SULT1A1

Sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1

PDB rendering based on 1cjm.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1LS6, 1Z28, 2D06, 3QVU, 3QVV, 3U3J, 3U3K, 3U3M, 3U3O, 3U3R, 4GRA

Identifiers

Symbols

SULT1A1 ; HAST1/HAST2; P-PST; PST; ST1A1; ST1A3; STP; STP1; TSPST1

External IDs

OMIM: 171150 MGI: 102896 HomoloGene: 134950 ChEMBL: 1743291 GeneCards: SULT1A1 Gene

EC number

2.8.2.1

Gene ontology
Molecular function	• aryl sulfotransferase activity • protein binding • sulfotransferase activity • flavonol 3-sulfotransferase activity • steroid sulfotransferase activity
Cellular component	• cytosol
Biological process	• catecholamine metabolic process • xenobiotic metabolic process • estrogen metabolic process • amine metabolic process • flavonoid metabolic process • small molecule metabolic process • 3'-phosphoadenosine 5'-phosphosulfate metabolic process • sulfation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 16:
28.61 – 28.62 Mb

Chr 7:
133.82 – 133.82 Mb

PubMed search

Sulfotransferase 1A1 is an enzyme that in humans is encoded by the SULT1A1 gene.^[1]^[2]^[3]

Sulfotransferase enzymes catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs, and xenobiotic compounds. These cytosolic enzymes are different in their tissue distributions and substrate specificities. The gene structure (number and length of exons) is similar among family members. This gene encodes one of two phenol sulfotransferases with thermostable enzyme activity. Multiple alternatively spliced variants that encode two isoforms have been identified for this gene.^[3]

References

↑ Dooley TP, Obermoeller RD, Leiter EH, Chapman HD, Falany CN, Deng Z, Siciliano MJ (Feb 1994). "Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7". Genomics 18 (2): 440–3. doi:10.1006/geno.1993.1494. PMID 8288252.
↑ Dooley TP, Huang Z (Dec 1996). "Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16". Biochem Biophys Res Commun 228 (1): 134–40. doi:10.1006/bbrc.1996.1628. PMID 8912648.
1 2 "Entrez Gene: SULT1A1 sulfotransferase family, cytosolic, 1A, phenol-preferring, member 1".

Weinshilboum RM, Otterness DM, Aksoy IA, et al. (1997). "Sulfation and sulfotransferases 1: Sulfotransferase molecular biology: cDNAs and genes.". FASEB J. 11 (1): 3–14. PMID 9034160.
Windmill KF, Christiansen A, Teusner JT, et al. (1998). "Localisation of aryl sulfotransferase expression in human tissues using hybridisation histochemistry and immunohistochemistry.". Chem. Biol. Interact. 109 (1–3): 341–6. doi:10.1016/S0009-2797(97)00144-0. PMID 9566757.
Glatt H, Engelke CE, Pabel U, et al. (2000). "Sulfotransferases: genetics and role in toxicology". Toxicol. Lett. 112-113: 341–8. doi:10.1016/S0378-4274(99)00214-3. PMID 10720750.
Glatt H (2001). "Sulfotransferases in the bioactivation of xenobiotics". Chem. Biol. Interact. 129 (1–2): 141–70. doi:10.1016/S0009-2797(00)00202-7. PMID 11154739.
Glatt H, Boeing H, Engelke CE, et al. (2001). "Human cytosolic sulphotransferases: genetics, characteristics, toxicological aspects". Mutat. Res. 482 (1–2): 27–40. doi:10.1016/S0027-5107(01)00207-X. PMID 11535246.
Ozawa S, Nagata K, Shimada M, et al. (1995). "Primary structures and properties of two related forms of aryl sulfotransferases in human liver". Pharmacogenetics. 5 Spec No: S135–40. doi:10.1097/00008571-199512001-00015. PMID 7581483.
Jones AL, Hagen M, Coughtrie MW, et al. (1995). "Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form". Biochem. Biophys. Res. Commun. 208 (2): 855–62. doi:10.1006/bbrc.1995.1414. PMID 7695643.
Hwang SR, Kohn AB, Hook VY (1995). "Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus". Biochem. Biophys. Res. Commun. 207 (2): 701–7. doi:10.1006/bbrc.1995.1244. PMID 7864863.
Yamazoe Y, Nagata K, Ozawa S, Kato R (1994). "Structural similarity and diversity of sulfotransferases". Chem. Biol. Interact. 92 (1–3): 107–17. doi:10.1016/0009-2797(94)90057-4. PMID 8033246.
Falany CN, Zhuang W, Falany JL (1994). "Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability". Chem. Biol. Interact. 92 (1–3): 57–66. doi:10.1016/0009-2797(94)90053-1. PMID 8033270.
Veronese ME, Burgess W, Zhu X, McManus ME (1994). "Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies". Biochem. J. 302 (2): 497–502. PMC 1137255. PMID 8093002.
Zhu X, Veronese ME, Bernard CC, et al. (1993). "Identification of two human brain aryl sulfotransferase cDNAs". Biochem. Biophys. Res. Commun. 195 (1): 120–7. doi:10.1006/bbrc.1993.2018. PMID 8363592.
Wilborn TW, Comer KA, Dooley TP, et al. (1993). "Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase". Mol. Pharmacol. 43 (1): 70–7. PMID 8423770.
Zhu X, Veronese ME, Sansom LN, McManus ME (1993). "Molecular characterisation of a human aryl sulfotransferase cDNA". Biochem. Biophys. Res. Commun. 192 (2): 671–6. doi:10.1006/bbrc.1993.1467. PMID 8484775.
Her C, Raftogianis R, Weinshilboum RM (1996). "Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization". Genomics 33 (3): 409–20. doi:10.1006/geno.1996.0216. PMID 8661000.
Bernier F, Soucy P, Luu-The V (1996). "Human phenol sulfotransferase gene contains two alternative promoters: Structure and expression of the gene". DNA Cell Biol. 15 (5): 367–75. doi:10.1089/dna.1996.15.367. PMID 8924211.
Raftogianis RB, Her C, Weinshilboum RM (1997). "Human phenol sulfotransferase pharmacogenetics: STP1 gene cloning and structural characterization". Pharmacogenetics 6 (6): 473–87. doi:10.1097/00008571-199612000-00001. PMID 9014197.

PDB gallery

1cjm: HUMAN SULT1A3 WITH SULFATE BOUND

1ls6: Human SULT1A1 complexed with PAP and p-Nitrophenol

1z28: Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (OH-AAF)

1z29: Crystal Structures of SULT1A2 and SULT1A1*3: Implications in the bioactivation of N-hydroxy-2-acetylamino fluorine (OH-AAF)

2a3r: Crystal Structure of Human Sulfotransferase SULT1A3 in Complex with Dopamine and 3-Phosphoadenosine 5-Phosphate

2d06: Human Sult1A1 Complexed With Pap and estradiol

Metabolism: lipid metabolism – ketones/cholesterol synthesis enzymes/steroid metabolism

Mevalonate pathway

To HMG-CoA	Acetyl-Coenzyme A acetyltransferase HMG-CoA synthase (regulated step)

Ketogenesis	HMG-CoA lyase 3-hydroxybutyrate dehydrogenase Thiophorase

To Mevalonic acid	HMG-CoA reductase

To DMAPP	Mevalonate kinase Phosphomevalonate kinase Pyrophosphomevalonate decarboxylase Isopentenyl-diphosphate delta isomerase

Geranyl-	Dimethylallyltranstransferase Geranyl pyrophosphate

To cholesterol

To lanosterol	Farnesyl-diphosphate farnesyltransferase Squalene monooxygenase Lanosterol synthase

7-Dehydrocholesterol path	Lanosterol 14α-demethylase Sterol-C5-desaturase-like 7-Dehydrocholesterol reductase

Desmosterol path	24-dehydrocholesterol reductase

To Bile acids

Steroidogenesis

To pregnenolone

Side-chain cleavage

To corticosteroids

aldosterone: 18-hydroxylase

To sex hormones

To androgens	17α-hydroxylase/17,20 lyase 3β dehydrogenase 17β dehydrogenase 5α reductase 1 2

To estrogens	Aromatase

Other/ungrouped

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SULT1A1

References

Further reading