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Bile salt sulfotransferase (EC 2.8.2.14) (Dehydroepiandrosterone sulfotransferase) (DHEA-ST) (Hydroxysteroid Sulfotransferase) (HST) (ST2) (ST2A3) (Sulfotransferase 2A1) (ST2A1)

 ST2A1_HUMAN             Reviewed;         285 AA.
Q06520;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 179.
RecName: Full=Bile salt sulfotransferase;
EC=2.8.2.14;
AltName: Full=Dehydroepiandrosterone sulfotransferase;
Short=DHEA-ST;
AltName: Full=Hydroxysteroid Sulfotransferase;
Short=HST;
AltName: Full=ST2;
AltName: Full=ST2A3;
AltName: Full=Sulfotransferase 2A1;
Short=ST2A1;
Name=SULT2A1; Synonyms=HST, STD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-65; 105-120 AND
274-285, AND VARIANT PRO-63.
TISSUE=Liver;
PubMed=7678732; DOI=10.1042/bj2890233;
Comer K.A., Falany J.L., Falany C.N.;
"Cloning and expression of human liver dehydroepiandrosterone
sulphotransferase.";
Biochem. J. 289:233-240(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 81-108 AND
177-199.
TISSUE=Liver;
PubMed=1588921;
Otterness D.M., Wieben E.D., Wood T.C., Watson R.W.G., Madden B.J.,
McCormick D.J., Weinshilboum R.M.;
"Human liver dehydroepiandrosterone sulfotransferase: molecular
cloning and expression of cDNA.";
Mol. Pharmacol. 41:865-872(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Adrenal gland;
PubMed=7589785; DOI=10.1016/0303-7207(95)03585-U;
Forbes K.J., Hagen M., Coughtrie M.W.H., Glatt H.R., Hume R.;
"Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning,
stable expression in V79 cells and functional characterisation of the
expressed enzyme.";
Mol. Cell. Endocrinol. 112:53-60(1995).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7598806; DOI=10.1089/dna.1995.14.511;
Luu-The V., Dufort I., Paquet N., Reimnitz G., Labrie F.;
"Structural characterization and expression of the human
dehydroepiandrosterone sulfotransferase gene.";
DNA Cell Biol. 14:511-518(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7710689; DOI=10.1089/dna.1995.14.331;
Otterness D.M., Her C., Aksoy S., Kimura S., Wieben E.D.,
Weinshilboum R.M.;
"Human dehydroepiandrosterone sulfotransferase gene: molecular cloning
and structural characterization.";
DNA Cell Biol. 14:331-341(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1520333; DOI=10.1016/S0006-291X(05)81514-1;
Kong A.-N.T., Yang L., Ma M., Tao D., Bjornsson T.D.;
"Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of
sulfotransferase from human liver.";
Biochem. Biophys. Res. Commun. 187:448-454(1992).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
CHARACTERIZATION.
PubMed=2268288; DOI=10.1042/bj2720597;
Radominska A., Comer K.A., Zimniak P., Falany J., Iscan M.,
Falany C.N.;
"Human liver steroid sulphotransferase sulphates bile acids.";
Biochem. J. 272:597-604(1990).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH
ADENOSINE-3'-5'-DIPHOSPHATE (PAP).
PubMed=10854859; DOI=10.1016/S0014-5793(00)01479-4;
Pedersen L.C., Petrotchenko E.V., Negishi M.;
"Crystal structure of SULT2A3, human hydroxysteroid
sulfotransferase.";
FEBS Lett. 475:61-64(2000).
[12]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH
DEHYDROEPIANDROSTERONE (DHEA).
PubMed=11988089;
Rehse P.H., Zhou M., Lin S.X.;
"Crystal structure of human dehydroepiandrosterone sulphotransferase
in complex with substrate.";
Biochem. J. 364:165-171(2002).
[13]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ANDROSTERONE
(ADT).
PubMed=14573603; DOI=10.1074/jbc.M310446200;
Chang H.J., Shi R., Rehse P., Lin S.X.;
"Identifying androsterone (ADT) as a cognate substrate for human
dehydroepiandrosterone sulfotransferase (DHEA-ST) important for
steroid homeostasis: structure of the enzyme-ADT complex.";
J. Biol. Chem. 279:2689-2696(2004).
-!- 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.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + taurolithocholate
= adenosine 3',5'-bisphosphate + taurolithocholate sulfate.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10854859,
ECO:0000269|PubMed:11988089, ECO:0000269|PubMed:14573603}.
-!- INTERACTION:
P40763:STAT3; NbExp=2; IntAct=EBI-3921363, EBI-518675;
O43704:SULT1B1; NbExp=7; IntAct=EBI-3921363, EBI-10179062;
-!- 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.
-!- PTM: 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.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
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EMBL; L20000; AAA35758.1; -; mRNA.
EMBL; X70222; CAA49755.1; -; mRNA.
EMBL; U08024; AAA17749.1; -; mRNA.
EMBL; U08025; AAA17750.1; -; mRNA.
EMBL; X84816; CAA59274.1; -; mRNA.
EMBL; L36196; AAA75491.1; -; Genomic_DNA.
EMBL; L36191; AAA75491.1; JOINED; Genomic_DNA.
EMBL; L36192; AAA75491.1; JOINED; Genomic_DNA.
EMBL; L36193; AAA75491.1; JOINED; Genomic_DNA.
EMBL; L36194; AAA75491.1; JOINED; Genomic_DNA.
EMBL; L36195; AAA75491.1; JOINED; Genomic_DNA.
EMBL; U13061; AAC51353.1; -; Genomic_DNA.
EMBL; U13056; AAC51353.1; JOINED; Genomic_DNA.
EMBL; U13057; AAC51353.1; JOINED; Genomic_DNA.
EMBL; U13058; AAC51353.1; JOINED; Genomic_DNA.
EMBL; U13059; AAC51353.1; JOINED; Genomic_DNA.
EMBL; U13060; AAC51353.1; JOINED; Genomic_DNA.
EMBL; S43859; AAB23169.2; -; mRNA.
EMBL; BC020755; AAH20755.1; -; mRNA.
CCDS; CCDS12707.1; -.
PIR; I53037; I38548.
RefSeq; NP_003158.2; NM_003167.3.
UniGene; Hs.515835; -.
PDB; 1EFH; X-ray; 2.40 A; A/B=1-281.
PDB; 1J99; X-ray; 1.99 A; A=2-285.
PDB; 1OV4; X-ray; 2.70 A; A=2-285.
PDB; 2QP3; X-ray; 2.60 A; A=2-285.
PDB; 2QP4; X-ray; 3.00 A; A=2-285.
PDB; 3F3Y; X-ray; 2.20 A; A/B/C/D=1-285.
PDB; 4IFB; X-ray; 2.30 A; A/B=1-285.
PDBsum; 1EFH; -.
PDBsum; 1J99; -.
PDBsum; 1OV4; -.
PDBsum; 2QP3; -.
PDBsum; 2QP4; -.
PDBsum; 3F3Y; -.
PDBsum; 4IFB; -.
ProteinModelPortal; Q06520; -.
SMR; Q06520; -.
BioGrid; 112691; 5.
IntAct; Q06520; 6.
STRING; 9606.ENSP00000222002; -.
BindingDB; Q06520; -.
ChEMBL; CHEMBL2077; -.
DrugBank; DB05812; Abiraterone.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB01812; Adenosine-3'-5'-Diphosphate.
DrugBank; DB02854; Aetiocholanolone.
DrugBank; DB04445; Mercury Diiodide.
DrugBank; DB01708; Prasterone.
SwissLipids; SLP:000001650; -.
iPTMnet; Q06520; -.
PhosphoSitePlus; Q06520; -.
BioMuta; SULT2A1; -.
DMDM; 1711591; -.
MaxQB; Q06520; -.
PaxDb; Q06520; -.
PeptideAtlas; Q06520; -.
PRIDE; Q06520; -.
DNASU; 6822; -.
Ensembl; ENST00000222002; ENSP00000222002; ENSG00000105398.
GeneID; 6822; -.
KEGG; hsa:6822; -.
UCSC; uc002phr.2; human.
CTD; 6822; -.
DisGeNET; 6822; -.
EuPathDB; HostDB:ENSG00000105398.3; -.
GeneCards; SULT2A1; -.
HGNC; HGNC:11458; SULT2A1.
HPA; CAB018755; -.
HPA; HPA041487; -.
HPA; HPA063633; -.
MIM; 125263; gene.
neXtProt; NX_Q06520; -.
OpenTargets; ENSG00000105398; -.
PharmGKB; PA346; -.
eggNOG; KOG1584; Eukaryota.
eggNOG; ENOG4111H56; LUCA.
GeneTree; ENSGT00760000118932; -.
HOGENOM; HOG000037209; -.
HOVERGEN; HBG001195; -.
InParanoid; Q06520; -.
KO; K11822; -.
OMA; RRGPHDC; -.
OrthoDB; EOG091G0D5F; -.
PhylomeDB; Q06520; -.
TreeFam; TF321745; -.
Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
Reactome; R-HSA-1989781; PPARA activates gene expression.
ChiTaRS; SULT2A1; human.
EvolutionaryTrace; Q06520; -.
GeneWiki; Bile_salt_sulfotransferase; -.
GenomeRNAi; 6822; -.
PRO; PR:Q06520; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105398; -.
CleanEx; HS_SULT2A1; -.
ExpressionAtlas; Q06520; baseline and differential.
Genevisible; Q06520; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0004062; F:aryl sulfotransferase activity; TAS:Reactome.
GO; GO:0047704; F:bile-salt sulfotransferase activity; IEA:UniProtKB-EC.
GO; GO:0004304; F:estrone sulfotransferase activity; TAS:Reactome.
GO; GO:0050294; F:steroid sulfotransferase activity; IDA:CAFA.
GO; GO:0008146; F:sulfotransferase activity; IDA:BHF-UCL.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
GO; GO:0007586; P:digestion; NAS:ProtInc.
GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0008202; P:steroid metabolic process; IDA:CAFA.
GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000863; Sulfotransferase_dom.
Pfam; PF00685; Sulfotransfer_1; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Bile acid catabolism; Complete proteome; Cytoplasm;
Direct protein sequencing; Lipid degradation; Lipid metabolism;
Phosphoprotein; Polymorphism; Reference proteome; Steroid metabolism;
Transferase.
CHAIN 1 285 Bile salt sulfotransferase.
/FTId=PRO_0000085141.
NP_BIND 44 49 PAPS.
NP_BIND 218 223 PAPS.
NP_BIND 247 249 PAPS.
ACT_SITE 99 99 Proton acceptor.
BINDING 72 72 Substrate.
BINDING 77 77 Substrate.
BINDING 121 121 PAPS.
BINDING 129 129 PAPS.
BINDING 184 184 PAPS.
MOD_RES 251 251 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 63 63 A -> P (in dbSNP:rs11569681).
{ECO:0000269|PubMed:7678732}.
/FTId=VAR_052520.
VARIANT 261 261 A -> T (in dbSNP:rs11569679).
/FTId=VAR_052521.
CONFLICT 90 90 T -> S (in Ref. 1; AAA35758/CAA49755).
{ECO:0000305}.
CONFLICT 119 119 L -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 159 159 L -> V (in Ref. 6; AAB23169).
{ECO:0000305}.
STRAND 4 8 {ECO:0000244|PDB:1J99}.
STRAND 11 13 {ECO:0000244|PDB:1J99}.
STRAND 15 17 {ECO:0000244|PDB:1J99}.
HELIX 20 28 {ECO:0000244|PDB:1J99}.
STRAND 37 40 {ECO:0000244|PDB:1J99}.
STRAND 43 46 {ECO:0000244|PDB:2QP4}.
HELIX 47 58 {ECO:0000244|PDB:1J99}.
TURN 59 61 {ECO:0000244|PDB:1J99}.
HELIX 64 68 {ECO:0000244|PDB:1J99}.
HELIX 71 74 {ECO:0000244|PDB:1J99}.
HELIX 81 87 {ECO:0000244|PDB:1J99}.
STRAND 95 98 {ECO:0000244|PDB:1J99}.
HELIX 102 104 {ECO:0000244|PDB:1J99}.
HELIX 107 111 {ECO:0000244|PDB:1J99}.
STRAND 115 120 {ECO:0000244|PDB:1J99}.
HELIX 123 134 {ECO:0000244|PDB:1J99}.
STRAND 137 140 {ECO:0000244|PDB:1EFH}.
HELIX 146 155 {ECO:0000244|PDB:1J99}.
HELIX 163 170 {ECO:0000244|PDB:1J99}.
HELIX 171 173 {ECO:0000244|PDB:1J99}.
STRAND 179 183 {ECO:0000244|PDB:1J99}.
HELIX 184 189 {ECO:0000244|PDB:1J99}.
HELIX 191 202 {ECO:0000244|PDB:1J99}.
HELIX 208 217 {ECO:0000244|PDB:1J99}.
HELIX 220 224 {ECO:0000244|PDB:1J99}.
TURN 227 229 {ECO:0000244|PDB:1J99}.
TURN 236 238 {ECO:0000244|PDB:1J99}.
STRAND 239 241 {ECO:0000244|PDB:3F3Y}.
HELIX 242 246 {ECO:0000244|PDB:1J99}.
HELIX 254 256 {ECO:0000244|PDB:1J99}.
HELIX 260 274 {ECO:0000244|PDB:1J99}.
HELIX 279 281 {ECO:0000244|PDB:1J99}.
SEQUENCE 285 AA; 33780 MW; 06DFF2006B284A08 CRC64;
MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL AEILCLMHSK
GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL PIQLFPKSFF SSKAKVIYLM
RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF EWFCQGTVLY GSWFDHIHGW MPMREEKNFL
LLSYEELKQD TGRTIEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV
DKAQLLRKGV SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE


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