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P50226 (ST1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Sulfotransferase 1A2
PRO_0000085128

Regions

Nucleotide binding48 – 536PAPS
Nucleotide binding227 – 2326PAPS
Nucleotide binding255 – 2595PAPS
Region106 – 1083Substrate binding By similarity

Sites

Active site1081Proton acceptor By similarity
Binding site1301PAPS
Binding site1381PAPS
Binding site1931PAPS

Natural variations

Natural variant71I → T. Ref.1 Ref.5 Ref.6
Corresponds to variant rs1136703 [ dbSNP | Ensembl ].
VAR_007426
Natural variant191P → L. Ref.2
Corresponds to variant rs10797300 [ dbSNP | Ensembl ].
VAR_057340
Natural variant621Y → F.
Corresponds to variant rs4987024 [ dbSNP | Ensembl ].
VAR_057341
Natural variant2351N → T. Ref.1 Ref.5 Ref.6 Ref.11
Corresponds to variant rs1059491 [ dbSNP | Ensembl ].
VAR_007427
Natural variant2391N → S.
Corresponds to variant rs45472392 [ dbSNP | Ensembl ].
VAR_057342
Natural variant2821K → E. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs27742 [ dbSNP | Ensembl ].
VAR_061887

Experimental info

Sequence conflict2901S → T in AAC51149. Ref.6
Sequence conflict2901S → T in ABX65442. Ref.6

Secondary structure

.................................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50226 [UniParc].

Last modified February 9, 2010. Version 2.
Checksum: EB505BBDAA3A2E09

FASTA29534,310
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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 expand/collapse EMBL AC list , 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.
CCDSCCDS10636.1.
PIRG01843.
JC5249.
S52791.
RefSeqNP_001045.1. NM_001054.3.
NP_803564.1. NM_177528.2.
XP_006721139.1. XM_006721076.1.
UniGeneHs.546304.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z29X-ray2.40A1-295[»]
ProteinModelPortalP50226.
SMRP50226. Positions 8-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112673. 2 interactions.
STRING9606.ENSP00000338742.

Chemistry

ChEMBLCHEMBL1743292.

PTM databases

PhosphoSiteP50226.

Polymorphism databases

DMDM288558827.

Proteomic databases

MaxQBP50226.
PaxDbP50226.
PRIDEP50226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335715; ENSP00000338742; ENSG00000197165.
ENST00000395630; ENSP00000378992; ENSG00000197165.
GeneID6799.
KEGGhsa:6799.
UCSCuc002dqg.2. human.

Organism-specific databases

CTD6799.
GeneCardsGC16M028603.
HGNCHGNC:11454. SULT1A2.
MIM601292. gene.
neXtProtNX_P50226.
PharmGKBPA341.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260792.
HOGENOMHOG000037209.
HOVERGENHBG001195.
InParanoidP50226.
KOK01014.
OMAWESFLEK.
PhylomeDBP50226.
TreeFamTF321745.

Enzyme and pathway databases

BRENDA2.8.2.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP50226.

Gene expression databases

ArrayExpressP50226.
BgeeP50226.
CleanExHS_SULT1A2.
GenevestigatorP50226.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP50226.
GeneWikiSULT1A2.
GenomeRNAi6799.
NextBio26553.
PROP50226.
SOURCESearch...

Entry information

Entry nameST1A2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM