Component

Ethanolamine

Independent biological entity. Read linked claims for experimental scope and 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 acts on it

  1. Human FLVCR1 facilitated concentration-driven ethanolamine transport across the plasma membrane.

    Human FLVCR1 / SLC49A1 → Ethanolamine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/38778100.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4", "start_char": 0, "end_char": 1367, "text_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4"}
    experimental_model
    Human transporter expression, uptake, cryo-EM and mutagenesis
    exposure
    Choline/ethanolamine substrate challenges and purified transporter structures
    limitations
    Concentration-driven transport in these preparations; not proof that a single transporter supplies every tissue. Historical heme assignments are not copied as established choline mechanisms.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human proteins in experimental systems
    plain_language
    FLVCR1 can move ethanolamine across the cell boundary.
    primary_references
    [choline-p38778100] Molecular mechanism of choline and ethanolamine transport in humans. (2024). https://pubmed.ncbi.nlm.nih.gov/38778100/ DOI: 10.1038/s41586-024-07444-7
    tissue_or_cell_type
    Plasma-membrane transport
    transport_effect
    depends Recorded as concentration-driven transport, so the net direction follows the gradient.
    transport_pool
    the cytosol across the plasma membrane Recorded as concentration-driven transport, so the net direction follows the gradient.

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 230–241

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human transporter expression, uptake, cryo-EM and mutagenesis · source_derived_draft · unverified_draft

    ### choline-flvcr1-ethanolamine Human FLVCR1 facilitated concentration-driven ethanolamine transport across the plasma membrane. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: FLVCR1 can move ethanolamine across the cell boundary. organism: Human proteins in experimental systems tissue_or_cell_type: Plasma-membrane transport experimental_model: Human transporter expression, uptake, cryo-EM and mutagenesis limitations: Concentration-driven transport in these preparations; not proof that a single transporter supplies every tissue. Historical heme assignments are not copied as established choline mechanisms. exposure: Choline/ethanolamine substrate challenges and purified transporter structures evidence_span: {"source_cache": "artifacts/choline-research/38778100.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4", "start_char": 0, "end_char": 1367, "text_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4"} [choline-p38778100] Molecular mechanism of choline and ethanolamine transport in humans. (2024). https://pubmed.ncbi.nlm.nih.gov/38778100/ DOI: 10.1038/s41586-024-07444-7
    Complete structured claim and evidence

  2. Human FLVCR2 facilitated concentration-driven ethanolamine transport across the plasma membrane.

    Human FLVCR2 / SLC49A2 → Ethanolamine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/38778100.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4", "start_char": 0, "end_char": 1367, "text_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4"}
    experimental_model
    Human transporter expression, uptake, cryo-EM and mutagenesis
    exposure
    Choline/ethanolamine substrate challenges and purified transporter structures
    limitations
    Concentration-driven transport in these preparations; not proof that a single transporter supplies every tissue. Historical heme assignments are not copied as established choline mechanisms.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human proteins in experimental systems
    plain_language
    FLVCR2 can move ethanolamine across the cell boundary.
    primary_references
    [choline-p38778100] Molecular mechanism of choline and ethanolamine transport in humans. (2024). https://pubmed.ncbi.nlm.nih.gov/38778100/ DOI: 10.1038/s41586-024-07444-7
    tissue_or_cell_type
    Plasma-membrane transport
    transport_effect
    depends Recorded as concentration-driven transport, so the net direction follows the gradient.
    transport_pool
    the cytosol across the plasma membrane Recorded as concentration-driven transport, so the net direction follows the gradient.

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 256–267

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human transporter expression, uptake, cryo-EM and mutagenesis · source_derived_draft · unverified_draft

    ### choline-flvcr2-ethanolamine Human FLVCR2 facilitated concentration-driven ethanolamine transport across the plasma membrane. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: FLVCR2 can move ethanolamine across the cell boundary. organism: Human proteins in experimental systems tissue_or_cell_type: Plasma-membrane transport experimental_model: Human transporter expression, uptake, cryo-EM and mutagenesis limitations: Concentration-driven transport in these preparations; not proof that a single transporter supplies every tissue. Historical heme assignments are not copied as established choline mechanisms. exposure: Choline/ethanolamine substrate challenges and purified transporter structures evidence_span: {"source_cache": "artifacts/choline-research/38778100.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4", "start_char": 0, "end_char": 1367, "text_sha256": "0c0c95f81ece7f339f1b92631ced5244c053d1b4a4cbfd9ef964ff0640b5aed4"} [choline-p38778100] Molecular mechanism of choline and ethanolamine transport in humans. (2024). https://pubmed.ncbi.nlm.nih.gov/38778100/ DOI: 10.1038/s41586-024-07444-7
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. CEPT1 also catalyzes phosphatidylethanolamine production, unlike the human CHPT1 specificity described in the study.

    Human choline/ethanolamine phosphotransferase 1 / CEPT1 → Phosphatidylethanolamine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/choline-research/40435706.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d08b2ce68e8731e88e1204dc1b09d1301020452752a630a880ec3a2cdb0f2351", "start_char": 0, "end_char": 1339, "text_sha256": "d08b2ce68e8731e88e1204dc1b09d1301020452752a630a880ec3a2cdb0f2351"}
    experimental_model
    Human CHPT1 cryo-EM, sequence analysis and biochemical characterization
    exposure
    CDP-choline/CDP-ethanolamine substrate selectivity
    limitations
    Human CHPT1 and CEPT1 remain separate. Evolutionary suggestions about oviparous species are not asserted as human bifunctionality.
    nutrient_topic
    Choline research collection; topical membership is not evidence of a direct dietary effect. · Choline
    organism
    Human proteins; evolutionary comparisons explicitly separate
    plain_language
    The related enzymes are not interchangeable in substrate preference.
    primary_references
    [choline-p40435706] Structural basis for substrate selectivity and evolutionary insights into human choline phosphotransferase 1. (2025). https://pubmed.ncbi.nlm.nih.gov/40435706/ DOI: 10.1016/j.bbrc.2025.152082
    tissue_or_cell_type
    Membrane phospholipid synthesis

    Choline: metabolism, signaling and nutrient connections (2026-09-17) · lines 789–800

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human CHPT1 cryo-EM, sequence analysis and biochemical characterization · source_derived_draft · unverified_draft

    ### choline-cept1-pe CEPT1 also catalyzes phosphatidylethanolamine production, unlike the human CHPT1 specificity described in the study. Condition category: normal nutrient_topic: Choline research collection; topical membership is not evidence of a direct dietary effect. plain_language: The related enzymes are not interchangeable in substrate preference. organism: Human proteins; evolutionary comparisons explicitly separate tissue_or_cell_type: Membrane phospholipid synthesis experimental_model: Human CHPT1 cryo-EM, sequence analysis and biochemical characterization limitations: Human CHPT1 and CEPT1 remain separate. Evolutionary suggestions about oviparous species are not asserted as human bifunctionality. exposure: CDP-choline/CDP-ethanolamine substrate selectivity evidence_span: {"source_cache": "artifacts/choline-research/40435706.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d08b2ce68e8731e88e1204dc1b09d1301020452752a630a880ec3a2cdb0f2351", "start_char": 0, "end_char": 1339, "text_sha256": "d08b2ce68e8731e88e1204dc1b09d1301020452752a630a880ec3a2cdb0f2351"} [choline-p40435706] Structural basis for substrate selectivity and evolutionary insights into human choline phosphotransferase 1. (2025). https://pubmed.ncbi.nlm.nih.gov/40435706/ DOI: 10.1016/j.bbrc.2025.152082
    Complete structured claim and evidence

  2. Human PHOSPHO1 hydrolyzes phosphoethanolamine, releasing inorganic phosphate and ethanolamine; the enzyme requires Mg2+ in the assay.

    Phosphoethanolamine → Inorganic phosphate (Pi; protonation depends on pH) source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Purified-enzyme substrate assay
    limitations
    Catalytic capacity does not quantify phosphate supply in vivo; Pi denotes pH-dependent protonation states.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Homo sapiens
    plain_language
    PHOSPHO1 can release phosphate from a membrane-headgroup metabolite.
    primary_references
    [roberts2004] Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities (2004). https://pubmed.ncbi.nlm.nih.gov/15175005/ DOI: 10.1042/BJ20040511
    tissue_or_cell_type
    Recombinant enzyme; mineralizing-cell context

    Calcium: mechanism-first literature curation (2026-09-17) · lines 897–906

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

    ### phospho1-phosphoethanolamine-hydrolysis Human PHOSPHO1 hydrolyzes phosphoethanolamine, releasing inorganic phosphate and ethanolamine; the enzyme requires Mg2+ in the assay. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: PHOSPHO1 can release phosphate from a membrane-headgroup metabolite. organism: Homo sapiens tissue_or_cell_type: Recombinant enzyme; mineralizing-cell context experimental_model: Purified-enzyme substrate assay limitations: Catalytic capacity does not quantify phosphate supply in vivo; Pi denotes pH-dependent protonation states. [roberts2004] Human PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities (2004). https://pubmed.ncbi.nlm.nih.gov/15175005/ DOI: 10.1042/BJ20040511
    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