EXO1 (exonuclease 1) is a nuclear, Mg2+-dependent structure-specific nuclease of the XPG/RAD2 (FEN1-like) family. Its N-terminal nuclease domain carries a robust 5'->3' exonuclease that is most active on blunt or 5'-recessed duplex DNA, plus a FEN1-like 5'-flap endonuclease and an RNase H activity; its long, disordered C-terminal region binds partner proteins (MSH2, MLH1, MSH3, PCNA). In DNA mismatch repair EXO1 is the excision nuclease: activated by MutSalpha, it removes the error-containing strand from a nick 5' to the mismatch, and with MutLalpha, PCNA and RFC it also supports excision directed from a 3' nick. In double-strand break repair EXO1, recruited by MRN and CtIP and stimulated by BLM and RPA, performs long-range 5'->3' end resection that creates the 3' single-stranded tails needed for homologous recombination and ATR signalling; ATM- and CDK-dependent phosphorylation tunes how far it resects. At telomeres lacking POT1-TPP1, NBS1 recruits EXO1 to resect the C-strand, feeding alternative end joining. Mouse genetics also implicate Exo1 in meiosis, somatic hypermutation and class switch recombination.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003677 DNA binding | IDA PMID:11842105 Molecular interactions of human Exo1 with DNA. | MODIFY | Summary: Human EXO1 binds DNA; hydroxyl radical footprinting showed it binds the minor groove of flap DNA downstream of the junction, and nuclease-dead HNPCC variants retain substrate binding. Reason: DNA binding is correct but general. The direct evidence in this paper is footprinting on a flap substrate, which supports flap-structured DNA binding. DNA binding here is the substrate engagement of the nuclease, not an independent function, so it is non-core. Proposed replacements: flap-structured DNA binding Supporting Evidence: PMID:11842105 Hydroxyl radical footprinting indicates that Exo1 binds predominantly along the minor groove of flap DNA, downstream of the junction. |
| GO:0003677 DNA binding | IEA GO_REF:0000002 | MODIFY | Summary: InterPro2GO mapping (HhH2 / EXO1 H3TH domains) to DNA binding. Reason: The mapping is correct but general; the same claim is refined on the IDA row to flap-structured DNA binding, which footprinting supports. Kept consistent with that row. Proposed replacements: flap-structured DNA binding Supporting Evidence: PMID:11842105 Exo1 binds predominantly along the minor groove of flap DNA |
| GO:0003677 DNA binding | TAS PMID:9685493 Hex1: a new human Rad2 nuclease family member with homology ... | MODIFY | Summary: TAS from the cloning paper of HEX1, which reports a 5'->3' exonuclease, implying substrate binding. Reason: The cited abstract shows nuclease activity rather than measured binding. DNA binding is true but general; refined consistently with the other rows to flap-structured DNA binding, supported by footprinting in PMID:11842105. Proposed replacements: flap-structured DNA binding Supporting Evidence: PMID:9685493 recombinant Hex1 exhibits a 5'-->3' exonuclease activity PMID:11842105 Exo1 binds predominantly along the minor groove of flap DNA |
| GO:0003682 chromatin binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer from mouse Exo1 (Ensembl Compara) of chromatin binding. Reason: EXO1 is recruited to DNA ends at damage sites through CtIP/MRN and, at telomeres, NBS1, but no human evidence shows a chromatin-binding activity distinct from its DNA-substrate binding. GFP-EXO1 is even lost under pre-extraction conditions. The transferred term overstates the evidence. Supporting Evidence: PMID:21052091 the localization of EXO1 to DSBs depends on both CtIP and MRN PMID:26240375 GFP-EXO1 signal was lost during the pre-extraction conditions used to immunostain RPA foci |
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO mapping to catalytic activity. Reason: True but uninformative; entailed by the accepted 5'-3' DNA exonuclease activity (GO:0035312) and double-stranded DNA 5'-3' DNA exonuclease activity. Supporting Evidence: PMID:10608837 exhibits both a robust 5' to 3' exonuclease activity on single- and double-stranded DNA substrates |
| GO:0004518 nuclease activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO mapping (XPG/Rad2 family) to nuclease activity. Reason: True but entailed by the specific accepted exonuclease and 5'-flap endonuclease activities. Supporting Evidence: PMID:10608837 exhibits both a robust 5' to 3' exonuclease activity on single- and double-stranded DNA substrates as well as a flap structure-specific endonuclease activity |
| GO:0004520 DNA endonuclease activity | IEA GO_REF:0000117 | TOO GENERAL | Summary: ARBA prediction of DNA endonuclease activity. Reason: EXO1 has a structure-specific 5'-flap endonuclease activity; GO:0017108 5'-flap endonuclease activity (kept elsewhere in this review) is_a DNA endonuclease activity, so this term adds nothing. EXO1 lacks endonuclease activity on bubbles, mismatches or uracil. Supporting Evidence: PMID:10608837 does not show specific endonuclease activity at 10-base pair bubble-like structures, G:T mismatches, or uracil residues |
| GO:0004523 RNA-DNA hybrid ribonuclease activity | TAS PMID:10364235 Human exonuclease 1 functionally complements its yeast homol... | KEEP AS NON CORE | Summary: Recombinant human EXO1 shows RNase H activity and complements yeast rad27 conditional lethality, suggesting a backup role to FEN1 in RNA primer removal. Reason: A genuine secondary activity reported biochemically; its physiological weight relative to RNase H2 and FEN1 is minor and it is a backup function, so non-core. Supporting Evidence: PMID:10364235 The purified recombinant enzyme not only displays 5'-3' double strand DNA exonuclease activity, but also shows an RNase H activity. |
| GO:0004527 exonuclease activity | TAS PMID:9788596 Human exonuclease I interacts with the mismatch repair prote... | MODIFY | Summary: TAS for exonuclease activity from the hExoI cloning paper. Reason: Correct but general. The specific, well-supported activity is 5'-3' DNA exonuclease activity, with double-stranded DNA as the preferred substrate. Proposed replacements: 5'-3' DNA exonuclease activity Supporting Evidence: PMID:9788596 Here, we report on a novel human exonuclease (hExoI) that is related to the yeast exonuclease 1. PMID:10608837 exhibits both a robust 5' to 3' exonuclease activity on single- and double-stranded DNA substrates |
| GO:0005515 protein binding | IPI PMID:10856833 Identification of factors interacting with hMSH2 in the feta... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MSH2. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MSH2. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:10856833 We demonstrate that hMSH2 interacts with a human 5'-3' exonuclease 1 (hEXO1/HEX1) and that this interaction is mediated through their C-terminal domains. |
| GO:0005515 protein binding | IPI PMID:11427529 The interaction of DNA mismatch repair proteins with human e... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MLH1, MSH2 and MSH3. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MLH1, MSH2 and MSH3. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:11427529 we demonstrate that hExoI binds strongly to hMLH1, and we describe interaction regions between hExoI and the MMR proteins hMSH2, hMSH3, and hMLH1 |
| GO:0005515 protein binding | IPI PMID:11427529 The interaction of DNA mismatch repair proteins with human e... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MLH1, MSH2 and MSH3. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MLH1, MSH2 and MSH3. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:11427529 we demonstrate that hExoI binds strongly to hMLH1, and we describe interaction regions between hExoI and the MMR proteins hMSH2, hMSH3, and hMLH1 |
| GO:0005515 protein binding | IPI PMID:11427529 The interaction of DNA mismatch repair proteins with human e... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MLH1, MSH2 and MSH3. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MLH1, MSH2 and MSH3. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:11427529 we demonstrate that hExoI binds strongly to hMLH1, and we describe interaction regions between hExoI and the MMR proteins hMSH2, hMSH3, and hMLH1 |
| GO:0005515 protein binding | IPI PMID:11429708 HNPCC mutations in the human DNA mismatch repair gene hMLH1 ... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MLH1. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MLH1. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:11429708 these mutant HNPCC-hMLH1 proteins are unable to form complexes with hEXO1 and hPMS2 in vivo |
| GO:0005515 protein binding | IPI PMID:11429708 HNPCC mutations in the human DNA mismatch repair gene hMLH1 ... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MLH1. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MLH1. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:11429708 these mutant HNPCC-hMLH1 proteins are unable to form complexes with hEXO1 and hPMS2 in vivo |
| GO:0005515 protein binding | IPI PMID:12414623 Functional alterations of human exonuclease 1 mutants identi... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MSH2. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MSH2. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:12414623 Three other mutants, P640S, G759E, and P770L, displayed a reduced capacity to interact with hMsh2. |
| GO:0005515 protein binding | IPI PMID:14676842 Characterization of human exonuclease 1 in complex with mism... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MLH1 and MSH2. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MLH1 and MSH2. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:14676842 both hMLH1-hPMS2 (MutLalpha) and hMLH1-hEXO1 complexes are formed in a reaction mixture containing all three proteins |
| GO:0005515 protein binding | IPI PMID:14676842 Characterization of human exonuclease 1 in complex with mism... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MLH1 and MSH2. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MLH1 and MSH2. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:14676842 both hMLH1-hPMS2 (MutLalpha) and hMLH1-hEXO1 complexes are formed in a reaction mixture containing all three proteins |
| GO:0005515 protein binding | IPI PMID:15225546 A defined human system that supports bidirectional mismatch-... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with PCNA. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with PCNA. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:15225546 EXOI interacts with PCNA. |
| GO:0005515 protein binding | IPI PMID:15886194 RECQ1 helicase interacts with human mismatch repair factors ... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with RECQ1. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with RECQ1. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:15886194 RECQ1 stimulates the incision activity of human exonuclease 1 |
| GO:0005515 protein binding | IPI PMID:21052091 DNA end resection by CtIP and exonuclease 1 prevents genomic... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with CtIP (RBBP8). Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with CtIP (RBBP8). The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:21052091 CtIP interacts with EXO1 and restrains its exonucleolytic activity in vitro |
| GO:0005515 protein binding | IPI PMID:2414623 [Pathophysiology of ulcer disease]. | REMOVE | Summary: Protein binding IPI (with MLH1, UniProtKB:P40692) keyed to PMID:2414623, which resolves to a 1985 German-language article on the pathophysiology of peptic ulcer disease. Reason: Bare protein binding is uninformative under the protein-binding policy, and the cited identifier is wrong: PMID:2414623 is not about EXO1 or MLH1. The EXO1-MLH1 interaction itself is real and documented in PMID:11427529 and PMID:11429708; the row is most likely a mistyped PMID (perhaps a dropped leading digit), but the intended paper cannot be determined with certainty. Supporting Evidence: PMID:11427529 we demonstrate that hExoI binds strongly to hMLH1, and we describe interaction regions between hExoI and the MMR proteins hMSH2, hMSH3, and hMLH1 |
| GO:0005515 protein binding | IPI PMID:26807646 EXD2 promotes homologous recombination by facilitating DNA e... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with CtIP (RBBP8). Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with CtIP (RBBP8). The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:26807646 cells have two alternate machineries, consisting of BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN that carry out long-range resection |
| GO:0005515 protein binding | IPI PMID:34552057 ZGRF1 promotes end resection of DNA homologous recombination... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with ZGRF1. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with ZGRF1. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:34552057 We demonstrate that ZGRF1 forms complexes with multiple HR repair proteins including EXO1 and BRCA1 |
| GO:0005515 protein binding | IPI PMID:9788596 Human exonuclease I interacts with the mismatch repair prote... | REMOVE | Summary: IPI evidence that EXO1 physically interacts with MSH2. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy; this does not dispute the reported interaction with MSH2. The functional consequences (EXO1 acting as the excision nuclease of mismatch repair downstream of MutSalpha/MutLalpha, and as a long-range resection nuclease in DSB repair) are captured by the nuclease activity and process annotations. Supporting Evidence: PMID:9788596 hExoI was found to interact strongly with the human MMR protein hMSH2 |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: IBA (PANTHER) nuclear localization for the EXO1 subfamily. Reason: EXO1 acts on nuclear DNA in mismatch repair and DSB resection; human EXO1 is nuclear by direct observation, and the IBA places this at the family level, consistent with the experimental rows. Supporting Evidence: file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005634 nucleus | IDA PMID:11429708 HNPCC mutations in the human DNA mismatch repair gene hMLH1 ... | ACCEPT | Summary: EXO1 forms complexes with MLH1 in vivo; UniProt cites this paper for nuclear localization. Reason: Nuclear localization is directly observed and is where all EXO1 functions act; defer to the curator on the full-text localization data. Supporting Evidence: file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005634 nucleus | IDA PMID:14676842 Characterization of human exonuclease 1 in complex with mism... | ACCEPT | Summary: GFP/immunolocalization shows EXO1 colocalizing with PCNA at nuclear replication sites. Reason: Direct evidence of nuclear localization, with the C-terminal region sufficient for targeting to replication foci. Supporting Evidence: PMID:14676842 We show that hEXO1 colocalizes with proliferating cell nuclear antigen (PCNA) at DNA replication sites and that the C-terminal region of hEXO1 is sufficient for this localization. |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location keyword mapping to nucleus. Reason: Consistent with the experimental localization on which the UniProt location statement rests. Supporting Evidence: file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Human Protein Atlas immunofluorescence localizes EXO1 to the nucleoplasm. Reason: Nucleoplasm is where EXO1 acts on DNA; consistent with nuclear foci colocalizing with PCNA. Supporting Evidence: file:human/EXO1/EXO1-uniprot.txt Note=Colocalizes with PCNA to discrete nuclear foci in S-phase. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5358597 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5358597 in the mismatch repair pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5358599 EXO1 exonucleolytically degrades the strand being repaired in a 5' to 3' direction file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5358599 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5358599 in the mismatch repair pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5358599 EXO1 exonucleolytically degrades the strand being repaired in a 5' to 3' direction file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684875 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5684875 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684882 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5684882 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5684887 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5684887 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685011 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5685011 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685156 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5685156 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685341 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5685341 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685838 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5685838 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685985 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5685985 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5685994 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5685994 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686410 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5686410 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686440 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5686440 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686469 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5686469 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686483 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5686483 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686642 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5686642 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686657 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5686657 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5686663 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5686663 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693539 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693539 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693542 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693542 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693561 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693561 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693564 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693564 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693580 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693580 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693584 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693584 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693589 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693589 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693593 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693593 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5693620 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-5693620 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-6799332 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-6799332 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9701199 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9701199 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704330 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9704330 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9704408 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9704408 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709571 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9709571 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9709601 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9709601 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9853389 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9853389 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980006 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9980006 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9980021 | ACCEPT | Summary: Reactome TAS placing EXO1 in the nucleoplasm, from reaction Reactome:R-HSA-9980021 in the homologous recombination / DSB resection pathway. Reason: Reactome places the EXO1 participant of its DNA repair reactions in the nucleoplasm, which matches the experimentally observed nuclear localization. Many of these downstream HR reactions (D-loop, Holliday junction resolution, ATR/CHEK1 activation) list EXO1-resected DNA as a participant rather than EXO1 acting in them, but the location claim itself is sound. Supporting Evidence: Reactome:R-HSA-5685994 DNA nucleases EXO1 and DNA2 function redundantly in yeast (Zhu et al. 2008) and humans (Nimonkar et al. 2011) in long-range resection of DNA double-strand breaks (DSBs). file:human/EXO1/EXO1-uniprot.txt SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11429708, ECO:0000269|PubMed:14676842, ECO:0000269|PubMed:17426132}. |
| GO:0006281 DNA repair | TAS PMID:10364235 Human exonuclease 1 functionally complements its yeast homol... | MODIFY | Summary: TAS for DNA repair from the yeast complementation study (UV resistance, mutation avoidance). Reason: Correct but general. EXO1 has two well-supported specific repair roles, both asserted elsewhere in this review - the excision nuclease of mismatch repair and the long-range resection nuclease of homologous-recombination DSB repair. Proposed replacements: mismatch repair double-strand break repair via homologous recombination Supporting Evidence: PMID:10364235 we show that the enzyme functionally complements Saccharomyces cerevisiae Exo1 in recombination of direct repeat DNA fragments, UV resistance, and mutation avoidance by in vivo assays PMID:11809771 Human exonuclease I is required for 5' and 3' mismatch repair. |
| GO:0006298 mismatch repair | IBA GO_REF:0000033 | ACCEPT | Summary: IBA mismatch repair for the EXO1 subfamily. Reason: Mismatch repair is a conserved core role of EXO1 (yeast, mouse, human), with human biochemical reconstitution showing EXO1 as the excision nuclease. Supporting Evidence: PMID:15225546 While MutSalpha, EXOI, and RPA are sufficient to support hydrolysis directed by a 5' strand break, 3' directed excision also requires MutLalpha, PCNA, and RFC. |
| GO:0006298 mismatch repair | IDA PMID:14636568 Mechanism of 5'-directed excision in human mismatch repair. | ACCEPT | Summary: Purified system showing MutSalpha-activated, mismatch-dependent 5'->3' excision by EXOI that terminates after mispair removal. Reason: Direct biochemical demonstration of EXO1 performing the excision step of MMR. Supporting Evidence: PMID:14636568 In the presence of RPA, ATP, and a mismatch, MutSalpha activates 5'-->3' excision by EXOI, and excision terminates after removal of the mispair. |
| GO:0006298 mismatch repair | IMP PMID:11809771 Human exonuclease I is required for 5' and 3' mismatch repai... | ACCEPT | Summary: EXOI co-purifies with and restores mismatch-provoked excision in depleted nuclear extracts, directed from either 5' or 3' nicks. Reason: Core function; EXO1 is required for and catalyses MMR excision. Supporting Evidence: PMID:11809771 Human EXOI co-purifies with the excision activity, and the purified activity can be replaced by near homogeneous recombinant hEXOI. |
| GO:0006298 mismatch repair | IPI PMID:9788596 Human exonuclease I interacts with the mismatch repair prote... | ACCEPT | Summary: Physical interaction of hExoI with MSH2, used to infer a role in MMR. Reason: The interaction alone only suggests involvement, but the process claim is independently established by reconstitution studies (PMID:11809771, PMID:14636568, PMID:15225546); accepted as consistent with the other MMR rows. Supporting Evidence: PMID:9788596 hExoI was found to interact strongly with the human MMR protein hMSH2, suggesting its involvement in the MMR process and/or DNA recombination. PMID:14636568 MutSalpha activates 5'-->3' excision by EXOI |
| GO:0006298 mismatch repair | ISS PMID:9685493 Hex1: a new human Rad2 nuclease family member with homology ... | ACCEPT | Summary: ISS from yeast/S. pombe Exo1 in the HEX1 cloning paper. Reason: The sequence-based inference has since been confirmed experimentally for the human protein. Supporting Evidence: PMID:9685493 Hex1 presumably functions as a nuclease in aspects of recombination or mismatch repair PMID:11809771 Human exonuclease I is required for 5' and 3' mismatch repair. |
| GO:0006298 mismatch repair | TAS PMID:9685493 Hex1: a new human Rad2 nuclease family member with homology ... | ACCEPT | Summary: TAS from the HEX1 cloning paper. Reason: Consistent with experimental MMR reconstitution data. Supporting Evidence: PMID:9685493 Hex1 presumably functions as a nuclease in aspects of recombination or mismatch repair PMID:15225546 Mismatch-provoked excision directed by a strand break located 3' or 5' to the mispair has been reconstituted using purified human proteins. |
| GO:0006298 mismatch repair | TAS Reactome:R-HSA-5358565 | ACCEPT | Summary: Reactome MutSalpha-directed MMR pathway, in which EXO1 is the excision nuclease. Reason: Core function, consistent with the reconstitution literature. Supporting Evidence: Reactome:R-HSA-5358599 EXO1 exonucleolytically degrades the strand being repaired in a 5' to 3' direction |
| GO:0006310 DNA recombination | IBA GO_REF:0000033 | MODIFY | Summary: IBA DNA recombination for the EXO1 subfamily. Reason: Correct but general. The recombination role of human EXO1 is resection of DSB ends to produce 3' ssDNA for homologous recombination, shown by reconstitution with BLM, MRN and RPA. Refine to double-strand break repair via homologous recombination; the step EXO1 performs (DSB end processing) is added as a NEW row. Propagation Review Root cause: NO FAILURE CORE Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN008960732 SUPPORTS TRANSFER EXO1-clade node carrying the DNA recombination IBD; human EXO1 sits inside the clade and retains the resection activity. The term is sound but general; refined to HR-mediated DSB repair. Proposed replacements: double-strand break repair via homologous recombination Supporting Evidence: PMID:21325134 In the other, EXO1 resects the DNA and is stimulated by BLM, MRN, and RPA. |
| GO:0006310 DNA recombination | IEA GO_REF:0000117 | MODIFY | Summary: ARBA prediction of DNA recombination. Reason: Same claim as the IBA row; refined to HR-mediated DSB repair, in which EXO1 performs long-range end resection. Proposed replacements: double-strand break repair via homologous recombination Supporting Evidence: PMID:21325134 Our results establish two of the core machineries that initiate recombinational DNA repair in human cells. |
| GO:0006310 DNA recombination | IGI PMID:10364235 Human exonuclease 1 functionally complements its yeast homol... | MODIFY | Summary: Human EXO1 complements yeast exo1 in direct-repeat recombination. Reason: The complementation supports a recombination role; the human-specific mechanism is DSB end resection for homologous recombination, so refine to GO:0000724. Proposed replacements: double-strand break repair via homologous recombination Supporting Evidence: PMID:10364235 we show that the enzyme functionally complements Saccharomyces cerevisiae Exo1 in recombination of direct repeat DNA fragments PMID:21325134 EXO1 resects the DNA and is stimulated by BLM, MRN, and RPA |
| GO:0006310 DNA recombination | TAS PMID:10364235 Human exonuclease 1 functionally complements its yeast homol... | MODIFY | Summary: TAS DNA recombination from the yeast complementation paper. Reason: Refined consistently with the other DNA recombination rows. Proposed replacements: double-strand break repair via homologous recombination Supporting Evidence: PMID:10364235 Yeast exonuclease 1 (Exo1) is induced during meiosis and plays an important role in DNA homologous recombination and mismatch correction pathways. |
| GO:0008409 5'-3' exonuclease activity | ISS PMID:9685493 Hex1: a new human Rad2 nuclease family member with homology ... | MODIFY | Summary: ISS 5'-3' exonuclease activity from yeast Exo1. Reason: Correct but general; the activity is on DNA, so refine to 5'-3' DNA exonuclease activity, which the gene carries by IDA and IBA. Proposed replacements: 5'-3' DNA exonuclease activity Supporting Evidence: PMID:9685493 Similar to the yeast proteins, recombinant Hex1 exhibits a 5'-->3' exonuclease activity. |
| GO:0008409 5'-3' exonuclease activity | TAS PMID:10364235 Human exonuclease 1 functionally complements its yeast homol... | MODIFY | Summary: TAS 5'-3' exonuclease activity. Reason: Refine to the DNA-specific child term, consistent with other rows. Proposed replacements: 5'-3' DNA exonuclease activity Supporting Evidence: PMID:10364235 The purified recombinant enzyme not only displays 5'-3' double strand DNA exonuclease activity |
| GO:0008409 5'-3' exonuclease activity | TAS Reactome:R-HSA-5358599 | MODIFY | Summary: Reactome TAS for 5'-3' exonuclease activity in MMR excision. Reason: Refine to 5'-3' DNA exonuclease activity, consistent with other rows. Proposed replacements: 5'-3' DNA exonuclease activity Supporting Evidence: Reactome:R-HSA-5358599 EXO1 exonucleolytically degrades the strand being repaired in a 5' to 3' direction |
| GO:0016604 nuclear body | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human Protein Atlas immunofluorescence places EXO1 in nuclear bodies. Reason: EXO1 forms discrete nuclear foci (with PCNA at replication sites, and at DSBs); an antibody-based nuclear-body call is plausible but not tied to a defined body or function. Supporting Evidence: file:human/EXO1/EXO1-uniprot.txt Note=Colocalizes with PCNA to discrete nuclear foci in S-phase. |
| GO:0016788 hydrolase activity, acting on ester bonds | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO mapping to hydrolase activity, acting on ester bonds. Reason: True but entailed by the accepted 5'-3' DNA exonuclease activity. Supporting Evidence: PMID:10608837 exhibits both a robust 5' to 3' exonuclease activity on single- and double-stranded DNA substrates |
| GO:0017108 5'-flap endonuclease activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA 5'-flap endonuclease activity (XPG/RAD2 family, PTN000118612). Reason: Human EXO1 cleaves 5' flaps with FEN1-like efficiency and incision site, so the IBA is sound; however its physiological roles (MMR excision, DSB resection) use the exonuclease, and flap cleavage is at most a backup to FEN1. Supporting Evidence: PMID:10608837 The flap endonuclease activity of HEX1-N2 is similar to that of human flap endonuclease-1, both in terms of turnover efficiency (k(cat)) and site of incision |
| GO:0035312 5'-3' DNA exonuclease activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA 5'-3' DNA exonuclease activity for the EXO1 subfamily. Reason: Core catalytic activity, conserved and directly demonstrated for human EXO1. Supporting Evidence: PMID:10608837 exhibits both a robust 5' to 3' exonuclease activity on single- and double-stranded DNA substrates |
| GO:0035312 5'-3' DNA exonuclease activity | IDA PMID:10608837 The RAD2 domain of human exonuclease 1 exhibits 5' to 3' exo... | ACCEPT | Summary: The RAD2 domain of human EXO1 has robust Mg2+-dependent 5'->3' exonuclease activity. Reason: Direct assay of the core activity. Supporting Evidence: PMID:10608837 Both the 5' to 3' exonuclease and flap endonuclease activities require a divalent metal cofactor, with Mg(2+) being the preferred metal ion. |
| GO:0035312 5'-3' DNA exonuclease activity | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro2GO mapping to 5'-3' DNA exonuclease activity. Reason: Correct core activity, matching experimental data. Supporting Evidence: PMID:10608837 exhibits both a robust 5' to 3' exonuclease activity on single- and double-stranded DNA substrates |
| GO:0045145 single-stranded DNA 5'-3' DNA exonuclease activity | IDA PMID:10608837 The RAD2 domain of human exonuclease 1 exhibits 5' to 3' exo... | KEEP AS NON CORE | Summary: EXO1 degrades single-stranded DNA 5'->3', at lower specific activity than blunt or 5'-recessed duplexes. Reason: Real measured activity, but duplex DNA is the preferred substrate and the biological roles (MMR excision, DSB resection) act on duplex DNA; the ssDNA activity is secondary. Supporting Evidence: PMID:10608837 The specific activity of its 5' to 3' exonuclease function is 2.5-7-fold higher on blunt end and 5'-recessed double-stranded DNA substrates compared with duplex 5'-overhang or single-stranded DNAs. |
| GO:0046872 metal ion binding | IEA GO_REF:0000002 | MODIFY | Summary: InterPro2GO mapping to metal ion binding. Reason: Correct but general. Nuclease activity requires divalent metal with Mg2+ preferred, and UniProt (by similarity) notes two Mg2+ ions per subunit; refine to magnesium ion binding. Proposed replacements: magnesium ion binding Supporting Evidence: PMID:10608837 require a divalent metal cofactor, with Mg(2+) being the preferred metal ion |
| GO:0048256 flap endonuclease activity | IDA PMID:10608837 The RAD2 domain of human exonuclease 1 exhibits 5' to 3' exo... | MODIFY | Summary: The RAD2 domain of EXO1 has flap structure-specific endonuclease activity comparable to FEN1. Reason: The flap substrate cleaved is a 5' flap (FEN1-like incision site), so refine to 5'-flap endonuclease activity (GO:0017108, a child of this term, already on the gene by IBA). Non-core relative to the exonuclease. Proposed replacements: 5'-flap endonuclease activity Supporting Evidence: PMID:10608837 The flap endonuclease activity of HEX1-N2 is similar to that of human flap endonuclease-1, both in terms of turnover efficiency (k(cat)) and site of incision |
| GO:0048256 flap endonuclease activity | IDA PMID:11842105 Molecular interactions of human Exo1 with DNA. | MODIFY | Summary: Mutagenesis and footprinting of EXO1 on flap DNA substrates. Reason: Refine to 5'-flap endonuclease activity, consistent with PMID:10608837 and UniProt's description of 5'-overhanging flap cleavage. Proposed replacements: 5'-flap endonuclease activity Supporting Evidence: PMID:11842105 Exo1 binds predominantly along the minor groove of flap DNA, downstream of the junction. file:human/EXO1/EXO1-uniprot.txt Also exhibits endonuclease activity against 5'-overhanging flap structures |
| GO:0051908 double-stranded DNA 5'-3' DNA exonuclease activity | IDA PMID:10608837 The RAD2 domain of human exonuclease 1 exhibits 5' to 3' exo... | ACCEPT | Summary: EXO1 5'->3' exonuclease is most active on blunt and 5'-recessed duplex DNA. Reason: Core catalytic activity at the right specificity; duplex DNA is the preferred substrate and the substrate in MMR excision and DSB resection. Supporting Evidence: PMID:10608837 The specific activity of its 5' to 3' exonuclease function is 2.5-7-fold higher on blunt end and 5'-recessed double-stranded DNA substrates |
| GO:0051908 double-stranded DNA 5'-3' DNA exonuclease activity | IDA PMID:11842105 Molecular interactions of human Exo1 with DNA. | ACCEPT | Summary: Catalytic residues D78, D173 and D225 required for EXO1 nuclease function on DNA substrates. Reason: Supports the core duplex DNA exonuclease activity and its catalytic site. Supporting Evidence: PMID:11842105 Site-specific mutagenesis studies demonstrate that amino acids D78, D173 and D225 are critical for Exo1 nuclease function. |
| GO:0090656 t-circle formation | TAS PMID:27918544 A balance between elongation and trimming regulates telomere... | REMOVE | Summary: TAS t-circle formation citing a study of telomere trimming in human stem cells. Reason: The full text attributes T-circle formation to NBS1 and C-rich overhangs to XRCC3; EXO1 depletion had no effect on C-circles, and the "Exo1" used as a 3'-5' ssDNA reagent is E. coli exonuclease I, not human EXO1. Nothing in the paper supports EXO1 in t-circle formation. Supporting Evidence: PMID:27918544 We demonstrate that XRCC3 and Nbs1 mediate telomere attrition by catalyzing the formation of T-circles and C-rich overhangs. PMID:27918544 Cells depleted of TRF1, BLM, WRN or Exo1, exhibited similar amounts of C-circles as control cells. |
| GO:0110025 DNA strand resection involved in replication fork processing | IMP PMID:26240375 ATM-dependent phosphorylation of MRE11 controls extent of re... | MODIFY | Summary: Loss of ATM-dependent EXO1 phosphorylation (non-phosphorylatable MRE11) causes over-extended resection by EXO1 at IR-induced DSBs in G2 cells. Reason: The paper measures resection at ionizing-radiation-induced double-strand breaks during homology-directed repair, not resection at stalled or reversed replication forks; the IMP supports EXO1 performing DSB end resection. Refine to DNA double-strand break processing. Proposed replacements: DNA double-strand break processing Supporting Evidence: PMID:26240375 If MRE11 is not phosphorylatable (MRE11S676AS678A) ATM is still normally autophosphorylated (ATMP) leading to induction of end processing, but in the absence of MRE11 phosphorylation there is no subsequent ATM-dependent phosphorylation of Exonuclease 1 (EXO1) leading to over extended resection by EXO1. |
| GO:0000729 DNA double-strand break processing | IDA PMID:21325134 BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end... | NEW | Summary: EXO1 resects double-strand break ends 5'->3' to produce the 3' single-stranded tails used in homologous recombination; in a reconstituted human system EXO1 is one of two long-range resection nucleases, stimulated by BLM, MRN and RPA. ATM-dependent EXO1 phosphorylation limits the extent of this resection in cells. Reason: EXO1 performs the catalytic step itself (participation test passed); the replication-fork resection IMP row is refined to this term, and DNA2 and MRE11, the other resection nucleases, are the comparators carrying DSB processing. DSB end resection is a core function of EXO1 that is otherwise represented only through general DNA recombination rows. Supporting Evidence: PMID:21325134 Repair of dsDNA breaks requires processing to produce 3'-terminated ssDNA. PMID:21325134 In the other, EXO1 resects the DNA and is stimulated by BLM, MRN, and RPA. PMID:21052091 the localization of EXO1 to DSBs depends on both CtIP and MRN |
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Download this section (compressed HTML)Q: Is the "cryptic" 3'->5' excision activity attributed to EXO1 in PCNA/RFC-dependent 3'-nick-directed mismatch repair intrinsic to EXO1, or does EXO1 play a structural role while another nuclease (e.g. MutLalpha endonuclease) supplies the 3' incision?
Q: Should the EXO1 IPI row keyed to PMID:2414623 (an unrelated 1985 ulcer-disease article) be repointed to the paper actually reporting the EXO1-MLH1 interaction?
Experiment: Compare MMR excision directed by a 3' nick in extracts complemented with wild-type versus nuclease-dead (D173A) EXO1 in the presence of PCNA, RFC and MutLalpha, to separate a catalytic from a structural EXO1 role in 3'-directed repair.
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