P50226 (ST1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfotransferase 1A2
Short name=ST1A2
EC=2.8.2.1

Alternative name(s):
Aryl sulfotransferase 2
Phenol sulfotransferase 2
Phenol-sulfating phenol sulfotransferase 2
Short name=P-PST 2

Gene names

Name:	SULT1A2
Synonyms:	STP2

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	295 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 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. Ref.10
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the sulfotransferase 1 family.

Ontologies

Keywords
Biological process	Catecholamine metabolism Lipid metabolism Steroid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome amine biosynthetic process Traceable author statement Ref.6. Source: ProtInc catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW phenol-containing compound metabolic process Inferred from direct assay Ref.10. Source: UniProtKB steroid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW sulfation Inferred from direct assay PubMed 20056724. Source: BHF-UCL xenobiotic metabolic process Inferred from direct assay Ref.10. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	aryl sulfotransferase activity Inferred from direct assay Ref.10. Source: UniProtKB flavonol 3-sulfotransferase activity Inferred from direct assay PubMed 20056724. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 295

295

Sulfotransferase 1A2

PRO_0000085128

Regions

Nucleotide binding

48 – 53

6

PAPS

Nucleotide binding

227 – 232

6

PAPS

Nucleotide binding

255 – 259

5

PAPS

Region

106 – 108

3

Substrate binding By similarity

Sites

Active site

108

1

Proton acceptor By similarity

Binding site

130

1

PAPS

Binding site

138

1

PAPS

Binding site

193

1

PAPS

Natural variations

Natural variant

7

1

I → T. Ref.1 Ref.5 Ref.6

VAR_007426

Natural variant

19

1

P → L. Ref.2
Corresponds to variant rs10797300 [ dbSNP | Ensembl ].

VAR_057340

Natural variant

62

1

Y → F.
Corresponds to variant rs4987024 [ dbSNP | Ensembl ].

VAR_057341

Natural variant

235

1

N → T. Ref.1 Ref.5 Ref.6 Ref.11
Corresponds to variant rs1059491 [ dbSNP | Ensembl ].

VAR_007427

Natural variant

239

1

N → S.
Corresponds to variant rs45472392 [ dbSNP | Ensembl ].

VAR_057342

Natural variant

282

1

K → E. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs27742 [ dbSNP | Ensembl ].

VAR_061887

Experimental info

Sequence conflict

290

1

S → T in AAC51149. Ref.6

Sequence conflict

290

1

S → T in ABX65442. Ref.6

Secondary structure

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295

Helix Strand Turn

Details...

Beta strand

13 – 15

3

Beta strand

18 – 20

3

Helix

22 – 26

5

Helix

30 – 32

3

Beta strand

41 – 46

6

Helix

51 – 62

12

Helix

75 – 78

4

Helix

92 – 95

4

Turn

96 – 98

3

Beta strand

104 – 107

4

Turn

111 – 113

3

Helix

116 – 120

5

Beta strand

124 – 129

6

Helix

132 – 145

14

Helix

155 – 163

9

Helix

172 – 182

11

Turn

183 – 185

3

Beta strand

188 – 192

5

Helix

193 – 198

6

Helix

200 – 210

11

Helix

217 – 226

10

Helix

229 – 234

6

Turn

236 – 238

3

Turn

245 – 247

3

Turn

250 – 252

3

Helix

263 – 266

4

Helix

270 – 283

14

Sequences

	Sequence		Length	Mass (Da)
	P50226 [UniParc]. Last modified February 9, 2010. Version 2. Checksum: EB505BBDAA3A2E09	FASTA	295	34,310
	10 20 30 40 50 60 MELIQDISRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG TTWVSQILDM 70 80 90 100 110 120 IYQGGDLEKC HRAPIFMRVP FLEFKVPGIP SGMETLKNTP APRLLKTHLP LALLPQTLLD 130 140 150 160 170 180 QKVKVVYVAR NAKDVAVSYY HFYHMAKVYP HPGTWESFLE KFMAGEVSYG SWYQHVQEWW 190 200 210 220 230 240 ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETV DLMVEHTSFK EMKKNPMTNY 250 260 270 280 290 TTVRREFMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AKKMAGCSLS FRSEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and expression of a new form of human aryl sulfotransferase." Zhu X., Veronese M.E., Iocco P., McManus M.E. Int. J. Biochem. Cell Biol. 28:565-571(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-7; THR-235 AND GLU-282. Tissue: Liver.
[2]	"Primary structures and properties of two related forms of aryl sulfotransferases in human liver." Ozawa S., Nagata K., Shimada M., Ueda M., Tsuzuki T., Yamazoe Y., Kato R. Pharmacogenetics 5:S135-S140(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-19 AND GLU-282. Tissue: Liver.
[3]	"Structural similarity and diversity of sulfotransferases." Yamazoe Y., Nagata K., Ozawa S., Kato R. Chem. Biol. Interact. 92:107-117(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Human phenol sulfotransferase STP2 gene: molecular cloning, structural characterization, and chromosomal localization." Her C., Raftogianis R., Weinshilboum R.M. Genomics 33:409-420(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-282.
[5]	"Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16." Dooley T.P., Huang Z. Biochem. Biophys. Res. Commun. 228:134-140(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-7; THR-235 AND GLU-282.
[6]	"Cloning, structural organization, and chromosomal mapping of the human phenol sulfotransferase STP2 gene." Gaedigk A., Beatty B.G., Grant D.M. Genomics 40:242-246(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-7; THR-235 AND GLU-282.
[7]	"The sequence and analysis of duplication-rich human chromosome 16." 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. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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], VARIANT GLU-282. Tissue: Brain.
[9]	"Characterization and expression of hepatic sulfotransferase involved in the metabolism of N-substituted aryl compounds." Yamazoe Y., Ozawa S., Nagata K., Gong D.-W., Kato R. Environ. Health Perspect. 102:99-103(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2." Lu J., Li H., Zhang J., Li M., Liu M.Y., An X., Liu M.C., Chang W. Biochem. Biophys. Res. Commun. 396:429-434(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE, CATALYTIC ACTIVITY.
[11]	"Association between functional genetic polymorphisms of human sulfotransferases 1A1 and 1A2." Engelke C.E., Meinl W., Boeing H., Glatt H. Pharmacogenetics 10:163-169(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-235.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U28170 mRNA. Translation: AAB09659.1.
U28169 mRNA. Translation: AAB09658.1.
X78282 mRNA. Translation: CAA55088.1.
U34804 Genomic DNA. Translation: AAB09758.1.
U72202 , U72196, U72197, U72198, U72199, U72200, U72201 Genomic DNA. Translation: AAB08970.1.
U76619 Genomic DNA. Translation: AAB18753.1.
U33886 Genomic DNA. Translation: AAC51149.1.
U33886 Genomic DNA. Translation: ABX65442.1.
AC020765 Genomic DNA. No translation available.
BC113727 mRNA. Translation: AAI13728.1.
BC113729 mRNA. Translation: AAI13730.1.

IPI

IPI00300027.

PIR

G01843.
JC5249.
S52791.

RefSeq

NP_001045.1. NM_001054.3.
NP_803564.1. NM_177528.2.

UniGene

Hs.546304.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z29	X-ray	2.40	A	1-295	[»]

ProteinModelPortal

P50226.

SMR

P50226. Positions 8-295.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000338742.

PTM databases

PhosphoSite

P50226.

Polymorphism databases

DMDM

288558827.

Proteomic databases

PaxDb

P50226.

PRIDE

P50226.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000335715; ENSP00000338742; ENSG00000197165.
ENST00000395630; ENSP00000378992; ENSG00000197165.

GeneID

6799.

KEGG

hsa:6799.

UCSC

uc002dqg.2. human.

Organism-specific databases

CTD

6799.

GeneCards

GC16M028603.

HGNC

HGNC:11454. SULT1A2.

MIM

601292. gene.

neXtProt

NX_P50226.

PharmGKB

PA341.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG260792.

HOGENOM

HOG000037209.

HOVERGEN

HBG001195.

InParanoid

P50226.

KO

K01014.

OMA

WESFLEK.

OrthoDB

EOG4255T9.

PhylomeDB

P50226.

Enzyme and pathway databases

BRENDA

2.8.2.1. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P50226.

Gene expression databases

ArrayExpress

P50226.

Bgee

P50226.

CleanEx

HS_SULT1A2.

Genevestigator

P50226.

GermOnline

ENSG00000197165. Homo sapiens.

Family and domain databases

InterPro

IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1743292.

EvolutionaryTrace

P50226.

GenomeRNAi

6799.

NextBio

26553.

SOURCE

Search...

Entry information

Entry name

ST1A2_HUMAN

Accession

Primary (citable) accession number: P50226
Secondary accession number(s): A9QY25, P78393, Q14CJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	February 9, 2010
Last modified:	April 3, 2013
This is version 116 of the entry and version 2 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.