Ing5 is a Drosophila member of the inhibitor of growth (ING) family, with a C-terminal PHD finger of the type that recognizes histone H3 trimethylated at lysine 4. It is a subunit of the Enok (MOZ/MORF-type) histone acetyltransferase complex with the catalytic subunit Enok, the scaffold Br140 and Eaf6, and is required for the complex's acetylation of histone H3 lysine 23 in vivo. Through the complex it contributes to promoting the G1/S transition by restraining PCNA unloading.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005634 nucleus | EXP PMID:27198229 The Enok acetyltransferase complex interacts with Elg1 and n... | ACCEPT | Summary: Ing5 is detected in nuclear fractions. Reason: Correct; consistent across Enok complex subunits. Supporting Evidence: file:DROME/Ing5/Ing5-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Ing5 is nuclear. Reason: Correct; consistent across Enok complex subunits. Supporting Evidence: file:DROME/Ing5/Ing5-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Ing5 is nuclear. Reason: Correct; consistent across Enok complex subunits. Supporting Evidence: file:DROME/Ing5/Ing5-uniprot.txt SUBCELLULAR LOCATION: Nucleus |
| GO:0005694 chromosome | IEA GO_REF:0000044 | ACCEPT | Summary: Chromosome localization by UniProt mapping and ISS from human ING5 (UniProtKB:Q8WYH8). Reason: ING proteins bind chromatin via their PHD finger; chromosome is as precise as these sources allow. Supporting Evidence: file:DROME/Ing5/Ing5-uniprot.txt Chromosome |
| GO:0005694 chromosome | ISS GO_REF:0000024 | ACCEPT | Summary: Chromosome localization by UniProt mapping and ISS from human ING5 (UniProtKB:Q8WYH8). Reason: ING proteins bind chromatin via their PHD finger; chromosome is as precise as these sources allow. Supporting Evidence: file:DROME/Ing5/Ing5-uniprot.txt Chromosome |
| 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:0006325 chromatin organization | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA for chromatin organization (PTN008942935; donors include FB:FBgn0030945, UniProtKB:Q8WYH8 ING5, Q9UNL4 ING4, yeast proteins). Reason: Plausible via the Enok complex's histone acetylation, but general and not Ing5's own activity. |
| GO:0006355 regulation of DNA-templated transcription | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: IBA for regulation of transcription (PTN000035903; donors include UniProtKB:Q8WYH8 ING5, Q9H160 ING2, Q9UNL4 ING4). Reason: Plausible for an ING subunit of a HAT complex; no Ing5-specific Drosophila evidence on direction or targets. |
| GO:0010698 acetyltransferase activator activity | IDA PMID:27198229 The Enok acetyltransferase complex interacts with Elg1 and n... | ACCEPT | Summary: Ing5 is required for the Enok complex's H3K23 acetyltransferase activity. Reason: Depletion of Ing5 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:0032991 protein-containing complex | IEA GO_REF:0000117 | MODIFY | Summary: ARBA prediction of protein-containing complex. Reason: Correct but uninformative; replace with GO:0070776 MOZ/MORF histone acetyltransferase complex, already annotated. Proposed replacements: MOZ/MORF histone acetyltransferase complex |
| GO:0070776 MOZ/MORF histone acetyltransferase complex | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for MOZ/MORF complex (PTN000817813; donors FB:FBgn0032516 Ing5 itself and UniProtKB:Q8WYH8 ING5). Reason: Consistent with direct biochemical evidence in flies. |
| 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. |
| GO:0140002 histone H3K4me3 reader activity | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for H3K4me3 reader activity (PTN008942935; donors include human ING proteins Q8WYH8, Q9H160, Q9NXR8, Q9UK53, yeast and Arabidopsis ING proteins). Reason: The ING PHD finger that reads H3K4me3 is conserved across the family, and Ing5 is inside the clade; consistent with ING5 function in the human MOZ/MORF and HBO1 complexes. Accepted as a phylogenetic inference; H3K4me3 binding has not been measured for fly Ing5, so it is not used as the core molecular function. |
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Download this section (compressed HTML)Q: Does Drosophila Ing5 also join the HBO1/Chameau complex, as human ING5 does, and how is it partitioned between complexes?
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Download this section (compressed HTML)Inhibitor of growth family member 5 (Ing5) encodes a histone acetyltransferase that forms part of the Enok complex, which interacts with the product of elg1 to promote the G1/S transition via proliferating cell nuclear antigen (PCNA) unloading.
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