P49888 (ST1E1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Lipid-binding Steroid-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome estrogen metabolic process Inferred from direct assay Ref.8. Source: UniProtKB female pregnancy Inferred from electronic annotation. Source: Compara sulfation Inferred from direct assay PubMed 20056724. Source: BHF-UCL xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nuclear membrane Inferred from direct assay. Source: HPA
Molecular_function	estrone sulfotransferase activity Traceable author statement Ref.1. Source: ProtInc flavonol 3-sulfotransferase activity Inferred from direct assay PubMed 20056724. Source: BHF-UCL steroid binding Inferred from electronic annotation. Source: UniProtKB-KW steroid sulfotransferase activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 294

294

Estrogen sulfotransferase

PRO_0000085153

Regions

Nucleotide binding

47 – 52

6

PAPS

Nucleotide binding

226 – 231

6

PAPS

Nucleotide binding

256 – 258

3

PAPS

Region

105 – 107

3

Substrate binding By similarity

Sites

Active site

107

1

Proton acceptor By similarity

Binding site

129

1

PAPS

Binding site

137

1

PAPS

Binding site

192

1

PAPS

Natural variations

Natural variant

22

1

D → Y. Ref.5
Corresponds to variant rs11569705 [ dbSNP | Ensembl ].

VAR_018907

Experimental info

Mutagenesis

137

1

S → A: Decreased gradually the catalytic activity. Ref.8

Mutagenesis

137

1

S → C: Decreased gradually the catalytic activity. Ref.8

Mutagenesis

269

1

V → E: Does not prevent the formation of homodimer.

Sequence conflict

154

1

F → L in AAH27956. Ref.6

Secondary structure

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294

Helix Strand Turn

Details...

Helix

4 – 10

7

Beta strand

11 – 14

4

Beta strand

17 – 20

4

Helix

21 – 25

5

Helix

27 – 31

5

Beta strand

40 – 45

6

Helix

50 – 61

12

Turn

62 – 64

3

Helix

66 – 69

4

Beta strand

70 – 72

3

Helix

74 – 77

4

Turn

86 – 88

3

Helix

91 – 96

6

Beta strand

103 – 106

4

Helix

110 – 112

3

Helix

115 – 119

5

Beta strand

123 – 128

6

Helix

131 – 144

14

Helix

154 – 162

9

Helix

171 – 181

11

Beta strand

187 – 191

5

Helix

192 – 197

6

Helix

199 – 209

11

Helix

216 – 225

10

Helix

228 – 233

6

Turn

235 – 237

3

Turn

244 – 246

3

Turn

249 – 251

3

Helix

262 – 265

4

Helix

269 – 283

15

Sequences

	Sequence		Length	Mass (Da)
	P49888 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 9EC8923D20757D57	FASTA	294	35,126
	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

References

	« Hide 'large scale' referencesShow '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

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00028623.

PIR

JC2229.

RefSeq

NP_005411.1. NM_005420.2.

UniGene

Hs.479898.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P49888.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49888. 11 interactions.

MINT

MINT-1368473.

STRING

9606.ENSP00000226444.

PTM databases

PhosphoSite

P49888.

Polymorphism databases

DMDM

1711604.

Proteomic databases

PaxDb

P49888.

PRIDE

P49888.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000226444; ENSP00000226444; ENSG00000109193.

GeneID

6783.

KEGG

hsa:6783.

UCSC

uc003heo.3. human.

Organism-specific databases

CTD

6783.

GeneCards

GC04M070676.

HGNC

HGNC:11377. SULT1E1.

HPA

CAB047344.
HPA028213.
HPA028728.

MIM

600043. gene.

neXtProt

NX_P49888.

PharmGKB

PA340.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG284811.

HOGENOM

HOG000037209.

HOVERGEN

HBG001195.

InParanoid

P49888.

KO

K01016.

OMA

VIFNRIP.

PhylomeDB

P49888.

Enzyme and pathway databases

BRENDA

2.8.2.4. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

P49888.

Bgee

P49888.

CleanEx

HS_SULT1E1.

Genevestigator

P49888.

GermOnline

ENSG00000109193. Homo sapiens.

Family and domain databases

InterPro

IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P49888.

ChEMBL

CHEMBL2346.

EvolutionaryTrace

P49888.

GenomeRNAi

6783.

NextBio

26488.

SOURCE

Search...

Entry information

Entry name

ST1E1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.