Component

IPMK (human inositol phosphate multikinase)

IPMK (human inositol phosphate multikinase). Species, exposure and limitations are retained in each linked claim.

3 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. Human IPMK has IP3 3-kinase activity, producing inositol 1,3,4,5-tetrakisphosphate.

    IPMK (human inositol phosphate multikinase) → IP3 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/28882892.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db", "start_char": 0, "end_char": 1781, "text_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db"}
    experimental_model
    Crystal structures and targeted human IPMK mutants
    exposure
    IP3 and PI(4,5)P2 substrate binding and phosphorylation
    limitations
    Human substrate specificity differs from yeast and plant orthologs; do not merge their regioselectivity.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human protein
    plain_language
    Soluble IP3 can be redirected into a more highly phosphorylated molecule.
    primary_references
    [ino-p28882892] Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. (2017). https://pubmed.ncbi.nlm.nih.gov/28882892/ DOI: 10.1074/jbc.m117.801845
    tissue_or_cell_type
    Purified IPMK

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 678–689

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures and targeted human IPMK mutants · source_derived_draft · unverified_draft

    ### ino-ipmk-ip4 Human IPMK has IP3 3-kinase activity, producing inositol 1,3,4,5-tetrakisphosphate. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: Soluble IP3 can be redirected into a more highly phosphorylated molecule. organism: Human protein tissue_or_cell_type: Purified IPMK experimental_model: Crystal structures and targeted human IPMK mutants limitations: Human substrate specificity differs from yeast and plant orthologs; do not merge their regioselectivity. exposure: IP3 and PI(4,5)P2 substrate binding and phosphorylation evidence_span: {"source_cache": "artifacts/inositol-research/28882892.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db", "start_char": 0, "end_char": 1781, "text_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db"} [ino-p28882892] Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. (2017). https://pubmed.ncbi.nlm.nih.gov/28882892/ DOI: 10.1074/jbc.m117.801845
    Complete structured claim and evidence

  2. Recombinant human IPMK phosphorylated IP3 at positions 3 and 6, reaching inositol 1,3,4,5,6-pentakisphosphate.

    IPMK (human inositol phosphate multikinase) → Inositol 1,3,4,5,6-pentakisphosphate source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/12027805.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d015b4f1e5198aceb869411c91fd2ab00da093fb573c1b195305fe8adfe66b26", "start_char": 0, "end_char": 1282, "text_sha256": "d015b4f1e5198aceb869411c91fd2ab00da093fb573c1b195305fe8adfe66b26"}
    experimental_model
    Human cDNA cloning and recombinant kinase characterization
    exposure
    IP3 phosphorylation and product analysis
    limitations
    Enzyme activity and expression-system localization do not establish dietary effects or a single obligatory route for all cells.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human protein expressed in bacteria and mammalian cells
    plain_language
    The multikinase supplies a route from IP3 toward the five-phosphate precursor of InsP6.
    primary_references
    [ino-p12027805] The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization. (2002). https://pubmed.ncbi.nlm.nih.gov/12027805/ DOI: 10.1042/bj20020327
    tissue_or_cell_type
    Recombinant enzyme and tagged-protein localization

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 704–715

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cDNA cloning and recombinant kinase characterization · source_derived_draft · unverified_draft

    ### ino-ipmk-ip5 Recombinant human IPMK phosphorylated IP3 at positions 3 and 6, reaching inositol 1,3,4,5,6-pentakisphosphate. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: The multikinase supplies a route from IP3 toward the five-phosphate precursor of InsP6. organism: Human protein expressed in bacteria and mammalian cells tissue_or_cell_type: Recombinant enzyme and tagged-protein localization experimental_model: Human cDNA cloning and recombinant kinase characterization limitations: Enzyme activity and expression-system localization do not establish dietary effects or a single obligatory route for all cells. exposure: IP3 phosphorylation and product analysis evidence_span: {"source_cache": "artifacts/inositol-research/12027805.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d015b4f1e5198aceb869411c91fd2ab00da093fb573c1b195305fe8adfe66b26", "start_char": 0, "end_char": 1282, "text_sha256": "d015b4f1e5198aceb869411c91fd2ab00da093fb573c1b195305fe8adfe66b26"} [ino-p12027805] The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization. (2002). https://pubmed.ncbi.nlm.nih.gov/12027805/ DOI: 10.1042/bj20020327
    Complete structured claim and evidence

  3. Human IPMK also has PI(4,5)P2 3-kinase activity, producing PI(3,4,5)P3.

    IPMK (human inositol phosphate multikinase) → Phosphatidylinositol 4,5-bisphosphate source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/28882892.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db", "start_char": 0, "end_char": 1781, "text_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db"}
    experimental_model
    Crystal structures and targeted human IPMK mutants
    exposure
    IP3 and PI(4,5)P2 substrate binding and phosphorylation
    limitations
    Human substrate specificity differs from yeast and plant orthologs; do not merge their regioselectivity.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human protein
    plain_language
    One enzyme acts on both soluble inositol phosphates and a membrane lipid.
    primary_references
    [ino-p28882892] Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. (2017). https://pubmed.ncbi.nlm.nih.gov/28882892/ DOI: 10.1074/jbc.m117.801845
    tissue_or_cell_type
    Purified IPMK

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 691–702

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Crystal structures and targeted human IPMK mutants · source_derived_draft · unverified_draft

    ### ino-ipmk-pip3 Human IPMK also has PI(4,5)P2 3-kinase activity, producing PI(3,4,5)P3. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: One enzyme acts on both soluble inositol phosphates and a membrane lipid. organism: Human protein tissue_or_cell_type: Purified IPMK experimental_model: Crystal structures and targeted human IPMK mutants limitations: Human substrate specificity differs from yeast and plant orthologs; do not merge their regioselectivity. exposure: IP3 and PI(4,5)P2 substrate binding and phosphorylation evidence_span: {"source_cache": "artifacts/inositol-research/28882892.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db", "start_char": 0, "end_char": 1781, "text_sha256": "39494635d8bd1a8a8df3ac71f8aa6c5f6440bd3c6fa7cb4756e52d572a8f16db"} [ino-p28882892] Structural features of human inositol phosphate multikinase rationalize its inositol phosphate kinase and phosphoinositide 3-kinase activities. (2017). https://pubmed.ncbi.nlm.nih.gov/28882892/ DOI: 10.1074/jbc.m117.801845
    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