ST2A1_HUMAN
ID ST2A1_HUMAN Reviewed; 285 AA.
AC Q06520;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Sulfotransferase 2A1;
DE Short=ST2A1;
DE EC=2.8.2.2 {ECO:0000269|PubMed:14573603, ECO:0000269|PubMed:18042734, ECO:0000269|PubMed:21187059, ECO:0000269|PubMed:2268288, ECO:0000269|PubMed:29671343, ECO:0000269|PubMed:7678732, ECO:0000269|PubMed:7854148};
DE AltName: Full=Bile salt sulfotransferase;
DE EC=2.8.2.14 {ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:2268288};
DE AltName: Full=Dehydroepiandrosterone sulfotransferase {ECO:0000303|PubMed:7678732};
DE Short=DHEA-ST {ECO:0000303|PubMed:7678732};
DE Short=DHEA-ST8 {ECO:0000303|PubMed:7678732};
DE AltName: Full=Hydroxysteroid Sulfotransferase;
DE Short=HST;
DE AltName: Full=ST2;
DE AltName: Full=SULT2A3 {ECO:0000303|PubMed:10854859};
GN Name=SULT2A1; Synonyms=HST, STD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-65; 105-120 AND 274-285,
RP VARIANT PRO-63, CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Liver;
RX PubMed=7678732; DOI=10.1042/bj2890233;
RA Comer K.A., Falany J.L., Falany C.N.;
RT "Cloning and expression of human liver dehydroepiandrosterone
RT sulphotransferase.";
RL Biochem. J. 289:233-240(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 81-108 AND 177-199.
RC TISSUE=Liver;
RX PubMed=1588921;
RA Otterness D.M., Wieben E.D., Wood T.C., Watson R.W.G., Madden B.J.,
RA McCormick D.J., Weinshilboum R.M.;
RT "Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and
RT expression of cDNA.";
RL Mol. Pharmacol. 41:865-872(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=7589785; DOI=10.1016/0303-7207(95)03585-u;
RA Forbes K.J., Hagen M., Coughtrie M.W.H., Glatt H.R., Hume R.;
RT "Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable
RT expression in V79 cells and functional characterisation of the expressed
RT enzyme.";
RL Mol. Cell. Endocrinol. 112:53-60(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7598806; DOI=10.1089/dna.1995.14.511;
RA Luu-The V., Dufort I., Paquet N., Reimnitz G., Labrie F.;
RT "Structural characterization and expression of the human
RT dehydroepiandrosterone sulfotransferase gene.";
RL DNA Cell Biol. 14:511-518(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7710689; DOI=10.1089/dna.1995.14.331;
RA Otterness D.M., Her C., Aksoy S., Kimura S., Wieben E.D.,
RA Weinshilboum R.M.;
RT "Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and
RT structural characterization.";
RL DNA Cell Biol. 14:331-341(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1520333; DOI=10.1016/s0006-291x(05)81514-1;
RA Kong A.-N.T., Yang L., Ma M., Tao D., Bjornsson T.D.;
RT "Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of
RT sulfotransferase from human liver.";
RL Biochem. Biophys. Res. Commun. 187:448-454(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2268288; DOI=10.1042/bj2720597;
RA Radominska A., Comer K.A., Zimniak P., Falany J., Iscan M., Falany C.N.;
RT "Human liver steroid sulphotransferase sulphates bile acids.";
RL Biochem. J. 272:597-604(1990).
RN [9]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=7854148; DOI=10.1093/mutage/9.6.553;
RA Glatt H., Seidel A., Harvey R.G., Coughtrie M.W.;
RT "Activation of benzylic alcohols to mutagens by human hepatic
RT sulphotransferases.";
RL Mutagenesis 9:553-557(1994).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE (PAP), AND SUBUNIT.
RX PubMed=10854859; DOI=10.1016/s0014-5793(00)01479-4;
RA Pedersen L.C., Petrotchenko E.V., Negishi M.;
RT "Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase.";
RL FEBS Lett. 475:61-64(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH
RP DEHYDROEPIANDROSTERONE (DHEA).
RX PubMed=11988089; DOI=10.1042/bj3640165;
RA Rehse P.H., Zhou M., Lin S.X.;
RT "Crystal structure of human dehydroepiandrosterone sulphotransferase in
RT complex with substrate.";
RL Biochem. J. 364:165-171(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ANDROSTERONE (ADT),
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=14573603; DOI=10.1074/jbc.m310446200;
RA Chang H.J., Shi R., Rehse P., Lin S.X.;
RT "Identifying androsterone (ADT) as a cognate substrate for human
RT dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid
RT homeostasis: structure of the enzyme-ADT complex.";
RL J. Biol. Chem. 279:2689-2696(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH
RP DEHYDROEPIANDROSTERONE (DHEA), MUTAGENESIS OF MET-137 AND TYR-238,
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RX PubMed=18042734; DOI=10.1124/mol.107.041038;
RA Lu L.Y., Hsieh Y.C., Liu M.Y., Lin Y.H., Chen C.J., Yang Y.S.;
RT "Identification and characterization of two amino acids critical for the
RT substrate inhibition of human dehydroepiandrosterone sulfotransferase
RT (SULT2A1).";
RL Mol. Pharmacol. 73:660-668(2008).
RN [16]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19589875; DOI=10.1124/dmd.108.025759;
RA Cook I.T., Duniec-Dmuchowski Z., Kocarek T.A., Runge-Morris M.,
RA Falany C.N.;
RT "24-hydroxycholesterol sulfation by human cytosolic sulfotransferases:
RT formation of monosulfates and disulfates, molecular modeling, sulfatase
RT sensitivity, and inhibition of liver x receptor activation.";
RL Drug Metab. Dispos. 37:2069-2078(2009).
RN [17]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21187059; DOI=10.1016/j.abb.2010.12.027;
RA Gulcan H.O., Duffel M.W.;
RT "Substrate inhibition in human hydroxysteroid sulfotransferase SULT2A1:
RT studies on the formation of catalytically non-productive enzyme
RT complexes.";
RL Arch. Biochem. Biophys. 507:232-240(2011).
RN [18]
RP CHARACTERIZATION OF VARIANTS GLU-44; THR-76; LYS-147; LYS-148; PRO-246;
RP LEU-258 AND GLU-262, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP FUNCTION.
RX PubMed=29671343; DOI=10.1139/bcb-2017-0341;
RA Abunnaja M.S., Alherz F.A., El Daibani A.A., Bairam A.F., Rasool M.I.,
RA Gohal S.A., Kurogi K., Suiko M., Sakakibara Y., Liu M.C.;
RT "Effects of genetic polymorphisms on the sulfation of
RT dehydroepiandrosterone and pregnenolone by human cytosolic sulfotransferase
RT SULT2A1.";
RL Biochem. Cell Biol. 96:655-662(2018).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and
CC bile acids in the liver and adrenal glands. Mediates the sulfation of a
CC wide range of steroids and sterols, including pregnenolone,
CC androsterone, DHEA, bile acids, cholesterol and as well many
CC xenobiotics that contain alcohol and phenol functional groups
CC (PubMed:7678732, PubMed:2268288, PubMed:14573603, PubMed:18042734,
CC PubMed:19589875, PubMed:21187059, PubMed:29671343, PubMed:7854148).
CC Sulfonation increases the water solubility of most compounds, and
CC therefore their renal excretion, but it can also result in
CC bioactivation to form active metabolites. Plays an important role in
CC maintening steroid and lipid homeostasis (PubMed:21187059,
CC PubMed:19589875, PubMed:14573603). Plays a key role in bile acid
CC metabolism (PubMed:2268288). In addition, catalyzes the metabolic
CC activation of potent carcinogenic polycyclic arylmethanols (By
CC similarity). {ECO:0000250|UniProtKB:P15709,
CC ECO:0000269|PubMed:14573603, ECO:0000269|PubMed:18042734,
CC ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21187059,
CC ECO:0000269|PubMed:2268288, ECO:0000269|PubMed:29671343,
CC ECO:0000269|PubMed:7678732, ECO:0000269|PubMed:7854148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-
CC bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2;
CC Evidence={ECO:0000269|PubMed:18042734, ECO:0000269|PubMed:19589875,
CC ECO:0000269|PubMed:21187059, ECO:0000269|PubMed:2268288,
CC ECO:0000269|PubMed:7678732, ECO:0000269|PubMed:7854148};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22553;
CC Evidence={ECO:0000269|PubMed:2268288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 24-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52344, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566;
CC Evidence={ECO:0000269|PubMed:19589875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52345;
CC Evidence={ECO:0000305|PubMed:19589875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)-
CC hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567;
CC Evidence={ECO:0000269|PubMed:19589875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349;
CC Evidence={ECO:0000305|PubMed:19589875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(24S)-hydroxycholesterol 24-sulfate + 3'-phosphoadenylyl
CC sulfate = (24S)-hydroxycholesterol 3,24-disulfate + adenosine 3',5'-
CC bisphosphate + H(+); Xref=Rhea:RHEA:52352, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136566,
CC ChEBI:CHEBI:136568; Evidence={ECO:0000269|PubMed:19589875};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52353;
CC Evidence={ECO:0000305|PubMed:19589875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one
CC = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate +
CC H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689,
CC ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343;
CC Evidence={ECO:0000269|PubMed:14573603, ECO:0000269|PubMed:18042734,
CC ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21187059,
CC ECO:0000269|PubMed:2268288, ECO:0000269|PubMed:7678732};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217;
CC Evidence={ECO:0000305|PubMed:19589875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'-
CC bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133000;
CC Evidence={ECO:0000269|PubMed:29671343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357;
CC Evidence={ECO:0000305|PubMed:29671343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3alpha-hydroxy-5alpha-androstan-
CC 17-one = adenosine 3',5'-bisphosphate + androsterone 3alpha-sulfate +
CC H(+); Xref=Rhea:RHEA:60644, ChEBI:CHEBI:15378, ChEBI:CHEBI:16032,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:133003;
CC Evidence={ECO:0000269|PubMed:14573603, ECO:0000269|PubMed:18042734};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60645;
CC Evidence={ECO:0000305|PubMed:14573603};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + taurolithocholate = adenosine
CC 3',5'-bisphosphate + H(+) + taurolithocholate 3-sulfate;
CC Xref=Rhea:RHEA:14013, ChEBI:CHEBI:15378, ChEBI:CHEBI:17179,
CC ChEBI:CHEBI:58301, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=2.8.2.14;
CC Evidence={ECO:0000269|PubMed:2268288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14014;
CC Evidence={ECO:0000305|PubMed:2268288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + lithocholate = adenosine 3',5'-
CC bisphosphate + H(+) + lithocholate sulfate; Xref=Rhea:RHEA:51064,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29744, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133940;
CC Evidence={ECO:0000269|PubMed:2268288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51065;
CC Evidence={ECO:0000305|PubMed:2268288};
CC -!- ACTIVITY REGULATION: Subject to substrate inhibition. Alternate
CC orientations for binding of steroid substrates to SULT2A1 may play a
CC role in substrate inhibition. {ECO:0000269|PubMed:18042734}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for DHEA {ECO:0000269|PubMed:21187059};
CC KM=3.1 uM for DHEA {ECO:0000269|PubMed:14573603};
CC KM=1.6 uM for DHEA {ECO:0000269|PubMed:2268288};
CC KM=0.1 uM for (24S)-hydroxycholesterol 24-sulfate
CC {ECO:0000269|PubMed:19589875};
CC KM=3.7 uM for (24S)-hydroxycholesterol {ECO:0000269|PubMed:19589875};
CC KM=1.5 uM for lithocholic acid {ECO:0000269|PubMed:2268288};
CC KM=4.2 uM for taurolithocholate {ECO:0000269|PubMed:2268288};
CC KM=2.1 uM for 3alpha-hydroxy-5alpha-androstan-17-one,
CC {ECO:0000269|PubMed:14573603};
CC KM=1.4 uM for androsterone {ECO:0000269|PubMed:18042734};
CC KM=24.88 uM for PAPS {ECO:0000269|PubMed:29671343};
CC Vmax=227 nmol/min/mg enzyme with DHEA {ECO:0000269|PubMed:18042734};
CC Vmax=22.55 nmol/min/mg enzyme with DHEA
CC {ECO:0000269|PubMed:29671343};
CC Vmax=54.3 umol/min/mg enzyme with lithocholic acid
CC {ECO:0000269|PubMed:2268288};
CC Vmax=203 nmol/min/mg enzyme with androsterone as substrate
CC {ECO:0000269|PubMed:18042734};
CC Vmax=245 nmol/min/mg enzyme with DHEA {ECO:0000269|PubMed:21187059};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10854859}.
CC -!- INTERACTION:
CC Q06520; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-3921363, EBI-740897;
CC Q06520; P40763: STAT3; NbExp=2; IntAct=EBI-3921363, EBI-518675;
CC Q06520; O43704: SULT1B1; NbExp=6; IntAct=EBI-3921363, EBI-10179062;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2268288}.
CC -!- TISSUE SPECIFICITY: Liver, adrenal and at lower level in the kidney. Is
CC present in human fetus in higher level in the adrenal than the liver
CC and the kidney.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; L20000; AAA35758.1; -; mRNA.
DR EMBL; X70222; CAA49755.1; -; mRNA.
DR EMBL; U08024; AAA17749.1; -; mRNA.
DR EMBL; U08025; AAA17750.1; -; mRNA.
DR EMBL; X84816; CAA59274.1; -; mRNA.
DR EMBL; L36196; AAA75491.1; -; Genomic_DNA.
DR EMBL; L36191; AAA75491.1; JOINED; Genomic_DNA.
DR EMBL; L36192; AAA75491.1; JOINED; Genomic_DNA.
DR EMBL; L36193; AAA75491.1; JOINED; Genomic_DNA.
DR EMBL; L36194; AAA75491.1; JOINED; Genomic_DNA.
DR EMBL; L36195; AAA75491.1; JOINED; Genomic_DNA.
DR EMBL; U13061; AAC51353.1; -; Genomic_DNA.
DR EMBL; U13056; AAC51353.1; JOINED; Genomic_DNA.
DR EMBL; U13057; AAC51353.1; JOINED; Genomic_DNA.
DR EMBL; U13058; AAC51353.1; JOINED; Genomic_DNA.
DR EMBL; U13059; AAC51353.1; JOINED; Genomic_DNA.
DR EMBL; U13060; AAC51353.1; JOINED; Genomic_DNA.
DR EMBL; S43859; AAB23169.2; -; mRNA.
DR EMBL; BC020755; AAH20755.1; -; mRNA.
DR CCDS; CCDS12707.1; -.
DR PIR; I53037; I38548.
DR RefSeq; NP_003158.2; NM_003167.3.
DR PDB; 1EFH; X-ray; 2.40 A; A/B=1-281.
DR PDB; 1J99; X-ray; 1.99 A; A=2-285.
DR PDB; 1OV4; X-ray; 2.70 A; A=2-285.
DR PDB; 2QP3; X-ray; 2.60 A; A=2-285.
DR PDB; 2QP4; X-ray; 3.00 A; A=2-285.
DR PDB; 3F3Y; X-ray; 2.20 A; A/B/C/D=1-285.
DR PDB; 4IFB; X-ray; 2.30 A; A/B=1-285.
DR PDBsum; 1EFH; -.
DR PDBsum; 1J99; -.
DR PDBsum; 1OV4; -.
DR PDBsum; 2QP3; -.
DR PDBsum; 2QP4; -.
DR PDBsum; 3F3Y; -.
DR PDBsum; 4IFB; -.
DR AlphaFoldDB; Q06520; -.
DR SMR; Q06520; -.
DR BioGRID; 112691; 6.
DR IntAct; Q06520; 6.
DR STRING; 9606.ENSP00000222002; -.
DR BindingDB; Q06520; -.
DR ChEMBL; CHEMBL2077; -.
DR DrugBank; DB05812; Abiraterone.
DR DrugBank; DB01812; Adenosine 3',5'-diphosphate.
DR DrugBank; DB02854; Aetiocholanolone.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB04445; Mercuric iodide.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB09073; Palbociclib.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB01708; Prasterone.
DR DrugBank; DB09288; Propacetamol.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB00871; Terbutaline.
DR SwissLipids; SLP:000001650; -.
DR iPTMnet; Q06520; -.
DR PhosphoSitePlus; Q06520; -.
DR BioMuta; SULT2A1; -.
DR DMDM; 1711591; -.
DR MassIVE; Q06520; -.
DR MaxQB; Q06520; -.
DR PaxDb; Q06520; -.
DR PeptideAtlas; Q06520; -.
DR PRIDE; Q06520; -.
DR ProteomicsDB; 58456; -.
DR Antibodypedia; 4362; 486 antibodies from 38 providers.
DR DNASU; 6822; -.
DR Ensembl; ENST00000222002.4; ENSP00000222002.2; ENSG00000105398.4.
DR GeneID; 6822; -.
DR KEGG; hsa:6822; -.
DR MANE-Select; ENST00000222002.4; ENSP00000222002.2; NM_003167.4; NP_003158.2.
DR UCSC; uc002phr.2; human.
DR CTD; 6822; -.
DR DisGeNET; 6822; -.
DR GeneCards; SULT2A1; -.
DR HGNC; HGNC:11458; SULT2A1.
DR HPA; ENSG00000105398; Tissue enriched (liver).
DR MIM; 125263; gene.
DR neXtProt; NX_Q06520; -.
DR OpenTargets; ENSG00000105398; -.
DR PharmGKB; PA346; -.
DR VEuPathDB; HostDB:ENSG00000105398; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000154432; -.
DR HOGENOM; CLU_027239_1_0_1; -.
DR InParanoid; Q06520; -.
DR OMA; PNMGFRS; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; Q06520; -.
DR TreeFam; TF321745; -.
DR BioCyc; MetaCyc:HS02732-MON; -.
DR PathwayCommons; Q06520; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SABIO-RK; Q06520; -.
DR SignaLink; Q06520; -.
DR BioGRID-ORCS; 6822; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; SULT2A1; human.
DR EvolutionaryTrace; Q06520; -.
DR GeneWiki; Bile_salt_sulfotransferase; -.
DR GenomeRNAi; 6822; -.
DR Pharos; Q06520; Tbio.
DR PRO; PR:Q06520; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q06520; protein.
DR Bgee; ENSG00000105398; Expressed in adrenal tissue and 88 other tissues.
DR ExpressionAtlas; Q06520; baseline and differential.
DR Genevisible; Q06520; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:UniProtKB.
DR GO; GO:0004027; F:alcohol sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0047704; F:bile-salt sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0050294; F:steroid sulfotransferase activity; IDA:CAFA.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:BHF-UCL.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
DR GO; GO:0030573; P:bile acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IDA:GO_Central.
DR GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IDA:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bile acid catabolism; Cytoplasm; Direct protein sequencing;
KW Lipid degradation; Lipid metabolism; Phosphoprotein; Reference proteome;
KW Steroid metabolism; Transferase.
FT CHAIN 1..285
FT /note="Sulfotransferase 2A1"
FT /id="PRO_0000085141"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:11988089,
FT ECO:0000269|PubMed:14573603"
FT BINDING 44..49
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:10854859"
FT BINDING 121
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:10854859"
FT BINDING 129
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:10854859"
FT BINDING 184
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:10854859"
FT BINDING 218..223
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:10854859"
FT BINDING 247..249
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000269|PubMed:10854859"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 44
FT /note="K -> E (sulfating activity toward both DHEA and
FT pregnenolone is completely abolished; dbSNP:rs772897551)"
FT /evidence="ECO:0000269|PubMed:29671343"
FT /id="VAR_083881"
FT VARIANT 63
FT /note="A -> P (in dbSNP:rs11569681)"
FT /evidence="ECO:0000269|PubMed:7678732"
FT /id="VAR_052520"
FT VARIANT 76
FT /note="P -> T (decreases of the sulfotransferase activity
FT toward DHEA; decreases of the sulfotransferase activity
FT toward pregnenolone; dbSNP:rs775030275)"
FT /evidence="ECO:0000269|PubMed:29671343"
FT /id="VAR_083882"
FT VARIANT 147
FT /note="E -> K (decreases of the sulfotransferase activity
FT toward DHEA; no effect on the sulfotransferase activity
FT toward pregnenolone; dbSNP:rs751309613)"
FT /evidence="ECO:0000269|PubMed:29671343"
FT /id="VAR_083883"
FT VARIANT 148
FT /note="E -> K (decreases of the sulfotransferase activity
FT toward DHEA; decreases of the sulfotransferase activity
FT toward pregnenolone; dbSNP:rs368067020)"
FT /evidence="ECO:0000269|PubMed:29671343"
FT /id="VAR_083884"
FT VARIANT 246
FT /note="L -> P (decreases of the sulfotransferase activity
FT toward DHEA; decreases of the sulfotransferase activity
FT toward pregnenolone; dbSNP:rs757338859)"
FT /evidence="ECO:0000269|PubMed:29671343"
FT /id="VAR_083885"
FT VARIANT 258
FT /note="F -> L (decreases of the sulfotransferase activity
FT toward DHEA; decreases of the sulfotransferase activity
FT toward pregnenolone; dbSNP:rs746239667 and
FT dbSNP:rs779218418)"
FT /evidence="ECO:0000269|PubMed:29671343"
FT /id="VAR_083886"
FT VARIANT 261
FT /note="A -> T (in dbSNP:rs11569679)"
FT /id="VAR_052521"
FT VARIANT 262
FT /note="Q -> E (decreases of the sulfotransferase activity
FT toward DHEA; no effect on the sulfotransferase activity
FT toward pregnenolone; dbSNP:rs753928755)"
FT /evidence="ECO:0000269|PubMed:29671343"
FT /id="VAR_083887"
FT MUTAGEN 137
FT /note="M->I: Strongly reduces substrate inhibition when ADT
FT or DHEA are used as substrates."
FT /evidence="ECO:0000269|PubMed:18042734"
FT MUTAGEN 137
FT /note="M->W: Substrate inhibition is completely eliminated
FT for DHEA; when associated with A-238."
FT /evidence="ECO:0000269|PubMed:18042734"
FT MUTAGEN 238
FT /note="Y->A: Completely eliminates the substrate inhibition
FT when ADT is used as substrate. Partially eliminates
FT substrate inhibition when DHEA is used as substrate.
FT Completely eliminates the substrate inhibition for DHEA,
FT when associated with I-137."
FT /evidence="ECO:0000269|PubMed:18042734"
FT MUTAGEN 238
FT /note="Y->F: Strongly reduces substrate inhibition when ADT
FT or DHEA are used as substrates."
FT /evidence="ECO:0000269|PubMed:18042734"
FT MUTAGEN 238
FT /note="Y->W: Strongly reduces substrate inhibition when ADT
FT or DHEA are used as substrates."
FT /evidence="ECO:0000269|PubMed:18042734"
FT CONFLICT 90
FT /note="T -> S (in Ref. 1; AAA35758/CAA49755)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="L -> D (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="L -> V (in Ref. 6; AAB23169)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2QP4"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:1J99"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 64..68
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1EFH"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:1J99"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:1J99"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1J99"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:3F3Y"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 260..274
FT /evidence="ECO:0007829|PDB:1J99"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1J99"
SQ 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
