Q06520 (ST2A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	SULT2A1
Synonyms:	HST, STD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Bile acid catabolism Lipid degradation Lipid metabolism Steroid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome bile acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW cellular lipid metabolic process Traceable author statement. Source: Reactome digestion Non-traceable author statement Ref.2. Source: ProtInc steroid metabolic process Traceable author statement Ref.2. Source: ProtInc sulfation Inferred from direct assay PubMed 20056724. Source: BHF-UCL xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	bile-salt sulfotransferase activity Inferred from electronic annotation. Source: EC sulfotransferase activity Inferred from direct assay PubMed 20056724. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAT3	P40763	2	EBI-3921363,EBI-518675

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 285

285

Bile salt sulfotransferase

PRO_0000085141

Regions

Nucleotide binding

44 – 49

6

PAPS

Nucleotide binding

218 – 223

6

PAPS

Nucleotide binding

247 – 249

3

PAPS

Sites

Active site

99

1

Proton acceptor

Binding site

72

1

Substrate

Binding site

77

1

Substrate

Binding site

121

1

PAPS

Binding site

129

1

PAPS

Binding site

184

1

PAPS

Natural variations

Natural variant

63

1

A → P. Ref.1
Corresponds to variant rs11569681 [ dbSNP | Ensembl ].

VAR_052520

Natural variant

261

1

A → T.
Corresponds to variant rs11569679 [ dbSNP | Ensembl ].

VAR_052521

Experimental info

Sequence conflict

90

1

T → S in AAA35758. Ref.1

Sequence conflict

90

1

T → S in CAA49755. Ref.1

Sequence conflict

119

1

L → D AA sequence Ref.1

Sequence conflict

159

1

L → V in AAB23169. Ref.6

Secondary structure

1

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285

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Beta strand

11 – 13

3

Beta strand

15 – 17

3

Helix

20 – 28

9

Beta strand

37 – 40

4

Beta strand

43 – 46

4

Helix

47 – 58

12

Turn

59 – 61

3

Helix

64 – 68

5

Helix

71 – 74

4

Helix

81 – 87

7

Beta strand

95 – 98

4

Helix

102 – 104

3

Helix

107 – 111

5

Beta strand

115 – 120

6

Helix

123 – 134

12

Beta strand

137 – 140

4

Helix

146 – 155

10

Helix

163 – 170

8

Helix

171 – 173

3

Beta strand

179 – 183

5

Helix

184 – 189

6

Helix

191 – 202

12

Helix

208 – 217

10

Helix

220 – 224

5

Turn

227 – 229

3

Turn

236 – 238

3

Beta strand

239 – 241

3

Helix

242 – 246

5

Helix

254 – 256

3

Helix

260 – 274

15

Helix

279 – 281

3

Sequences

	Sequence		Length	Mass (Da)
	Q06520 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 06DFF2006B284A08	FASTA	285	33,780
	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

References

	« Hide 'large scale' referencesShow '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 , 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.

IPI

IPI00216133.

PIR

I38548. I53037.

RefSeq

NP_003158.2. NM_003167.3.

UniGene

Hs.515835.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EFH	X-ray	2.40	A/B	1-279	[»]
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	[»]

ProteinModelPortal

Q06520.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q06520. 4 interactions.

MINT

MINT-5002735.

STRING

9606.ENSP00000222002.

PTM databases

PhosphoSite

Q06520.

Polymorphism databases

DMDM

1711591.

Proteomic databases

PaxDb

Q06520.

PRIDE

Q06520.

Protocols and materials databases

DNASU

6822.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000222002; ENSP00000222002; ENSG00000105398.

GeneID

6822.

KEGG

hsa:6822.

UCSC

uc002phr.2. human.

Organism-specific databases

CTD

6822.

GeneCards

GC19M048373.

HGNC

HGNC:11458. SULT2A1.

HPA

CAB018755.

MIM

125263. gene.

neXtProt

NX_Q06520.

PharmGKB

PA346.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG274515.

HOGENOM

HOG000037209.

HOVERGEN

HBG001195.

InParanoid

Q06520.

KO

K11822.

OMA

FLWFEGI.

OrthoDB

EOG4NS3CD.

PhylomeDB

Q06520.

Enzyme and pathway databases

BRENDA

2.8.2.2. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q06520.

Bgee

Q06520.

CleanEx

HS_SULT2A1.

Genevestigator

Q06520.

GermOnline

ENSG00000105398. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL2077.

ChiTaRS

SULT2A1. human.

EvolutionaryTrace

Q06520.

GenomeRNAi

6822.

NextBio

26647.

SOURCE

Search...

Entry information

Entry name

ST2A1_HUMAN

Accession

Primary (citable) accession number: Q06520

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 139 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.