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SULT2B1

Chr 19q13.33

sulfotransferase family 2B member 1

Aliases:
HSST2
MANE:
ENST00000201586.7

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Predicted protein structure

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

  • Autosomal recessive congenital ichthyosis

    BIALLELIC, autosomal or pseudoautosomal
  • Fetal anomalies

    BIALLELIC, autosomal or pseudoautosomal
  • Ichthyosis and erythrokeratoderma

    BIALLELIC, autosomal or pseudoautosomal
  • Palmoplantar keratodermas

    BIALLELIC, autosomal or pseudoautosomal

Disease associations (Open Targets)

  • ichthyosis, congenital, autosomal recessive 14

    0.69
  • congenital non-bullous ichthyosiform erythroderma

    0.56
  • Ichthyosis-hypotrichosis syndrome

    0.55
  • self-healing collodion baby

    0.46
  • ichthyosis

    0.38
  • inherited ichthyosis

    0.37
  • lamellar ichthyosis

    0.37
  • congenital reticular ichthyosiform erythroderma

    0.37
  • autosomal recessive congenital ichthyosis

    0.35
  • hereditary disease

    0.19

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Sulfotransferase 2B1

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol (PubMed:12145317, PubMed:19589875). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA) (PubMed:12145317, PubMed:16855051, PubMed:21855633, PubMed:9799594). Preferentially sulfonates cholesterol, while it also has significant activity with pregnenolone and DHEA (PubMed:12145317, PubMed:21855633). Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (PubMed:28575648)

Data sources: HGNC (CC BY 4.0), AlphaFold (CC BY 4.0, Jumper et al. Nature 2021), Genomics England PanelApp (CC BY 4.0), ClinGen, Open Targets (CC0), UniProt.

Not for sole clinical decision-making. Always verify against primary sources.