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Sulfotransferase 1A2 (ST1A2) (EC 2.8.2.1) (Aryl sulfotransferase 2) (Phenol sulfotransferase 2) (Phenol-sulfating phenol sulfotransferase 2) (P-PST 2)

 ST1A2_HUMAN             Reviewed;         295 AA.
P50226; A9QY25; P78393; Q14CJ7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 2.
27-SEP-2017, entry version 153.
RecName: Full=Sulfotransferase 1A2;
Short=ST1A2;
EC=2.8.2.1;
AltName: Full=Aryl sulfotransferase 2;
AltName: Full=Phenol sulfotransferase 2;
AltName: Full=Phenol-sulfating phenol sulfotransferase 2;
Short=P-PST 2;
Name=SULT1A2; Synonyms=STP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-7; THR-235 AND GLU-282.
TISSUE=Liver;
PubMed=8697101; DOI=10.1016/1357-2725(95)00164-6;
Zhu X., Veronese M.E., Iocco P., McManus M.E.;
"cDNA cloning and expression of a new form of human aryl
sulfotransferase.";
Int. J. Biochem. Cell Biol. 28:565-571(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LEU-19 AND GLU-282.
TISSUE=Liver;
PubMed=7581483;
Ozawa S., Nagata K., Shimada M., Ueda M., Tsuzuki T., Yamazoe Y.,
Kato R.;
"Primary structures and properties of two related forms of aryl
sulfotransferases in human liver.";
Pharmacogenetics 5:S135-S140(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8033246; DOI=10.1016/0009-2797(94)90057-4;
Yamazoe Y., Nagata K., Ozawa S., Kato R.;
"Structural similarity and diversity of sulfotransferases.";
Chem. Biol. Interact. 92:107-117(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-282.
PubMed=8661000; DOI=10.1006/geno.1996.0216;
Her C., Raftogianis R., Weinshilboum R.M.;
"Human phenol sulfotransferase STP2 gene: molecular cloning,
structural characterization, and chromosomal localization.";
Genomics 33:409-420(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-7; THR-235 AND
GLU-282.
PubMed=8912648; DOI=10.1006/bbrc.1996.1628;
Dooley T.P., Huang Z.;
"Genomic organization and DNA sequences of two human phenol
sulfotransferase genes (STP1 and STP2) on the short arm of chromosome
16.";
Biochem. Biophys. Res. Commun. 228:134-140(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-7; THR-235 AND
GLU-282.
PubMed=9119390; DOI=10.1006/geno.1996.4575;
Gaedigk A., Beatty B.G., Grant D.M.;
"Cloning, structural organization, and chromosomal mapping of the
human phenol sulfotransferase STP2 gene.";
Genomics 40:242-246(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-282.
TISSUE=Brain;
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).
[9]
CHARACTERIZATION.
PubMed=7889867; DOI=10.1289/ehp.94102s699;
Yamazoe Y., Ozawa S., Nagata K., Gong D.-W., Kato R.;
"Characterization and expression of hepatic sulfotransferase involved
in the metabolism of N-substituted aryl compounds.";
Environ. Health Perspect. 102:99-103(1994).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH
ADENOSINE-3'-5'-DIPHOSPHATE, AND CATALYTIC ACTIVITY.
PubMed=20417180; DOI=10.1016/j.bbrc.2010.04.109;
Lu J., Li H., Zhang J., Li M., Liu M.Y., An X., Liu M.C., Chang W.;
"Crystal structures of SULT1A2 and SULT1A1 *3: insights into the
substrate inhibition and the role of Tyr149 in SULT1A2.";
Biochem. Biophys. Res. Commun. 396:429-434(2010).
[11]
VARIANT THR-235.
PubMed=10762004; DOI=10.1097/00008571-200003000-00008;
Engelke C.E., Meinl W., Boeing H., Glatt H.;
"Association between functional genetic polymorphisms of human
sulfotransferases 1A1 and 1A2.";
Pharmacogenetics 10:163-169(2000).
-!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl
sulfate (PAPS) as sulfonate donor to catalyze the sulfate
conjugation of catecholamines, phenolic drugs and
neurotransmitters. Is also responsible for the sulfonation and
activation of minoxidil. Mediates the metabolic activation of
carcinogenic N-hydroxyarylamines to DNA binding products and could
so participate as modulating factor of cancer risk.
-!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + a phenol =
adenosine 3',5'-bisphosphate + an aryl sulfate.
{ECO:0000269|PubMed:20417180}.
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- INTERACTION:
Q9GZT8:NIF3L1; NbExp=3; IntAct=EBI-6137631, EBI-740897;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the sulfotransferase 1 family.
{ECO:0000305}.
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EMBL; U28170; AAB09659.1; -; mRNA.
EMBL; U28169; AAB09658.1; -; mRNA.
EMBL; X78282; CAA55088.1; -; mRNA.
EMBL; U34804; AAB09758.1; -; Genomic_DNA.
EMBL; U72202; AAB08970.1; -; Genomic_DNA.
EMBL; U72196; AAB08970.1; JOINED; Genomic_DNA.
EMBL; U72197; AAB08970.1; JOINED; Genomic_DNA.
EMBL; U72198; AAB08970.1; JOINED; Genomic_DNA.
EMBL; U72199; AAB08970.1; JOINED; Genomic_DNA.
EMBL; U72200; AAB08970.1; JOINED; Genomic_DNA.
EMBL; U72201; AAB08970.1; JOINED; Genomic_DNA.
EMBL; U76619; AAB18753.1; -; Genomic_DNA.
EMBL; U33886; AAC51149.1; -; Genomic_DNA.
EMBL; U33886; ABX65442.1; -; Genomic_DNA.
EMBL; AC020765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC113727; AAI13728.1; -; mRNA.
EMBL; BC113729; AAI13730.1; -; mRNA.
CCDS; CCDS10636.1; -.
PIR; G01843; G01843.
PIR; JC5249; JC5249.
PIR; S52791; S52791.
RefSeq; NP_001045.1; NM_001054.3.
RefSeq; NP_803564.1; NM_177528.2.
UniGene; Hs.546304; -.
PDB; 1Z29; X-ray; 2.40 A; A=1-295.
PDBsum; 1Z29; -.
ProteinModelPortal; P50226; -.
SMR; P50226; -.
BioGrid; 112673; 9.
IntAct; P50226; 1.
STRING; 9606.ENSP00000338742; -.
ChEMBL; CHEMBL1743292; -.
iPTMnet; P50226; -.
PhosphoSitePlus; P50226; -.
BioMuta; SULT1A2; -.
DMDM; 288558827; -.
EPD; P50226; -.
MaxQB; P50226; -.
PaxDb; P50226; -.
PeptideAtlas; P50226; -.
PRIDE; P50226; -.
Ensembl; ENST00000335715; ENSP00000338742; ENSG00000197165.
Ensembl; ENST00000395630; ENSP00000378992; ENSG00000197165.
GeneID; 6799; -.
KEGG; hsa:6799; -.
UCSC; uc002dqg.3; human.
CTD; 6799; -.
DisGeNET; 6799; -.
EuPathDB; HostDB:ENSG00000197165.10; -.
GeneCards; SULT1A2; -.
HGNC; HGNC:11454; SULT1A2.
HPA; HPA049500; -.
HPA; HPA051051; -.
MIM; 601292; gene.
neXtProt; NX_P50226; -.
OpenTargets; ENSG00000197165; -.
PharmGKB; PA341; -.
eggNOG; KOG1584; Eukaryota.
eggNOG; ENOG4111H56; LUCA.
GeneTree; ENSGT00760000118932; -.
HOGENOM; HOG000037209; -.
HOVERGEN; HBG001195; -.
InParanoid; P50226; -.
KO; K01014; -.
OMA; MRRMRLY; -.
OrthoDB; EOG091G0D5F; -.
PhylomeDB; P50226; -.
TreeFam; TF321745; -.
BioCyc; MetaCyc:HS11091-MONOMER; -.
BRENDA; 2.8.2.1; 2681.
BRENDA; 2.8.2.9; 2681.
Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules.
SABIO-RK; P50226; -.
EvolutionaryTrace; P50226; -.
GeneWiki; SULT1A2; -.
GenomeRNAi; 6799; -.
PRO; PR:P50226; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000197165; -.
CleanEx; HS_SULT1A2; -.
ExpressionAtlas; P50226; baseline and differential.
Genevisible; P50226; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0004062; F:aryl sulfotransferase activity; IDA:UniProtKB.
GO; GO:0047894; F:flavonol 3-sulfotransferase activity; IDA:BHF-UCL.
GO; GO:0008146; F:sulfotransferase activity; TAS:Reactome.
GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA.
GO; GO:0009309; P:amine biosynthetic process; TAS:ProtInc.
GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
GO; GO:0006068; P:ethanol catabolic process; IDA:CAFA.
GO; GO:0018958; P:phenol-containing compound metabolic process; IDA:UniProtKB.
GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
GO; GO:0051923; P:sulfation; IDA:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
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; Catecholamine metabolism; Complete proteome; Cytoplasm;
Lipid metabolism; Polymorphism; Reference proteome;
Steroid metabolism; Transferase.
CHAIN 1 295 Sulfotransferase 1A2.
/FTId=PRO_0000085128.
NP_BIND 48 53 PAPS.
NP_BIND 227 232 PAPS.
NP_BIND 255 259 PAPS.
REGION 106 108 Substrate binding. {ECO:0000250}.
ACT_SITE 108 108 Proton acceptor. {ECO:0000250}.
BINDING 130 130 PAPS.
BINDING 138 138 PAPS.
BINDING 193 193 PAPS.
VARIANT 7 7 I -> T (in dbSNP:rs1136703).
{ECO:0000269|PubMed:8697101,
ECO:0000269|PubMed:8912648,
ECO:0000269|PubMed:9119390}.
/FTId=VAR_007426.
VARIANT 19 19 P -> L (in dbSNP:rs10797300).
{ECO:0000269|PubMed:7581483}.
/FTId=VAR_057340.
VARIANT 62 62 Y -> F (in dbSNP:rs4987024).
/FTId=VAR_057341.
VARIANT 235 235 N -> T (in dbSNP:rs1059491).
{ECO:0000269|PubMed:10762004,
ECO:0000269|PubMed:8697101,
ECO:0000269|PubMed:8912648,
ECO:0000269|PubMed:9119390}.
/FTId=VAR_007427.
VARIANT 239 239 N -> S (in dbSNP:rs45472392).
/FTId=VAR_057342.
VARIANT 282 282 K -> E (in dbSNP:rs27742).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7581483,
ECO:0000269|PubMed:8661000,
ECO:0000269|PubMed:8697101,
ECO:0000269|PubMed:8912648,
ECO:0000269|PubMed:9119390}.
/FTId=VAR_061887.
CONFLICT 290 290 S -> T (in Ref. 6; AAC51149/ABX65442).
{ECO:0000305}.
STRAND 13 15 {ECO:0000244|PDB:1Z29}.
STRAND 18 20 {ECO:0000244|PDB:1Z29}.
HELIX 22 26 {ECO:0000244|PDB:1Z29}.
HELIX 30 32 {ECO:0000244|PDB:1Z29}.
STRAND 41 46 {ECO:0000244|PDB:1Z29}.
HELIX 51 62 {ECO:0000244|PDB:1Z29}.
HELIX 75 78 {ECO:0000244|PDB:1Z29}.
HELIX 92 95 {ECO:0000244|PDB:1Z29}.
TURN 96 98 {ECO:0000244|PDB:1Z29}.
STRAND 104 107 {ECO:0000244|PDB:1Z29}.
TURN 111 113 {ECO:0000244|PDB:1Z29}.
HELIX 116 120 {ECO:0000244|PDB:1Z29}.
STRAND 124 129 {ECO:0000244|PDB:1Z29}.
HELIX 132 145 {ECO:0000244|PDB:1Z29}.
HELIX 155 163 {ECO:0000244|PDB:1Z29}.
HELIX 172 182 {ECO:0000244|PDB:1Z29}.
TURN 183 185 {ECO:0000244|PDB:1Z29}.
STRAND 188 192 {ECO:0000244|PDB:1Z29}.
HELIX 193 198 {ECO:0000244|PDB:1Z29}.
HELIX 200 210 {ECO:0000244|PDB:1Z29}.
HELIX 217 226 {ECO:0000244|PDB:1Z29}.
HELIX 229 234 {ECO:0000244|PDB:1Z29}.
TURN 236 238 {ECO:0000244|PDB:1Z29}.
TURN 245 247 {ECO:0000244|PDB:1Z29}.
TURN 250 252 {ECO:0000244|PDB:1Z29}.
HELIX 263 266 {ECO:0000244|PDB:1Z29}.
HELIX 270 283 {ECO:0000244|PDB:1Z29}.
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


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