Component

Human pantothenate kinase 4 / PANK4

Human pantothenate kinase 4 / PANK4. See linked evidence for experiment-specific scope.

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 it acts on

  1. Re-expression of active PANK4 in PANK4-knockout AKT p.E17K/+ MCF10A cells suppressed newly synthesized CoA, whereas phosphatase-inactive mutants did not reproduce the suppression.

    Human pantothenate kinase 4 / PANK4 → Cellular de novo coenzyme A synthesis source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays
    exposure
    Wild-type versus D623A or D659A PANK4 re-expression; 3-hour carbon-13/nitrogen-15 vitamin-B5 labelling with growth factors.
    limitations
    Engineered cellular PI3K–AKT context; isotope concentration not verified. No claim that PANK4 controls every tissue or that dietary B5 produces the same response.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    PANK4 phosphatase activity can reduce new CoA production in cultured cells.
    primary_references
    [b5-bio-dibble2022] PI3K drives the de novo synthesis of coenzyme A from vitamin B5. (2022). https://pubmed.ncbi.nlm.nih.gov/35896750/ DOI: 10.1038/s41586-022-04984-8
    tissue_or_cell_type
    Human MCF10A mammary epithelial cells

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (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 · Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays · source_derived_draft · unverified_draft

    ### b5-bio-pank4-flux-suppression Re-expression of active PANK4 in PANK4-knockout AKT p.E17K/+ MCF10A cells suppressed newly synthesized CoA, whereas phosphatase-inactive mutants did not reproduce the suppression. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: PANK4 phosphatase activity can reduce new CoA production in cultured cells. organism: Homo sapiens tissue_or_cell_type: Human MCF10A mammary epithelial cells experimental_model: Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays limitations: Engineered cellular PI3K–AKT context; isotope concentration not verified. No claim that PANK4 controls every tissue or that dietary B5 produces the same response. exposure: Wild-type versus D623A or D659A PANK4 re-expression; 3-hour carbon-13/nitrogen-15 vitamin-B5 labelling with growth factors. cross_nutrient: false [b5-bio-dibble2022] PI3K drives the de novo synthesis of coenzyme A from vitamin B5. (2022). https://pubmed.ncbi.nlm.nih.gov/35896750/ DOI: 10.1038/s41586-022-04984-8
    Complete structured claim and evidence

  2. Immunopurified full-length human PANK4 hydrolyzed phosphate from 4′-phosphopantetheine; D623A or D659A substitutions abolished the phosphatase activity.

    Human pantothenate kinase 4 / PANK4 → 4′-Phosphopantetheine source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays
    exposure
    Primary Fig. 4 biochemical assays with immunopurified Flag-PANK4, wild type versus D623A or D659A; substrate concentration not extracted.
    limitations
    Direct phosphatase assay. Divalent-metal participation was reported, but a particular nutritional mineral requirement is not assigned from these experiments.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    PANK4 can remove a phosphate from a CoA-building intermediate.
    primary_references
    [b5-bio-dibble2022] PI3K drives the de novo synthesis of coenzyme A from vitamin B5. (2022). https://pubmed.ncbi.nlm.nih.gov/35896750/ DOI: 10.1038/s41586-022-04984-8
    tissue_or_cell_type
    Purified recombinant protein; no intact tissue

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 665–676

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays · source_derived_draft · unverified_draft

    ### b5-bio-pank4-phosphatase Immunopurified full-length human PANK4 hydrolyzed phosphate from 4′-phosphopantetheine; D623A or D659A substitutions abolished the phosphatase activity. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: PANK4 can remove a phosphate from a CoA-building intermediate. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays limitations: Direct phosphatase assay. Divalent-metal participation was reported, but a particular nutritional mineral requirement is not assigned from these experiments. exposure: Primary Fig. 4 biochemical assays with immunopurified Flag-PANK4, wild type versus D623A or D659A; substrate concentration not extracted. cross_nutrient: false [b5-bio-dibble2022] PI3K drives the de novo synthesis of coenzyme A from vitamin B5. (2022). https://pubmed.ncbi.nlm.nih.gov/35896750/ DOI: 10.1038/s41586-022-04984-8
    Complete structured claim and evidence

  3. Biochemical testing found that human PANK4 lacks pantothenate kinase activity, unlike active PANK1–3 enzymes.

    Human pantothenate kinase 4 / PANK4 → Pantothenate (vitamin B5) source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Recombinant human PANK4 biochemistry with evolutionary sequence and mutagenesis comparisons
    exposure
    Recombinant enzyme and catalytic-residue mutagenesis comparison; assay concentrations not extracted.
    limitations
    This is evidence about an enzyme paralogue, not loss of all cellular pantothenate phosphorylation. Other species PANK4 enzymes differ.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    The protein named PANK4 is not another working B5 kinase in humans.
    primary_references
    [b5-bio-pank4pseudo] Human pantothenate kinase 4 is a pseudo-pantothenate kinase. (2019). https://pubmed.ncbi.nlm.nih.gov/30927326/ DOI: 10.1002/pro.3611
    tissue_or_cell_type
    Purified recombinant protein; no intact tissue

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (2026-09-17) · lines 652–663

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Recombinant human PANK4 biochemistry with evolutionary sequence and mutagenesis comparisons · source_derived_draft · unverified_draft

    ### b5-bio-pank4-pseudokinase Biochemical testing found that human PANK4 lacks pantothenate kinase activity, unlike active PANK1–3 enzymes. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: The protein named PANK4 is not another working B5 kinase in humans. organism: Homo sapiens tissue_or_cell_type: Purified recombinant protein; no intact tissue experimental_model: Recombinant human PANK4 biochemistry with evolutionary sequence and mutagenesis comparisons limitations: This is evidence about an enzyme paralogue, not loss of all cellular pantothenate phosphorylation. Other species PANK4 enzymes differ. exposure: Recombinant enzyme and catalytic-residue mutagenesis comparison; assay concentrations not extracted. cross_nutrient: false [b5-bio-pank4pseudo] Human pantothenate kinase 4 is a pseudo-pantothenate kinase. (2019). https://pubmed.ncbi.nlm.nih.gov/30927326/ DOI: 10.1002/pro.3611
    Complete structured claim and evidence

What acts on it

  1. AKT phosphorylation of PANK4 relieved its suppression of de novo CoA synthesis in the study models.

    AKT serine/threonine kinase family → Human pantothenate kinase 4 / PANK4 source_derived_draftungraded
    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays
    exposure
    PI3K–AKT signalling and PANK4 phosphorylation manipulations; no nutrient dosing trial.
    limitations
    Primary abstract with supporting cellular assays; mechanism is not a rationale for treating insulin signalling or increasing B5 intake.
    nutrient_topic
    Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. · Pantothenate (vitamin B5)
    organism
    Homo sapiens
    plain_language
    Growth-factor signalling can ease the PANK4 brake on CoA production.
    primary_references
    [b5-bio-dibble2022] PI3K drives the de novo synthesis of coenzyme A from vitamin B5. (2022). https://pubmed.ncbi.nlm.nih.gov/35896750/ DOI: 10.1038/s41586-022-04984-8
    tissue_or_cell_type
    Human cultured-cell models

    Pantothenic acid (vitamin B5): coenzyme A, deficiency and nutrient interactions (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 · Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays · source_derived_draft · unverified_draft

    ### b5-bio-akt-pank4-regulation AKT phosphorylation of PANK4 relieved its suppression of de novo CoA synthesis in the study models. Condition category: normal nutrient_topic: Pantothenic acid (vitamin B5) research collection; topical membership is not evidence of a direct dietary effect. plain_language: Growth-factor signalling can ease the PANK4 brake on CoA production. organism: Homo sapiens tissue_or_cell_type: Human cultured-cell models experimental_model: Human cultured-cell metabolomics and isotope tracing, PANK4 editing/re-expression and immunopurified human PANK4 phosphatase assays limitations: Primary abstract with supporting cellular assays; mechanism is not a rationale for treating insulin signalling or increasing B5 intake. exposure: PI3K–AKT signalling and PANK4 phosphorylation manipulations; no nutrient dosing trial. cross_nutrient: false [b5-bio-dibble2022] PI3K drives the de novo synthesis of coenzyme A from vitamin B5. (2022). https://pubmed.ncbi.nlm.nih.gov/35896750/ DOI: 10.1038/s41586-022-04984-8
    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