
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