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P50226

- ST1A2_HUMAN

UniProt

P50226 - ST1A2_HUMAN

Protein

Sulfotransferase 1A2

Gene

SULT1A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (09 Feb 2010)
      Previous versions | rss
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    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

    1. aryl sulfotransferase activity Source: UniProtKB
    2. flavonol 3-sulfotransferase activity Source: BHF-UCL
    3. sulfotransferase activity Source: ProtInc

    GO - Biological processi

    1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
    2. amine biosynthetic process Source: ProtInc
    3. catecholamine metabolic process Source: UniProtKB-KW
    4. phenol-containing compound metabolic process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. steroid metabolic process Source: UniProtKB-KW
    7. sulfation Source: BHF-UCL
    8. xenobiotic metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Catecholamine metabolism, Lipid metabolism, Steroid metabolism

    Enzyme and pathway databases

    BRENDAi2.8.2.1. 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: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11454. SULT1A2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA341.

    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

    ArrayExpressiP50226.
    BgeeiP50226.
    CleanExiHS_SULT1A2.
    GenevestigatoriP50226.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi112673. 2 interactions.
    STRINGi9606.ENSP00000338742.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000037209.
    HOVERGENiHBG001195.
    InParanoidiP50226.
    KOiK01014.
    OMAiWESFLEK.
    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

    MELIQDISRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG    50
    TTWVSQILDM IYQGGDLEKC HRAPIFMRVP FLEFKVPGIP SGMETLKNTP 100
    APRLLKTHLP LALLPQTLLD QKVKVVYVAR NAKDVAVSYY HFYHMAKVYP 150
    HPGTWESFLE KFMAGEVSYG SWYQHVQEWW ELSRTHPVLY LFYEDMKENP 200
    KREIQKILEF VGRSLPEETV DLMVEHTSFK EMKKNPMTNY TTVRREFMDH 250
    SISPFMRKGM AGDWKTTFTV AQNERFDADY AKKMAGCSLS FRSEL 295
    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:
    EMBL
    GenBank
    DDBJ
    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_006721076.1.
    UniGeneiHs.546304.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi288558827.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10636.1.
    PIRi G01843.
    JC5249.
    S52791.
    RefSeqi NP_001045.1. NM_001054.3.
    NP_803564.1. NM_177528.2.
    XP_006721139.1. XM_006721076.1.
    UniGenei Hs.546304.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z29 X-ray 2.40 A 1-295 [» ]
    ProteinModelPortali P50226.
    SMRi P50226. Positions 8-295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112673. 2 interactions.
    STRINGi 9606.ENSP00000338742.

    Chemistry

    ChEMBLi CHEMBL1743292.

    PTM databases

    PhosphoSitei P50226.

    Polymorphism databases

    DMDMi 288558827.

    Proteomic databases

    MaxQBi P50226.
    PaxDbi P50226.
    PRIDEi P50226.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000335715 ; ENSP00000338742 ; ENSG00000197165 .
    ENST00000395630 ; ENSP00000378992 ; ENSG00000197165 .
    GeneIDi 6799.
    KEGGi hsa:6799.
    UCSCi uc002dqg.2. human.

    Organism-specific databases

    CTDi 6799.
    GeneCardsi GC16M028603.
    HGNCi HGNC:11454. SULT1A2.
    MIMi 601292. gene.
    neXtProti NX_P50226.
    PharmGKBi PA341.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260792.
    HOGENOMi HOG000037209.
    HOVERGENi HBG001195.
    InParanoidi P50226.
    KOi K01014.
    OMAi WESFLEK.
    PhylomeDBi P50226.
    TreeFami TF321745.

    Enzyme and pathway databases

    BRENDAi 2.8.2.1. 2681.
    Reactomei REACT_6913. Cytosolic sulfonation of small molecules.
    SABIO-RK P50226.

    Miscellaneous databases

    EvolutionaryTracei P50226.
    GeneWikii SULT1A2.
    GenomeRNAii 6799.
    NextBioi 26553.
    PROi P50226.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50226.
    Bgeei P50226.
    CleanExi HS_SULT1A2.
    Genevestigatori P50226.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view ]
    Pfami PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 129 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