ST1A2_HUMAN
ID ST1A2_HUMAN Reviewed; 295 AA.
AC P50226; A9QY25; P78393; Q14CJ7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Sulfotransferase 1A2;
DE Short=ST1A2;
DE EC=2.8.2.1;
DE AltName: Full=Aryl sulfotransferase 2;
DE AltName: Full=Phenol sulfotransferase 2;
DE AltName: Full=Phenol-sulfating phenol sulfotransferase 2;
DE Short=P-PST 2;
GN Name=SULT1A2; Synonyms=STP2;
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], AND VARIANTS THR-7; THR-235 AND GLU-282.
RC TISSUE=Liver;
RX PubMed=8697101; DOI=10.1016/1357-2725(95)00164-6;
RA Zhu X., Veronese M.E., Iocco P., McManus M.E.;
RT "cDNA cloning and expression of a new form of human aryl
RT sulfotransferase.";
RL Int. J. Biochem. Cell Biol. 28:565-571(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-19 AND GLU-282.
RC TISSUE=Liver;
RX PubMed=7581483; DOI=10.1097/00008571-199512001-00015;
RA Ozawa S., Nagata K., Shimada M., Ueda M., Tsuzuki T., Yamazoe Y., Kato R.;
RT "Primary structures and properties of two related forms of aryl
RT sulfotransferases in human liver.";
RL Pharmacogenetics 5:S135-S140(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8033246; DOI=10.1016/0009-2797(94)90057-4;
RA Yamazoe Y., Nagata K., Ozawa S., Kato R.;
RT "Structural similarity and diversity of sulfotransferases.";
RL Chem. Biol. Interact. 92:107-117(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-282.
RX PubMed=8661000; DOI=10.1006/geno.1996.0216;
RA Her C., Raftogianis R., Weinshilboum R.M.;
RT "Human phenol sulfotransferase STP2 gene: molecular cloning, structural
RT characterization, and chromosomal localization.";
RL Genomics 33:409-420(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-7; THR-235 AND GLU-282.
RX PubMed=8912648; DOI=10.1006/bbrc.1996.1628;
RA Dooley T.P., Huang Z.;
RT "Genomic organization and DNA sequences of two human phenol
RT sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16.";
RL Biochem. Biophys. Res. Commun. 228:134-140(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-7; THR-235 AND GLU-282.
RX PubMed=9119390; DOI=10.1006/geno.1996.4575;
RA Gaedigk A., Beatty B.G., Grant D.M.;
RT "Cloning, structural organization, and chromosomal mapping of the human
RT phenol sulfotransferase STP2 gene.";
RL Genomics 40:242-246(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-282.
RC TISSUE=Brain;
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 [9]
RP CHARACTERIZATION.
RX PubMed=7889867; DOI=10.2307/3432160;
RA Yamazoe Y., Ozawa S., Nagata K., Gong D.-W., Kato R.;
RT "Characterization and expression of hepatic sulfotransferase involved in
RT the metabolism of N-substituted aryl compounds.";
RL Environ. Health Perspect. 102:99-103(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH
RP ADENOSINE-3'-5'-DIPHOSPHATE, AND CATALYTIC ACTIVITY.
RX PubMed=20417180; DOI=10.1016/j.bbrc.2010.04.109;
RA Lu J., Li H., Zhang J., Li M., Liu M.Y., An X., Liu M.C., Chang W.;
RT "Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate
RT inhibition and the role of Tyr149 in SULT1A2.";
RL Biochem. Biophys. Res. Commun. 396:429-434(2010).
RN [11]
RP VARIANT THR-235.
RX PubMed=10762004; DOI=10.1097/00008571-200003000-00008;
RA Engelke C.E., Meinl W., Boeing H., Glatt H.;
RT "Association between functional genetic polymorphisms of human
RT sulfotransferases 1A1 and 1A2.";
RL Pharmacogenetics 10:163-169(2000).
CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate
CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation of
CC catecholamines, phenolic drugs and neurotransmitters. Is also
CC responsible for the sulfonation and activation of minoxidil. Mediates
CC the metabolic activation of carcinogenic N-hydroxyarylamines to DNA
CC binding products and could so participate as modulating factor of
CC cancer risk.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-
CC bisphosphate + an aryl sulfate + H(+); Xref=Rhea:RHEA:12164,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1;
CC Evidence={ECO:0000269|PubMed:20417180};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P50226; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-6137631, EBI-740897;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
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DR EMBL; U28170; AAB09659.1; -; mRNA.
DR EMBL; U28169; AAB09658.1; -; mRNA.
DR EMBL; X78282; CAA55088.1; -; mRNA.
DR EMBL; U34804; AAB09758.1; -; Genomic_DNA.
DR EMBL; U72202; AAB08970.1; -; Genomic_DNA.
DR EMBL; U72196; AAB08970.1; JOINED; Genomic_DNA.
DR EMBL; U72197; AAB08970.1; JOINED; Genomic_DNA.
DR EMBL; U72198; AAB08970.1; JOINED; Genomic_DNA.
DR EMBL; U72199; AAB08970.1; JOINED; Genomic_DNA.
DR EMBL; U72200; AAB08970.1; JOINED; Genomic_DNA.
DR EMBL; U72201; AAB08970.1; JOINED; Genomic_DNA.
DR EMBL; U76619; AAB18753.1; -; Genomic_DNA.
DR EMBL; U33886; AAC51149.1; -; Genomic_DNA.
DR EMBL; U33886; ABX65442.1; -; Genomic_DNA.
DR EMBL; AC020765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113727; AAI13728.1; -; mRNA.
DR EMBL; BC113729; AAI13730.1; -; mRNA.
DR CCDS; CCDS10636.1; -.
DR PIR; G01843; G01843.
DR PIR; JC5249; JC5249.
DR PIR; S52791; S52791.
DR RefSeq; NP_001045.1; NM_001054.3.
DR RefSeq; NP_803564.1; NM_177528.2.
DR PDB; 1Z29; X-ray; 2.40 A; A=1-295.
DR PDBsum; 1Z29; -.
DR AlphaFoldDB; P50226; -.
DR SMR; P50226; -.
DR BioGRID; 112673; 18.
DR IntAct; P50226; 1.
DR STRING; 9606.ENSP00000378992; -.
DR ChEMBL; CHEMBL1743292; -.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00871; Terbutaline.
DR DrugBank; DB09100; Thyroid, porcine.
DR iPTMnet; P50226; -.
DR PhosphoSitePlus; P50226; -.
DR BioMuta; SULT1A2; -.
DR DMDM; 288558827; -.
DR jPOST; P50226; -.
DR MassIVE; P50226; -.
DR MaxQB; P50226; -.
DR PaxDb; P50226; -.
DR PeptideAtlas; P50226; -.
DR PRIDE; P50226; -.
DR ProteomicsDB; 56211; -.
DR Antibodypedia; 66741; 86 antibodies from 19 providers.
DR DNASU; 6799; -.
DR Ensembl; ENST00000335715.9; ENSP00000338742.4; ENSG00000197165.11.
DR Ensembl; ENST00000395630.5; ENSP00000378992.1; ENSG00000197165.11.
DR GeneID; 6799; -.
DR KEGG; hsa:6799; -.
DR MANE-Select; ENST00000335715.9; ENSP00000338742.4; NM_001054.4; NP_001045.2.
DR UCSC; uc002dqg.3; human.
DR CTD; 6799; -.
DR DisGeNET; 6799; -.
DR GeneCards; SULT1A2; -.
DR HGNC; HGNC:11454; SULT1A2.
DR HPA; ENSG00000197165; Group enriched (intestine, liver).
DR MIM; 601292; gene.
DR neXtProt; NX_P50226; -.
DR OpenTargets; ENSG00000197165; -.
DR PharmGKB; PA341; -.
DR VEuPathDB; HostDB:ENSG00000197165; -.
DR eggNOG; KOG1584; Eukaryota.
DR GeneTree; ENSGT00940000163450; -.
DR HOGENOM; CLU_027239_1_2_1; -.
DR InParanoid; P50226; -.
DR OMA; AQYEKFE; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; P50226; -.
DR TreeFam; TF321745; -.
DR BioCyc; MetaCyc:HS11091-MON; -.
DR BRENDA; 2.8.2.1; 2681.
DR BRENDA; 2.8.2.2; 2681.
DR BRENDA; 2.8.2.9; 2681.
DR PathwayCommons; P50226; -.
DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
DR SABIO-RK; P50226; -.
DR SignaLink; P50226; -.
DR BioGRID-ORCS; 6799; 19 hits in 1062 CRISPR screens.
DR ChiTaRS; SULT1A2; human.
DR EvolutionaryTrace; P50226; -.
DR GeneWiki; SULT1A2; -.
DR GenomeRNAi; 6799; -.
DR Pharos; P50226; Tbio.
DR PRO; PR:P50226; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P50226; protein.
DR Bgee; ENSG00000197165; Expressed in duodenum and 92 other tissues.
DR ExpressionAtlas; P50226; baseline and differential.
DR Genevisible; P50226; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0047894; F:flavonol 3-sulfotransferase activity; IDA:BHF-UCL.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
DR GO; GO:0009309; P:amine biosynthetic process; TAS:ProtInc.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
DR GO; GO:0018958; P:phenol-containing compound metabolic process; IDA:UniProtKB.
DR GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
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; Catecholamine metabolism; Cytoplasm; Lipid metabolism;
KW Reference proteome; Steroid metabolism; Transferase.
FT CHAIN 1..295
FT /note="Sulfotransferase 1A2"
FT /id="PRO_0000085128"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 48..53
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 106..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 138
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 193
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 227..232
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT BINDING 255..259
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT VARIANT 7
FT /note="I -> T (in dbSNP:rs1136703)"
FT /evidence="ECO:0000269|PubMed:8697101,
FT ECO:0000269|PubMed:8912648, ECO:0000269|PubMed:9119390"
FT /id="VAR_007426"
FT VARIANT 19
FT /note="P -> L (in dbSNP:rs10797300)"
FT /evidence="ECO:0000269|PubMed:7581483"
FT /id="VAR_057340"
FT VARIANT 62
FT /note="Y -> F (in dbSNP:rs4987024)"
FT /id="VAR_057341"
FT VARIANT 235
FT /note="N -> T (in dbSNP:rs1059491)"
FT /evidence="ECO:0000269|PubMed:10762004,
FT ECO:0000269|PubMed:8697101, ECO:0000269|PubMed:8912648,
FT ECO:0000269|PubMed:9119390"
FT /id="VAR_007427"
FT VARIANT 239
FT /note="N -> S (in dbSNP:rs45472392)"
FT /id="VAR_057342"
FT VARIANT 282
FT /note="K -> E (in dbSNP:rs27742)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7581483, ECO:0000269|PubMed:8661000,
FT ECO:0000269|PubMed:8697101, ECO:0000269|PubMed:8912648,
FT ECO:0000269|PubMed:9119390"
FT /id="VAR_061887"
FT CONFLICT 290
FT /note="S -> T (in Ref. 6; AAC51149/ABX65442)"
FT /evidence="ECO:0000305"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:1Z29"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1Z29"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:1Z29"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1Z29"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1Z29"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:1Z29"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 132..145
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 172..182
FT /evidence="ECO:0007829|PDB:1Z29"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1Z29"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:1Z29"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1Z29"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:1Z29"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:1Z29"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:1Z29"
SQ SEQUENCE 295 AA; 34310 MW; EB505BBDAA3A2E09 CRC64;
MELIQDISRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG TTWVSQILDM
IYQGGDLEKC HRAPIFMRVP FLEFKVPGIP SGMETLKNTP APRLLKTHLP LALLPQTLLD
QKVKVVYVAR NAKDVAVSYY HFYHMAKVYP HPGTWESFLE KFMAGEVSYG SWYQHVQEWW
ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETV DLMVEHTSFK EMKKNPMTNY
TTVRREFMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AKKMAGCSLS FRSEL
