Component
Human KEOPS catalytic subunit / OSGEP
Context-specific entity; species, compartment and exposure are stated on each claim.
2 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
Cytosolic t6A formation uses sequential YRDC and OSGEP activities, with OSGEP operating within the KEOPS complex.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Primary human genetics and structural study of the t6A pathway.
- limitations
- OSGEP and mitochondrial OSGEPL1 are distinct proteins; threonyl-tRNA loading is a separate reaction.
- nutrient_topic
- L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
- plain_language
- The cytosol uses a different downstream machine from the mitochondrial pathway.
- primary_references
- Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x
L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 442–448
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Primary human genetics and structural study of the t6A pathway. · source_derived_draft · unverified_draft
## l-threonine-cytosolic-keops The cytosol uses a different downstream machine from the mitochondrial pathway. Cytosolic t6A formation uses sequential YRDC and OSGEP activities, with OSGEP operating within the KEOPS complex. Model: Primary human genetics and structural study of the t6A pathway. Limitations: OSGEP and mitochondrial OSGEPL1 are distinct proteins; threonyl-tRNA loading is a separate reaction. Evidence access: Primary abstract Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x
Complete structured claim and evidence
Where it participates (unsigned role)
Human GON7 became partly structured upon binding LAGE3 in the GON7/LAGE3/OSGEP subcomplex, supporting its proposed role in KEOPS stability and organization.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Crystal structure and cellular characterization of human KEOPS components.
- limitations
- The structural observation supports a stabilizing role; it does not establish that extra threonine repairs a subunit defect.
- nutrient_topic
- L-Threonine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Threonine
- plain_language
- An organizing subunit helps assemble the RNA-modifying machine.
- primary_references
- Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x
L-Threonine: translation, intestinal barrier, metabolism and cross-nutrient mechanisms (2026-09-19) · lines 450–456
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Crystal structure and cellular characterization of human KEOPS components. · source_derived_draft · unverified_draft
## l-threonine-gon7-complex An organizing subunit helps assemble the RNA-modifying machine. Human GON7 became partly structured upon binding LAGE3 in the GON7/LAGE3/OSGEP subcomplex, supporting its proposed role in KEOPS stability and organization. Model: Crystal structure and cellular characterization of human KEOPS components. Limitations: The structural observation supports a stabilizing role; it does not establish that extra threonine repairs a subunit defect. Evidence access: Primary abstract Defects in t6A tRNA modification due to GON7 and YRDC mutations lead to Galloway-Mowat syndrome. · 2019 · https://pubmed.ncbi.nlm.nih.gov/31481669/ · DOI 10.1038/s41467-019-11951-x
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.