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Q06520

- ST2A1_HUMAN

UniProt

Q06520 - ST2A1_HUMAN

Protein

Bile salt sulfotransferase

Gene

SULT2A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands.

    Catalytic activityi

    3'-phosphoadenylyl sulfate + glycolithocholate = adenosine 3',5'-bisphosphate + glycolithocholate 3-sulfate.
    3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei72 – 721Substrate
    Binding sitei77 – 771Substrate
    Active sitei99 – 991Proton acceptor
    Binding sitei121 – 1211PAPS
    Binding sitei129 – 1291PAPS
    Binding sitei184 – 1841PAPS

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi44 – 496PAPS
    Nucleotide bindingi218 – 2236PAPS
    Nucleotide bindingi247 – 2493PAPS

    GO - Molecular functioni

    1. bile-salt sulfotransferase activity Source: UniProtKB-EC
    2. protein binding Source: IntAct
    3. sulfotransferase activity Source: BHF-UCL

    GO - Biological processi

    1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
    2. bile acid catabolic process Source: UniProtKB-KW
    3. cellular lipid metabolic process Source: Reactome
    4. digestion Source: ProtInc
    5. small molecule metabolic process Source: Reactome
    6. steroid metabolic process Source: ProtInc
    7. sulfation Source: BHF-UCL
    8. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Bile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

    Enzyme and pathway databases

    BRENDAi2.8.2.2. 2681.
    ReactomeiREACT_116145. PPARA activates gene expression.
    REACT_6913. Cytosolic sulfonation of small molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bile salt sulfotransferase (EC:2.8.2.14)
    Alternative name(s):
    Dehydroepiandrosterone sulfotransferase
    Short name:
    DHEA-ST
    Hydroxysteroid Sulfotransferase
    Short name:
    HST
    ST2
    ST2A3
    Sulfotransferase 2A1
    Short name:
    ST2A1
    Gene namesi
    Name:SULT2A1
    Synonyms:HST, STD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:11458. SULT2A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA346.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 285285Bile salt sulfotransferasePRO_0000085141Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.

    Proteomic databases

    MaxQBiQ06520.
    PaxDbiQ06520.
    PRIDEiQ06520.

    PTM databases

    PhosphoSiteiQ06520.

    Expressioni

    Tissue specificityi

    Liver, adrenal and at lower level in the kidney. Is present in human fetus in higher level in the adrenal than the liver and the kidney.

    Gene expression databases

    ArrayExpressiQ06520.
    BgeeiQ06520.
    CleanExiHS_SULT2A1.
    GenevestigatoriQ06520.

    Organism-specific databases

    HPAiCAB018755.
    HPA041487.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    STAT3P407632EBI-3921363,EBI-518675

    Protein-protein interaction databases

    BioGridi112691. 5 interactions.
    IntActiQ06520. 4 interactions.
    MINTiMINT-5002735.
    STRINGi9606.ENSP00000222002.

    Structurei

    Secondary structure

    1
    285
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi11 – 133
    Beta strandi15 – 173
    Helixi20 – 289
    Beta strandi37 – 404
    Beta strandi43 – 464
    Helixi47 – 5812
    Turni59 – 613
    Helixi64 – 685
    Helixi71 – 744
    Helixi81 – 877
    Beta strandi95 – 984
    Helixi102 – 1043
    Helixi107 – 1115
    Beta strandi115 – 1206
    Helixi123 – 13412
    Beta strandi137 – 1404
    Helixi146 – 15510
    Helixi163 – 1708
    Helixi171 – 1733
    Beta strandi179 – 1835
    Helixi184 – 1896
    Helixi191 – 20212
    Helixi208 – 21710
    Helixi220 – 2245
    Turni227 – 2293
    Turni236 – 2383
    Beta strandi239 – 2413
    Helixi242 – 2465
    Helixi254 – 2563
    Helixi260 – 27415
    Helixi279 – 2813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EFHX-ray2.40A/B1-281[»]
    1J99X-ray1.99A2-285[»]
    1OV4X-ray2.70A2-285[»]
    2QP3X-ray2.60A2-285[»]
    2QP4X-ray3.00A2-285[»]
    3F3YX-ray2.20A/B/C/D1-285[»]
    4IFBX-ray2.30A/B1-285[»]
    ProteinModelPortaliQ06520.
    SMRiQ06520. Positions 4-285.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06520.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    Phylogenomic databases

    eggNOGiNOG274515.
    HOGENOMiHOG000037209.
    HOVERGENiHBG001195.
    InParanoidiQ06520.
    KOiK11822.
    OMAiXVYGSWF.
    OrthoDBiEOG7V49ZK.
    PhylomeDBiQ06520.
    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.

    Q06520-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL    50
    AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL 100
    PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF 150
    EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ 200
    FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV 250
    SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE 285
    Length:285
    Mass (Da):33,780
    Last modified:January 23, 2007 - v3
    Checksum:i06DFF2006B284A08
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901T → S in AAA35758. (PubMed:7678732)Curated
    Sequence conflicti90 – 901T → S in CAA49755. (PubMed:7678732)Curated
    Sequence conflicti119 – 1191L → D AA sequence (PubMed:7678732)Curated
    Sequence conflicti159 – 1591L → V in AAB23169. (PubMed:1520333)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti63 – 631A → P.1 Publication
    Corresponds to variant rs11569681 [ dbSNP | Ensembl ].
    VAR_052520
    Natural varianti261 – 2611A → T.
    Corresponds to variant rs11569679 [ dbSNP | Ensembl ].
    VAR_052521

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20000 mRNA. Translation: AAA35758.1.
    X70222 mRNA. Translation: CAA49755.1.
    U08024 mRNA. Translation: AAA17749.1.
    U08025 mRNA. Translation: AAA17750.1.
    X84816 mRNA. Translation: CAA59274.1.
    L36196
    , L36191, L36192, L36193, L36194, L36195 Genomic DNA. Translation: AAA75491.1.
    U13061
    , U13056, U13057, U13058, U13059, U13060 Genomic DNA. Translation: AAC51353.1.
    S43859 mRNA. Translation: AAB23169.2.
    BC020755 mRNA. Translation: AAH20755.1.
    CCDSiCCDS12707.1.
    PIRiI53037. I38548.
    RefSeqiNP_003158.2. NM_003167.3.
    UniGeneiHs.515835.

    Genome annotation databases

    EnsembliENST00000222002; ENSP00000222002; ENSG00000105398.
    GeneIDi6822.
    KEGGihsa:6822.
    UCSCiuc002phr.2. human.

    Polymorphism databases

    DMDMi1711591.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20000 mRNA. Translation: AAA35758.1 .
    X70222 mRNA. Translation: CAA49755.1 .
    U08024 mRNA. Translation: AAA17749.1 .
    U08025 mRNA. Translation: AAA17750.1 .
    X84816 mRNA. Translation: CAA59274.1 .
    L36196
    , L36191 , L36192 , L36193 , L36194 , L36195 Genomic DNA. Translation: AAA75491.1 .
    U13061
    , U13056 , U13057 , U13058 , U13059 , U13060 Genomic DNA. Translation: AAC51353.1 .
    S43859 mRNA. Translation: AAB23169.2 .
    BC020755 mRNA. Translation: AAH20755.1 .
    CCDSi CCDS12707.1.
    PIRi I53037. I38548.
    RefSeqi NP_003158.2. NM_003167.3.
    UniGenei Hs.515835.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EFH X-ray 2.40 A/B 1-281 [» ]
    1J99 X-ray 1.99 A 2-285 [» ]
    1OV4 X-ray 2.70 A 2-285 [» ]
    2QP3 X-ray 2.60 A 2-285 [» ]
    2QP4 X-ray 3.00 A 2-285 [» ]
    3F3Y X-ray 2.20 A/B/C/D 1-285 [» ]
    4IFB X-ray 2.30 A/B 1-285 [» ]
    ProteinModelPortali Q06520.
    SMRi Q06520. Positions 4-285.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112691. 5 interactions.
    IntActi Q06520. 4 interactions.
    MINTi MINT-5002735.
    STRINGi 9606.ENSP00000222002.

    Chemistry

    ChEMBLi CHEMBL2077.

    PTM databases

    PhosphoSitei Q06520.

    Polymorphism databases

    DMDMi 1711591.

    Proteomic databases

    MaxQBi Q06520.
    PaxDbi Q06520.
    PRIDEi Q06520.

    Protocols and materials databases

    DNASUi 6822.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222002 ; ENSP00000222002 ; ENSG00000105398 .
    GeneIDi 6822.
    KEGGi hsa:6822.
    UCSCi uc002phr.2. human.

    Organism-specific databases

    CTDi 6822.
    GeneCardsi GC19M048373.
    HGNCi HGNC:11458. SULT2A1.
    HPAi CAB018755.
    HPA041487.
    MIMi 125263. gene.
    neXtProti NX_Q06520.
    PharmGKBi PA346.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG274515.
    HOGENOMi HOG000037209.
    HOVERGENi HBG001195.
    InParanoidi Q06520.
    KOi K11822.
    OMAi XVYGSWF.
    OrthoDBi EOG7V49ZK.
    PhylomeDBi Q06520.
    TreeFami TF321745.

    Enzyme and pathway databases

    BRENDAi 2.8.2.2. 2681.
    Reactomei REACT_116145. PPARA activates gene expression.
    REACT_6913. Cytosolic sulfonation of small molecules.

    Miscellaneous databases

    ChiTaRSi SULT2A1. human.
    EvolutionaryTracei Q06520.
    GeneWikii Bile_salt_sulfotransferase.
    GenomeRNAii 6822.
    NextBioi 26647.
    PROi Q06520.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06520.
    Bgeei Q06520.
    CleanExi HS_SULT2A1.
    Genevestigatori Q06520.

    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. "Cloning and expression of human liver dehydroepiandrosterone sulphotransferase."
      Comer K.A., Falany J.L., Falany C.N.
      Biochem. J. 289:233-240(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 61-65; 105-120 AND 274-285, VARIANT PRO-63.
      Tissue: Liver.
    2. "Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA."
      Otterness D.M., Wieben E.D., Wood T.C., Watson R.W.G., Madden B.J., McCormick D.J., Weinshilboum R.M.
      Mol. Pharmacol. 41:865-872(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 81-108 AND 177-199.
      Tissue: Liver.
    3. "Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme."
      Forbes K.J., Hagen M., Coughtrie M.W.H., Glatt H.R., Hume R.
      Mol. Cell. Endocrinol. 112:53-60(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adrenal gland.
    4. "Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene."
      Luu-The V., Dufort I., Paquet N., Reimnitz G., Labrie F.
      DNA Cell Biol. 14:511-518(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization."
      Otterness D.M., Her C., Aksoy S., Kimura S., Wieben E.D., Weinshilboum R.M.
      DNA Cell Biol. 14:331-341(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver."
      Kong A.-N.T., Yang L., Ma M., Tao D., Bjornsson T.D.
      Biochem. Biophys. Res. Commun. 187:448-454(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    7. "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].
      Tissue: Liver.
    8. "Human liver steroid sulphotransferase sulphates bile acids."
      Radominska A., Comer K.A., Zimniak P., Falany J., Iscan M., Falany C.N.
      Biochem. J. 272:597-604(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of SULT2A3, human hydroxysteroid sulfotransferase."
      Pedersen L.C., Petrotchenko E.V., Negishi M.
      FEBS Lett. 475:61-64(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE (PAP).
    11. "Crystal structure of human dehydroepiandrosterone sulphotransferase in complex with substrate."
      Rehse P.H., Zhou M., Lin S.X.
      Biochem. J. 364:165-171(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH DEHYDROEPIANDROSTERONE (DHEA).
    12. "Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex."
      Chang H.J., Shi R., Rehse P., Lin S.X.
      J. Biol. Chem. 279:2689-2696(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ANDROSTERONE (ADT).

    Entry informationi

    Entry nameiST2A1_HUMAN
    AccessioniPrimary (citable) accession number: Q06520
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 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

    Miscellaneous

    Estrogens present in maternal circulation is predominantly derived from fetal dehydroepiandosterone sulfate which is hydrolyzed and metabolized to estrogens in placenta.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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