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Protein

Sulfotransferase family cytosolic 2B member 1

Gene

SULT2B1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol.2 Publications

Catalytic activityi

3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate.

Kineticsi

  1. KM=10.9 µM for DHEA (at 37 degrees Celsius, in the presence of 1 mM MgCl2)2 Publications
  2. KM=3.8 µM for DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2)2 Publications
  3. KM=11.8 µM for pregnenolone (at 37 degrees Celsius, in the presence of 1 mM MgCl2)2 Publications
  4. KM=0.6 µM for PAPS (at 37 degrees Celsius, in the presence of 1 mM MgCl2)2 Publications
  1. Vmax=1752 pmol/min/mg enzyme toward DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2)2 Publications

Temperature dependencei

Optimum temperature is 37 degrees Celsius. Retains 70% and 20% of activity when incubated at 42 degrees Celsius for 45 and 120 minutes, respectively. Activity is lost after 200 minutes incubation at 42 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei98Substrate1
Binding sitei103Substrate1
Active sitei125Proton acceptor1
Binding sitei125Substrate1
Binding sitei147PAPS1
Binding sitei155PAPS1
Binding sitei210PAPS1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi70 – 75PAPS6
Nucleotide bindingi244 – 249PAPS6
Nucleotide bindingi274 – 276PAPS3

GO - Molecular functioni

  • alcohol sulfotransferase activity Source: Reactome
  • steroid sulfotransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BioCyciZFISH:HS01587-MONOMER.
ReactomeiR-HSA-156584. Cytosolic sulfonation of small molecules.

Names & Taxonomyi

Protein namesi
Recommended name:
Sulfotransferase family cytosolic 2B member 1 (EC:2.8.2.2)
Short name:
ST2B1
Short name:
Sulfotransferase 2B1
Alternative name(s):
Alcohol sulfotransferase
Hydroxysteroid sulfotransferase 2
Gene namesi
Name:SULT2B1
Synonyms:HSST2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11459. SULT2B1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1 – 23Missing : Loss of the cholesterol sulfotransferase activity. 1 PublicationAdd BLAST23
Mutagenesisi1 – 18Missing : Increases the cholesterol sulfotransferase activity. 1 PublicationAdd BLAST18
Mutagenesisi19D → A: Increases the cholesterol sulfotransferase activity. 1 Publication1
Mutagenesisi20I → A: Loss of the cholesterol sulfotransferase activity. 1 Publication1
Mutagenesisi21S → A: Increases the cholesterol sulfotransferase activity. 1 Publication1
Mutagenesisi22E → A: Increases the cholesterol sulfotransferase activity. 1 Publication1
Mutagenesisi23I → A: Loss of the cholesterol sulfotransferase activity. 1 Publication1
Mutagenesisi347S → A: No change in subcellular localization. 1 Publication1
Mutagenesisi348S → D: 10-fold increase in specific activity for DHEA sulfation. 10-fold increase in substrate affinity for DHEA and pregnenolone. No effect on substrate affinity for PAPS. Increases enzyme stability. 1 Publication1
Mutagenesisi348S → G: Abolishes nuclear localization. 1 Publication1
Mutagenesisi352S → G: No change in subcellular localization. 1 Publication1
Mutagenesisi357S → G: No change in subcellular localization. 1 Publication1

Organism-specific databases

DisGeNETi6820.
OpenTargetsiENSG00000088002.
PharmGKBiPA36249.

Chemistry databases

ChEMBLiCHEMBL1743297.

Polymorphism and mutation databases

BioMutaiSULT2B1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000851491 – 365Sulfotransferase family cytosolic 2B member 1Add BLAST365

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei348Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00204.
PaxDbiO00204.
PeptideAtlasiO00204.
PRIDEiO00204.

PTM databases

iPTMnetiO00204.
PhosphoSitePlusiO00204.

Expressioni

Tissue specificityi

Expressed highly in placenta, prostate and trachea and lower expression in the small intestine and lung.1 Publication

Gene expression databases

BgeeiENSG00000088002.
CleanExiHS_SULT2B1.
GenevisibleiO00204. HS.

Organism-specific databases

HPAiCAB033013.
HPA041724.
HPA043539.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ACYP2P146213EBI-749441,EBI-10198377
ALS2CR12Q96Q358EBI-749441,EBI-750451
PRICKLE3O439003EBI-749441,EBI-1751761
SULT1A1P502253EBI-749441,EBI-2814403
SULT1B1O437045EBI-749441,EBI-10179062

Protein-protein interaction databases

BioGridi112689. 12 interactors.
IntActiO00204. 9 interactors.
MINTiMINT-1440870.
STRINGi9606.ENSP00000201586.

Structurei

Secondary structure

1365
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 25Combined sources7
Beta strandi31 – 34Combined sources4
Beta strandi37 – 41Combined sources5
Helixi46 – 54Combined sources9
Beta strandi63 – 68Combined sources6
Helixi73 – 84Combined sources12
Turni85 – 87Combined sources3
Helixi90 – 94Combined sources5
Helixi97 – 100Combined sources4
Beta strandi103 – 106Combined sources4
Helixi110 – 112Combined sources3
Beta strandi121 – 124Combined sources4
Turni128 – 130Combined sources3
Helixi133 – 135Combined sources3
Beta strandi141 – 146Combined sources6
Helixi149 – 162Combined sources14
Beta strandi163 – 166Combined sources4
Helixi172 – 180Combined sources9
Helixi189 – 196Combined sources8
Helixi197 – 199Combined sources3
Beta strandi205 – 209Combined sources5
Helixi210 – 215Combined sources6
Helixi217 – 228Combined sources12
Helixi234 – 244Combined sources11
Helixi246 – 250Combined sources5
Turni253 – 255Combined sources3
Turni256 – 259Combined sources4
Turni262 – 264Combined sources3
Turni267 – 269Combined sources3
Helixi280 – 283Combined sources4
Helixi287 – 300Combined sources14
Turni301 – 303Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q1QX-ray2.91A24-365[»]
1Q1ZX-ray2.40A19-312[»]
1Q20X-ray2.30A19-312[»]
1Q22X-ray2.50A19-312[»]
DisProtiDP00404.
ProteinModelPortaliO00204.
SMRiO00204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00204.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi305 – 365Pro/Ser-richAdd BLAST61

Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiO00204.
KOiK01015.
OMAiPVGIYSP.
OrthoDBiEOG091G0D5F.
PhylomeDBiO00204.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O00204-1) [UniParc]FASTAAdd to basket
Also known as: SULT2B1b, B

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDGPAEPQIP GLWDTYEDDI SEISQKLPGE YFRYKGVPFP VGLYSLESIS
60 70 80 90 100
LAENTQDVRD DDIFIITYPK SGTTWMIEII CLILKEGDPS WIRSVPIWER
110 120 130 140 150
APWCETIVGA FSLPDQYSPR LMSSHLPIQI FTKAFFSSKA KVIYMGRNPR
160 170 180 190 200
DVVVSLYHYS KIAGQLKDPG TPDQFLRDFL KGEVQFGSWF DHIKGWLRMK
210 220 230 240 250
GKDNFLFITY EELQQDLQGS VERICGFLGR PLGKEALGSV VAHSTFSAMK
260 270 280 290 300
ANTMSNYTLL PPSLLDHRRG AFLRKGVCGD WKNHFTVAQS EAFDRAYRKQ
310 320 330 340 350
MRGMPTFPWD EDPEEDGSPD PEPSPEPEPK PSLEPNTSLE REPRPNSSPS
360
PSPGQASETP HPRPS
Length:365
Mass (Da):41,308
Last modified:January 4, 2005 - v2
Checksum:i13E95248DD40DF91
GO
Isoform 2 (identifier: O00204-2) [UniParc]FASTAAdd to basket
Also known as: SULT2B1a, A

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MDGPAEPQIPGLWDTYEDDISEI → MASPPPFH

Show »
Length:350
Mass (Da):39,599
Checksum:iCE5BAA8F8874E3A4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti350S → N in AAC78498 (PubMed:9799594).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02088751L → S.Corresponds to variant rs16982149dbSNPEnsembl.1
Natural variantiVAR_021988240V → I.Corresponds to variant rs2302947dbSNPEnsembl.1
Natural variantiVAR_020888345P → L.Corresponds to variant rs17842463dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0125101 – 23MDGPA…DISEI → MASPPPFH in isoform 2. 1 PublicationAdd BLAST23

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U92314 mRNA. Translation: AAC78498.1.
U92315 mRNA. Translation: AAC78499.1.
U92322
, U92316, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78553.1.
U92322
, U92316, U92317, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78554.1.
AC008403 Genomic DNA. No translation available.
BC034694 mRNA. Translation: AAH34694.1.
CCDSiCCDS12723.1. [O00204-1]
CCDS12724.1. [O00204-2]
RefSeqiNP_004596.2. NM_004605.2. [O00204-2]
NP_814444.1. NM_177973.1. [O00204-1]
UniGeneiHs.369331.

Genome annotation databases

EnsembliENST00000201586; ENSP00000201586; ENSG00000088002. [O00204-1]
ENST00000323090; ENSP00000312880; ENSG00000088002. [O00204-2]
GeneIDi6820.
KEGGihsa:6820.
UCSCiuc002pjl.4. human. [O00204-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U92314 mRNA. Translation: AAC78498.1.
U92315 mRNA. Translation: AAC78499.1.
U92322
, U92316, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78553.1.
U92322
, U92316, U92317, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78554.1.
AC008403 Genomic DNA. No translation available.
BC034694 mRNA. Translation: AAH34694.1.
CCDSiCCDS12723.1. [O00204-1]
CCDS12724.1. [O00204-2]
RefSeqiNP_004596.2. NM_004605.2. [O00204-2]
NP_814444.1. NM_177973.1. [O00204-1]
UniGeneiHs.369331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q1QX-ray2.91A24-365[»]
1Q1ZX-ray2.40A19-312[»]
1Q20X-ray2.30A19-312[»]
1Q22X-ray2.50A19-312[»]
DisProtiDP00404.
ProteinModelPortaliO00204.
SMRiO00204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112689. 12 interactors.
IntActiO00204. 9 interactors.
MINTiMINT-1440870.
STRINGi9606.ENSP00000201586.

Chemistry databases

ChEMBLiCHEMBL1743297.

PTM databases

iPTMnetiO00204.
PhosphoSitePlusiO00204.

Polymorphism and mutation databases

BioMutaiSULT2B1.

Proteomic databases

MaxQBiO00204.
PaxDbiO00204.
PeptideAtlasiO00204.
PRIDEiO00204.

Protocols and materials databases

DNASUi6820.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000201586; ENSP00000201586; ENSG00000088002. [O00204-1]
ENST00000323090; ENSP00000312880; ENSG00000088002. [O00204-2]
GeneIDi6820.
KEGGihsa:6820.
UCSCiuc002pjl.4. human. [O00204-1]

Organism-specific databases

CTDi6820.
DisGeNETi6820.
GeneCardsiSULT2B1.
HGNCiHGNC:11459. SULT2B1.
HPAiCAB033013.
HPA041724.
HPA043539.
MIMi604125. gene.
neXtProtiNX_O00204.
OpenTargetsiENSG00000088002.
PharmGKBiPA36249.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1584. Eukaryota.
ENOG4111H56. LUCA.
GeneTreeiENSGT00760000118932.
HOGENOMiHOG000037209.
HOVERGENiHBG001195.
InParanoidiO00204.
KOiK01015.
OMAiPVGIYSP.
OrthoDBiEOG091G0D5F.
PhylomeDBiO00204.
TreeFamiTF321745.

Enzyme and pathway databases

BioCyciZFISH:HS01587-MONOMER.
ReactomeiR-HSA-156584. Cytosolic sulfonation of small molecules.

Miscellaneous databases

EvolutionaryTraceiO00204.
GeneWikiiSULT2B1.
GenomeRNAii6820.
PROiO00204.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000088002.
CleanExiHS_SULT2B1.
GenevisibleiO00204. HS.

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.
ProtoNetiSearch...

Entry informationi

Entry nameiST2B1_HUMAN
AccessioniPrimary (citable) accession number: O00204
Secondary accession number(s): O00205, O75814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: November 30, 2016
This is version 147 of the entry and version 2 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 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.