Eaf6 is the Drosophila homolog of the small, conserved MEAF6/EAF6 subunit shared by several MYST histone acetyltransferase complexes. It is a subunit of the Enok (MOZ/MORF-type) complex with the catalytic subunit Enok, the scaffold Br140 and Ing5, and is required for the complex's acetylation of histone H3 lysine 23 in vivo. By orthology with yeast and human EAF6 it is inferred to belong also to Tip60/NuA4-type acetyltransferase complexes, but direct evidence for this in flies is unresolved. Through the Enok complex it contributes to H3K23 acetylation and to promoting the G1/S transition.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000123 histone acetyltransferase complex | IEA GO_REF:0000120 | MODIFY | Summary: Electronic histone acetyltransferase complex annotation (EAF6 family). Reason: Correct but general; the HAT complex experimentally established for fly Eaf6 is the Enok (MOZ/MORF-type) complex, already annotated. NuA4 is not used as a replacement because fly NuA4 membership is not established (see the GO:0035267 rows). Proposed replacements: MOZ/MORF histone acetyltransferase complex |
| GO:0005634 nucleus | EXP PMID:27198229 The Enok acetyltransferase complex interacts with Elg1 and n... | ACCEPT | Summary: Eaf6 is detected in nuclear fractions. Reason: Correct; consistent across Enok complex subunits. Supporting Evidence: file:DROME/Eaf6/Eaf6-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: Eaf6 is nuclear. Reason: Correct; consistent across Enok complex subunits. Supporting Evidence: file:DROME/Eaf6/Eaf6-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0006271 DNA strand elongation involved in DNA replication | IDA PMID:27198229 The Enok acetyltransferase complex interacts with Elg1 and n... | MODIFY | Summary: The Enok complex promotes the G1/S transition by restraining Elg1-mediated PCNA unloading. Reason: The study shows a G1/S block and reduced chromatin-bound PCNA after Enok depletion and an Enok complex-Elg1 interaction; it does not measure DNA strand elongation. Replace with GO:0000082 G1/S transition of mitotic cell cycle. Shared complex process treated identically across the four Enok complex subunits. Proposed replacements: G1/S transition of mitotic cell cycle Supporting Evidence: PMID:27198229 Depletion of Enok resulted in an Elg1-dependent block at the G1/S transition and reduced chromatin-bound PCNA levels. |
| GO:0010698 acetyltransferase activator activity | IDA PMID:27198229 The Enok acetyltransferase complex interacts with Elg1 and n... | ACCEPT | Summary: Eaf6 is required for the Enok complex's H3K23 acetyltransferase activity. Reason: Depletion of Eaf6 reduces H3K23ac; shared term treated identically across Br140, Ing5 and Eaf6. Supporting Evidence: PMID:27198229 Depletion of any of the four subunits led to reductions in the H3K23ac levels without affecting the H3K14ac levels PMID:27198229 we concluded that all four subunits are important for full HAT activity of the Enok complex |
| GO:0035267 NuA4 histone acetyltransferase complex | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for NuA4 complex (PTN000336570; donors FB:FBgn0035624 Eaf6 itself, CGD:CAL0000192577, UniProtKB:Q9HAF1 MEAF6). Reason: Accepted as a phylogenetic inference - EAF6/MEAF6 is a NuA4/TIP60 subunit in yeast, Candida and human, and fly Eaf6 is inside that clade. Fly-specific experimental support is unresolved (both experimental rows are UNDECIDED), so NuA4 is not used as a core function. |
| GO:0035267 NuA4 histone acetyltransferase complex | IDA PMID:15528408 Acetylation by Tip60 is required for selective histone varia... | UNDECIDED | Summary: Eaf6 reported in the purified dTip60 complex. Reason: The cached record is abstract-only and does not mention Eaf6, so the evidence cannot be checked here; stable membership of fly Eaf6 in Tip60/NuA4-type complexes is unresolved (Eaf6 is absent from the stringent DOM-A purification of PMID:32432549). Left undecided, consistent with the other experimental NuA4 row. |
| GO:0035267 NuA4 histone acetyltransferase complex | IPI PMID:32432549 Drosophila SWR1 and NuA4 complexes are defined by DOMINO iso... | UNDECIDED | Summary: IPI placing Eaf6 in the DOM-A (NuA4-like) complex. Reason: The cached full text of this paper does not mention Eaf6, and the deep-research synthesis reports that Eaf6 was absent from the stringent DOM-A purification described there (a later preprint links Eaf6 abundance to Tip60). The curator may have used supplementary proteomic data not visible here, so this row is left undecided rather than removed. Supporting Evidence: file:DROME/Eaf6/Eaf6-deep-research-falcon.md but neither demonstrates direct binding nor resolves why Eaf6 was absent from the stringent 2020 DOM-A purification |
| GO:0045893 positive regulation of DNA-templated transcription | NAS PMID:32432549 Drosophila SWR1 and NuA4 complexes are defined by DOMINO iso... | KEEP AS NON CORE | Summary: DOM-A and DOM-B complexes are necessary for transcriptional regulation. Reason: Plausible contribution through HAT complexes, but stated without Eaf6-specific data; kept non-core. Supporting Evidence: PMID:32432549 Both complexes are necessary for transcriptional regulation but through different mechanisms. |
| GO:0070776 MOZ/MORF histone acetyltransferase complex | IDA PMID:27198229 The Enok acetyltransferase complex interacts with Elg1 and n... | ACCEPT | Summary: Subunit of the Enok (KAT6, MOZ/MORF-type) acetyltransferase complex. Reason: Core complex. Enok, Br140, Ing5 and Eaf6 co-purify reciprocally and each is required for the complex's H3K23 acetylation; shared complex term treated identically across the four subunits. Supporting Evidence: PMID:27198229 MudPIT analysis of Flag affinity purifications of Flag-HA-tagged Enok, Br140, Eaf6, and Ing5 showed copurification of these four components. |
| GO:0070776 MOZ/MORF histone acetyltransferase complex | IPI PMID:27198229 The Enok acetyltransferase complex interacts with Elg1 and n... | ACCEPT | Summary: Subunit of the Enok (KAT6, MOZ/MORF-type) acetyltransferase complex. Reason: Core complex. Enok, Br140, Ing5 and Eaf6 co-purify reciprocally and each is required for the complex's H3K23 acetylation; shared complex term treated identically across the four subunits. Supporting Evidence: PMID:27198229 MudPIT analysis of Flag affinity purifications of Flag-HA-tagged Enok, Br140, Eaf6, and Ing5 showed copurification of these four components. |
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