Component
Human phosphoseryl-tRNA kinase / PSTK
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 it acts on
Human PSTK phosphorylates serine attached to tRNA Sec as part of the specialized selenocysteine synthesis pathway.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Purified human PSTK with tRNA substrates; comparison with KTI12.
- limitations
- This is tRNA-bound serine chemistry, not direct conversion of free serine into free selenocysteine.
- nutrient_topic
- L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
- plain_language
- A serine molecule already loaded onto a tRNA is processed into a selenium-containing amino-acid precursor.
- primary_references
- Same but different - Molecular comparison of human KTI12 and PSTK. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33417976/ · DOI 10.1016/j.bbamcr.2020.118945
L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 382–388
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Purified human PSTK with tRNA substrates; comparison with KTI12. · source_derived_draft · unverified_draft
## l-serine-pstk-serine A serine molecule already loaded onto a tRNA is processed into a selenium-containing amino-acid precursor. Human PSTK phosphorylates serine attached to tRNA Sec as part of the specialized selenocysteine synthesis pathway. Model: Purified human PSTK with tRNA substrates; comparison with KTI12. Limitations: This is tRNA-bound serine chemistry, not direct conversion of free serine into free selenocysteine. Evidence access: Primary abstract Same but different - Molecular comparison of human KTI12 and PSTK. · 2021 · https://pubmed.ncbi.nlm.nih.gov/33417976/ · DOI 10.1016/j.bbamcr.2020.118945
Complete structured claim and evidence
Where it participates (unsigned role)
Human SerRS also attached L-serine to tRNA Sec, initiating the specialized pathway that later converts its attached amino acid into selenocysteine.
Experimental context and source evidence
- evidence_access
- Primary abstract
- experimental_model
- Human cytosolic SerRS substrate-recognition and aminoacylation experiments.
- limitations
- Serylation does not itself add selenium; PSTK and SEPSECS act in later steps.
- nutrient_topic
- L-Serine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Serine
- plain_language
- The same loading enzyme feeds both ordinary protein synthesis and selenium-dependent decoding.
- primary_references
- Insights into substrate promiscuity of human seryl-tRNA synthetase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28808125/ · DOI 10.1261/rna.061069.117
L-Serine: synthesis, one-carbon metabolism, lipids and cross-nutrient mechanisms (2026-09-19) · lines 454–460
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cytosolic SerRS substrate-recognition and aminoacylation experiments. · source_derived_draft · unverified_draft
## l-serine-serrs-selenium-route The same loading enzyme feeds both ordinary protein synthesis and selenium-dependent decoding. Human SerRS also attached L-serine to tRNA Sec, initiating the specialized pathway that later converts its attached amino acid into selenocysteine. Model: Human cytosolic SerRS substrate-recognition and aminoacylation experiments. Limitations: Serylation does not itself add selenium; PSTK and SEPSECS act in later steps. Evidence access: Primary abstract Insights into substrate promiscuity of human seryl-tRNA synthetase. · 2017 · https://pubmed.ncbi.nlm.nih.gov/28808125/ · DOI 10.1261/rna.061069.117
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.