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O00204 (ST2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfotransferase family cytosolic 2B member 1

Short name=ST2B1
Short name=Sulfotransferase 2B1
EC=2.8.2.2
Alternative name(s):
Alcohol sulfotransferase
Hydroxysteroid sulfotransferase 2
Gene names
Name:SULT2B1
Synonyms:HSST2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length365 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 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. Ref.1 Ref.4

Catalytic activity

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

Subcellular location

Cytoplasm. Microsome. Nucleus. Note: Phosphorylation of Ser-348 is required for translocation to the nucleus. Ref.5 Ref.6

Tissue specificity

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

Sequence similarities

Belongs to the sulfotransferase 1 family.

Biophysicochemical properties

Kinetic parameters:

KM=10.9 µM for DHEA (at 37 degrees Celsius, in the presence of 1mM MgCl2) Ref.5 Ref.6

KM=3.8 µM for DHEA (at 37 degrees Celsius, in the presence of 10mM MgCl2)

KM=11.8 µM for pregnenolone (at 37 degrees Celsius, in the presence of 1mM MgCl2)

KM=0.6 µM for PAPS (at 37 degrees Celsius, in the presence of 1mM MgCl2)

Vmax=1752 pmol/min/mg enzyme toward DHEA (at 37 degrees Celsius, in the presence of 10 mM MgCl2)

Temperature dependence:

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ALS2CR12Q96Q353EBI-749441,EBI-750451

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00204-1)

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.
Isoform 2 (identifier: O00204-2)

Also known as: SULT2B1a; A;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Sulfotransferase family cytosolic 2B member 1
PRO_0000085149

Regions

Nucleotide binding70 – 756PAPS
Nucleotide binding244 – 2496PAPS
Nucleotide binding274 – 2763PAPS
Compositional bias305 – 36561Pro/Ser-rich

Sites

Active site1251Proton acceptor
Binding site981Substrate
Binding site1031Substrate
Binding site1251Substrate
Binding site1471PAPS
Binding site1551PAPS
Binding site2101PAPS

Amino acid modifications

Modified residue3481Phosphoserine Ref.6

Natural variations

Alternative sequence1 – 2323MDGPA…DISEI → MASPPPFH in isoform 2.
VSP_012510
Natural variant511L → S.
Corresponds to variant rs16982149 [ dbSNP | Ensembl ].
VAR_020887
Natural variant2401V → I.
Corresponds to variant rs2302947 [ dbSNP | Ensembl ].
VAR_021988
Natural variant3451P → L.
Corresponds to variant rs17842463 [ dbSNP | Ensembl ].
VAR_020888

Experimental info

Mutagenesis1 – 2323Missing: Loss of the cholesterol sulfotransferase activity. Ref.4
Mutagenesis1 – 1818Missing: Increases the cholesterol sulfotransferase activity. Ref.4
Mutagenesis191D → A: Increases the cholesterol sulfotransferase activity. Ref.4
Mutagenesis201I → A: Loss of the cholesterol sulfotransferase activity. Ref.4
Mutagenesis211S → A: Increases the cholesterol sulfotransferase activity. Ref.4
Mutagenesis221E → A: Increases the cholesterol sulfotransferase activity. Ref.4
Mutagenesis231I → A: Loss of the cholesterol sulfotransferase activity. Ref.4
Mutagenesis3471S → A: No change in subcellular localization. Ref.6
Mutagenesis3481S → 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. Ref.6
Mutagenesis3481S → G: Abolishes nuclear localization. Ref.6
Mutagenesis3521S → G: No change in subcellular localization. Ref.6
Mutagenesis3571S → G: No change in subcellular localization. Ref.6
Sequence conflict3501S → N in AAC78498. Ref.1

Secondary structure

........................................................... 365
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SULT2B1b) (B) [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 13E95248DD40DF91

FASTA36541,308
        10         20         30         40         50         60 
MDGPAEPQIP GLWDTYEDDI SEISQKLPGE YFRYKGVPFP VGLYSLESIS LAENTQDVRD 

        70         80         90        100        110        120 
DDIFIITYPK SGTTWMIEII CLILKEGDPS WIRSVPIWER APWCETIVGA FSLPDQYSPR 

       130        140        150        160        170        180 
LMSSHLPIQI FTKAFFSSKA KVIYMGRNPR DVVVSLYHYS KIAGQLKDPG TPDQFLRDFL 

       190        200        210        220        230        240 
KGEVQFGSWF DHIKGWLRMK GKDNFLFITY EELQQDLQGS VERICGFLGR PLGKEALGSV 

       250        260        270        280        290        300 
VAHSTFSAMK ANTMSNYTLL PPSLLDHRRG AFLRKGVCGD WKNHFTVAQS EAFDRAYRKQ 

       310        320        330        340        350        360 
MRGMPTFPWD EDPEEDGSPD PEPSPEPEPK PSLEPNTSLE REPRPNSSPS PSPGQASETP 


HPRPS 

« Hide

Isoform 2 (SULT2B1a) (A) [UniParc].

Checksum: CE5BAA8F8874E3A4
Show »

FASTA35039,599

References

« Hide 'large scale' references
[1]"Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a single chromosome 19 gene."
Her C., Wood T.C., Eichler E.E., Mohrenweiser H.W., Ramagli L.S., Siciliano M.J., Weinshilboum R.M.
Genomics 53:284-295(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Placenta.
[2]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 1).
Tissue: Skin.
[4]"Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase."
Fuda H., Lee Y.C., Shimizu C., Javitt N.B., Strott C.A.
J. Biol. Chem. 277:36161-36166(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 1-MET--ASP-18; 1-MET--ILE-23; ASP-19; ILE-20; SER-21; GLU-22 AND ILE-23.
[5]"Characterization of proline-serine-rich carboxyl terminus in human sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic properties, and phosphorylation."
He D., Falany C.N.
Drug Metab. Dispos. 34:1749-1755(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[6]"Site-directed mutagenesis of human cytosolic sulfotransferase (SULT) 2B1b to phospho-mimetic Ser348Asp results in an isoform with increased catalytic activity."
Salman E.D., He D., Runge-Morris M., Kocarek T.A., Falany C.N.
J. Steroid Biochem. Mol. Biol. 127:315-323(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-348, MUTAGENESIS OF SER-347; SER-348; SER-352 AND SER-357.
[7]"Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms."
Lee K.A., Fuda H., Lee Y.C., Negishi M., Strott C.A., Pedersen L.C.
J. Biol. Chem. 278:44593-44599(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-312 IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE (PAP) AND PREGNENOLONE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U92314 mRNA. Translation: AAC78498.1.
U92315 mRNA. Translation: AAC78499.1.
U92322 expand/collapse EMBL AC list , U92316, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78553.1.
U92322 expand/collapse EMBL AC list , U92316, U92317, U92318, U92319, U92320, U92321 Genomic DNA. Translation: AAC78554.1.
AC008403 Genomic DNA. No translation available.
BC034694 mRNA. Translation: AAH34694.1.
RefSeqNP_004596.2. NM_004605.2.
NP_814444.1. NM_177973.1.
UniGeneHs.369331.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q1QX-ray2.91A24-365[»]
1Q1ZX-ray2.40A19-312[»]
1Q20X-ray2.30A19-312[»]
1Q22X-ray2.50A19-312[»]
DisProtDP00404.
ProteinModelPortalO00204.
SMRO00204. Positions 19-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112689. 2 interactions.
IntActO00204. 2 interactions.
MINTMINT-1440870.
STRING9606.ENSP00000201586.

Chemistry

ChEMBLCHEMBL1743297.

PTM databases

PhosphoSiteO00204.

Proteomic databases

PaxDbO00204.
PRIDEO00204.

Protocols and materials databases

DNASU6820.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000201586; ENSP00000201586; ENSG00000088002. [O00204-1]
ENST00000323090; ENSP00000312880; ENSG00000088002. [O00204-2]
GeneID6820.
KEGGhsa:6820.
UCSCuc002pjl.3. human. [O00204-1]
uc002pjm.3. human. [O00204-2]

Organism-specific databases

CTD6820.
GeneCardsGC19P049055.
HGNCHGNC:11459. SULT2B1.
HPACAB033013.
HPA041724.
HPA043539.
MIM604125. gene.
neXtProtNX_O00204.
PharmGKBPA36249.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296990.
HOGENOMHOG000037209.
HOVERGENHBG001195.
InParanoidO00204.
KOK01015.
OMAHATTGMV.
OrthoDBEOG7V49ZK.
PhylomeDBO00204.
TreeFamTF321745.

Enzyme and pathway databases

BRENDA2.8.2.2. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeO00204.
CleanExHS_SULT2B1.
GenevestigatorO00204.

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

EvolutionaryTraceO00204.
GeneWikiSULT2B1.
GenomeRNAi6820.
NextBio26633.
PROO00204.
SOURCESearch...

Entry information

Entry nameST2B1_HUMAN
AccessionPrimary (citable) accession number: O00204
Secondary accession number(s): O00205, O75814
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 123 of the entry and version 2 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 19

Human chromosome 19: entries, gene names and cross-references to MIM