AGO1 encodes a human Argonaute protein that binds small-RNA guides, loads miRNA duplexes and promotes their maturation into active RNA-induced silencing complexes. Its PAZ, MID and PIWI-containing architecture holds the guide and recognizes complementary target RNAs. Wild-type AGO1 lacks efficient target-RNA slicing activity but recruits TNRC6/GW182-associated effectors to repress translation and promote mRNA decay. It acts principally in the cytoplasm, including P-bodies and other ribonucleoprotein assemblies, and also has a nuclear pool associated with transcriptional regulation. A C-terminally extended readthrough proteoform, AGO1x, has been reported with distinct miRNA-inhibitory and nuclear dsRNA-regulatory properties; endogenous abundance and reporter-based readthrough estimates remain experimentally disputed.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: AGO1 has a nuclear pool associated with transcriptional regulation. Reason: The cached PAINT IBD at PTN001875625 supports inherited nuclear localization; independent human AGO1 promoter ChIP and nuclear transcription-complex association corroborate a nuclear pool. This compartment is retained as a contextual location alongside the principal cytoplasmic miRISC role. Canonical AGO1 evidence here does not depend on AGO1x. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN001875625 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN001875625. Its descendant experiments ground the ancestral assertion rather than a pairwise transfer. Independent human AGO1 promoter recruitment corroborates nuclear localization; this node is not claimed to have AGO1 itself among its experimental seeds. Supporting Evidence: PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site PMID:25336585 Through co-immunoprecipitation assay, we found that both Ago1 and Ago2 bound to Pol II (Fig. 1E) and TBP (Fig. 1F) in HEK293T cells. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: AGO1 operates in cytoplasmic RNA-silencing complexes. Reason: The PAINT IBD at PTN000527275 is corroborated by human AGO1 cytoplasmic ribonucleoprotein complexes. Cytoplasm is valid at the source resolution and need not be replaced with one particular granule or subcompartment. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000527275 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN000527275. Human AGO1 evidence corroborates the inherited function/location. Extant descendants are grounding for the ancestral assertion, not pairwise transfers; AGO1 among the seeds is legitimate experimental support. Supporting Evidence: PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0035194 regulatory ncRNA-mediated post-transcriptional gene silencing | IBA GO_REF:0000033 | ACCEPT | Summary: AGO1 is a small-RNA-guided post-transcriptional silencing effector. Reason: The PTN001113179 PAINT assertion agrees with direct human guide loading, translational repression and recruitment of TNRC6-dependent decay. AGO1 performs target recognition and effector recruitment despite lacking target-slicing activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001113179 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN001113179. Human AGO1 evidence corroborates the inherited function/location. Extant descendants are grounding for the ancestral assertion, not pairwise transfers; AGO1 among the seeds is legitimate experimental support. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). PMID:19383768 Our findings indicate that TNRC6A, TNRC6B, and TNRC6C are recruited to miRNA targets through an interaction between their N-terminal domain and an Argonaute protein; the TNRC6s then promote translational repression and/or degradation of miRNA targets through a C-terminal silencing domain. |
| GO:0016442 RISC complex | IBA GO_REF:0000033 | ACCEPT | Summary: AGO1 is a core protein component of RISC. Reason: PAINT PTN001113179 places inherited RISC membership on the animal Argonaute lineage. Membership is independently supported by human AGO1-small-RNA complexes; RISC membership does not require each Argonaute to be an endonuclease. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001113179 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN001113179. Human AGO1 evidence corroborates the inherited function/location. Extant descendants are grounding for the ancestral assertion, not pairwise transfers; AGO1 among the seeds is legitimate experimental support. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0036464 cytoplasmic ribonucleoprotein granule | IBA GO_REF:0000033 | ACCEPT | Summary: AGO1 localizes to cytoplasmic RNP granules including P-bodies. Reason: PAINT PTN001113179 carries the cytoplasmic RNP-granule IBD. Human AGO1 colocalization with TNRC6A/DDX6 in P-bodies is independently described in PMID:28683311. Granule localization is retained without claiming visible P-bodies are required for silencing. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001113179 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN001113179. Human AGO1 evidence corroborates the inherited function/location. Extant descendants are grounding for the ancestral assertion, not pairwise transfers; AGO1 among the seeds is legitimate experimental support. Supporting Evidence: PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0031054 pre-miRNA processing | IBA GO_REF:0000033 | ACCEPT | Summary: AGO1 contributes to late miRNA maturation through guide-duplex loading and unwinding. Reason: The cached PTHR22891 PAINT table places this IBD at PTN000527278 and includes human AGO1 experimental support among its descendants. There is no AGO1-specific loss of guide-duplex maturation that would invalidate that placement. GO:0031054 encompasses conversion to a mature miRNA, rather than requiring the annotated protein itself to cleave the precursor hairpin. AGO1 directly holds and resolves the duplex into a functional guide-loaded complex; Dicer performs the precursor cleavage. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000527278 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN000527278. Human AGO1 evidence corroborates the inherited function/location. Extant descendants are grounding for the ancestral assertion, not pairwise transfers; AGO1 among the seeds is legitimate experimental support. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0035198 miRNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: AGO1 binds miRNA guides in silencing complexes. Reason: The PTN001113179 PAINT IBD is directly corroborated in human AGO1. miRNA binding is a central molecular activity and is distinct from whether the protein can catalyse target cleavage. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001113179 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN001113179. Human AGO1 evidence corroborates the inherited function/location. Extant descendants are grounding for the ancestral assertion, not pairwise transfers; AGO1 among the seeds is legitimate experimental support. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). |
| GO:0003727 single-stranded RNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: AGO1 binds single-stranded guide RNA. Reason: The ssRNA-binding IBD at PTN000527276 is corroborated by AGO1 structural and RISC-maturation experiments; its broad RNA scope is not an over-propagation. The substrate-class term correctly covers guide RNA beyond a single miRNA sequence; it does not imply indiscriminate binding to every single-stranded RNA. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000527276 SUPPORTS TRANSFER The cached PTHR22891 PAINT table contains this term-specific IBD at PTN000527276. Human AGO1 evidence corroborates the inherited function/location. Extant descendants are grounding for the ancestral assertion, not pairwise transfers; AGO1 among the seeds is legitimate experimental support. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. |
| GO:0000932 P-body | IEA GO_REF:0000120 | ACCEPT | Summary: AGO1 localizes to cytoplasmic RNP granules including P-bodies. Reason: The combined mapping cites mouse Ago1 and UniProt subcellular-location SL-0230; the exact mouse imaging assay was not separately reconstructed. Human AGO1 colocalization with TNRC6A/DDX6 in P-bodies is independently described in PMID:28683311. Granule localization is retained without claiming visible P-bodies are required for silencing. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB-SubCell:SL-0230 SUPPORTS TRANSFER UniProt P-body location mapping is corroborated by human AGO1/TNRC6A/DDX6 colocalization in PMID:28683311. UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. Supporting Evidence: PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | ACCEPT | Summary: AGO1 binds nucleic acid through its conserved RNA-binding architecture. Reason: The InterPro IPR003165/IPR036397 mapping is broad but accurate for an Argonaute with direct RNA-bound structural evidence. The domain-to-GO rule is not interpreted as a claim of endonuclease activity, or of DNA-binding specificity. More specific RNA-binding annotations coexist without invalidating this broad mapping. Propagation Review Root cause: UNRESOLVED Sources checked: InterPro:IPR003165 UNRESOLVED This domain-to-GO source was identified from WITH/FROM. Direct human AGO1 RNA-bound structure independently supports the broad binding assignment; current mapping internals were not inspected. InterPro:IPR036397 UNRESOLVED This domain-to-GO source was identified from WITH/FROM. Direct human AGO1 RNA-bound structure independently supports the broad binding assignment; current mapping internals were not inspected. Supporting Evidence: PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. |
| GO:0003723 RNA binding | IEA GO_REF:0000120 | ACCEPT | Summary: AGO1 binds RNA as the guide-bearing effector of RISC. Reason: The combined source cites mouse Ago1 and PAZ-domain InterPro IPR003100. Those independent source branches were identified, but the mouse primary assay and exact current mapping predicates were not reconstructed. RNA binding is biologically correct at this source resolution; guide and target binding are not exhausted by the narrower miRNA-binding annotation. Propagation Review Root cause: UNRESOLVED Sources checked: InterPro:IPR003100 UNRESOLVED This domain-to-GO source was identified from WITH/FROM. Direct human AGO1 RNA-bound structure independently supports the broad binding assignment; current mapping internals were not inspected. UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. Supporting Evidence: PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. |
| GO:0003725 double-stranded RNA binding | IEA GO_REF:0000117 | ACCEPT | Summary: AGO1 binds small-RNA duplexes during RISC loading. Reason: ARBA00028403 is the rule source; its internals were not inspected, so the biological judgment rests on direct human experiments. Duplex recognition is an experimentally established stage of AGO1 function, not an unsupported inference from mature single-stranded miRNA binding. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00028403 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0003727 single-stranded RNA binding | IEA GO_REF:0000117 | ACCEPT | Summary: AGO1 binds single-stranded guide RNA. Reason: ARBA00089173 predicts ssRNA binding. Its predicates remain uninspected, but AGO1 guide-binding structures and strand-resolved RISC assays provide independent support. The substrate-class term correctly covers guide RNA beyond a single miRNA sequence; it does not imply indiscriminate binding to every single-stranded RNA. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00089173 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. |
| GO:0031054 pre-miRNA processing | IEA GO_REF:0000117 | ACCEPT | Summary: AGO1 contributes to late miRNA maturation through guide-duplex loading and unwinding. Reason: The ARBA00027506 rule predicates were not available for independent assessment; the biological annotation is independently supported by human AGO1 loading and passenger-strand release assays. GO:0031054 encompasses conversion to a mature miRNA, rather than requiring the annotated protein itself to cleave the precursor hairpin. AGO1 directly holds and resolves the duplex into a functional guide-loaded complex; Dicer performs the precursor cleavage. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00027506 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0035278 miRNA-mediated gene silencing by inhibition of translation | IEA GO_REF:0000117 | ACCEPT | Summary: AGO1 mediates miRNA-guided translational repression. Reason: ARBA00091152 predicts a function independently supported by human AGO1 repression assays and TNRC6 recruitment. Rule predicates were not examined; acceptance concerns the well-supported biological activity. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00091152 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. Supporting Evidence: PMID:19383768 Our findings indicate that TNRC6A, TNRC6B, and TNRC6C are recruited to miRNA targets through an interaction between their N-terminal domain and an Argonaute protein; the TNRC6s then promote translational repression and/or degradation of miRNA targets through a C-terminal silencing domain. PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). |
| GO:0036464 cytoplasmic ribonucleoprotein granule | IEA GO_REF:0000117 | ACCEPT | Summary: AGO1 localizes to cytoplasmic RNP granules including P-bodies. Reason: ARBA00026950 supplies the automated granule mapping; its full predicates were not inspected. Human AGO1 colocalization with TNRC6A/DDX6 in P-bodies is independently described in PMID:28683311. Granule localization is retained without claiming visible P-bodies are required for silencing. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00026950 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. Supporting Evidence: PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0070578 RISC-loading complex | IEA GO_REF:0000117 | UNDECIDED | Summary: AGO1 participates in RISC loading, while membership in the specifically defined RLC remains unresolved. Reason: ARBA00085164 predicts RISC-loading-complex membership, but its premises were not recovered. The current GO:0070578 definition specifies a DICER1βTARBP2βAGO2 trimer with precursor-processing activity. This is not equivalent to every duplex-bound Ago1 pre-RISC. Direct AGO1βDicer interactions are real, but the assessed evidence does not establish the exact trimeric AGO1 complex. Retain uncertainty rather than deny loading or assume an obligatory composition. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00085164 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. Supporting Evidence: PMID:19966796 the previously designated βhuman RLCβ composed of Ago2, Dicer, and TRBP does not correspond to a canonical RISC-loading complex PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:12526743 Immunoprecipitation experiments suggest that, in human and mouse cells, complex formation occurs between Dicer and eIF2C1 or 2 |
| GO:0070922 RISC complex assembly | IEA GO_REF:0000117 | ACCEPT | Summary: AGO1 directly contributes to RISC assembly. Reason: ARBA00086266 is supported independently by human Ago1 loading/maturation experiments; its rule internals were not inspected. AGO1 supplies the guide-binding scaffold and promotes passenger-strand release, so it performs a step of assembly rather than merely being required downstream. ATP dependence of cell-extract loading does not assign ATPase activity to AGO1. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00086266 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0005515 protein binding | IPI PMID:12526743 Short-interfering-RNA-mediated gene silencing in mammalian c... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in DICER1 association. Reason: The source abstract explicitly identifies eIF2C1βDicer complex formation in human/mouse cells. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:12526743 Immunoprecipitation experiments suggest that, in human and mouse cells, complex formation occurs between Dicer and eIF2C1 or 2 |
| GO:0005515 protein binding | IPI PMID:16756390 Translation repression in human cells by microRNA-induced ge... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in AGO2/RISC association. Reason: The GOA partner is AGO2 Q9UKV8; the paper studies RCK/p54-associated active RISC and AGO interactions. Its experiments must not be relabeled as an AGO1 catalytic or chaperone function. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:16756390 RCK/p54, a DEAD box helicase, interacts with argonaute proteins, Ago1 and Ago2 |
| GO:0005515 protein binding | IPI PMID:17891150 A conserved motif in Argonaute-interacting proteins mediates... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in TNRC6B isoform association. Reason: The GOA partner is Q9UPQ9-2. The source examines conserved GW-rich Ago-hook/PIWI interaction with yeast and mammalian experiments; the abstract does not independently resolve this exact human pair. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:17891150 binds Ago proteins through their PIWI domains in vitro and in vivo |
| GO:0005515 protein binding | IPI PMID:17932509 Proteomic and functional analysis of Argonaute-containing mR... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in AGO1 mRNP protein associations. Reason: The human Ago1/Ago2 proteomic study maps multiple partners and tests RNA dependence. Co-complex and RNA-bridged associations do not by themselves specify a new AGO1 molecular function. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:17932509 By using co-immunoprecipitation experiments followed by RNase treatment, we biochemically mapped interactions within Ago mRNPs. |
| GO:0005515 protein binding | IPI PMID:18482256 Protein microarray analysis identifies human cellular prion ... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in prion-protein association. Reason: The row maps PRNP P04156 from a recombinant human PrP protein-array screen. The cached abstract identifies the screen but not the AGO1 spot/validation; no RISC-cofactor mechanism is inferred from that dataset. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:18482256 We identified 47 novel PrPIPs by probing an array of 5000 human proteins with recombinant human PrPC |
| GO:0005515 protein binding | IPI PMID:19167051 Importin 8 is a gene silencing factor that targets argonaute... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in importin-8 association. Reason: The original paper supports an importinβAgo association; its highlighted nuclear-localization and mRNA-recruitment tests concern Ago2. AGO1 is a cargo/interaction partner here, not thereby a nuclear import receptor. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:19167051 We show that Imp8 interacts with Ago proteins and localizes to cytoplasmic processing bodies |
| GO:0005515 protein binding | IPI PMID:19324964 The C-terminal half of human Ago2 binds to multiple GW-rich ... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in TNRC6A association. Reason: Despite its Ago2-focused title, the source explicitly assays GW182 interaction across all four human Ago proteins. This supports the actual interaction but not a more specific unrepresented activity from this IPI row alone. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:19324964 the interaction with GW182 was observed in all four human Ago proteins. |
| GO:0005515 protein binding | IPI PMID:19383768 The C-terminal domains of human TNRC6A, TNRC6B, and TNRC6C s... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in TNRC6A/B/C associations. Reason: The source explicitly reports interactions of all four human Argonautes with TNRC6 N-terminal regions. TNRC6 silencing-domain effector activity must not be assigned to AGO1 itself. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:19383768 the N-terminal GW-repeat-containing regions of all three TNRC6s interact with the four human Argonaute proteins |
| GO:0005515 protein binding | IPI PMID:19716330 Mammalian miRNA RISC recruits CAF1 and PABP to affect PABP-d... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in GW182/Dicer-associated miRISC. Reason: The full source includes tagged human Ago1 purification and CAF1/PABP association, while most extract deadenylase activity tests use mouse Krebs extract and Ago2. The row does not establish AGO1 deadenylase catalysis. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:19716330 PABP was identified in both Ago1 and Ago2 immunopurifications |
| GO:0005515 protein binding | IPI PMID:22484317 Human prion protein binds Argonaute and promotes accumulatio... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in PRNP/TNRC6A-associated miRISC. Reason: The source supports GW/WG-dependent prion-protein association and stabilization of AGO/TNRC6 effector complexes. These interactions do not turn AGO1 into a prion-processing enzyme. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:22484317 the octarepeat domain of human PrP(C) contains GW/WG motifs that bind Argonaute (AGO) proteins |
| GO:0005515 protein binding | IPI PMID:25036637 A quantitative chaperone interaction network reveals the arc... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in HSP90AB1 association. Reason: This chaperone network maps AGO1 with HSP90AB1 P08238. The partial local extraction supports the study design but not an independently rechecked pair record. Client association does not establish AGO1 chaperone activity. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:25036637 systematically characterize the chaperone-cochaperone-client interaction network in human cells. |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in PPP5C association. Reason: This phosphatase interaction screen maps partner P53041. The cached abstract does not provide the AGO1 pair-level result or an AGO1 catalytic role. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:28330616 quantitative affinity proteomics to assay protein-protein interactions for 54 phosphatases |
| GO:0005515 protein binding | IPI PMID:28683311 Argonaute Utilization for miRNA Silencing Is Determined by P... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in LIMD1 association. Reason: The full source tests AGO1 and AGO4 interactions as well as AGO2, including phosphorylation-dependent interaction experiments in supplementary figures. LIMD1 supplies the bridging adaptor activity; the association does not establish an independent AGO1 adaptor mechanism beyond the existing RNA-silencing functions. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:28683311 association with AGO1 and 4 is also dependent on the ability of this conserved serine residue to be phosphorylated |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in BioPlex interaction mapping. Reason: BioPlex records partners HSP90AB1, TNRC6A, AGO2 and DICER1 for this grouped row. The local extraction is partial and the exact pair records were not reanalysed; retain the underlying interaction assertions without treating AP-MS as a defined AGO1 activity. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:33961781 Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in OpenCell interaction mapping. Reason: The endogenous-tagging dataset maps TNRC6A, TNRC6C and AGO2 partners. Its partial cache does not expose all AGO1-specific measurements, so no additional specific activity is inferred. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:35271311 We combined genome engineering, confocal live-cell imaging, mass spectrometry, and data science |
| GO:0005515 protein binding | IPI PMID:35709258 Spatial centrosome proteome of human neural cells uncovers d... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in centrosome-proximity interaction mapping. Reason: The source maps partner Q66GS9 in human neural-cell spatial proteomics. The abstract does not resolve the AGO1 pair or establish that AGO1 catalyses a centrosomal reaction. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:35709258 We used spatial proteomics to elucidate protein interaction networks at the centrosome of human induced pluripotent stem cell-derived neural stem cells |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in multimodal human-cell interaction mapping. Reason: The U2OS cell-map study supplies several physical-association records. Its AGO1-specific interactions were not reanalysed from the supplementary data, and the map does not itself define a new AGO1 molecular function. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:40205054 joint measurement of biophysical interactions and immunofluorescence images for over 5,100 proteins in U2OS osteosarcoma cells. |
| GO:0000976 transcription cis-regulatory region binding | IEA GO_REF:0000107 | UNDECIDED | Summary: Promoter recruitment is experimentally supported, while the precise DNA-binding attribution remains unresolved. Reason: The Ensembl donor is mouse Ago1 Q8CJG1/ENSMUSP00000095498. The MGI graph generated 2023-03-10 maps this term to J:197739, PMID:22053081. Its full text assays mouse NIH/3T3 and TRAMP cells, with endogenous Ago1 knockdown and explicitly human HA-AGO1 transgenes for promoter ChIP and fractionation. It establishes Ccnb1 promoter recruitment and miRNA-dependent activation, but discusses promoter-associated RNA as a possible target. Human PMID:25336585 independently demonstrates let-7i-dependent IL2 promoter occupancy. These positive experiments do not distinguish AGO1 DNA contact from guide-RNA or protein-mediated recruitment. Preserve uncertainty about the molecular attribution without denying nuclear recruitment or requiring a purified-protein assay as the only possible evidence. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 identity is resolved; historical MGI IMP annotation for this exact term traces J:197739/PMID:22053081. The primary study includes human HA-AGO1 in mouse cells and positive Ccnb1 promoter ChIP. Ago1 dna contact versus RNA/protein-mediated recruitment remains unresolved. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 identity is resolved; historical MGI IMP annotation for this exact term traces J:197739/PMID:22053081. The primary study includes human HA-AGO1 in mouse cells and positive Ccnb1 promoter ChIP. Ago1 dna contact versus RNA/protein-mediated recruitment remains unresolved. Supporting Evidence: PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site PMID:25336585 Through co-immunoprecipitation assay, we found that both Ago1 and Ago2 bound to Pol II (Fig. 1E) and TBP (Fig. 1F) in HEK293T cells. PMID:22053081 ChIP analysis further indicated a selective enrichment of only Ago1 protein at the Ccnb1 promoter. |
| GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding | IEA GO_REF:0000107 | UNDECIDED | Summary: Promoter recruitment is experimentally supported, while the precise DNA-binding attribution remains unresolved. Reason: The Ensembl donor is mouse Ago1 Q8CJG1/ENSMUSP00000095498. The MGI graph generated 2023-03-10 maps this term to J:197739, PMID:22053081. Its full text assays mouse NIH/3T3 and TRAMP cells, with endogenous Ago1 knockdown and explicitly human HA-AGO1 transgenes for promoter ChIP and fractionation. It establishes Ccnb1 promoter recruitment and miRNA-dependent activation, but discusses promoter-associated RNA as a possible target. Human PMID:25336585 independently demonstrates let-7i-dependent IL2 promoter occupancy. These positive experiments do not distinguish sequence-specific DNA recognition by AGO1 from guide-RNA or protein-mediated recruitment. Preserve uncertainty about the molecular attribution without denying nuclear recruitment or requiring a purified-protein assay as the only possible evidence. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 identity is resolved; historical MGI IDA annotation for this exact term traces J:197739/PMID:22053081. The primary study includes human HA-AGO1 in mouse cells and positive Ccnb1 promoter ChIP. Sequence-specific dna recognition by ago1 versus RNA/protein-mediated recruitment remains unresolved. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 identity is resolved; historical MGI IDA annotation for this exact term traces J:197739/PMID:22053081. The primary study includes human HA-AGO1 in mouse cells and positive Ccnb1 promoter ChIP. Sequence-specific dna recognition by ago1 versus RNA/protein-mediated recruitment remains unresolved. Supporting Evidence: PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site PMID:25336585 Through co-immunoprecipitation assay, we found that both Ago1 and Ago2 bound to Pol II (Fig. 1E) and TBP (Fig. 1F) in HEK293T cells. PMID:22053081 ChIP analysis further indicated a selective enrichment of only Ago1 protein at the Ccnb1 promoter. |
| GO:0005634 nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: AGO1 has a nuclear pool associated with transcriptional regulation. Reason: The Ensembl donor is mouse Ago1 Q8CJG1/ENSMUSP00000095498. Historical MGI nucleus IDA maps J:197739 to PMID:22053081, whose full text demonstrates nuclear and cytoplasmic HA-tagged human AGO1 in mouse NIH/3T3 cells with compartment markers. Independent human-cell AGO1 promoter ChIP and nuclear-complex evidence in PMID:25336585 corroborate the location. Retain this contextual nuclear pool alongside the principal cytoplasmic miRISC role; none of this evidence depends on AGO1x. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8CJG1 SUPPORTS TRANSFER The MGI nucleus IDA source is J:197739/PMID:22053081. The full study includes human HA-AGO1 transgenes in mouse NIH/3T3 cells and nuclear/cytoplasmic fractionation with controls, so the observed compartment has direct human-protein support as well as independent human-cell corroboration. ensembl:ENSMUSP00000095498 SUPPORTS TRANSFER The MGI nucleus IDA source is J:197739/PMID:22053081. The full study includes human HA-AGO1 transgenes in mouse NIH/3T3 cells and nuclear/cytoplasmic fractionation with controls, so the observed compartment has direct human-protein support as well as independent human-cell corroboration. Supporting Evidence: PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site PMID:25336585 Through co-immunoprecipitation assay, we found that both Ago1 and Ago2 bound to Pol II (Fig. 1E) and TBP (Fig. 1F) in HEK293T cells. PMID:22053081 ChIP analysis further indicated a selective enrichment of only Ago1 protein at the Ccnb1 promoter. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: AGO1 acts in the cytosol as a guide-loaded RNA-silencing protein. Reason: The Ensembl donor is mouse Ago1 Q8CJG1/ENSMUSP00000095498. Its exact source experiment was not reconstructed, but the transferred broad compartment is independently supported by human cytoplasmic mRNP/RISC experiments and by the nonendonucleolytic RISC model. Cytosolic localization is not restricted to visible P-bodies. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. Supporting Evidence: PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0016442 RISC complex | IEA GO_REF:0000120 | ACCEPT | Summary: AGO1 is a core protein component of RISC. Reason: The combined electronic row cites ARBA00044873 and mouse Ago1; the individual mapping predicates and donor experiment were not reconstructed. Membership is independently supported by human AGO1-small-RNA complexes; RISC membership does not require each Argonaute to be an endonuclease. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00044873 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0035198 miRNA binding | IEA GO_REF:0000120 | ACCEPT | Summary: AGO1 binds miRNA guides in silencing complexes. Reason: The combined mapping cites ARBA00091599 and mouse Ago1; independent human miRNA immunopurification supports the assigned function even though rule internals and the mouse experiment were not reconstructed. miRNA binding is a central molecular activity and is distinct from whether the protein can catalyse target cleavage. Propagation Review Root cause: UNRESOLVED Sources checked: ARBA:ARBA00091599 UNRESOLVED This exact ARBA rule occurs in WITH/FROM, but its predicates and training evidence were not inspected. The annotation judgment rests on the separately cited biological evidence; rule validity is not claimed. UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 source Q8CJG1/ENSMUSP00000095498 identified. The exact source experiment for this term was not recovered. Use the independently cited human evidence where sufficient; donor identity alone is not proof of the functional transfer. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). |
| GO:1901224 positive regulation of non-canonical NF-kappaB signal transduction | IEA GO_REF:0000107 | UNDECIDED | Summary: AGO1-dependent TNFAIP3 regulation is reported, while specificity for the non-canonical NF-kappaB branch remains unresolved. Reason: The Ensembl donor is mouse Ago1 Q8CJG1/ENSMUSP00000095498. The MGI graph generated 2023-03-10 maps the exact process IMP to J:233964, PMID:26764146. The primary PubMed abstract reports increased AGO1/AGO3 in CVB3-infected mouse hearts and in vitro miR-19a/b-dependent repression of the NF-kappaB inhibitor TNFAIP3. This supports a positive NF-kappaB regulatory mechanism, but the accessible abstract does not resolve the NIK/non-canonical branch. The recovered normal cache now contains the abstract; the full experimental body remains unavailable. Preserve UNDECIDED for the exact branch rather than infer an incorrect transfer from incomplete evidence; no corresponding AGO1 GO-CAM was found locally. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q8CJG1 UNRESOLVED Mouse Ago1 source and historical term-specific IMP are identified: MGI J:233964/PMID:26764146. Primary abstract supports AGO1/AGO3 regulation of miR-19a/b-targeted TNFAIP3 in the CVB3 model. The exact NIK/non-canonical assay and human transfer remain unresolved without the full study. ensembl:ENSMUSP00000095498 UNRESOLVED Mouse Ago1 source and historical term-specific IMP are identified: MGI J:233964/PMID:26764146. Primary abstract supports AGO1/AGO3 regulation of miR-19a/b-targeted TNFAIP3 in the CVB3 model. The exact NIK/non-canonical assay and human transfer remain unresolved without the full study. |
| GO:0035196 miRNA processing | NAS PMID:28781232 Multivalent Recruitment of Human Argonaute by GW182. | ACCEPT | Summary: AGO1 participates in production of functional, guide-loaded miRNA complexes. Reason: GO:0035196 includes generation of functional miRNA and is not restricted to precursor cleavage. The original NAS source PMID:28781232 establishes mature RNA-loaded AGO1 recruitment of GW182, principally an effector-complex result. Independent direct human PAZ-mutant experiments in PMID:22795694 establish the more relevant duplex-unwinding/maturation step. Acceptance is therefore supported by combined evidence, not a claim that the 2017 GW182 structure alone demonstrates miRNA biogenesis. Supporting Evidence: PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. PMID:28781232 miRNA binding increases hAgo's affinity to GW182. |
| GO:0036464 cytoplasmic ribonucleoprotein granule | IDA GO_REF:0000052 | ACCEPT | Summary: AGO1 localizes to cytoplasmic RNP granules including P-bodies. Reason: The HPA IDA row records cytoplasmic RNP-granule localization; the raw HPA image/antibody panels were not independently reanalysed. Human AGO1 colocalization with TNRC6A/DDX6 in P-bodies is independently described in PMID:28683311. Granule localization is retained without claiming visible P-bodies are required for silencing. Supporting Evidence: PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0005737 cytoplasm | IDA PMID:17932509 Proteomic and functional analysis of Argonaute-containing mR... | ACCEPT | Summary: AGO1 operates in cytoplasmic RNA-silencing complexes. Reason: PMID:17932509 studies human Ago1-containing mRNP complexes and maps their interactions. Cytoplasm is valid at the source resolution and need not be replaced with one particular granule or subcompartment. Supporting Evidence: PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0016525 negative regulation of angiogenesis | IMP PMID:23426184 Hypoxia-responsive miRNAs target argonaute 1 to promote angi... | KEEP AS NON CORE | Summary: AGO1 can restrain angiogenesis through endothelial miRNA repression. Reason: The source reports AGO1 perturbation and rescue in a hypoxia-responsive miRNA/VEGF pathway: AGO1 knockdown increases angiogenesis, whereas an AGO1 construct lacking its regulatory 3β²UTR opposes the hypoxic response. This is a supported regulatory outcome of the core RNA-silencing activity, retained as a context-specific process rather than a separate catalytic core. Supporting Evidence: PMID:23426184 Inhibition of HRM or overexpression of AGO1 without the 3' untranslated region decreased hypoxia-induced angiogenesis. PMID:23426184 AGO1 knockdown increased angiogenesis under normoxia in vivo. |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IMP PMID:25336585 Cellular microRNAs up-regulate transcription via interaction... | KEEP AS NON CORE | Summary: AGO1 contributes to let-7i-dependent activation of the IL2 promoter. Reason: The full human-cell study combines AGO1 depletion, promoter-reporter effects, promoter ChIP and association with the basal transcription machinery. This supports positive transcriptional regulation in the tested context without making all AGO1 nuclear activity activating or adding an independent core. Supporting Evidence: PMID:25336585 When Ago1 and Ago2 proteins were knocked down by siRNAs (Supplemental Fig. S4D), the activating effect of IL-2 promoter by let-7i was significantly impaired PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site |
| GO:0001046 core promoter sequence-specific DNA binding | IMP PMID:25336585 Cellular microRNAs up-regulate transcription via interaction... | UNDECIDED | Summary: AGO1 promoter occupancy is supported; the exact sequence-specific DNA-binding activity is not resolved. Reason: PMID:25336585 demonstrates AGO1 enrichment at the IL2 promoter by ChIP and dependence of transcriptional activation on AGO1. The compensatory sequence mutations test let-7i/promoter complementarity. These establish a sequence-directed AGO1-containing assembly but do not separate direct AGO1βDNA recognition from RNA-mediated recruitment or other protein contacts. Retain uncertainty for this exact MF while retaining the supported nuclear location and transcriptional process. Supporting Evidence: PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site PMID:25336585 When Ago1 and Ago2 proteins were knocked down by siRNAs (Supplemental Fig. S4D), the activating effect of IL-2 promoter by let-7i was significantly impaired |
| GO:0005634 nucleus | IC PMID:25336585 Cellular microRNAs up-regulate transcription via interaction... | KEEP AS NON CORE | Summary: AGO1 has a nuclear pool associated with transcriptional regulation. Reason: The IC annotation is supported by AGO1 ChIP at the human IL2 promoter and association with the basal transcription machinery in PMID:25336585. This compartment is retained as a contextual location alongside the principal cytoplasmic miRISC role. Canonical AGO1 evidence here does not depend on AGO1x. Supporting Evidence: PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site PMID:25336585 Through co-immunoprecipitation assay, we found that both Ago1 and Ago2 bound to Pol II (Fig. 1E) and TBP (Fig. 1F) in HEK293T cells. |
| GO:0000993 RNA polymerase II complex binding | IDA PMID:25336585 Cellular microRNAs up-regulate transcription via interaction... | KEEP AS NON CORE | Summary: AGO1 associates with the RNA polymerase II transcription machinery. Reason: PMID:25336585 directly co-immunoprecipitates HA-tagged human AGO1 with Pol II in HEK293T cells. This supports complex binding in the studied nuclear regulatory context; no autonomous DNA-recognition or polymerase catalytic activity is implied. Supporting Evidence: PMID:25336585 Through co-immunoprecipitation assay, we found that both Ago1 and Ago2 bound to Pol II (Fig. 1E) and TBP (Fig. 1F) in HEK293T cells. |
| GO:0005515 protein binding | IPI PMID:25336585 Cellular microRNAs up-regulate transcription via interaction... | MODIFY | Summary: AGO1 associates with TBP in a human nuclear transcription-regulatory context. Reason: PMID:25336585 Figure 1F co-immunoprecipitates HA-tagged human AGO1 with TBP in HEK293T cells, alongside the Pol II association in Figure 1E. The partner identity supports the specific GO:0017025 TBP-class protein binding term instead of generic protein binding. This is contextual association with transcription machinery, assessed at the same co-immunoprecipitation resolution as the retained Pol II binding annotation; it does not establish an isolated binary contact, autonomous DNA recognition, or a separate core function. Proposed replacements: TBP-class protein binding Supporting Evidence: PMID:25336585 Through co-immunoprecipitation assay, we found that both Ago1 and Ago2 bound to Pol II (Fig. 1E) and TBP (Fig. 1F) in HEK293T cells. |
| GO:0035196 miRNA processing | IMP PMID:22795694 Slicing-independent RISC activation requires the argonaute P... | ACCEPT | Summary: The AGO1 PAZ domain supports miRNA-duplex maturation into functional RISC. Reason: PMID:22795694 explicitly tests human AGO1 PAZ-deletion mutants. The mutants still associate with duplexes but fail to unwind them and restore silencing, directly placing AGO1 in the production of functional miRNA-loaded complexes. GO:0035196 encompasses this late maturation step and does not require AGO1 to perform Dicer cleavage. Supporting Evidence: PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0031054 pre-miRNA processing | IDA PMID:19966796 ATP-dependent human RISC assembly pathways. | ACCEPT | Summary: AGO1 contributes to late miRNA maturation through guide-duplex loading and unwinding. Reason: PMID:19966796 assays human Ago1 pre-RISC and mature RISC, demonstrating duplex loading and subsequent unwinding, while explicitly separating these steps from dicing. GO:0031054 encompasses conversion to a mature miRNA, rather than requiring the annotated protein itself to cleave the precursor hairpin. AGO1 directly holds and resolves the duplex into a functional guide-loaded complex; Dicer performs the precursor cleavage. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0003725 double-stranded RNA binding | IDA PMID:19966796 ATP-dependent human RISC assembly pathways. | ACCEPT | Summary: AGO1 binds small-RNA duplexes during RISC loading. Reason: PMID:19966796 distinguishes duplex-containing Ago1 pre-RISC from the single-guide mature complex by native gels and RNA analysis. Duplex recognition is an experimentally established stage of AGO1 function, not an unsupported inference from mature single-stranded miRNA binding. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0003727 single-stranded RNA binding | IDA PMID:19966796 ATP-dependent human RISC assembly pathways. | ACCEPT | Summary: AGO1 binds single-stranded guide RNA. Reason: PMID:19966796 recovers single-stranded guide-containing mature human Ago1 RISC after duplex unwinding. The substrate-class term correctly covers guide RNA beyond a single miRNA sequence; it does not imply indiscriminate binding to every single-stranded RNA. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. |
| GO:0016442 RISC complex | IDA PMID:19966796 ATP-dependent human RISC assembly pathways. | ACCEPT | Summary: AGO1 is a core protein component of RISC. Reason: PMID:19966796 directly distinguishes pre-RISC and mature RISC containing transfected human Ago1. Membership is independently supported by human AGO1-small-RNA complexes; RISC membership does not require each Argonaute to be an endonuclease. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0070578 RISC-loading complex | IDA PMID:19966796 ATP-dependent human RISC assembly pathways. | UNDECIDED | Summary: AGO1 participates in RISC loading, while membership in the specifically defined RLC remains unresolved. Reason: PMID:19966796 directly demonstrates human Ago1 pre-RISC loading and maturation, but explicitly questions the historical human RLC model. The current GO:0070578 definition specifies a DICER1βTARBP2βAGO2 trimer with precursor-processing activity. This is not equivalent to every duplex-bound Ago1 pre-RISC. Direct AGO1βDicer interactions are real, but the assessed evidence does not establish the exact trimeric AGO1 complex. Retain uncertainty rather than deny loading or assume an obligatory composition. Supporting Evidence: PMID:19966796 the previously designated βhuman RLCβ composed of Ago2, Dicer, and TRBP does not correspond to a canonical RISC-loading complex PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:12526743 Immunoprecipitation experiments suggest that, in human and mouse cells, complex formation occurs between Dicer and eIF2C1 or 2 |
| GO:0070922 RISC complex assembly | IDA PMID:19966796 ATP-dependent human RISC assembly pathways. | ACCEPT | Summary: AGO1 directly contributes to RISC assembly. Reason: PMID:19966796 directly follows the assembly of human Ago1-containing pre-RISC and mature guide-loaded RISC. AGO1 supplies the guide-binding scaffold and promotes passenger-strand release, so it performs a step of assembly rather than merely being required downstream. ATP dependence of cell-extract loading does not assign ATPase activity to AGO1. Supporting Evidence: PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:22795694 Thus, Ago1/3/4-ΞPAZ maintained their ability to physically associate with small-RNA duplexes, but not the ability to unwind and form active RISC. |
| GO:0090625 siRNA-mediated gene silencing by mRNA destabilization | IDA NOT PMID:15260970 Human Argonaute2 mediates RNA cleavage targeted by miRNAs an... | UNDECIDED | Summary: The negated process annotation remains unresolved because target cleavage and nonendonucleolytic mRNA destabilization have different scope. Reason: The current GO:0090625 definition describes small-RNA-directed target cleavage, although its name describes mRNA destabilization more broadly. The accessible original abstract of PMID:15260970 supports AGO2-specific endonuclease activity, and the independent human AGO1 structure and cleavage assays in PMID:23809764 support lack of wild-type AGO1 slicing. These findings support a cleavage-scoped negative, but they do not exclude AGO1 recruitment of nonendonucleolytic decay, supported by PMID:18771919 and TNRC6 mechanisms. Full assay details of the original 2004 source remain inaccessible, and intended scope of the process term is unresolved. Preserve the source negation while withholding a confident decision on this process assertion; the separate NOT RNA endonuclease activity annotation remains accepted on direct AGO1 evidence. Supporting Evidence: PMID:15260970 Purification of the FLAG/HA-epitope-tagged Ago containing complexes from different human cell lines revealed that endonuclease activity is exclusively associated with Ago2. PMID:18771919 the four tethered proteins caused nearly equal reductions in cytoplasmic mRNA concentration, suggesting that each has a similar capacity to destabilize mRNA. |
| GO:0005737 cytoplasm | IDA PMID:15260970 Human Argonaute2 mediates RNA cleavage targeted by miRNAs an... | ACCEPT | Summary: AGO1 operates in cytoplasmic RNA-silencing complexes. Reason: PMID:15260970 purifies human Ago1-containing miRNPs; the source location is consistent with independent human cytoplasmic AGO1 assays. Cytoplasm is valid at the source resolution and need not be replaced with one particular granule or subcompartment. Supporting Evidence: PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0016442 RISC complex | IDA PMID:15260970 Human Argonaute2 mediates RNA cleavage targeted by miRNAs an... | ACCEPT | Summary: AGO1 is a core protein component of RISC. Reason: PMID:15260970 directly isolates human AGO1 miRNA-containing complexes, separately from AGO2-dependent cleavage. Membership is independently supported by human AGO1-small-RNA complexes; RISC membership does not require each Argonaute to be an endonuclease. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0035198 miRNA binding | IDA PMID:15260970 Human Argonaute2 mediates RNA cleavage targeted by miRNAs an... | ACCEPT | Summary: AGO1 binds miRNA guides in silencing complexes. Reason: PMID:15260970 directly compares miRNAs associated with the four human Argonautes. miRNA binding is a central molecular activity and is distinct from whether the protein can catalyse target cleavage. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). |
| GO:0035279 miRNA-mediated gene silencing by mRNA destabilization | IDA NOT PMID:15260970 Human Argonaute2 mediates RNA cleavage targeted by miRNAs an... | UNDECIDED | Summary: The negated process annotation remains unresolved because target cleavage and nonendonucleolytic mRNA destabilization have different scope. Reason: The current GO:0035279 definition describes small-RNA-directed target cleavage, although its name describes mRNA destabilization more broadly. Its related deadenylation synonyms additionally conflict with a cleavage-only reading. The accessible original abstract of PMID:15260970 supports AGO2-specific endonuclease activity, and the independent human AGO1 structure and cleavage assays in PMID:23809764 support lack of wild-type AGO1 slicing. These findings support a cleavage-scoped negative, but they do not exclude AGO1 recruitment of nonendonucleolytic decay, supported by PMID:18771919 and TNRC6 mechanisms. Full assay details of the original 2004 source remain inaccessible, and intended scope of the process term is unresolved. Preserve the source negation while withholding a confident decision on this process assertion; the separate NOT RNA endonuclease activity annotation remains accepted on direct AGO1 evidence. Supporting Evidence: PMID:15260970 Purification of the FLAG/HA-epitope-tagged Ago containing complexes from different human cell lines revealed that endonuclease activity is exclusively associated with Ago2. PMID:18771919 the four tethered proteins caused nearly equal reductions in cytoplasmic mRNA concentration, suggesting that each has a similar capacity to destabilize mRNA. |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-5578742 | KEEP AS NON CORE | Summary: AGO1 occurs in nucleoplasmic chromatin-associated RNA complexes. Reason: The cached Reactome event explicitly describes nuclear AGO1 and AGO2 complexes, AGO1 association with RNA polymerase II at active and silenced promoters, and possible transcript-mediated chromatin recruitment. This is a source-supported contextual nuclear pool, independently corroborated by human AGO1 ChIP. It does not depend on the disputed AGO1x proteoform. Supporting Evidence: Reactome:R-HSA-5578742 AGO1 also associates with RNA polymerase II at active promoters PMID:25336585 Significant enrichment of Ago1 and Ago2 were detected in the region of -146 to -8 of the IL-2 promoter, which covers the identified let-7i target site |
| GO:0003723 RNA binding | IDA PMID:23809764 Eukaryote-specific insertion elements control human ARGONAUT... | ACCEPT | Summary: AGO1 binds RNA as the guide-bearing effector of RISC. Reason: PMID:23809764 solves human AGO1 bound to endogenous guide RNAs recovered from insect-cell expression. The mostly viral guide pool does not justify narrowing this particular experimental row to miRNA alone. RNA binding is biologically correct at this source resolution; guide and target binding are not exhausted by the narrower miRNA-binding annotation. Supporting Evidence: PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. |
| GO:0004521 RNA endonuclease activity | IDA NOT PMID:23809764 Eukaryote-specific insertion elements control human ARGONAUT... | ACCEPT | Summary: Wild-type human AGO1 lacks the tested target-RNA endonuclease activity. Reason: The NOT flag is consistent with the human AGO1 structure and direct cleavage assays in PMID:23809764. Engineering catalytic-site and channel-loop substitutions can partially restore slicing, which does not assign that engineered activity to wild-type AGO1. RNA guide binding and nonendonucleolytic repression remain intact. Supporting Evidence: PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. PMID:23809764 reconstitution of the catalytic tetrad with R805H led to low-level hAGO1 cleavage activity |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | ACCEPT | Summary: AGO1 binds RNA as the guide-bearing effector of RISC. Reason: PMID:22681889 uses photoreactive-nucleotide UV crosslinking and oligo(dT) purification of mRNA-bound proteins in human embryonic kidney cells. The AGO1-specific supplementary hit was not recovered from the abstract-only local cache; retain the broad curator-assigned binding because independent AGO1 structure and target-RNA assays establish it. RNA binding is biologically correct at this source resolution; guide and target binding are not exhausted by the narrower miRNA-binding annotation. Supporting Evidence: PMID:23809764 We have solved the crystal structure of human ARGONAUTE1 (hAGO1) bound to endogenous 5'-phosphorylated guide RNAs. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1606561 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR449 microRNAs bind 3'UTR of NOTCH1 mRNA context. Reason: The cached event describes MIR449 microRNAs bind 3'UTR of NOTCH1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1606561 Translation of NOTCH1 mRNA is negatively regulated by MIR449 microRNAs (MIR449A, MIR449B and MIR449C), which bind to the 3'UTR of NOTCH1. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1606682 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR34 microRNAs bind 3'UTR of NOTCH1 mRNA context. Reason: The cached event describes MIR34 microRNAs bind 3'UTR of NOTCH1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1606682 Translation of NOTCH1 mRNA is inhibited by MIR34 microRNAs (MIR34A, MIR34B and MIR34C), which bind to the 3'UTR of NOTCH1 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1912362 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR150 microRNA binds 3'UTR of NOTCH3 mRNA context. Reason: The cached event describes MIR150 microRNA binds 3'UTR of NOTCH3 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1912362 Translation of NOTCH3 mRNA is inhibited by miR-150 microRNA which binds to the 3'UTR of NOTCH3 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1912363 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR200B/C microRNAs bind NOTCH1 mRNA context. Reason: The cached event describes MIR200B/C microRNAs bind NOTCH1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1912363 Translation of NOTCH1 mRNA is inhibited by microRNAs miR-200B and miR-200C, which bind to the 3'UTR of NOTCH1 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1912364 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR181C microRNA binds 3'UTR of NOTCH4 mRNA context. Reason: The cached event describes MIR181C microRNA binds 3'UTR of NOTCH4 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1912364 miR-181C microRNA inhibits translation of NOTCH4 mRNA by binding to its 3'UTR. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1912366 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR206 microRNA binds 3'UTR of NOTCH3 mRNA context. Reason: The cached event describes MIR206 microRNA binds 3'UTR of NOTCH3 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1912366 Translation of NOTCH3 mRNA is inhibited by microRNA miR-206 which binds to the 3'UTR of NOTCH3 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1912367 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR34 microRNAs bind 3'UTR of NOTCH2 mRNA context. Reason: The cached event describes MIR34 microRNAs bind 3'UTR of NOTCH2 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1912367 Translation of NOTCH2 mRNA is inhibited by MIR34 microRNAs (MIR34A, MIR34B and MIR34C), which bind to the 3'UTR of NOTCH2 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1912368 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR302A microRNA binds 3'UTR of NOTCH4 mRNA context. Reason: The cached event describes MIR302A microRNA binds 3'UTR of NOTCH4 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1912368 MicroRNA miR-302A, upregulated in melanoma, binds the 3'UTR of NOTCH4, resulting in inhibition of NOTCH4 mRNA translation. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1912406 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated p53 positively regulates transcription of MIR34 microRNAs context. Reason: The cached event describes p53 positively regulates transcription of MIR34 microRNAs. This transcriptional event or pathway context includes regulatory-miRNA production and does not by itself establish AGO1 as the named transcription factor. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-1912406 Transcription of microRNA MIR34A is directly induced by the tumor suppressor p53, which binds to the conserved p53 binding site located in the vicinity of the MIR34A transcription start (Chang et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2318752 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-26A microRNAs bind PTEN mRNA context. Reason: The cached event describes miR-26A microRNAs bind PTEN mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-2318752 MIR26A microRNAs, miR-26A1 and miR-26A2, transcribed from genes on chromosome 3 and 12, respectively, bind PTEN mRNA (Huse et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3209151 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-24 binds p16INK4A and p14ARF mRNAs context. Reason: The cached event describes miR-24 binds p16INK4A and p14ARF mRNAs. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-3209151 MicroRNA miR-24 is able to bind both p16INK4A mRNA (Lal et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-426489 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated RISC binds inexactly matching target RNAs context. Reason: The cached event describes RISC binds inexactly matching target RNAs. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-426489 RISCs can bind target RNAs that do not exactly match the guide RNA carried by an Argonaute. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-426522 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated Nonendonucleolytic RISC binds exactly matching target RNAs context. Reason: The cached event describes Nonendonucleolytic RISC binds exactly matching target RNAs. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-426522 RISCs containing Argonaute-1 (AGO1, EIF2C1), AGO3 (EIF2C3), and AGO4 (EIF2C4) bind to target RNAs by base-pairing between the target RNA and the guide RNA of the RISC. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-4518575 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-92b binds 3'UTR of NLK mRNA context. Reason: The cached event describes miR-92b binds 3'UTR of NLK mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-4518575 NLK mRNA is a direct target of miR-92b which binds the 3' UTR and promotes degradation (Wang et al, 2013). PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5687103 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated FOXO3 regulates MIR34B,C expression context. Reason: The cached event describes FOXO3 regulates MIR34B,C expression. This transcriptional event or pathway context includes regulatory-miRNA production and does not by itself establish AGO1 as the named transcription factor. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-5687103 p-S215 FOXO3 binds to the promoter of the MIR34B and C gene and promotes its expression (Kress et al, 2011). PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8935766 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-378 binds RUNX1 mRNA context. Reason: The cached event describes miR-378 binds RUNX1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8935766 The mature microRNA miR-378a-3p, one of the two single strand products derived from microRNA miR-378 encoded by the MIR378 gene locus, binds the 3'UTR of the RUNX1 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8937097 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MIR27A gene transcription is stimulated by the complex containing RUNX1, PRMT1 and GATA1 and inhibited by the complex of RUNX1, SIN3A and PRMT6 context. Reason: The cached event describes MIR27A gene transcription is stimulated by the complex containing RUNX1, PRMT1 and GATA1 and inhibited by the complex of RUNX1, SIN3A and PRMT6. This transcriptional event or pathway context includes regulatory-miRNA production and does not by itself establish AGO1 as the named transcription factor. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8937097 The RUNX1:CBFB complex binds the promoter of the MIR27A gene, encoding microRNA miR-27a, and stimulates MIR27A transcription. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8937134 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-27a binds RUNX1 mRNA context. Reason: The cached event describes miR-27a binds RUNX1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8937134 MicroRNA miR-27a binds the 3'UTR of the RUNX1 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8938440 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-17 binds RUNX1 mRNA context. Reason: The cached event describes miR-17 binds RUNX1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8938440 MicroRNA miR-17 binds the 3' UTR of the RUNX1 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8938487 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-20a binds RUNX1 mRNA context. Reason: The cached event describes miR-20a binds RUNX1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8938487 MicroRNA miR-20a binds the 3' UTR of the RUNX1 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8938507 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-106a binds RUNX1 mRNA context. Reason: The cached event describes miR-106a binds RUNX1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8938507 MicroRNA miR-106a binds the 3' UTR of the RUNX1 mRNA. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8944650 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-214 microRNA binds PTEN mRNA context. Reason: The cached event describes miR-214 microRNA binds PTEN mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8944650 MicroRNA miR-214-3p, one of the two mature products of miR-214, binds to the 3'UTR of the PTEN mRNA and inhibits PTEN mRNA translation. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8944684 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-205 microRNA binds PTEN mRNA context. Reason: The cached event describes miR-205 microRNA binds PTEN mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8944684 MicroRNA miR-205-5p, one of the two mature products of miR-205, binds the 3'UTR of the PTEN mRNA, resulting in downregulation of PTEN mRNA and protein levels. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8944706 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-21 nonendonucleolytic RISC binds PTEN mRNA context. Reason: The cached event describes miR-21 nonendonucleolytic RISC binds PTEN mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-8944706 miR-21-5p, one of the two mature products of miR-21, binds the 3'UTR of PTEN mRNA to inhibit PTEN mRNA translation. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9011958 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-26A and B bind to the 3'UTR of the GREB1 mRNA context. Reason: The cached event describes miR-26A and B bind to the 3'UTR of the GREB1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9011958 Translation of GREB1 mRNA is negatively regulated by mIR-26A and B, which bind directly to the 3'UTR. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9012203 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-26A and B bind to the 3'UTR of the CHD11 mRNA context. Reason: The cached event describes miR-26A and B bind to the 3'UTR of the CHD11 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9012203 Translation of CHD1 mRNA is negatively regulated by mIR-26A and B, which bind directly to the 3'UTR. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9012208 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-26A and B bind to the 3'UTR of the KPNA2 mRNA context. Reason: The cached event describes miR-26A and B bind to the 3'UTR of the KPNA2 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9012208 Translation of KPNA2 mRNA is negatively regulated by mIR-26A and B, which bind directly to the 3'UTR. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9038545 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-613 binds to the 3'UTR of the NR1H3 mRNA context. Reason: The cached event describes miR-613 binds to the 3'UTR of the NR1H3 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9038545 Translation of liver X receptor Ξ± (LXRΞ± or NR1H3) mRNA is negatively regulated by microRNA 613 (miR-613), which binds directly to the specific miRNA response element (613MRE) within the 3'UTR of NR1H3 mRNA (Ou Z et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9618392 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-26 binds to the 3'UTR of the ARL4C mRNA context. Reason: The cached event describes miR-26 binds to the 3'UTR of the ARL4C mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9618392 A small non-coding RNA miR-26 was identified as a liver X receptor (LXR or NR1H2,3)-responsive miRNA that is downregulated in the presence of LXR agonist T0901317 (Sun D et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9618486 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-26 binds to the 3'UTR of the ABCA1 mRNA context. Reason: The cached event describes miR-26 binds to the 3'UTR of the ABCA1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9618486 Micro RNA miR-26 was identified as a liver X receptor (LXR or NR1H2,3)-repressed miRNA in macrophage cell lines (Sun D et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9624925 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-33 binds to the 3'UTR of the ABCA1 mRNA context. Reason: The cached event describes miR-33 binds to the 3'UTR of the ABCA1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9624925 ATP-binding cassette transporter A1 (ABCA1) is a target of micro RNA 33 (miR-33) (Rayner KJ et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9657791 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-144 binds to the 3'UTR of the ABCA1 mRNA context. Reason: The cached event describes miR-144 binds to the 3'UTR of the ABCA1 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9657791 Expression of the ATP-binding cassette transporter A1 (ABCA1) gene is induced by oxysterol-activated transcription factors liver X receptor Ξ± (LXRΞ±, NR1H3) and LXRΞ² (NR1H2) and their heterodimeric partners, retinoid X receptors (RXR) via functional LXR response element (LXRE) (Costet P et al. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9858289 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated MITF-M-dependent miR-211 expression context. Reason: The cached event describes MITF-M-dependent miR-211 expression. This transcriptional event or pathway context includes regulatory-miRNA production and does not by itself establish AGO1 as the named transcription factor. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9858289 MIR211, encoding the microRNA miR-211 is an MITF-M-dependent target gene that is expressed in the melanocyte lineage and is frequently downregulated in melanoma (Hunter et al, 1998; Duncan et al, 1998; Duncan et al, 2001). PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9858309 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated miR-211 RISC binds POU3F2 mRNA context. Reason: The cached event describes miR-211 RISC binds POU3F2 mRNA. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9858309 miR-211 is an MITF-M-dependent target gene that is expressed in the melanocyte lineage and is frequently downregulated in melanoma (Hunter et al, 1998; Duncan et al, 1998; Duncan et al, 2001). PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9924921 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated CD274 mRNA binds miR-34 RISC context. Reason: The cached event describes CD274 mRNA binds miR-34 RISC. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9924921 MicroRNA-34a (miR-34a), a central regulator within the T cell regulatory network, plays a crucial role in T cell activation. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9925095 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated CD274 mRNA binds miR-340 RISC context. Reason: The cached event describes CD274 mRNA binds miR-340 RISC. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9925095 MicroRNA-340 (miR-340) plays a critical role in osteoclast differentiation and tumor progression. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9925158 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated CD274 mRNA binds miR-152 RISC context. Reason: The cached event describes CD274 mRNA binds miR-152 RISC. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9925158 MicroRNA-152 (miR-152) is a critical regulator of innate immune response. PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9925159 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated CD274 mRNA binds miR-140 RISC context. Reason: The cached event describes CD274 mRNA binds miR-140 RISC. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9925159 microRNA-140 (miR-140) plays a key role in T cell differentiation to regulate immune homeostasis and in disease like osteoarthritis, cancer (Ghafouri-Fard et al., 2020, Guan et al., 2016). PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9925324 | ACCEPT | Summary: Cytosolic AGO1 is compatible with the curated CD274 mRNA binds miR-200B/C RISC context. Reason: The cached event describes CD274 mRNA binds miR-200B/C RISC. The GOA assertion under review is the broad cytosolic compartment, independently supported by human AGO1 miRNP experiments. Retain that location without interpreting every miRNA-target study as an AGO1-specific perturbation or assigning its downstream developmental/metabolic phenotype to AGO1. Supporting Evidence: Reactome:R-HSA-9925324 microRNA-200 family of microRNAs play an important role in T cell function regulation in normal and disease conditions like cancers (Humphries et al., 2015). PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0005515 protein binding | IPI PMID:22915799 HIV-1 replication and APOBEC3 antiviral activity are not reg... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in APOBEC3 associations. Reason: The source studies APOBEC3βArgonaute/P-body associations while finding no specific APOBEC3 regulation of miRNA function. It does not establish AGO1 cytidine-deaminase or antiviral catalytic activity. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:22915799 some APOBEC3 proteins interact with several Argonaute proteins |
| GO:0005515 protein binding | IPI PMID:16289642 Identification of novel argonaute-associated proteins. | REMOVE | Summary: Generic protein binding does not specify AGO1 function in MOV10-associated mRNP. Reason: The source explicitly purifies human Ago1/Ago2 complexes and identifies associated MOV10/TNRC6B proteins; AGO1 is not assigned their helicase or effector activities. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:16289642 we purified Ago1- and Ago2-containing complexes from human cells. |
| GO:0005515 protein binding | IPI PMID:20616046 LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for... | REMOVE | Summary: Generic protein binding does not specify AGO1 function in Ajuba-family associations. Reason: The source explicitly reports Ago1/2 association with LIMD1, AJUBA and WTIP. Its proposed molecular bridge is supplied by the LIM proteins; interaction alone does not define a distinct AGO1 protein-adaptor activity. Remove the uninformative generic molecular-function label without denying the reported interaction or claiming it is misattributed. No evidence-backed, distinct specific MF replacement is established by this row. Supporting Evidence: PMID:20616046 LIMD1, Ajuba, and WTIP bind to Ago1/2, RCK, Dcp2, and eIF4E in vivo |
| GO:0005737 cytoplasm | IDA PMID:20014101 Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing... | ACCEPT | Summary: AGO1 operates in cytoplasmic RNA-silencing complexes. Reason: The PMID:20014101 abstract explicitly reports EIF2C1/AGO1 colocalization with ectopically expressed ZAR1L in somatic-cell P-body foci. The full construct/species details are unavailable locally, so retain the broad curator-assigned human cytoplasmic location with independent corroboration rather than infer a wrong-species annotation from the mouse ZAR1L title. Cytoplasm is valid at the source resolution and need not be replaced with one particular granule or subcompartment. Supporting Evidence: PMID:20014101 When ectopically expressed in somatic cells, ZAR1L colocalized with P-body components including EIF2C1(AGO1), EIF2C2(AGO2), DDX6 and LSM14A PMID:28683311 Loss of LIMD1 had no visible effect on AGO1, 2, or 3 colocalization with TNRC6A or DDX6 in P-bodies |
| GO:0016442 RISC complex | IDA PMID:17932509 Proteomic and functional analysis of Argonaute-containing mR... | ACCEPT | Summary: AGO1 is a core protein component of RISC. Reason: PMID:17932509 directly resolves human AGO1-containing mRNP complexes with silencing-associated activities. Membership is independently supported by human AGO1-small-RNA complexes; RISC membership does not require each Argonaute to be an endonuclease. Supporting Evidence: PMID:15260970 Our results suggest that miRNAs are incorporated indiscriminately of their sequence into Ago1 through Ago4 containing microRNPs (miRNPs). PMID:19966796 Examination of RNA species in the complexes revealed that the upper complex (complex I) contained small-RNA duplexes, and the lower complex (complex II) contained single-stranded small RNAs annealed with target ASO, indicating that they represent pre-RISC and mature RISC, respectively PMID:17932509 Separation of Ago-associated messenger ribonucleoproteins (mRNPs) showed that Ago1 and Ago2 reside in three complexes with distinct Dicer and RNA-induced silencing complex activities. |
| GO:0000956 nuclear-transcribed mRNA catabolic process | IDA PMID:18771919 Importance of translation and nonnucleolytic ago proteins fo... | ACCEPT | Summary: AGO1 participates in nonendonucleolytic mRNA decay. Reason: PMID:18771919 directly tests tethered human AGO1βAGO4 in 293T cells and finds similar reductions in cytoplasmic reporter mRNA, interpreted as comparable destabilizing capacity. This is an engineered recruitment assay and steady-state abundance measurement, not a purified nuclease assay or direct half-life measurement. Together with AGO1βTNRC6/CAF1 interactions, it supports a core role in recruiting decay machinery. The term concerns nucleus-transcribed mRNA, not a requirement for degradation inside the nucleus. Supporting Evidence: PMID:18771919 the four tethered proteins caused nearly equal reductions in cytoplasmic mRNA concentration, suggesting that each has a similar capacity to destabilize mRNA. PMID:19716330 As CAF1 interacts with both Ago1 and Ago2 in HEK293 cells, this suggests that both Ago proteins are involved in facilitating miRNA-mediated deadenylation in mammals. PMID:19383768 Our findings indicate that TNRC6A, TNRC6B, and TNRC6C are recruited to miRNA targets through an interaction between their N-terminal domain and an Argonaute protein; the TNRC6s then promote translational repression and/or degradation of miRNA targets through a C-terminal silencing domain. |
| GO:0035278 miRNA-mediated gene silencing by inhibition of translation | IDA PMID:18771919 Importance of translation and nonnucleolytic ago proteins fo... | ACCEPT | Summary: AGO1 mediates noncleavage translational repression. Reason: The human Ago1 tethering experiments in PMID:18771919 compare reporter protein output with mRNA abundance and support translational repression in addition to nonendonucleolytic transcript destabilization. Repression potency in the tested 293T boxB reporter system ranked Ago4 > Ago3 > Ago2 >= Ago1; at low concentrations Ago4 was about sixfold more potent than Ago1, whereas the four proteins caused similar reductions in mRNA abundance. Thus AGO1 can repress translation, but it was the weakest paralog in this assay. This relative potency is not a universal ranking across endogenous targets or cell types. Independent TNRC6 recruitment supports its central miRISC effector role. Supporting Evidence: PMID:18771919 This finding indicates that the marked disparities between the effects of the tethered Ago proteins on gene expression result almost entirely from significant differences in the ability of each to repress translation (Figure 2B). PMID:18771919 At low concentrations, where the differences were greatest, Ago4, Ago3, and Ago2 were about 6-fold, 2.7-fold, and 1.6-fold more potent than Ago1, respectively. PMID:19383768 Our findings indicate that TNRC6A, TNRC6B, and TNRC6C are recruited to miRNA targets through an interaction between their N-terminal domain and an Argonaute protein; the TNRC6s then promote translational repression and/or degradation of miRNA targets through a C-terminal silencing domain. |
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Download this section (compressed HTML)Q: How should GO:0035279 and GO:0090625 names and synonyms be reconciled with their target-cleavage definitions, so NOT annotations on nonslicing Argonautes do not imply an absence of TNRC6-mediated decay?
Q: Does GO:0070578 describe only the DICER1βTARBP2βAGO2 trimer in its current definition, or should AGO1-containing loading intermediates have a separately supported complex representation?
Q: Do the AGO1-dependent TNFAIP3 assays in PMID:26764146 establish regulation of the NIK/non-canonical NF-kappaB branch specifically, and is the same mechanism supported in human AGO1?
Q: Does AGO1 itself contact promoter DNA in the let-7i/IL2 system, or is its sequence-directed occupancy mediated by the bound guide and other nuclear factors?
Q: What is the endogenous abundance and functional contribution of AGO1x after accounting for both sides of the 2025 readthrough-method debate?
Suggested experts: Loughran G, Eswarappa SM, Zavolan M
Experiment: Measure AGO1-specific guide and target occupancy together with translation and mRNA half-lives after paralog-specific depletion and rescue.
Hypothesis: AGO1 recruitment can separate translational repression from nonendonucleolytic decay without requiring target slicing.
Type: RNA-protein interaction profiling and kinetic RNA analysis
Experiment: Resolve the composition of human AGO1 loading intermediates and directly compare them with DICER1βTARBP2βAGO2 complexes.
Hypothesis: AGO1 duplex loading and maturation need not use the exact historical trimeric RLC composition.
Type: Endogenous complex purification and biochemical reconstitution
What is not known β curated, literature-grounded statements of the open unknowns (the inverse of core functions).
Gap: Endogenous AGO1 stop-codon readthrough efficiency and the quantitative contribution of AGO1x differ among the reported assays and remain disputed after the 2025 critique and response.
OPEN BIOLOGY
What is known: Canonical AGO1 RNA binding, RISC maturation and nonendonucleolytic silencing are independently established. No seeded GOA annotation cites the AGO1x papers. Orthogonal evidence for the reported proteoform is not negated solely by the reporter disagreement.
Significance: The reported extended proteoform has functions and localization distinct from canonical AGO1, making quantitative proteoform-specific assays important for interpreting nuclear and interferon phenotypes.
What would resolve it: Compare matched reporter designs and perform quantitative endogenous peptide measurements, with genomic controls that distinguish altered RNA regulation from loss of the C-terminal extension. Assess both PMID:40500330 and the response PMID:40500329.
Provenance (the field's own admissions):
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