Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q06520 (ST2A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SULT2A1
Synonyms:HST, STD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

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.

Post-translational modification

The N-terminus is blocked.

Miscellaneous

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

Sequence similarities

Belongs to the sulfotransferase 1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAT3P407632EBI-3921363,EBI-518675

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Bile salt sulfotransferase
PRO_0000085141

Regions

Nucleotide binding44 – 496PAPS
Nucleotide binding218 – 2236PAPS
Nucleotide binding247 – 2493PAPS

Sites

Active site991Proton acceptor
Binding site721Substrate
Binding site771Substrate
Binding site1211PAPS
Binding site1291PAPS
Binding site1841PAPS

Natural variations

Natural variant631A → P. Ref.1
Corresponds to variant rs11569681 [ dbSNP | Ensembl ].
VAR_052520
Natural variant2611A → T.
Corresponds to variant rs11569679 [ dbSNP | Ensembl ].
VAR_052521

Experimental info

Sequence conflict901T → S in AAA35758. Ref.1
Sequence conflict901T → S in CAA49755. Ref.1
Sequence conflict1191L → D AA sequence Ref.1
Sequence conflict1591L → V in AAB23169. Ref.6

Secondary structure

........................................................... 285
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06520 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 06DFF2006B284A08

FASTA28533,780
        10         20         30         40         50         60 
MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL AEILCLMHSK 

        70         80         90        100        110        120 
GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL PIQLFPKSFF SSKAKVIYLM 

       130        140        150        160        170        180 
RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF EWFCQGTVLY GSWFDHIHGW MPMREEKNFL 

       190        200        210        220        230        240 
LLSYEELKQD TGRTIEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV 

       250        260        270        280 
DKAQLLRKGV SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE 

« Hide

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , L36191, L36192, L36193, L36194, L36195 Genomic DNA. Translation: AAA75491.1.
U13061 expand/collapse EMBL AC list , U13056, U13057, U13058, U13059, U13060 Genomic DNA. Translation: AAC51353.1.
S43859 mRNA. Translation: AAB23169.2.
BC020755 mRNA. Translation: AAH20755.1.
PIRI38548. I53037.
RefSeqNP_003158.2. NM_003167.3.
UniGeneHs.515835.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFHX-ray2.40A/B1-279[»]
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[»]
ProteinModelPortalQ06520.
SMRQ06520. Positions 4-285.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112691. 5 interactions.
IntActQ06520. 4 interactions.
MINTMINT-5002735.
STRING9606.ENSP00000222002.

Chemistry

ChEMBLCHEMBL2077.

PTM databases

PhosphoSiteQ06520.

Polymorphism databases

DMDM1711591.

Proteomic databases

PaxDbQ06520.
PRIDEQ06520.

Protocols and materials databases

DNASU6822.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222002; ENSP00000222002; ENSG00000105398.
GeneID6822.
KEGGhsa:6822.
UCSCuc002phr.2. human.

Organism-specific databases

CTD6822.
GeneCardsGC19M048373.
HGNCHGNC:11458. SULT2A1.
HPACAB018755.
HPA041487.
MIM125263. gene.
neXtProtNX_Q06520.
PharmGKBPA346.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG274515.
HOGENOMHOG000037209.
HOVERGENHBG001195.
InParanoidQ06520.
KOK11822.
OMAEFVIRDE.
OrthoDBEOG7V49ZK.
PhylomeDBQ06520.
TreeFamTF321745.

Enzyme and pathway databases

BRENDA2.8.2.2. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ06520.
BgeeQ06520.
CleanExHS_SULT2A1.
GenevestigatorQ06520.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSULT2A1. human.
EvolutionaryTraceQ06520.
GeneWikiBile_salt_sulfotransferase.
GenomeRNAi6822.
NextBio26647.
PROQ06520.
SOURCESearch...

Entry information

Entry nameST2A1_HUMAN
AccessionPrimary (citable) accession number: Q06520
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM