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P49888

- ST1E1_HUMAN

UniProt

P49888 - ST1E1_HUMAN

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Protein
Estrogen sulfotransferase
Gene
SULT1E1, STE
Organism
Homo sapiens (Human)
Status
Reviewed - 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 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 acceptor By 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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

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 sulfotransferase
PRO_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.

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP49888.

Family & Domainsi

Region

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

Sequence similaritiesi

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti154 – 1541F → L in AAH27956. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 130 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

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