Component
Histone H3 unmethylated at K4
Protein-bound site or substrate state, not free dietary L-lysine. Sequence and assay context limit the relationship.
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
SETD7 transfers a methyl group from SAM to histone H3 Lys4 in peptide assays.
Experimental context and source evidence
- experimental_model
- Purified human SET7/9 structure and H3-peptide assays.
- limitations
- Peptide activity does not establish SETD7 as the dominant H3K4 writer in every chromatin context. 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
- SAM provides the methyl group; the protein-bound lysine receives it.
- primary_references
- [setd7-2002] Crystal structure and functional analysis of the histone methyltransferase SET7/9 (2002). https://pubmed.ncbi.nlm.nih.gov/12372304/ DOI: 10.1016/s0092-8674(02)00964-9
- tissue_or_cell_type
- Not specified as a whole tissue; see experimental model.
L-Lysine: mechanism-first literature curation (2026-09-17) · lines 547–555
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human SET7/9 structure and H3-peptide assays. · source_derived_draft · unverified_draft
### setd7-h3k4-methylation SETD7 transfers a methyl group from SAM to histone H3 Lys4 in peptide assays. Plain language: SAM provides the methyl group; the protein-bound lysine receives it. Condition category: normal organism: Human tissue_or_cell_type: Not specified as a whole tissue; see experimental model. experimental_model: Purified human SET7/9 structure and H3-peptide assays. limitations: Peptide activity does not establish SETD7 as the dominant H3K4 writer in every chromatin context. This reaction modifies lysine already in a protein. It does not show that extra oral lysine increases the reaction or improves a clinical outcome. [setd7-2002] Crystal structure and functional analysis of the histone methyltransferase SET7/9 (2002). https://pubmed.ncbi.nlm.nih.gov/12372304/ DOI: 10.1016/s0092-8674(02)00964-9
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.