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Protein

Bile salt sulfotransferase

Gene

SULT2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Miscellaneous

Estrogens present in maternal circulation is predominantly derived from fetal dehydroepiandosterone sulfate which is hydrolyzed and metabolized to estrogens in placenta.

Catalytic activityi

3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate.
3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei72Substrate1
Binding sitei77Substrate1
Active sitei99Proton acceptor1
Binding sitei121PAPS1
Binding sitei129PAPS1
Binding sitei184PAPS1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 49PAPS6
Nucleotide bindingi218 – 223PAPS6
Nucleotide bindingi247 – 249PAPS3

GO - Molecular functioni

  • aryl sulfotransferase activity Source: Reactome
  • bile-salt sulfotransferase activity Source: GO_Central
  • estrone sulfotransferase activity Source: Reactome
  • 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
  • lipid catabolic process Source: UniProtKB-KW
  • regulation of lipid metabolic process Source: Reactome
  • steroid metabolic process Source: GO_Central
  • sulfation Source: BHF-UCL

Keywordsi

Molecular functionTransferase
Biological processBile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-156584 Cytosolic sulfonation of small molecules
R-HSA-1989781 PPARA activates gene expression

Chemistry databases

SwissLipidsiSLP:000001650

Names & Taxonomyi

Protein namesi
Recommended name:
Bile salt sulfotransferase (EC:2.8.2.14)
Alternative name(s):
Dehydroepiandrosterone sulfotransferase
Short name:
DHEA-ST
Hydroxysteroid Sulfotransferase
Short name:
HST
ST2
ST2A3
Sulfotransferase 2A1
Short name:
ST2A1
Gene namesi
Name:SULT2A1
Synonyms:HST, STD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000105398.3
HGNCiHGNC:11458 SULT2A1
MIMi125263 gene
neXtProtiNX_Q06520

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi6822
OpenTargetsiENSG00000105398
PharmGKBiPA346

Chemistry databases

ChEMBLiCHEMBL2077
DrugBankiDB05812 Abiraterone
DB00316 Acetaminophen
DB01812 Adenosine-3'-5'-Diphosphate
DB02854 Aetiocholanolone
DB04445 Mercury Diiodide
DB01708 Prasterone

Polymorphism and mutation databases

BioMutaiSULT2A1
DMDMi1711591

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000851411 – 285Bile salt sulfotransferaseAdd BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei251PhosphoserineCombined sources1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06520
PaxDbiQ06520
PeptideAtlasiQ06520
PRIDEiQ06520

PTM databases

iPTMnetiQ06520
PhosphoSitePlusiQ06520

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

BgeeiENSG00000105398
CleanExiHS_SULT2A1
ExpressionAtlasiQ06520 baseline and differential
GenevisibleiQ06520 HS

Organism-specific databases

HPAiCAB018755
HPA041487
HPA063633

Interactioni

Subunit structurei

Homodimer.3 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi112691, 5 interactors
IntActiQ06520, 6 interactors
STRINGi9606.ENSP00000222002

Chemistry databases

BindingDBiQ06520

Structurei

Secondary structure

1285
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi11 – 13Combined sources3
Beta strandi15 – 17Combined sources3
Helixi20 – 28Combined sources9
Beta strandi37 – 40Combined sources4
Beta strandi43 – 46Combined sources4
Helixi47 – 58Combined sources12
Turni59 – 61Combined sources3
Helixi64 – 68Combined sources5
Helixi71 – 74Combined sources4
Helixi81 – 87Combined sources7
Beta strandi95 – 98Combined sources4
Helixi102 – 104Combined sources3
Helixi107 – 111Combined sources5
Beta strandi115 – 120Combined sources6
Helixi123 – 134Combined sources12
Beta strandi137 – 140Combined sources4
Helixi146 – 155Combined sources10
Helixi163 – 170Combined sources8
Helixi171 – 173Combined sources3
Beta strandi179 – 183Combined sources5
Helixi184 – 189Combined sources6
Helixi191 – 202Combined sources12
Helixi208 – 217Combined sources10
Helixi220 – 224Combined sources5
Turni227 – 229Combined sources3
Turni236 – 238Combined sources3
Beta strandi239 – 241Combined sources3
Helixi242 – 246Combined sources5
Helixi254 – 256Combined sources3
Helixi260 – 274Combined sources15
Helixi279 – 281Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EFHX-ray2.40A/B1-281[»]
1J99X-ray1.99A2-285[»]
1OV4X-ray2.70A2-285[»]
2QP3X-ray2.60A2-285[»]
2QP4X-ray3.00A2-285[»]
3F3YX-ray2.20A/B/C/D1-285[»]
4IFBX-ray2.30A/B1-285[»]
ProteinModelPortaliQ06520
SMRiQ06520
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06520

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG1584 Eukaryota
ENOG4111H56 LUCA
GeneTreeiENSGT00760000118932
HOGENOMiHOG000037209
HOVERGENiHBG001195
InParanoidiQ06520
KOiK11822
OMAiRRGPHDC
OrthoDBiEOG091G0D5F
PhylomeDBiQ06520
TreeFamiTF321745

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR000863 Sulfotransferase_dom
PfamiView protein in Pfam
PF00685 Sulfotransfer_1, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit

Sequencei

Sequence statusi: Complete.

Q06520-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:285
Mass (Da):33,780
Last modified:January 23, 2007 - v3
Checksum:i06DFF2006B284A08
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90T → S in AAA35758 (PubMed:7678732).Curated1
Sequence conflicti90T → S in CAA49755 (PubMed:7678732).Curated1
Sequence conflicti119L → D AA sequence (PubMed:7678732).Curated1
Sequence conflicti159L → V in AAB23169 (PubMed:1520333).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05252063A → P1 PublicationCorresponds to variant dbSNP:rs11569681Ensembl.1
Natural variantiVAR_052521261A → T. Corresponds to variant dbSNP:rs11569679Ensembl.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
CCDSiCCDS12707.1
PIRiI53037 I38548
RefSeqiNP_003158.2, NM_003167.3
UniGeneiHs.515835

Genome annotation databases

EnsembliENST00000222002; ENSP00000222002; ENSG00000105398
GeneIDi6822
KEGGihsa:6822
UCSCiuc002phr.2 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiST2A1_HUMAN
AccessioniPrimary (citable) accession number: Q06520
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 25, 2018
This is version 180 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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, Complete proteome, Direct protein sequencing, Reference proteome

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