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Protein

Estrogen sulfotransferase

Gene

SULT1E1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei107Proton acceptorBy similarity1
Binding sitei129PAPS1
Binding sitei137PAPS1
Binding sitei192PAPS1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi47 – 52PAPS6
Nucleotide bindingi226 – 231PAPS6
Nucleotide bindingi256 – 258PAPS3

GO - Molecular functioni

  • aryl sulfotransferase activity Source: Reactome
  • estrone sulfotransferase activity Source: Reactome
  • flavonol 3-sulfotransferase activity Source: BHF-UCL
  • steroid binding Source: UniProtKB-KW
  • steroid sulfotransferase activity Source: UniProtKB
  • sulfotransferase activity Source: MGI

GO - Biological processi

  • 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: CAFA
  • estrogen catabolic process Source: CAFA
  • estrogen metabolic process Source: UniProtKB
  • ethanol catabolic process Source: CAFA
  • positive regulation of fat cell differentiation Source: CACAO
  • steroid metabolic process Source: ProtInc
  • sulfation Source: BHF-UCL

Keywordsi

Molecular functionTransferase
LigandLipid-binding, Steroid-binding

Enzyme and pathway databases

BRENDAi2.8.2.4 2681
ReactomeiR-HSA-156584 Cytosolic sulfonation of small molecules
SIGNORiP49888

Chemistry databases

SwissLipidsiSLP:000001693

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
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000109193.10
HGNCiHGNC:11377 SULT1E1
MIMi600043 gene
neXtProtiNX_P49888

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi137S → A: Decreased gradually the catalytic activity. 1 Publication1
Mutagenesisi137S → C: Decreased gradually the catalytic activity. 1 Publication1
Mutagenesisi269V → E: Does not prevent the formation of homodimer. 1

Organism-specific databases

DisGeNETi6783
OpenTargetsiENSG00000109193
PharmGKBiPA340

Chemistry databases

ChEMBLiCHEMBL2346
DrugBankiDB02902 3'-Phosphate-Adenosine-5'-Phosphate Sulfate
DB00316 Acetaminophen
DB01812 Adenosine-3'-5'-Diphosphate
DB01176 Cyclizine

Polymorphism and mutation databases

BioMutaiSULT1E1
DMDMi1711604

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000851531 – 294Estrogen sulfotransferaseAdd BLAST294

Proteomic databases

PaxDbiP49888
PeptideAtlasiP49888
PRIDEiP49888

PTM databases

iPTMnetiP49888
PhosphoSitePlusiP49888

Expressioni

Tissue specificityi

Liver, intestine and at lower level in the kidney.

Gene expression databases

BgeeiENSG00000109193
CleanExiHS_SULT1E1
ExpressionAtlasiP49888 baseline and differential
GenevisibleiP49888 HS

Organism-specific databases

HPAiCAB047344
HPA028213
HPA028728

Interactioni

Subunit structurei

Homodimer.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE9AO760833EBI-712512,EBI-742764

Protein-protein interaction databases

BioGridi112660, 14 interactors
IntActiP49888, 12 interactors
STRINGi9606.ENSP00000226444

Chemistry databases

BindingDBiP49888

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 10Combined sources7
Beta strandi11 – 14Combined sources4
Beta strandi17 – 20Combined sources4
Helixi21 – 25Combined sources5
Helixi27 – 31Combined sources5
Beta strandi40 – 45Combined sources6
Helixi50 – 61Combined sources12
Turni62 – 64Combined sources3
Helixi66 – 69Combined sources4
Beta strandi70 – 72Combined sources3
Helixi74 – 77Combined sources4
Turni86 – 88Combined sources3
Helixi91 – 96Combined sources6
Beta strandi103 – 106Combined sources4
Helixi110 – 112Combined sources3
Helixi115 – 119Combined sources5
Beta strandi123 – 128Combined sources6
Helixi131 – 144Combined sources14
Helixi154 – 162Combined sources9
Helixi171 – 181Combined sources11
Beta strandi187 – 191Combined sources5
Helixi192 – 197Combined sources6
Helixi199 – 209Combined sources11
Helixi216 – 225Combined sources10
Helixi228 – 233Combined sources6
Turni235 – 237Combined sources3
Turni244 – 246Combined sources3
Turni249 – 251Combined sources3
Helixi262 – 265Combined sources4
Helixi269 – 283Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49888

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni105 – 107Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG1584 Eukaryota
ENOG4111H56 LUCA
GeneTreeiENSGT00760000118932
HOGENOMiHOG000037209
HOVERGENiHBG001195
InParanoidiP49888
KOiK01016
OMAiNQKVSPF
OrthoDBiEOG091G0D5F
PhylomeDBiP49888
TreeFamiTF321745

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR000863 Sulfotransferase_dom
PfamiView protein in Pfam
PF00685 Sulfotransfer_1, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit

Sequencei

Sequence statusi: Complete.

P49888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSELDYYEK FEEVHGILMY KDFVKYWDNV EAFQARPDDL VIATYPKSGT
60 70 80 90 100
TWVSEIVYMI YKEGDVEKCK EDVIFNRIPF LECRKENLMN GVKQLDEMNS
110 120 130 140 150
PRIVKTHLPP ELLPASFWEK DCKIIYLCRN AKDVAVSFYY FFLMVAGHPN
160 170 180 190 200
PGSFPEFVEK FMQGQVPYGS WYKHVKSWWE KGKSPRVLFL FYEDLKEDIR
210 220 230 240 250
KEVIKLIHFL ERKPSEELVD RIIHHTSFQE MKNNPSTNYT TLPDEIMNQK
260 270 280 290
LSPFMRKGIT GDWKNHFTVA LNEKFDKHYE QQMKESTLKF RTEI
Length:294
Mass (Da):35,126
Last modified:October 1, 1996 - v1
Checksum:i9EC8923D20757D57
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti154F → L in AAH27956 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01890722D → Y1 PublicationCorresponds to variant dbSNP:rs11569705Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiST1E1_HUMAN
AccessioniPrimary (citable) accession number: P49888
Secondary accession number(s): Q8N6X5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 28, 2018
This is version 159 of the entry and version 1 of the sequence. See 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

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