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O00204 (ST2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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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)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes 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 By similarity.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q8N1B63EBI-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 binding147 – 1559PAPS
Nucleotide binding210 – 24637PAPS
Compositional bias305 – 36460Pro-rich

Sites

Active site1251Proton acceptor
Binding site2751PAPS

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
Sequence conflict3501S → N in AAC78498. Ref.1

Secondary structure

1 ........................................................... 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: 9799594] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / 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: 15057824] [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: 15489334] [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: 12145317] [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]"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: 12923182] [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.
IPIIPI00008179.
IPI00328142.
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[»]
ProteinModelPortalO00204.
SMRO00204. Positions 19-311.
DisProtDP00404.
ModBaseSearch...

Protein-protein interaction databases

IntActO00204. 2 interactions.
MINTMINT-1440870.
STRINGO00204.

PTM databases

PhosphoSiteO00204.

Proteomic databases

PRIDEO00204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000201586; ENSP00000201586; ENSG00000088002.
GeneID6820.
KEGGhsa:6820.
NMPDRfig|9606.3.peg.16810.
UCSCuc002pjl.1. human.
uc002pjm.1. human.

Organism-specific databases

CTD6820.
GeneCardsGC19P049055.
H-InvDBHIX0017516.
HGNCHGNC:11459. SULT2B1.
HPACAB033013.
MIM604125. gene.
neXtProtNX_O00204.
PharmGKBPA36249.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG15600.
GeneTreeENSGT00570000079072.
HOGENOMHBG744340.
HOVERGENHBG001195.
InParanoidO00204.
OMAEGDPSWI.
OrthoDBEOG4NS3CD.
PhylomeDBO00204.

Enzyme and pathway databases

BRENDA2.8.2.2. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO00204.
BgeeO00204.
CleanExHS_SULT2B1.
GenevestigatorO00204.
GermOnlineENSG00000088002. Homo sapiens.

Family and domain databases

InterProIPR000863. Sulfotransferase_dom.
[Graphical view]
KOK01015.
PfamPF00685. Sulfotransfer_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio26633.
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: January 25, 2012
This is version 100 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

Human chromosome 19

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents