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P49888 (ST1E1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Estrogen sulfotransferase

EC=2.8.2.4
Alternative name(s):
EST-1
Sulfotransferase 1E1
Short name=ST1E1
Sulfotransferase, estrogen-preferring
Gene names
Name:SULT1E1
Synonyms:STE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Catalytic activity

3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate. Ref.8

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Liver, intestine and at lower level in the kidney.

Sequence similarities

Belongs to the sulfotransferase 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Estrogen sulfotransferase
PRO_0000085153

Regions

Nucleotide binding47 – 526PAPS
Nucleotide binding226 – 2316PAPS
Nucleotide binding256 – 2583PAPS
Region105 – 1073Substrate binding By similarity

Sites

Active site1071Proton acceptor By similarity
Binding site1291PAPS
Binding site1371PAPS
Binding site1921PAPS

Natural variations

Natural variant221D → Y. Ref.5
Corresponds to variant rs11569705 [ dbSNP | Ensembl ].
VAR_018907

Experimental info

Mutagenesis1371S → A: Decreased gradually the catalytic activity. Ref.8
Mutagenesis1371S → C: Decreased gradually the catalytic activity. Ref.8
Mutagenesis2691V → E: Does not prevent the formation of homodimer.
Sequence conflict1541F → L in AAH27956. Ref.6

Secondary structure

........................................................ 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49888 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9EC8923D20757D57

FASTA29435,126
        10         20         30         40         50         60 
MNSELDYYEK FEEVHGILMY KDFVKYWDNV EAFQARPDDL VIATYPKSGT TWVSEIVYMI 

        70         80         90        100        110        120 
YKEGDVEKCK EDVIFNRIPF LECRKENLMN GVKQLDEMNS PRIVKTHLPP ELLPASFWEK 

       130        140        150        160        170        180 
DCKIIYLCRN AKDVAVSFYY FFLMVAGHPN PGSFPEFVEK FMQGQVPYGS WYKHVKSWWE 

       190        200        210        220        230        240 
KGKSPRVLFL FYEDLKEDIR KEVIKLIHFL ERKPSEELVD RIIHHTSFQE MKNNPSTNYT 

       250        260        270        280        290 
TLPDEIMNQK LSPFMRKGIT GDWKNHFTVA LNEKFDKHYE QQMKESTLKF RTEI 

« Hide

References

« Hide 'large scale' references
[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).
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U08098 mRNA. Translation: AAA82125.1.
U20521 expand/collapse EMBL AC list , 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.
PIRJC2229.
RefSeqNP_005411.1. NM_005420.2.
UniGeneHs.479898.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP49888.
SMRP49888. Positions 3-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112660. 11 interactions.
IntActP49888. 11 interactions.
MINTMINT-1368473.
STRING9606.ENSP00000226444.

Chemistry

BindingDBP49888.
ChEMBLCHEMBL2346.

PTM databases

PhosphoSiteP49888.

Polymorphism databases

DMDM1711604.

Proteomic databases

PaxDbP49888.
PRIDEP49888.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226444; ENSP00000226444; ENSG00000109193.
GeneID6783.
KEGGhsa:6783.
UCSCuc003heo.3. human.

Organism-specific databases

CTD6783.
GeneCardsGC04M070676.
HGNCHGNC:11377. SULT1E1.
HPACAB047344.
HPA028213.
HPA028728.
MIM600043. gene.
neXtProtNX_P49888.
PharmGKBPA340.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG284811.
HOGENOMHOG000037209.
HOVERGENHBG001195.
InParanoidP49888.
KOK01016.
OMAQMKESTL.
PhylomeDBP49888.
TreeFamTF321745.

Enzyme and pathway databases

BRENDA2.8.2.4. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP49888.
BgeeP49888.
CleanExHS_SULT1E1.
GenevestigatorP49888.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP49888.
GeneWikiSULT1E1.
GenomeRNAi6783.
NextBio26488.
PROP49888.
SOURCESearch...

Entry information

Entry nameST1E1_HUMAN
AccessionPrimary (citable) accession number: P49888
Secondary accession number(s): Q8N6X5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM