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Q06520

- ST2A1_HUMAN

UniProt

Q06520 - ST2A1_HUMAN

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Protein

Bile salt sulfotransferase

Gene

SULT2A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721Substrate
Binding sitei77 – 771Substrate
Active sitei99 – 991Proton acceptor
Binding sitei121 – 1211PAPS
Binding sitei129 – 1291PAPS
Binding sitei184 – 1841PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 496PAPS
Nucleotide bindingi218 – 2236PAPS
Nucleotide bindingi247 – 2493PAPS

GO - Molecular functioni

  1. bile-salt sulfotransferase activity Source: UniProtKB-EC
  2. sulfotransferase activity Source: BHF-UCL

GO - Biological processi

  1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
  2. bile acid catabolic process Source: UniProtKB-KW
  3. cellular lipid metabolic process Source: Reactome
  4. digestion Source: ProtInc
  5. small molecule metabolic process Source: Reactome
  6. steroid metabolic process Source: ProtInc
  7. sulfation Source: BHF-UCL
  8. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BRENDAi2.8.2.2. 2681.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_6913. Cytosolic sulfonation of small molecules.

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
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:11458. SULT2A1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA346.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Bile salt sulfotransferasePRO_0000085141Add
BLAST

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiQ06520.
PaxDbiQ06520.
PRIDEiQ06520.

PTM databases

PhosphoSiteiQ06520.

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

BgeeiQ06520.
CleanExiHS_SULT2A1.
ExpressionAtlasiQ06520. baseline and differential.
GenevestigatoriQ06520.

Organism-specific databases

HPAiCAB018755.
HPA041487.

Interactioni

Subunit structurei

Homodimer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
STAT3P407632EBI-3921363,EBI-518675

Protein-protein interaction databases

BioGridi112691. 5 interactions.
IntActiQ06520. 4 interactions.
MINTiMINT-5002735.
STRINGi9606.ENSP00000222002.

Structurei

Secondary structure

1
285
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi11 – 133Combined sources
Beta strandi15 – 173Combined sources
Helixi20 – 289Combined sources
Beta strandi37 – 404Combined sources
Beta strandi43 – 464Combined sources
Helixi47 – 5812Combined sources
Turni59 – 613Combined sources
Helixi64 – 685Combined sources
Helixi71 – 744Combined sources
Helixi81 – 877Combined sources
Beta strandi95 – 984Combined sources
Helixi102 – 1043Combined sources
Helixi107 – 1115Combined sources
Beta strandi115 – 1206Combined sources
Helixi123 – 13412Combined sources
Beta strandi137 – 1404Combined sources
Helixi146 – 15510Combined sources
Helixi163 – 1708Combined sources
Helixi171 – 1733Combined sources
Beta strandi179 – 1835Combined sources
Helixi184 – 1896Combined sources
Helixi191 – 20212Combined sources
Helixi208 – 21710Combined sources
Helixi220 – 2245Combined sources
Turni227 – 2293Combined sources
Turni236 – 2383Combined sources
Beta strandi239 – 2413Combined sources
Helixi242 – 2465Combined sources
Helixi254 – 2563Combined sources
Helixi260 – 27415Combined sources
Helixi279 – 2813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06520.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiNOG274515.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiQ06520.
KOiK11822.
OMAiXVYGSWF.
OrthoDBiEOG7V49ZK.
PhylomeDBiQ06520.
TreeFamiTF321745.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901T → S in AAA35758. (PubMed:7678732)Curated
Sequence conflicti90 – 901T → S in CAA49755. (PubMed:7678732)Curated
Sequence conflicti119 – 1191L → D AA sequence (PubMed:7678732)Curated
Sequence conflicti159 – 1591L → V in AAB23169. (PubMed:1520333)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631A → P.1 Publication
Corresponds to variant rs11569681 [ dbSNP | Ensembl ].
VAR_052520
Natural varianti261 – 2611A → T.
Corresponds to variant rs11569679 [ dbSNP | Ensembl ].
VAR_052521

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.

Polymorphism databases

DMDMi1711591.

Keywords - Coding sequence diversityi

Polymorphism

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.
UniGenei Hs.515835.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali Q06520.
SMRi Q06520. Positions 4-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112691. 5 interactions.
IntActi Q06520. 4 interactions.
MINTi MINT-5002735.
STRINGi 9606.ENSP00000222002.

Chemistry

ChEMBLi CHEMBL2077.
DrugBanki DB05812. Abiraterone.
DB00316. Acetaminophen.

PTM databases

PhosphoSitei Q06520.

Polymorphism databases

DMDMi 1711591.

Proteomic databases

MaxQBi Q06520.
PaxDbi Q06520.
PRIDEi Q06520.

Protocols and materials databases

DNASUi 6822.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000222002 ; ENSP00000222002 ; ENSG00000105398 .
GeneIDi 6822.
KEGGi hsa:6822.
UCSCi uc002phr.2. human.

Organism-specific databases

CTDi 6822.
GeneCardsi GC19M048373.
HGNCi HGNC:11458. SULT2A1.
HPAi CAB018755.
HPA041487.
MIMi 125263. gene.
neXtProti NX_Q06520.
PharmGKBi PA346.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG274515.
GeneTreei ENSGT00760000118932.
HOGENOMi HOG000037209.
HOVERGENi HBG001195.
InParanoidi Q06520.
KOi K11822.
OMAi XVYGSWF.
OrthoDBi EOG7V49ZK.
PhylomeDBi Q06520.
TreeFami TF321745.

Enzyme and pathway databases

BRENDAi 2.8.2.2. 2681.
Reactomei REACT_116145. PPARA activates gene expression.
REACT_6913. Cytosolic sulfonation of small molecules.

Miscellaneous databases

ChiTaRSi SULT2A1. human.
EvolutionaryTracei Q06520.
GeneWikii Bile_salt_sulfotransferase.
GenomeRNAii 6822.
NextBioi 26647.
PROi Q06520.
SOURCEi Search...

Gene expression databases

Bgeei Q06520.
CleanExi HS_SULT2A1.
ExpressionAtlasi Q06520. baseline and differential.
Genevestigatori Q06520.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view ]
Pfami PF00685. Sulfotransfer_1. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of human liver dehydroepiandrosterone sulphotransferase."
    Comer K.A., Falany J.L., Falany C.N.
    Biochem. J. 289:233-240(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-65; 105-120 AND 274-285, VARIANT PRO-63.
    Tissue: Liver.
  2. "Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA."
    Otterness D.M., Wieben E.D., Wood T.C., Watson R.W.G., Madden B.J., McCormick D.J., Weinshilboum R.M.
    Mol. Pharmacol. 41:865-872(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 81-108 AND 177-199.
    Tissue: Liver.
  3. "Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme."
    Forbes K.J., Hagen M., Coughtrie M.W.H., Glatt H.R., Hume R.
    Mol. Cell. Endocrinol. 112:53-60(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Adrenal gland.
  4. "Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene."
    Luu-The V., Dufort I., Paquet N., Reimnitz G., Labrie F.
    DNA Cell Biol. 14:511-518(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization."
    Otterness D.M., Her C., Aksoy S., Kimura S., Wieben E.D., Weinshilboum R.M.
    DNA Cell Biol. 14:331-341(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver."
    Kong A.-N.T., Yang L., Ma M., Tao D., Bjornsson T.D.
    Biochem. Biophys. Res. Commun. 187:448-454(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  8. "Human liver steroid sulphotransferase sulphates bile acids."
    Radominska A., Comer K.A., Zimniak P., Falany J., Iscan M., Falany C.N.
    Biochem. J. 272:597-604(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase."
    Pedersen L.C., Petrotchenko E.V., Negishi M.
    FEBS Lett. 475:61-64(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE (PAP).
  11. "Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate."
    Rehse P.H., Zhou M., Lin S.X.
    Biochem. J. 364:165-171(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH DEHYDROEPIANDROSTERONE (DHEA).
  12. "Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex."
    Chang H.J., Shi R., Rehse P., Lin S.X.
    J. Biol. Chem. 279:2689-2696(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ANDROSTERONE (ADT).

Entry informationi

Entry nameiST2A1_HUMAN
AccessioniPrimary (citable) accession number: Q06520
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 153 of the entry and version 3 of the sequence. [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

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3