UniProtKB - Q06520 (ST2A1_HUMAN)
Protein
Sulfotransferase 2A1
Gene
SULT2A1
Organism
Homo sapiens (Human)
Status
Functioni
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups (PubMed:7678732, PubMed:2268288, PubMed:14573603, PubMed:18042734, PubMed:19589875, PubMed:21187059, PubMed:29671343, PubMed:7854148). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis (PubMed:21187059, PubMed:19589875, PubMed:14573603). Plays a key role in bile acid metabolism (PubMed:2268288). In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity).By similarity8 Publications
Catalytic activityi
- 3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H+6 PublicationsEC:2.8.2.26 PublicationsThis reaction proceeds in the forward1 Publication direction.
- (24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-hydroxycholesterol 24-sulfate + adenosine 3',5'-bisphosphate + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (24S)-hydroxycholesterol 24-sulfate + 3'-phosphoadenylyl sulfate = (24S)-hydroxycholesterol 3,24-disulfate + adenosine 3',5'-bisphosphate + H+1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 3'-phosphoadenylyl sulfate + 3β-hydroxyandrost-5-en-17-one = 3β-sulfooxy-androst-5-en-17-one + adenosine 3',5'-bisphosphate + H+6 PublicationsThis reaction proceeds in the forward1 Publication direction.
- 3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-bisphosphate + H+ + pregnenolone sulfate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 3'-phosphoadenylyl sulfate + 3α-hydroxy-5α-androstan-17-one = 3α-sulfooxy-5α-androstan-17-one + adenosine 3',5'-bisphosphate + H+2 PublicationsThis reaction proceeds in the forward1 Publication direction.
- 3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + H+ + taurolithocholate sulfate1 PublicationEC:2.8.2.141 PublicationThis reaction proceeds in the forward1 Publication direction.
- 3'-phosphoadenylyl sulfate + lithocholate = adenosine 3',5'-bisphosphate + H+ + lithocholate sulfate1 PublicationThis reaction proceeds in the forward1 Publication direction.
Activity regulationi
Subject to substrate inhibition. Alternate orientations for binding of steroid substrates to SULT2A1 may play a role in substrate inhibition.1 Publication
Kineticsi
- KM=0.8 µM for DHEA1 Publication
- KM=3.1 µM for DHEA1 Publication
- KM=1.6 µM for DHEA1 Publication
- KM=0.1 µM for (24S)-hydroxycholesterol 24-sulfate1 Publication
- KM=3.7 µM for (24S)-hydroxycholesterol1 Publication
- KM=1.5 µM for lithocholic acid1 Publication
- KM=4.2 µM for taurolithocholate1 Publication
- KM=2.1 µM for 3alpha-hydroxy-5alpha-androstan-17-one,1 Publication
- KM=1.4 µM for androsterone1 Publication
- KM=24.88 µM for PAPS1 Publication
- Vmax=227 nmol/min/mg enzyme with DHEA1 Publication
- Vmax=22.55 nmol/min/mg enzyme with DHEA1 Publication
- Vmax=54.3 µmol/min/mg enzyme with lithocholic acid1 Publication
- Vmax=203 nmol/min/mg enzyme with androsterone as substrate1 Publication
- Vmax=245 nmol/min/mg enzyme with DHEA1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 99 | Proton acceptor2 Publications | 1 | |
Binding sitei | 121 | PAPS1 Publication | 1 | |
Binding sitei | 129 | PAPS1 Publication | 1 | |
Binding sitei | 184 | PAPS1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 44 – 49 | PAPS1 Publication | 6 | |
Nucleotide bindingi | 218 – 223 | PAPS1 Publication | 6 | |
Nucleotide bindingi | 247 – 249 | PAPS1 Publication | 3 |
GO - Molecular functioni
- bile-salt sulfotransferase activity Source: GO_Central
- steroid sulfotransferase activity Source: CAFA
- sulfotransferase activity Source: BHF-UCL
GO - Biological processi
- 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: CAFA
- bile acid catabolic process Source: UniProtKB-KW
- ethanol catabolic process Source: CAFA
- regulation of lipid metabolic process Source: Reactome
- steroid metabolic process Source: GO_Central
- sulfation Source: BHF-UCL
Keywordsi
Molecular function | Transferase |
Biological process | Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism |
Enzyme and pathway databases
BioCyci | MetaCyc:HS02732-MONOMER |
PathwayCommonsi | Q06520 |
Reactomei | R-HSA-156584, Cytosolic sulfonation of small molecules R-HSA-1989781, PPARA activates gene expression |
SABIO-RKi | Q06520 |
Chemistry databases
SwissLipidsi | SLP:000001650 |
Names & Taxonomyi
Protein namesi | Recommended name: Sulfotransferase 2A1 (EC:2.8.2.27 Publications)Short name: ST2A1 Alternative name(s): Bile salt sulfotransferase (EC:2.8.2.142 Publications) Dehydroepiandrosterone sulfotransferase1 Publication Short name: DHEA-ST1 Publication Short name: DHEA-ST81 Publication Hydroxysteroid Sulfotransferase Short name: HST ST2 SULT2A31 Publication |
Gene namesi | Name:SULT2A1 Synonyms:HST, STD |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
EuPathDBi | HostDB:ENSG00000105398.3 |
HGNCi | HGNC:11458, SULT2A1 |
MIMi | 125263, gene |
neXtProti | NX_Q06520 |
Subcellular locationi
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 137 | M → I: Strongly reduces substrate inhibition when ADT or DHEA are used as substrates. 1 Publication | 1 | |
Mutagenesisi | 137 | M → W: Substrate inhibition is completly eliminated for DHEA; when associated with A-238. 1 Publication | 1 | |
Mutagenesisi | 238 | Y → A: Completely eliminates the substrate inhibition when ADT is used as substrate. Partially eliminates substrate inhibition when DHEA is used as substrate. Completely eliminates the substrate inhibition for DHEA, when associated with I-137. 1 Publication | 1 | |
Mutagenesisi | 238 | Y → F: Strongly reduces substrate inhibition when ADT or DHEA are used as substrates. 1 Publication | 1 | |
Mutagenesisi | 238 | Y → W: Strongly reduces substrate inhibition when ADT or DHEA are used as substrates. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 6822 |
OpenTargetsi | ENSG00000105398 |
PharmGKBi | PA346 |
Miscellaneous databases
Pharosi | Q06520, Tbio |
Chemistry databases
ChEMBLi | CHEMBL2077 |
DrugBanki | DB05812, Abiraterone DB01812, Adenosine 3',5'-diphosphate DB02854, Aetiocholanolone DB04445, Mercuric iodide DB09073, Palbociclib DB01708, Prasterone DB09288, Propacetamol DB00675, Tamoxifen |
Polymorphism and mutation databases
BioMutai | SULT2A1 |
DMDMi | 1711591 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000085141 | 1 – 285 | Sulfotransferase 2A1Add BLAST | 285 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 251 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
The N-terminus is blocked.
Keywords - PTMi
PhosphoproteinProteomic databases
MassIVEi | Q06520 |
MaxQBi | Q06520 |
PaxDbi | Q06520 |
PeptideAtlasi | Q06520 |
PRIDEi | Q06520 |
ProteomicsDBi | 58456 |
PTM databases
iPTMneti | Q06520 |
PhosphoSitePlusi | Q06520 |
Expressioni
Tissue specificityi
Liver, adrenal and at lower level in the kidney. Is present in human fetus in higher level in the adrenal than the liver and the kidney.
Gene expression databases
Bgeei | ENSG00000105398, Expressed in metanephros and 94 other tissues |
ExpressionAtlasi | Q06520, baseline and differential |
Genevisiblei | Q06520, HS |
Organism-specific databases
HPAi | ENSG00000105398, Tissue enriched (liver) |
Interactioni
Subunit structurei
Homodimer.
1 PublicationBinary interactionsi
Hide detailsQ06520
With | #Exp. | IntAct |
---|---|---|
NIF3L1 [Q9GZT8] | 3 | EBI-3921363,EBI-740897 |
STAT3 [P40763] | 2 | EBI-3921363,EBI-518675 |
SULT1B1 [O43704] | 6 | EBI-3921363,EBI-10179062 |
Protein-protein interaction databases
BioGRIDi | 112691, 6 interactors |
IntActi | Q06520, 6 interactors |
STRINGi | 9606.ENSP00000222002 |
Chemistry databases
BindingDBi | Q06520 |
Miscellaneous databases
RNActi | Q06520, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q06520 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q06520 |
Family & Domainsi
Sequence similaritiesi
Belongs to the sulfotransferase 1 family.Curated
Phylogenomic databases
eggNOGi | KOG1584, Eukaryota |
GeneTreei | ENSGT00940000154432 |
HOGENOMi | CLU_027239_1_0_1 |
InParanoidi | Q06520 |
OMAi | HAMKENK |
OrthoDBi | 780670at2759 |
PhylomeDBi | Q06520 |
TreeFami | TF321745 |
Family and domain databases
InterProi | View protein in InterPro IPR027417, P-loop_NTPase IPR000863, Sulfotransferase_dom |
Pfami | View protein in Pfam PF00685, Sulfotransfer_1, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit |
i Sequence
Sequence statusi: Complete.
Q06520-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL
60 70 80 90 100
AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL
110 120 130 140 150
PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF
160 170 180 190 200
EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ
210 220 230 240 250
FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV
260 270 280
SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 90 | T → S in AAA35758 (PubMed:7678732).Curated | 1 | |
Sequence conflicti | 90 | T → S in CAA49755 (PubMed:7678732).Curated | 1 | |
Sequence conflicti | 119 | L → D AA sequence (PubMed:7678732).Curated | 1 | |
Sequence conflicti | 159 | L → V in AAB23169 (PubMed:1520333).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_083881 | 44 | K → E Sulfating activity toward both DHEA and pregnenolone is completely abolished. 1 Publication | 1 | |
Natural variantiVAR_052520 | 63 | A → P1 PublicationCorresponds to variant dbSNP:rs11569681EnsemblClinVar. | 1 | |
Natural variantiVAR_083882 | 76 | P → T Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 Publication | 1 | |
Natural variantiVAR_083883 | 147 | E → K Decreases of the sulfotransferase activity toward DHEA; no effect on the sulfotransferase activity toward pregnenolone. 1 Publication | 1 | |
Natural variantiVAR_083884 | 148 | E → K Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 Publication | 1 | |
Natural variantiVAR_083885 | 246 | L → P Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 Publication | 1 | |
Natural variantiVAR_083886 | 258 | F → L Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 Publication | 1 | |
Natural variantiVAR_052521 | 261 | A → T. Corresponds to variant dbSNP:rs11569679Ensembl. | 1 | |
Natural variantiVAR_083887 | 262 | Q → E Decreases of the sulfotransferase activity toward DHEA; no effect on the sulfotransferase activity toward pregnenolone. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L20000 mRNA Translation: AAA35758.1 X70222 mRNA Translation: CAA49755.1 U08024 mRNA Translation: AAA17749.1 U08025 mRNA Translation: AAA17750.1 X84816 mRNA Translation: CAA59274.1 L36196 , L36191, L36192, L36193, L36194, L36195 Genomic DNA Translation: AAA75491.1 U13061 , U13056, U13057, U13058, U13059, U13060 Genomic DNA Translation: AAC51353.1 S43859 mRNA Translation: AAB23169.2 BC020755 mRNA Translation: AAH20755.1 |
CCDSi | CCDS12707.1 |
PIRi | I53037, I38548 |
RefSeqi | NP_003158.2, NM_003167.3 |
Genome annotation databases
Ensembli | ENST00000222002; ENSP00000222002; ENSG00000105398 |
GeneIDi | 6822 |
KEGGi | hsa:6822 |
UCSCi | uc002phr.2, human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L20000 mRNA Translation: AAA35758.1 X70222 mRNA Translation: CAA49755.1 U08024 mRNA Translation: AAA17749.1 U08025 mRNA Translation: AAA17750.1 X84816 mRNA Translation: CAA59274.1 L36196 , L36191, L36192, L36193, L36194, L36195 Genomic DNA Translation: AAA75491.1 U13061 , U13056, U13057, U13058, U13059, U13060 Genomic DNA Translation: AAC51353.1 S43859 mRNA Translation: AAB23169.2 BC020755 mRNA Translation: AAH20755.1 |
CCDSi | CCDS12707.1 |
PIRi | I53037, I38548 |
RefSeqi | NP_003158.2, NM_003167.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EFH | X-ray | 2.40 | A/B | 1-281 | [»] | |
1J99 | X-ray | 1.99 | A | 2-285 | [»] | |
1OV4 | X-ray | 2.70 | A | 2-285 | [»] | |
2QP3 | X-ray | 2.60 | A | 2-285 | [»] | |
2QP4 | X-ray | 3.00 | A | 2-285 | [»] | |
3F3Y | X-ray | 2.20 | A/B/C/D | 1-285 | [»] | |
4IFB | X-ray | 2.30 | A/B | 1-285 | [»] | |
SMRi | Q06520 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 112691, 6 interactors |
IntActi | Q06520, 6 interactors |
STRINGi | 9606.ENSP00000222002 |
Chemistry databases
BindingDBi | Q06520 |
ChEMBLi | CHEMBL2077 |
DrugBanki | DB05812, Abiraterone DB01812, Adenosine 3',5'-diphosphate DB02854, Aetiocholanolone DB04445, Mercuric iodide DB09073, Palbociclib DB01708, Prasterone DB09288, Propacetamol DB00675, Tamoxifen |
SwissLipidsi | SLP:000001650 |
PTM databases
iPTMneti | Q06520 |
PhosphoSitePlusi | Q06520 |
Polymorphism and mutation databases
BioMutai | SULT2A1 |
DMDMi | 1711591 |
Proteomic databases
MassIVEi | Q06520 |
MaxQBi | Q06520 |
PaxDbi | Q06520 |
PeptideAtlasi | Q06520 |
PRIDEi | Q06520 |
ProteomicsDBi | 58456 |
Protocols and materials databases
Antibodypediai | 4362, 452 antibodies |
DNASUi | 6822 |
Genome annotation databases
Ensembli | ENST00000222002; ENSP00000222002; ENSG00000105398 |
GeneIDi | 6822 |
KEGGi | hsa:6822 |
UCSCi | uc002phr.2, human |
Organism-specific databases
CTDi | 6822 |
DisGeNETi | 6822 |
EuPathDBi | HostDB:ENSG00000105398.3 |
GeneCardsi | SULT2A1 |
HGNCi | HGNC:11458, SULT2A1 |
HPAi | ENSG00000105398, Tissue enriched (liver) |
MIMi | 125263, gene |
neXtProti | NX_Q06520 |
OpenTargetsi | ENSG00000105398 |
PharmGKBi | PA346 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1584, Eukaryota |
GeneTreei | ENSGT00940000154432 |
HOGENOMi | CLU_027239_1_0_1 |
InParanoidi | Q06520 |
OMAi | HAMKENK |
OrthoDBi | 780670at2759 |
PhylomeDBi | Q06520 |
TreeFami | TF321745 |
Enzyme and pathway databases
BioCyci | MetaCyc:HS02732-MONOMER |
PathwayCommonsi | Q06520 |
Reactomei | R-HSA-156584, Cytosolic sulfonation of small molecules R-HSA-1989781, PPARA activates gene expression |
SABIO-RKi | Q06520 |
Miscellaneous databases
BioGRID-ORCSi | 6822, 2 hits in 842 CRISPR screens |
ChiTaRSi | SULT2A1, human |
EvolutionaryTracei | Q06520 |
GeneWikii | Bile_salt_sulfotransferase |
GenomeRNAii | 6822 |
Pharosi | Q06520, Tbio |
PROi | PR:Q06520 |
RNActi | Q06520, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000105398, Expressed in metanephros and 94 other tissues |
ExpressionAtlasi | Q06520, baseline and differential |
Genevisiblei | Q06520, HS |
Family and domain databases
InterProi | View protein in InterPro IPR027417, P-loop_NTPase IPR000863, Sulfotransferase_dom |
Pfami | View protein in Pfam PF00685, Sulfotransfer_1, 1 hit |
SUPFAMi | SSF52540, SSF52540, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ST2A1_HUMAN | |
Accessioni | Q06520Primary (citable) accession number: Q06520 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1995 |
Last sequence update: | January 23, 2007 | |
Last modified: | December 2, 2020 | |
This is version 197 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 19
Human chromosome 19: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations