Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Sulfotransferase 1A2

Gene

SULT1A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei108 – 1081Proton acceptorBy similarity
Binding sitei130 – 1301PAPS
Binding sitei138 – 1381PAPS
Binding sitei193 – 1931PAPS

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi48 – 536PAPS
Nucleotide bindingi227 – 2326PAPS
Nucleotide bindingi255 – 2595PAPS

GO - Molecular functioni

  • aryl sulfotransferase activity Source: UniProtKB
  • flavonol 3-sulfotransferase activity Source: BHF-UCL
  • sulfotransferase activity Source: ProtInc

GO - Biological processi

  • 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
  • amine biosynthetic process Source: ProtInc
  • catecholamine metabolic process Source: UniProtKB-KW
  • phenol-containing compound metabolic process Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • steroid metabolic process Source: UniProtKB-KW
  • sulfation Source: BHF-UCL
  • xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Catecholamine metabolism, Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
2.8.2.9. 2681.
ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.
SABIO-RKP50226.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfotransferase 1A2 (EC:2.8.2.1)
Short name:
ST1A2
Alternative name(s):
Aryl sulfotransferase 2
Phenol sulfotransferase 2
Phenol-sulfating phenol sulfotransferase 2
Short name:
P-PST 2
Gene namesi
Name:SULT1A2
Synonyms:STP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:11454. SULT1A2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA341.

Polymorphism and mutation databases

BioMutaiSULT1A2.
DMDMi288558827.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Sulfotransferase 1A2PRO_0000085128Add
BLAST

Proteomic databases

MaxQBiP50226.
PaxDbiP50226.
PRIDEiP50226.

PTM databases

PhosphoSiteiP50226.

Expressioni

Gene expression databases

BgeeiP50226.
CleanExiHS_SULT1A2.
ExpressionAtlasiP50226. baseline and differential.
GenevisibleiP50226. HS.

Organism-specific databases

HPAiHPA049500.
HPA051051.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NIF3L1Q9GZT83EBI-6137631,EBI-740897

Protein-protein interaction databases

BioGridi112673. 9 interactions.
IntActiP50226. 1 interaction.
STRINGi9606.ENSP00000338742.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 153Combined sources
Beta strandi18 – 203Combined sources
Helixi22 – 265Combined sources
Helixi30 – 323Combined sources
Beta strandi41 – 466Combined sources
Helixi51 – 6212Combined sources
Helixi75 – 784Combined sources
Helixi92 – 954Combined sources
Turni96 – 983Combined sources
Beta strandi104 – 1074Combined sources
Turni111 – 1133Combined sources
Helixi116 – 1205Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 14514Combined sources
Helixi155 – 1639Combined sources
Helixi172 – 18211Combined sources
Turni183 – 1853Combined sources
Beta strandi188 – 1925Combined sources
Helixi193 – 1986Combined sources
Helixi200 – 21011Combined sources
Helixi217 – 22610Combined sources
Helixi229 – 2346Combined sources
Turni236 – 2383Combined sources
Turni245 – 2473Combined sources
Turni250 – 2523Combined sources
Helixi263 – 2664Combined sources
Helixi270 – 28314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z29X-ray2.40A1-295[»]
ProteinModelPortaliP50226.
SMRiP50226. Positions 8-295.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50226.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 1083Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiNOG260792.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiP50226.
KOiK01014.
OMAiILEFVGH.
PhylomeDBiP50226.
TreeFamiTF321745.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P50226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELIQDISRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG
60 70 80 90 100
TTWVSQILDM IYQGGDLEKC HRAPIFMRVP FLEFKVPGIP SGMETLKNTP
110 120 130 140 150
APRLLKTHLP LALLPQTLLD QKVKVVYVAR NAKDVAVSYY HFYHMAKVYP
160 170 180 190 200
HPGTWESFLE KFMAGEVSYG SWYQHVQEWW ELSRTHPVLY LFYEDMKENP
210 220 230 240 250
KREIQKILEF VGRSLPEETV DLMVEHTSFK EMKKNPMTNY TTVRREFMDH
260 270 280 290
SISPFMRKGM AGDWKTTFTV AQNERFDADY AKKMAGCSLS FRSEL
Length:295
Mass (Da):34,310
Last modified:February 9, 2010 - v2
Checksum:iEB505BBDAA3A2E09
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti290 – 2901S → T in AAC51149 (PubMed:9119390).Curated
Sequence conflicti290 – 2901S → T in ABX65442 (PubMed:9119390).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71I → T.3 Publications
Corresponds to variant rs1136703 [ dbSNP | Ensembl ].
VAR_007426
Natural varianti19 – 191P → L.1 Publication
Corresponds to variant rs10797300 [ dbSNP | Ensembl ].
VAR_057340
Natural varianti62 – 621Y → F.
Corresponds to variant rs4987024 [ dbSNP | Ensembl ].
VAR_057341
Natural varianti235 – 2351N → T.4 Publications
Corresponds to variant rs1059491 [ dbSNP | Ensembl ].
VAR_007427
Natural varianti239 – 2391N → S.
Corresponds to variant rs45472392 [ dbSNP | Ensembl ].
VAR_057342
Natural varianti282 – 2821K → E.6 Publications
Corresponds to variant rs27742 [ dbSNP | Ensembl ].
VAR_061887

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10636.1.
PIRiG01843.
JC5249.
S52791.
RefSeqiNP_001045.1. NM_001054.3.
NP_803564.1. NM_177528.2.
XP_006721139.1. XM_006721076.2.
XP_011544224.1. XM_011545922.1.
XP_011544225.1. XM_011545923.1.
UniGeneiHs.546304.

Genome annotation databases

EnsembliENST00000335715; ENSP00000338742; ENSG00000197165.
ENST00000395630; ENSP00000378992; ENSG00000197165.
GeneIDi6799.
KEGGihsa:6799.
UCSCiuc002dqg.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10636.1.
PIRiG01843.
JC5249.
S52791.
RefSeqiNP_001045.1. NM_001054.3.
NP_803564.1. NM_177528.2.
XP_006721139.1. XM_006721076.2.
XP_011544224.1. XM_011545922.1.
XP_011544225.1. XM_011545923.1.
UniGeneiHs.546304.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z29X-ray2.40A1-295[»]
ProteinModelPortaliP50226.
SMRiP50226. Positions 8-295.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112673. 9 interactions.
IntActiP50226. 1 interaction.
STRINGi9606.ENSP00000338742.

Chemistry

ChEMBLiCHEMBL1743292.

PTM databases

PhosphoSiteiP50226.

Polymorphism and mutation databases

BioMutaiSULT1A2.
DMDMi288558827.

Proteomic databases

MaxQBiP50226.
PaxDbiP50226.
PRIDEiP50226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335715; ENSP00000338742; ENSG00000197165.
ENST00000395630; ENSP00000378992; ENSG00000197165.
GeneIDi6799.
KEGGihsa:6799.
UCSCiuc002dqg.2. human.

Organism-specific databases

CTDi6799.
GeneCardsiGC16M028603.
HGNCiHGNC:11454. SULT1A2.
HPAiHPA049500.
HPA051051.
MIMi601292. gene.
neXtProtiNX_P50226.
PharmGKBiPA341.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG260792.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiP50226.
KOiK01014.
OMAiILEFVGH.
PhylomeDBiP50226.
TreeFamiTF321745.

Enzyme and pathway databases

BRENDAi2.8.2.1. 2681.
2.8.2.9. 2681.
ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.
SABIO-RKP50226.

Miscellaneous databases

EvolutionaryTraceiP50226.
GeneWikiiSULT1A2.
GenomeRNAii6799.
NextBioi26553.
PROiP50226.
SOURCEiSearch...

Gene expression databases

BgeeiP50226.
CleanExiHS_SULT1A2.
ExpressionAtlasiP50226. baseline and differential.
GenevisibleiP50226. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamiPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiST1A2_HUMAN
AccessioniPrimary (citable) accession number: P50226
Secondary accession number(s): A9QY25, P78393, Q14CJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: February 9, 2010
Last modified: July 22, 2015
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.