Component

EP300

Independent protein record; interpretation is limited by each linked claim and its study context.

4 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. EP300 knockdown induced autophagy and reduced mTORC1 activity in the acetyltransferase screen.

    EP300 → Human cultured-cell autophagic flux source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human-cell RNA interference screen of 43 acetyltransferases.
    limitations
    Does not prove all spermidine effects are mediated by EP300.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    Removing a regulator supports a causal pathway.
    primary_references
    Spermidine induces autophagy by inhibiting the acetyltransferase EP300. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25526088/ · DOI 10.1038/cdd.2014.215
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 174–180

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human-cell RNA interference screen of 43 acetyltransferases. · source_derived_draft · unverified_draft

    ## spermidine-ep300-loss Removing a regulator supports a causal pathway. EP300 knockdown induced autophagy and reduced mTORC1 activity in the acetyltransferase screen. Model: Human-cell RNA interference screen of 43 acetyltransferases. Limitations: Does not prove all spermidine effects are mediated by EP300. Evidence access: Primary abstract Spermidine induces autophagy by inhibiting the acetyltransferase EP300. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25526088/ · DOI 10.1038/cdd.2014.215
    Complete structured claim and evidence

  2. EP300 transfers an acetyl group from acetyl-CoA to a protein lysine side chain.

    EP300 → Protein-bound lysine residue source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Human p300 catalytic-domain structure and biochemical assays.
    limitations
    This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome.
    organism
    Human
    plain_language
    Acetyl groups can be written onto lysines already present in proteins.
    primary_references
    [p300-2008] The structural basis of protein acetylation by the p300/CBP transcriptional coactivator (2008). https://pubmed.ncbi.nlm.nih.gov/18273021/ DOI: 10.1038/nature06546
    tissue_or_cell_type
    Not specified as a whole tissue; see experimental model.

    L-Lysine: mechanism-first literature curation (2026-09-17) · lines 527–535

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human p300 catalytic-domain structure and biochemical assays. · source_derived_draft · unverified_draft

    ### ep300-lysine-acetylation EP300 transfers an acetyl group from acetyl-CoA to a protein lysine side chain. Plain language: Acetyl groups can be written onto lysines already present in proteins. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Human p300 catalytic-domain structure and biochemical assays. limitations: This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [p300-2008] The structural basis of protein acetylation by the p300/CBP transcriptional coactivator (2008). https://pubmed.ncbi.nlm.nih.gov/18273021/ DOI: 10.1038/nature06546
    Complete structured claim and evidence

What acts on it

  1. Curcumin inhibited p300 acetyltransferase activity in the tested systems.

    Curcumin → EP300 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/curcumin-research/15383533.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e9d4ab7547b17835d52e1845559cc5eaead6c13d30c54d48d716ee3b9cff94f1", "start_char": 0, "end_char": 1248, "text_sha256": "e9d4ab7547b17835d52e1845559cc5eaead6c13d30c54d48d716ee3b9cff94f1"}
    experimental_model
    Purified acetyltransferase and cell experiments
    exposure
    Curcumin tested against p300/CBP and PCAF; exact concentrations not resolved from abstract
    limitations
    Historical biochemical specificity is limited to the tested comparators, not proof of selective human epigenome reprogramming. No antiviral treatment conclusion is imported.
    nutrient_topic
    Curcumin research collection; topical membership is not evidence of a direct dietary effect. · Curcumin
    organism
    Human protein/cell assay systems
    plain_language
    The study reported an effect on an enzyme that adds acetyl marks.
    primary_references
    [curcumin-p15383533] Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription. (2004). https://pubmed.ncbi.nlm.nih.gov/15383533/ DOI: 10.1074/jbc.m409024200
    tissue_or_cell_type
    Histone and nonhistone acetylation

    Curcumin: metabolism, signaling and nutrient connections (2026-09-17) · lines 554–565

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified acetyltransferase and cell experiments · source_derived_draft · unverified_draft

    ### curcumin-ep300 Curcumin inhibited p300 acetyltransferase activity in the tested systems. Condition category: normal nutrient_topic: Curcumin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The study reported an effect on an enzyme that adds acetyl marks. organism: Human protein/cell assay systems tissue_or_cell_type: Histone and nonhistone acetylation experimental_model: Purified acetyltransferase and cell experiments limitations: Historical biochemical specificity is limited to the tested comparators, not proof of selective human epigenome reprogramming. No antiviral treatment conclusion is imported. exposure: Curcumin tested against p300/CBP and PCAF; exact concentrations not resolved from abstract evidence_span: {"source_cache": "artifacts/curcumin-research/15383533.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "e9d4ab7547b17835d52e1845559cc5eaead6c13d30c54d48d716ee3b9cff94f1", "start_char": 0, "end_char": 1248, "text_sha256": "e9d4ab7547b17835d52e1845559cc5eaead6c13d30c54d48d716ee3b9cff94f1"} [curcumin-p15383533] Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription. (2004). https://pubmed.ncbi.nlm.nih.gov/15383533/ DOI: 10.1074/jbc.m409024200
    Complete structured claim and evidence

  2. Spermidine inhibited acetyltransferase activity of recombinant EP300 in vitro.

    Spermidine → EP300 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human EP300 assay with companion human-cell experiments.
    limitations
    Biochemical inhibition is not proof of selective target engagement after dietary exposure.
    nutrient_topic
    Spermidine collection; molecular form, preparation, species, exposure and manipulation remain explicit. · Spermidine
    plain_language
    One route changes protein acetylation.
    primary_references
    Spermidine induces autophagy by inhibiting the acetyltransferase EP300. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25526088/ · DOI 10.1038/cdd.2014.215

    Spermidine: biosynthesis, hypusination, transport and cross-nutrient mechanisms (2026-09-19) · lines 150–156

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human EP300 assay with companion human-cell experiments. · source_derived_draft · unverified_draft

    ## spermidine-ep300 One route changes protein acetylation. Spermidine inhibited acetyltransferase activity of recombinant EP300 in vitro. Model: Recombinant human EP300 assay with companion human-cell experiments. Limitations: Biochemical inhibition is not proof of selective target engagement after dietary exposure. Evidence access: Primary abstract Spermidine induces autophagy by inhibiting the acetyltransferase EP300. · 2015 · https://pubmed.ncbi.nlm.nih.gov/25526088/ · DOI 10.1038/cdd.2014.215
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards