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P49888

- ST1E1_HUMAN

UniProt

P49888 - ST1E1_HUMAN

Protein

Estrogen sulfotransferase

Gene

SULT1E1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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 estradiol and estrone. May play a role in the regulation of estrogen receptor activity by metabolizing free estradiol. Maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. Also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated.1 Publication

    Catalytic activityi

    3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei107 – 1071Proton acceptorBy similarity
    Binding sitei129 – 1291PAPS
    Binding sitei137 – 1371PAPS
    Binding sitei192 – 1921PAPS

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi47 – 526PAPS
    Nucleotide bindingi226 – 2316PAPS
    Nucleotide bindingi256 – 2583PAPS

    GO - Molecular functioni

    1. estrone sulfotransferase activity Source: ProtInc
    2. flavonol 3-sulfotransferase activity Source: BHF-UCL
    3. steroid binding Source: UniProtKB-KW
    4. steroid sulfotransferase activity Source: UniProtKB

    GO - Biological processi

    1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
    2. estrogen metabolic process Source: UniProtKB
    3. female pregnancy Source: Ensembl
    4. small molecule metabolic process Source: Reactome
    5. steroid metabolic process Source: ProtInc
    6. sulfation Source: BHF-UCL
    7. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Lipid-binding, Steroid-binding

    Enzyme and pathway databases

    BRENDAi2.8.2.4. 2681.
    ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Estrogen sulfotransferase (EC:2.8.2.4)
    Alternative name(s):
    EST-1
    Sulfotransferase 1E1
    Short name:
    ST1E1
    Sulfotransferase, estrogen-preferring
    Gene namesi
    Name:SULT1E1
    Synonyms:STE
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:11377. SULT1E1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi137 – 1371S → A: Decreased gradually the catalytic activity. 1 Publication
    Mutagenesisi137 – 1371S → C: Decreased gradually the catalytic activity. 1 Publication
    Mutagenesisi269 – 2691V → E: Does not prevent the formation of homodimer.

    Organism-specific databases

    PharmGKBiPA340.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 294294Estrogen sulfotransferasePRO_0000085153Add
    BLAST

    Proteomic databases

    MaxQBiP49888.
    PaxDbiP49888.
    PRIDEiP49888.

    PTM databases

    PhosphoSiteiP49888.

    Expressioni

    Tissue specificityi

    Liver, intestine and at lower level in the kidney.

    Gene expression databases

    ArrayExpressiP49888.
    BgeeiP49888.
    CleanExiHS_SULT1E1.
    GenevestigatoriP49888.

    Organism-specific databases

    HPAiCAB047344.
    HPA028213.
    HPA028728.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi112660. 11 interactions.
    IntActiP49888. 11 interactions.
    MINTiMINT-1368473.
    STRINGi9606.ENSP00000226444.

    Structurei

    Secondary structure

    1
    294
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 107
    Beta strandi11 – 144
    Beta strandi17 – 204
    Helixi21 – 255
    Helixi27 – 315
    Beta strandi40 – 456
    Helixi50 – 6112
    Turni62 – 643
    Helixi66 – 694
    Beta strandi70 – 723
    Helixi74 – 774
    Turni86 – 883
    Helixi91 – 966
    Beta strandi103 – 1064
    Helixi110 – 1123
    Helixi115 – 1195
    Beta strandi123 – 1286
    Helixi131 – 14414
    Helixi154 – 1629
    Helixi171 – 18111
    Beta strandi187 – 1915
    Helixi192 – 1976
    Helixi199 – 20911
    Helixi216 – 22510
    Helixi228 – 2336
    Turni235 – 2373
    Turni244 – 2463
    Turni249 – 2513
    Helixi262 – 2654
    Helixi269 – 28315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1G3MX-ray1.70A/B1-294[»]
    1HY3X-ray1.80A/B1-294[»]
    4JVLX-ray1.94A/B1-294[»]
    4JVMX-ray1.99A/B1-294[»]
    4JVNX-ray2.05A/B1-294[»]
    ProteinModelPortaliP49888.
    SMRiP49888. Positions 3-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49888.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni105 – 1073Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    Phylogenomic databases

    eggNOGiNOG284811.
    HOGENOMiHOG000037209.
    HOVERGENiHBG001195.
    InParanoidiP49888.
    KOiK01016.
    OMAiQMKESTL.
    PhylomeDBiP49888.
    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.

    P49888-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSELDYYEK FEEVHGILMY KDFVKYWDNV EAFQARPDDL VIATYPKSGT    50
    TWVSEIVYMI YKEGDVEKCK EDVIFNRIPF LECRKENLMN GVKQLDEMNS 100
    PRIVKTHLPP ELLPASFWEK DCKIIYLCRN AKDVAVSFYY FFLMVAGHPN 150
    PGSFPEFVEK FMQGQVPYGS WYKHVKSWWE KGKSPRVLFL FYEDLKEDIR 200
    KEVIKLIHFL ERKPSEELVD RIIHHTSFQE MKNNPSTNYT TLPDEIMNQK 250
    LSPFMRKGIT GDWKNHFTVA LNEKFDKHYE QQMKESTLKF RTEI 294
    Length:294
    Mass (Da):35,126
    Last modified:October 1, 1996 - v1
    Checksum:i9EC8923D20757D57
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti154 – 1541F → L in AAH27956. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221D → Y.1 Publication
    Corresponds to variant rs11569705 [ dbSNP | Ensembl ].
    VAR_018907

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08098 mRNA. Translation: AAA82125.1.
    U20521
    , U20515, U20516, U20517, U20518, U20519, U20520 Genomic DNA. Translation: AAC50286.1.
    S77383 mRNA. Translation: AAB34601.1.
    Y11195 mRNA. Translation: CAA72079.1.
    AY436634 Genomic DNA. Translation: AAQ97179.1.
    BC027956 mRNA. Translation: AAH27956.1.
    U55764 mRNA. Translation: AAB51658.1.
    CCDSiCCDS3531.1.
    PIRiJC2229.
    RefSeqiNP_005411.1. NM_005420.2.
    UniGeneiHs.479898.

    Genome annotation databases

    EnsembliENST00000226444; ENSP00000226444; ENSG00000109193.
    GeneIDi6783.
    KEGGihsa:6783.
    UCSCiuc003heo.3. human.

    Polymorphism databases

    DMDMi1711604.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U08098 mRNA. Translation: AAA82125.1 .
    U20521
    , U20515 , U20516 , U20517 , U20518 , U20519 , U20520 Genomic DNA. Translation: AAC50286.1 .
    S77383 mRNA. Translation: AAB34601.1 .
    Y11195 mRNA. Translation: CAA72079.1 .
    AY436634 Genomic DNA. Translation: AAQ97179.1 .
    BC027956 mRNA. Translation: AAH27956.1 .
    U55764 mRNA. Translation: AAB51658.1 .
    CCDSi CCDS3531.1.
    PIRi JC2229.
    RefSeqi NP_005411.1. NM_005420.2.
    UniGenei Hs.479898.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1G3M X-ray 1.70 A/B 1-294 [» ]
    1HY3 X-ray 1.80 A/B 1-294 [» ]
    4JVL X-ray 1.94 A/B 1-294 [» ]
    4JVM X-ray 1.99 A/B 1-294 [» ]
    4JVN X-ray 2.05 A/B 1-294 [» ]
    ProteinModelPortali P49888.
    SMRi P49888. Positions 3-292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112660. 11 interactions.
    IntActi P49888. 11 interactions.
    MINTi MINT-1368473.
    STRINGi 9606.ENSP00000226444.

    Chemistry

    BindingDBi P49888.
    ChEMBLi CHEMBL2346.

    PTM databases

    PhosphoSitei P49888.

    Polymorphism databases

    DMDMi 1711604.

    Proteomic databases

    MaxQBi P49888.
    PaxDbi P49888.
    PRIDEi P49888.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000226444 ; ENSP00000226444 ; ENSG00000109193 .
    GeneIDi 6783.
    KEGGi hsa:6783.
    UCSCi uc003heo.3. human.

    Organism-specific databases

    CTDi 6783.
    GeneCardsi GC04M070676.
    HGNCi HGNC:11377. SULT1E1.
    HPAi CAB047344.
    HPA028213.
    HPA028728.
    MIMi 600043. gene.
    neXtProti NX_P49888.
    PharmGKBi PA340.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG284811.
    HOGENOMi HOG000037209.
    HOVERGENi HBG001195.
    InParanoidi P49888.
    KOi K01016.
    OMAi QMKESTL.
    PhylomeDBi P49888.
    TreeFami TF321745.

    Enzyme and pathway databases

    BRENDAi 2.8.2.4. 2681.
    Reactomei REACT_6913. Cytosolic sulfonation of small molecules.

    Miscellaneous databases

    EvolutionaryTracei P49888.
    GeneWikii SULT1E1.
    GenomeRNAii 6783.
    NextBioi 26488.
    PROi P49888.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49888.
    Bgeei P49888.
    CleanExi HS_SULT1E1.
    Genevestigatori P49888.

    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. "Human liver estrogen sulfotransferase: identification by cDNA cloning and expression."
      Aksoy I.A., Wood T.C., Weinshilboum R.M.
      Biochem. Biophys. Res. Commun. 200:1621-1629(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Human estrogen sulfotransferase gene (STE): cloning, structure, and chromosomal localization."
      Her C., Aksoy I.A., Kimura S., Brandriff B.F., Wasmuth J.J., Weinshilboum R.M.
      Genomics 29:16-23(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Liver.
    3. "Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase."
      Falany C.N., Krasnykh V., Falany J.L.
      J. Steroid Biochem. Mol. Biol. 52:529-539(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. "Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy."
      Rubin G.L., Harrold A.J., Mills J.A., Falany C.N., Coughtrie M.W.H.
      Mol. Hum. Reprod. 5:995-1002(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. NIEHS SNPs program
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TYR-22.
    6. "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: Lung.
    7. Her C., Szumlanski C., Aksoy I., Weinshilboum R.M.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 182-294.
      Tissue: Liver and Spleen.
    8. "Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction."
      Pedersen L.C., Petrotchenko E., Shevtsov S., Negishi M.
      J. Biol. Chem. 277:17928-17932(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT VAL-269 IN COMPLEX WITH 3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE (PAPS), FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-137.
    9. "Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase."
      Shevtsov S., Petrotchenko E.V., Pedersen L.C., Negishi M.
      Environ. Health Perspect. 111:884-888(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH ADENOSINE 3',5'-BISPHOSPHATE (PAP) AND A HYDROXYLATED POLYCHLORINATED BIPHENYL (OH-PCB).

    Entry informationi

    Entry nameiST1E1_HUMAN
    AccessioniPrimary (citable) accession number: P49888
    Secondary accession number(s): Q8N6X5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 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 4
      Human chromosome 4: 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