Affinage

SULT2A1

Sulfotransferase 2A1 · UniProt Q06520

Length
285 aa
Mass
33.8 kDa
Annotated
2026-06-10
52 papers in source corpus 23 papers cited in narrative 22 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

SULT2A1 is a cytosolic hydroxysteroid sulfotransferase that catalyzes PAPS-dependent sulfonation of steroid hormones, bile acids, and amine- and hydroxyl-containing xenobiotics, functioning as the principal enzyme for steroid and drug sulfoconjugation in liver and adrenal tissue (PMID:14573603, PMID:20102295, PMID:19420132). Its catalytic cycle has been resolved as an eight-form kinetic mechanism transferring the sulfuryl group from PAPS to acceptor hydroxyls and amines (PMID:25056952), and crystal structures with androsterone and DHEA show that closely related substrates adopt distinct binding orientations governed by active-site residues (PMID:14573603). SULT2A1 acts as a homodimer in which each subunit carries a catalytic and an allosteric DHEA-binding site; dimerization enhances allosteric DHEA binding and produces the characteristic substrate inhibition, which is mechanistically explained by non-productive dead-end ternary complexes with the nucleotide product PAP and which depends on residues Tyr-238 (substrate release) and Met-137 (binding orientation) (PMID:18042734, PMID:21822453, PMID:25961208, PMID:21187059). Efficient cellular DHEA sulfation further requires a direct protein-protein interaction between SULT2A1 and PAPSS2, but not PAPSS1, channeling PAPS to the enzyme (PMID:29743239). The substrate repertoire spans DHEA, androsterone, and a graded series of bile acids whose affinity rises as hydroxylation falls—lithocholic acid being the highest-affinity acceptor (PMID:14573603, PMID:20102295)—as well as quinolone and other amine drugs for which SULT2A1 is the sole responsible human SULT (PMID:19420132), stereoisomers of alpha-hydroxytamoxifen (PMID:15371299), and hydroxylated PCB metabolites that serve as both substrates and inhibitors (PMID:17112228). SULT2A1 transcription is controlled by a network of nuclear receptors—including VDR acting with C/EBP-alpha, HNF4alpha (antagonized by PXR), ERRalpha, RORalpha/gamma, and LXRalpha (PMID:16357103, PMID:17687072, PMID:15878968, PMID:23211525, PMID:25028566)—and is post-transcriptionally suppressed by miR-495-3p and miR-486-5p and downregulated by inflammatory cytokines TNF and IL-1 (PMID:31445882, PMID:15198932).

Mechanistic history

Synthesis pass · year-by-year structured walk · 15 steps
  1. 2002 Medium

    Establishing that natural coding variation alters SULT2A1 function showed both protein abundance and dimerization as determinants of enzyme activity, defining a pharmacogenetic basis for inter-individual differences.

    Evidence Heterologous expression of coding SNP allozymes in COS-1 cells with Western blot, gel filtration, and activity assays

    PMID:11990382

    Open questions at the time
    • Phenotypic consequences in vivo not established
    • Allele frequencies and clinical correlation outside studied population unknown
  2. 2003 High

    The first crystal structure with androsterone answered how SULT2A1 accommodates structurally similar steroids, revealing distinct substrate orientations and differing kinetics for androsterone versus DHEA.

    Evidence X-ray crystallography at 2.7 Å plus in vitro kinetics of purified recombinant enzyme

    PMID:14573603

    Open questions at the time
    • Structural basis of substrate inhibition not resolved from this structure alone
    • Dimer-level allostery not captured
  3. 2004 Medium

    Inflammatory suppression of SULT2A1 linked the enzyme to acute-phase regulation of circulating steroid sulfates, showing cytokine control over DHEA sulfation capacity.

    Evidence LPS challenge in mice plus TNF/IL-1 treatment of Hep3B cells with RT-PCR, activity, and serum steroid measurement

    PMID:15198932

    Open questions at the time
    • Direct promoter/transcription-factor target of cytokine signaling not mapped
    • Reliance on mouse Sult2A1 for in vivo arm
  4. 2005 High

    Identification of VDR/C-EBP-alpha and ERRalpha cis-elements established that SULT2A1 transcription is directed by combinatorial nuclear-receptor inputs in hepatic and adrenal contexts.

    Evidence Reporter assays, EMSA, DNase footprinting, ChIP, and Co-IP for VDR/C-EBP-alpha; reporter and EMSA for ERRalpha

    PMID:15878968 PMID:16357103

    Open questions at the time
    • Relative contribution of each receptor in physiological tissue not quantified
    • Endogenous coactivator stoichiometry undefined
  5. 2007 High

    Defining HNF4alpha as a central activator antagonized by PXR clarified how xenobiotic-sensing signaling reshapes hepatic SULT2A1 expression.

    Evidence Reporter assays, in vitro binding, mutagenesis, ChIP, and siRNA in HepG2 cells and primary human hepatocytes

    PMID:17687072

    Open questions at the time
    • Mechanism by which PXR interferes with HNF4alpha activity not fully defined
    • Interplay with other identified receptors not integrated
  6. 2009 Medium

    Demonstrating SULT2A1 as the unique human SULT for quinolone N-sulfoconjugation extended its role from steroid metabolism to drug detoxification.

    Evidence Recombinant SULT panel and human liver cytosol kinetic correlation

    PMID:19420132

    Open questions at the time
    • In vivo pharmacokinetic relevance not established
    • Toxicological consequences of N-sulfo metabolites unaddressed
  7. 2010 High

    Multiple studies resolved the homodimeric, allosterically inhibited architecture: a monomeric fusion lacks substrate inhibition, two DHEA sites exist per subunit, and inhibition arises from PAP-containing dead-end complexes, explaining the enzyme's nonlinear kinetics.

    Evidence Size-exclusion chromatography, intrinsic fluorescence, and initial-velocity/equilibrium binding studies with purified recombinant enzyme

    PMID:21187059 PMID:21822453 PMID:25961208

    Open questions at the time
    • Physiological significance of substrate inhibition in vivo unclear
    • Structural snapshot of the allosteric DHEA-bound dimer not solved
  8. 2010 Medium

    Systematic bile-acid kinetics established that sulfation affinity scales inversely with hydroxyl number, positioning SULT2A1 to preferentially detoxify the most hydrophobic, toxic monohydroxy bile acids.

    Evidence Stable HEK293 expression with kinetic enzymatic assays across 15 bile acids

    PMID:20102295

    Open questions at the time
    • In vivo contribution to bile-acid homeostasis not measured
    • Competition with steroid substrates not assessed
  9. 2011 Medium

    Discovery that ERRalpha can also repress the SULT2A1 promoter by competing at overlapping nuclear-receptor elements revealed context-dependent, bidirectional control of the gene.

    Evidence Reporter deletion assays, EMSA, and ChIP in HepG2 cells

    PMID:21513704

    Open questions at the time
    • Reconciliation of activating versus repressing ERRalpha roles across tissues unresolved
    • Competing factors at the overlapping elements not all identified
  10. 2012 Medium

    RORalpha/gamma and LXRalpha were added as activators acting through promoter elements, broadening the lipid/sterol-sensing receptor network governing SULT2A1.

    Evidence Reporter assays, EMSA, ChIP, and siRNA in HepG2 cells and primary human hepatocytes (RORalpha/gamma 2012; LXRalpha 2014)

    PMID:23211525 PMID:25028566

    Open questions at the time
    • Hierarchy among the overlapping ROR/CAR and other receptor elements not resolved
    • Ligand-dependence in vivo not established
  11. 2007 High

    Mutagenesis pinpointed Tyr-238 and Met-137 as the residues governing substrate inhibition, assigning specific structural determinants to substrate release and binding orientation.

    Evidence Site-directed mutagenesis, kinetic assays, and crystal structures of Met-137 mutants

    PMID:18042734

    Open questions at the time
    • Link between these residues and the dimer-dependent allosteric site not structurally co-resolved
  12. 2014 High

    A complete eight-form, 22-rate-constant kinetic mechanism provided a quantitative description of sulfuryl transfer, anchoring all prior phenomenological kinetics in a unified scheme.

    Evidence Comprehensive in vitro kinetic analysis with independently determined rate constants

    PMID:25056952

    Open questions at the time
    • Mechanism derived in vitro; cellular PAPS channeling not incorporated
    • Allosteric inhibition not embedded in the scheme
  13. 2018 Medium

    Identifying a direct SULT2A1-PAPSS2 interaction explained selective sulfodonor channeling, connecting cofactor supply physically to the sulfotransferase.

    Evidence Proximity ligation assay, siRNA knockdown in NCI-H295R1 cells, and molecular docking

    PMID:29743239

    Open questions at the time
    • Interaction not confirmed by reciprocal structural or co-purification methods
    • Docked binding site not experimentally validated
  14. 2019 Medium

    Identification of miR-495-3p and miR-486-5p added a post-transcriptional layer of SULT2A1 control through 3'-UTR binding and mRNA destabilization.

    Evidence RNA EMSA, luciferase reporter, and miRNA gain/loss-of-function in HepG2 cells

    PMID:31445882

    Open questions at the time
    • In vivo regulatory relevance not shown
    • Upstream signals controlling these miRNAs unknown
  15. 2021 Low

    Pharmacological inputs (metformin via AMPK-CAR, dopamine D1 receptor via cAMP) were shown to modulate SULT2A1, extending its regulation to drug- and signaling-driven contexts.

    Evidence HepaRG metformin study with nuclear fractionation; HepG2 DRD1 study with RT-PCR, Western blot, cAMP, and siRNA (2014)

    PMID:24909515 PMID:33643408

    Open questions at the time
    • Single-lab studies without orthogonal mechanistic validation
    • Promoter-level targets of these signals not mapped
    • In vivo relevance unestablished

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the in vitro allosteric/substrate-inhibition mechanism and the PAPSS2-channeled, nuclear-receptor- and miRNA-regulated cellular state integrate to set tissue-specific steroid and bile-acid sulfation flux in vivo remains unresolved.
  • No structural model of the allosteric DHEA-bound dimer
  • PAPSS2 interaction lacks structural confirmation
  • Physiological consequence of substrate inhibition unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016740 transferase activity 4 GO:0016787 hydrolase activity 1
Localization
GO:0005829 cytosol 1
Pathway
R-HSA-74160 Gene expression (Transcription) 4 R-HSA-1430728 Metabolism 2 R-HSA-9748784 Drug ADME 2
Partners
CEBPAESRRAHNF4ANR1H3PAPSS2RORARORCVDR

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 Crystal structure of human DHEA-ST (SULT2A1) in complex with androsterone (ADT) solved at 2.7 Å, revealing that ADT binds with a different orientation than DHEA despite similar overall complex structure, and demonstrating that SULT2A1 catalyzes androsterone sulfation with similar kinetics but ~2-fold higher specificity and stronger substrate inhibition than DHEA. X-ray crystallography (2.7 Å), in vitro enzymatic kinetics with purified recombinant protein The Journal of biological chemistry High 14573603
2007 Active-site mutagenesis of SULT2A1 identified Tyr-238 and Met-137 as the two amino acids critical for substrate inhibition: Tyr-238 regulates release of bound substrate (Y238A mutation abolishes substrate inhibition for ADT and increases Ki for DHEA), while Met-137 controls substrate binding orientation of both DHEA and ADT. Crystal structures of Met-137 mutants confirmed these binding orientation changes. Site-directed mutagenesis, in vitro enzymatic assays, X-ray crystallography of mutant proteins Molecular pharmacology High 18042734
2014 Complete quantitative kinetic mechanism of SULT2A1 determined: the mechanism comprises eight enzyme forms interconverting via 22 rate constants, each determined independently, providing a full description of sulfuryl transfer from PAPS to acceptor hydroxyls/amines. Comprehensive kinetic analysis with independently determined rate constants; in vitro enzymatic assays The Journal of biological chemistry High 25056952
2010 SULT2A1 functions as a homodimer; a monomeric MBP-SULT2A1 fusion protein retains similar Km and Vmax for DHEA but lacks substrate inhibition. Intrinsic fluorescence showed two DHEA molecules bind each subunit (one catalytic, one allosteric); dimerization increases DHEA binding at the allosteric site, which is responsible for substrate inhibition. Size exclusion chromatography, intrinsic fluorescence binding assays, initial-rate kinetics with purified recombinant protein Hormone molecular biology and clinical investigation High 21822453 25961208
2010 Substrate inhibition of SULT2A1 by DHEA is mechanistically explained by formation of non-productive ternary dead-end complexes involving the nucleotide product PAP; equilibrium binding and initial velocity studies showed negative cooperativity in DHEA binding, consistent with involvement of both DHEA and DHEA-sulfate in these complexes. Initial velocity studies, equilibrium binding assays, in vitro enzymatic assays with purified recombinant hSULT2A1 Archives of biochemistry and biophysics Medium 21187059
2018 SULT2A1 physically interacts with PAPS synthase 2 (PAPSS2) but only weakly with PAPSS1, as demonstrated by proximity ligation assay; molecular docking identified a putative binding site for SULT2A1 within the PAPSS2 APS kinase domain. Knockdown experiments confirmed PAPSS2, but not PAPSS1, is required for efficient DHEA sulfation in adrenocortical NCI-H295R1 cells, establishing a direct protein–protein interaction underlying selective PAPS channeling to SULT2A1. Proximity ligation assay, siRNA knockdown in NCI-H295R1 cells, molecular docking The Journal of biological chemistry Medium 29743239
2002 Three non-synonymous coding SNPs in SULT2A1 (found in African-American subjects) significantly decrease enzyme activity; decreased immunoreactive protein levels are the major mechanism, though apparent Km values also vary. One variant disrupts the dimerization interface causing the allozyme to behave as a monomer by gel filtration. Heterologous expression in COS-1 cells, Western blot, gel filtration chromatography, enzyme activity assays The pharmacogenomics journal Medium 11990382
2010 SULT2A1 sulfates 15 human bile acids with Michaelis–Menten kinetics; sulfation affinity (Km) is inversely proportional to the number of hydroxyl groups—lithocholic acid (monohydroxy) shows highest affinity and cholic acid (trihydroxy) the lowest. DHEA sulfation Km = 3.8 µM, Vmax = 130.8 pmol/min/mg in stably transfected HEK293 cells. Stable HEK293 cell expression system, kinetic enzymatic assays Xenobiotica Medium 20102295
2009 SULT2A1 is the sole human cytosolic sulfotransferase responsible for N-sulfoconjugation of quinolone drugs (ciprofloxacin, moxifloxacin, garenoxacin) and other amine-containing drugs (desipramine, metoclopramide); the other five SULT isoforms tested showed no activity. Human liver cytosol N-sulfation kinetics were monophasic with Km values matching those of recombinant SULT2A1. In vitro enzymatic assays with purified recombinant SULTs and human liver cytosols, kinetic analysis Drug metabolism and disposition Medium 19420132
2005 Vitamin D receptor (VDR) induces SULT2A1 transcription through a composite element containing an imperfect inverted-repeat VDRE and a C/EBP-alpha binding site 9 bp downstream. C/EBP-alpha is essential for this induction: mutations abolish induction, C/EBP-alpha-deficient cells require cotransfected C/EBP-alpha, and C/EBP-beta cannot substitute. VDR and C/EBP-alpha form a DNA-dependent, coimmunoprecipitable complex at the element, with concurrent recruitment of coactivators p300, SRC-1, and SRC-2 (but not SRC-3). Reporter gene assays, EMSA, DNase I footprinting, antibody supershift, chromatin immunoprecipitation (ChIP), co-immunoprecipitation, site-directed mutagenesis Molecular endocrinology High 16357103
2007 HNF4α plays a central role in SULT2A1 transcription: two HNF4α-binding sites in the SULT2A1 5'-flanking region (-6160 and -54) were identified by in vitro binding and site-directed mutagenesis; HNF4α binds the endogenous gene (confirmed by ChIP). Rifampicin-activated PXR suppresses SULT2A1 by interfering with HNF4α activity; PXR knockdown by RNAi diminished this suppression. Transient transfection reporter assays, in vitro binding, site-directed mutagenesis, ChIP, siRNA knockdown in HepG2 cells, primary human hepatocytes The Journal of pharmacology and experimental therapeutics High 17687072
2005 Estrogen-related receptor alpha (ERRα) activates SULT2A1 transcription in adrenal cells: three functional ERRα-binding cis-elements (sharing SF1 similarity) were identified in the SULT2A1 5'-flanking region by serial deletion and EMSA; ERRα stimulated SULT2A1 promoter activity more strongly than SF1. Reporter gene assays, EMSA, serial deletion analysis, cotransfection experiments Endocrinology Medium 15878968
2012 RORα and RORγ transactivate SULT2A1 gene expression through a ROR response element in the SULT2A1 promoter (overlapping with a previously identified CAR response element), as demonstrated by reporter assays, EMSA, and ChIP; siRNA knockdown of RORα/RORγ reduced endogenous SULT2A1 expression in human hepatocytes. Promoter reporter assays, EMSA, ChIP, siRNA knockdown in primary human hepatocytes Molecular endocrinology Medium 23211525
2014 LXRα (NR1H3) transactivates SULT2A1 via specific binding to the -500 to -258 bp region of the SULT2A1 promoter; LXRα siRNA knockdown showed LXRα, but not LXRβ, dominantly regulates SULT2A1 expression at mRNA, protein, and enzymatic levels. Promoter reporter assays, ChIP, siRNA knockdown, enzyme activity assays in HepG2 cells and primary human hepatocytes Drug metabolism and disposition Medium 25028566
2011 ERRα represses SULT2A1 promoter transcription in HepG2 cells through two ERRα response elements (ERRE188 and ERRE155) in the -188 to -130 bp region that overlap with IR2 and DR4 nuclear receptor elements; ERRα competes with other nuclear receptors for binding to these elements, confirmed by EMSA and ChIP. Reporter gene assays with deletion analysis, EMSA, ChIP in HepG2 cells Chemico-biological interactions Medium 21513704
2019 hsa-miR-495-3p and hsa-miR-486-5p post-transcriptionally suppress SULT2A1 expression by binding directly to miRNA response elements in the SULT2A1 3'-UTR and decreasing mRNA stability; this was demonstrated by RNA EMSA, luciferase reporter assays, and gain/loss-of-function experiments in HepG2 cells. Fluorescence-based RNA EMSA, luciferase reporter assays, miRNA overexpression/inhibition in HepG2 cells Biochemical pharmacology Medium 31445882
2006 Hydroxylated PCB metabolites (OHPCBs) act as both substrates and inhibitors of purified recombinant SULT2A1: 4-OH PCB 34 and 4'-OH PCB 68 are substrates (with 4-OH PCB 34 showing substrate inhibition similar to DHEA), while 4'-OH PCB 9 is an inhibitor but not a substrate. In vitro enzymatic assays with purified recombinant SULT2A1 Chemical research in toxicology Medium 17112228
2004 During the LPS-induced acute-phase response in mice, hepatic Sult2A1 mRNA and enzyme activity are suppressed in a time- and dose-dependent manner, accompanied by decreased serum DHEA-S; TNF and IL-1 mediate this suppression in human Hep3B cells, suggesting that inflammatory cytokine-driven suppression of FXR/PXR/CAR leads to decreased SULT2A1-mediated DHEA sulfation. LPS treatment in mice, RT-PCR, enzyme activity assay, serum steroid measurement, cytokine treatment of Hep3B cells American journal of physiology. Endocrinology and metabolism Medium 15198932
2010 Glycyrrhetinic acid (the active component of liquorice) directly inhibits adrenal SULT2A1 activity with an IC50 of ~7 µM, decreasing sulfoconjugation of DHEA and deoxycorticosterone in adrenocortical H295 cells without altering SULT2A1 mRNA levels, increasing free DHEA and deoxycorticosterone. Adrenocortical H295 cell incubations, radiolabeled steroid conjugation assays, mRNA analysis Molecular and cellular endocrinology Medium 21184804
2021 Metformin suppresses CAR-induced (but not basal) SULT2A1 expression by blocking CAR nuclear translocation via an AMPK-dependent mechanism in HepaRG cells. Western blot, cell viability assay, nuclear fractionation, HepaRG cell model with pharmacological activators/inhibitors International journal of endocrinology Low 33643408
2014 Dopamine D1 receptor (DRD1) activation in HepG2 cells upregulates SULT2A1 mRNA, protein, and enzyme activity via elevated cAMP; this effect is partially blocked by DRD1 antagonist SCH23390 and reduced by DRD1-specific siRNA knockdown. RT-PCR, Western blot, HPLC enzyme activity assay, cAMP measurement, siRNA knockdown in HepG2 cells Acta pharmacologica Sinica Low 24909515
2004 Alpha-hydroxytamoxifen (alpha-OHTAM) stereoisomers are all substrates for human SULT2A1 (unlike rat STa where only one enantiomer is a substrate); Z-enantiomers show higher kcat/Km values with SULT2A1 than E-enantiomers, demonstrating stereospecificity in SULT2A1-catalyzed sulfation. In vitro enzymatic assays with highly purified recombinant SULT2A1, kinetic analysis of stereoisomers Drug metabolism and disposition Medium 15371299

Source papers

Stage 0 corpus · 52 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 Suppression of DHEA sulfotransferase (Sult2A1) during the acute-phase response. American journal of physiology. Endocrinology and metabolism 76 15198932
2005 Vitamin D receptor regulation of the steroid/bile acid sulfotransferase SULT2A1. Methods in enzymology 72 16399349
2002 Human sulfotransferase SULT2A1 pharmacogenetics: genotype-to-phenotype studies. The pharmacogenomics journal 70 11990382
2003 Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms. The Journal of biological chemistry 62 12923182
2006 Hydroxylated polychlorinated biphenyls are substrates and inhibitors of human hydroxysteroid sulfotransferase SULT2A1. Chemical research in toxicology 56 17112228
2003 Conservation of the hydroxysteroid sulfotransferase SULT2B1 gene structure in the mouse: pre- and postnatal expression, kinetic analysis of isoforms, and comparison with prototypical SULT2A1. Endocrinology 54 12639899
2007 Positive and negative regulation of human hepatic hydroxysteroid sulfotransferase (SULT2A1) gene transcription by rifampicin: roles of hepatocyte nuclear factor 4alpha and pregnane X receptor. The Journal of pharmacology and experimental therapeutics 52 17687072
2003 Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex. The Journal of biological chemistry 47 14573603
2005 Transcriptional regulation of dehydroepiandrosterone sulfotransferase (SULT2A1) by estrogen-related receptor alpha. Endocrinology 46 15878968
2010 Kinetic analysis of bile acid sulfation by stably expressed human sulfotransferase 2A1 (SULT2A1). Xenobiotica; the fate of foreign compounds in biological systems 45 20102295
2007 Identification and characterization of two amino acids critical for the substrate inhibition of human dehydroepiandrosterone sulfotransferase (SULT2A1). Molecular pharmacology 41 18042734
2011 Structure-activity relationships for hydroxylated polychlorinated biphenyls as inhibitors of the sulfation of dehydroepiandrosterone catalyzed by human hydroxysteroid sulfotransferase SULT2A1. Chemical research in toxicology 39 21913674
2014 Paradigms of sulfotransferase catalysis: the mechanism of SULT2A1. The Journal of biological chemistry 36 25056952
2012 Regulation of the human hydroxysteroid sulfotransferase (SULT2A1) by RORα and RORγ and its potential relevance to human liver diseases. Molecular endocrinology (Baltimore, Md.) 36 23211525
2010 Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1: studies on the formation of catalytically non-productive enzyme complexes. Archives of biochemistry and biophysics 35 21187059
2018 Human DHEA sulfation requires direct interaction between PAPS synthase 2 and DHEA sulfotransferase SULT2A1. The Journal of biological chemistry 33 29743239
2009 Selective role of sulfotransferase 2A1 (SULT2A1) in the N-sulfoconjugation of quinolone drugs in humans. Drug metabolism and disposition: the biological fate of chemicals 33 19420132
2005 An essential role of the CAAT/enhancer binding protein-alpha in the vitamin D-induced expression of the human steroid/bile acid-sulfotransferase (SULT2A1). Molecular endocrinology (Baltimore, Md.) 31 16357103
2010 Liquorice and glycyrrhetinic acid increase DHEA and deoxycorticosterone levels in vivo and in vitro by inhibiting adrenal SULT2A1 activity. Molecular and cellular endocrinology 29 21184804
2006 Molecular cloning and regulation of porcine SULT2A1: relationship between SULT2A1 expression and sulfoconjugation of androstenone. Journal of molecular endocrinology 29 16595701
2018 Hydroxylated and sulfated metabolites of commonly occurring airborne polychlorinated biphenyls inhibit human steroid sulfotransferases SULT1E1 and SULT2A1. Environmental toxicology and pharmacology 23 29408762
2013 Variants in SULT2A1 affect the DHEA sulphate to DHEA ratio in patients with polycystic ovary syndrome but not the hyperandrogenic phenotype. The Journal of clinical endocrinology and metabolism 23 23861462
2001 Natural products isolated from Mexican medicinal plants: novel inhibitors of sulfotransferases, SULT1A1 and SULT2A1. Phytomedicine : international journal of phytotherapy and phytopharmacology 21 11824526
2015 Ethanol up-regulates phenol sulfotransferase (SULT1A1) and hydroxysteroid sulfotransferase (SULT2A1) in rat liver and intestine. Archives of physiology and biochemistry 19 25720860
2004 Interactions of the stereoisomers of alpha-hydroxytamoxifen with human hydroxysteroid sulfotransferase SULT2A1 and rat hydroxysteroid sulfotransferase STa. Drug metabolism and disposition: the biological fate of chemicals 19 15371299
2006 Association of SULT2A1 allelic variants with plasma adrenal androgens and prostate cancer in African American men. The Journal of steroid biochemistry and molecular biology 18 16617014
2015 Genetic variation, expression and ontogeny of sulfotransferase SULT2A1 in humans. The pharmacogenomics journal 17 25802089
2013 SULT2A1 Gene Copy Number Variation is Associated with Urinary Excretion Rate of Steroid Sulfates. Frontiers in endocrinology 17 23874324
2019 MicroRNAs hsa-miR-495-3p and hsa-miR-486-5p suppress basal and rifampicin-induced expression of human sulfotransferase 2A1 (SULT2A1) by facilitating mRNA degradation. Biochemical pharmacology 16 31445882
2008 Effect of insulin and testosterone on androgen production and transcription of SULT2A1 in the NCI-H295R adrenocortical cell line. Fertility and sterility 14 18684447
2006 Xenobiotic- and vitamin D-responsive induction of the steroid/bile acid-sulfotransferase Sult2A1 in young and old mice: the role of a gene enhancer in the liver chromatin. Gene 14 17123747
2014 Dopamine D1 receptor activation induces dehydroepiandrosterone sulfotransferase (SULT2A1) in HepG2 cells. Acta pharmacologica Sinica 13 24909515
2018 Identification of Galeterone and Abiraterone as Inhibitors of Dehydroepiandrosterone Sulfonation Catalyzed by Human Hepatic Cytosol, SULT2A1, SULT2B1b, and SULT1E1. Drug metabolism and disposition: the biological fate of chemicals 12 29436390
2018 SULFATION PATHWAYS: Expression of SULT2A1, SULT2B1 and HSD3B1 in the porcine testis and epididymis. Journal of molecular endocrinology 12 29588428
2017 Polymorphisms of STS gene and SULT2A1 gene and neurosteroid levels in Han Chinese boys with attention-deficit/hyperactivity disorder: an exploratory investigation. Scientific reports 12 28367959
2010 Lack of substrate inhibition in a monomeric form of human cytosolic SULT2A1. Hormone molecular biology and clinical investigation 10 21822453
2022 27-Hydroxycholesterol promotes metastasis by SULT2A1-dependent alteration in hepatocellular carcinoma. Cancer science 9 35599597
2020 Potentially functional genetic variants in PLIN2, SULT2A1 and UGT1A9 genes of the ketone pathway and survival of nonsmall cell lung cancer. International journal of cancer 9 32072637
2014 On the relationship between an Asian haplotype on chromosome 6 that reduces androstenone levels in boars and the differential expression of SULT2A1 in the testis. BMC genetics 7 24405739
2014 Transcriptional regulation of human hydroxysteroid sulfotransferase SULT2A1 by LXRα. Drug metabolism and disposition: the biological fate of chemicals 7 25028566
2013 Relationship between polymorphisms in the sulfotransferase SULT2A1 gene and dehydroepiandrosterone sulfate concentration in children. Experimental biology and medicine (Maywood, N.J.) 7 23436881
2011 Estrogen-related receptor ERRα-mediated downregulation of human hydroxysteroid sulfotransferase (SULT2A1) in Hep G2 cells. Chemico-biological interactions 7 21513704
2018 Effects of genetic polymorphisms on the sulfation of dehydroepiandrosterone and pregnenolone by human cytosolic sulfotransferase SULT2A1. Biochemistry and cell biology = Biochimie et biologie cellulaire 6 29671343
2008 Allosteric modulation of SULT2A1 by celecoxib and nimesulide: computational analyses. Drug metabolism letters 6 19356094
2024 An integrated investigation of sulfotransferases (SULTs) in hepatocellular carcinoma and identification of the role of SULT2A1 on stemness. Apoptosis : an international journal on programmed cell death 5 38411862
2021 Constitutive Androstane Receptor-Mediated Inhibition of Metformin on Phase II Metabolic Enzyme SULT2A1. International journal of endocrinology 5 33643408
2010 Lack of substrate inhibition in a monomeric form of human cytosolic SULT2A1. Hormone molecular biology and clinical investigation 5 25961208
2015 Preliminary study of FMO1, FMO5, CYP21, ESR1, PLIN2 and SULT2A1 as candidate gene for compounds related to boar taint. Meat science 3 26047979
2025 Association of SULT2A1 Locus With Abiraterone Clearance in the Alliance A031201: Randomized Phase III Study of Enzalutamide Compared With Enzalutamide Plus Abiraterone for Metastatic Castration-Resistant Prostate Cancer. Clinical and translational science 1 41346252
2022 Sulfation of 12-hydroxy-nevirapine by human SULTs and the effects of genetic polymorphisms of SULT1A1 and SULT2A1. Biochemical pharmacology 1 36084709
2026 Alkaline mineral complex water protects piglets against viral infection by driving cholesterol consumption through the GPAT2/SULT2A1 axis. Science China. Life sciences 0 41838342
2026 Immune checkpoint blockade as an accelerator of adrenal aging: a testable model linking low-grade cortical inflammation to proteostasis failure, LDLR/SULT2A1 suppression, and reduced DHEA output. Journal for immunotherapy of cancer 0 42044975

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