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O43704 (ST1B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfotransferase family cytosolic 1B member 1

Short name=ST1B1
Short name=Sulfotransferase 1B1
EC=2.8.2.-
Alternative name(s):
Sulfotransferase 1B2
Short name=ST1B2
Thyroid hormone sulfotransferase
Gene names
Name:SULT1B1
Synonyms:ST1B2, SULT1B2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length296 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 dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine, reverse triiodothyronine and thyroxine. Ref.1 Ref.2

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in the liver, peripheral blood leukocytes, colon (mucosal lining), small intestine (jejunum) and spleen. A lesser expression was observed in the lung, placenta and thymus. Ref.2

Sequence similarities

Belongs to the sulfotransferase 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296Sulfotransferase family cytosolic 1B member 1
PRO_0000085161

Regions

Nucleotide binding48 – 536PAPS
Nucleotide binding228 – 2336PAPS
Nucleotide binding258 – 2603PAPS
Region107 – 1093Substrate binding By similarity

Sites

Active site1091Proton acceptor By similarity
Binding site1311PAPS
Binding site1391PAPS
Binding site1941PAPS

Experimental info

Sequence conflict1831K → R in AAH10895. Ref.3
Sequence conflict1861E → G in BAA24547. Ref.1

Secondary structure

.......................................................... 296
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O43704 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: AFEB61B21DBD782C

FASTA29634,899
        10         20         30         40         50         60 
MLSPKDILRK DLKLVHGYPM TCAFASNWEK IEQFHSRPDD IVIATYPKSG TTWVSEIIDM 

        70         80         90        100        110        120 
ILNDGDIEKC KRGFITEKVP MLEMTLPGLR TSGIEQLEKN PSPRIVKTHL PTDLLPKSFW 

       130        140        150        160        170        180 
ENNCKMIYLA RNAKDVSVSY YHFDLMNNLQ PFPGTWEEYL EKFLTGKVAY GSWFTHVKNW 

       190        200        210        220        230        240 
WKKKEEHPIL FLYYEDMKEN PKEEIKKIIR FLEKNLNDEI LDRIIHHTSF EVMKDNPLVN 

       250        260        270        280        290 
YTHLPTTVMD HSKSPFMRKG TAGDWKNYFT VAQNEKFDAI YETEMSKTAL QFRTEI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfotransferases."
Fujita K., Nagata K., Ozawa S., Sasano H., Yamazoe Y.
J. Biochem. 122:1052-1061(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Liver.
[2]"Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver."
Wang J., Falany J.L., Falany C.N.
Mol. Pharmacol. 53:274-282(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Liver.
[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].
Tissue: Bone marrow.
[4]"Mapping of the SULT1B2 gene to human chromosome 4q11-13."
Falany C.N., Wang J.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
[5]"Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3'- 5'-diphosphate (PAP)."
Dombrovski L., Dong A., Bochkarev A., Plotnikov A.N.
Proteins 64:1091-1094(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE.
[6]"Crystal structure of human cytosolic sulfotransferase SULT1B1 in complex with PAP and resveratrol."
Structural genomics consortium (SGC)
Submitted (APR-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE AND RESVERATROL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89479 mRNA. Translation: BAA24547.1.
U95726 mRNA. Translation: AAB65154.1.
BC010895 mRNA. Translation: AAH10895.1.
AF184894 Genomic DNA. Translation: AAF05917.1.
CCDSCCDS3530.1.
PIRJC5885.
RefSeqNP_055280.2. NM_014465.3.
XP_005265734.1. XM_005265677.1.
UniGeneHs.129742.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Z5FX-ray2.10A/B1-296[»]
3CKLX-ray2.00A/B1-296[»]
ProteinModelPortalO43704.
SMRO43704. Positions 1-296.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118108. 1 interaction.

Chemistry

ChEMBLCHEMBL1743294.

PTM databases

PhosphoSiteO43704.

Proteomic databases

MaxQBO43704.
PaxDbO43704.
PRIDEO43704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310613; ENSP00000308770; ENSG00000173597.
GeneID27284.
KEGGhsa:27284.
UCSCuc003hen.3. human.

Organism-specific databases

CTD27284.
GeneCardsGC04M070641.
HGNCHGNC:17845. SULT1B1.
HPAHPA002107.
MIM608436. gene.
neXtProtNX_O43704.
PharmGKBPA415.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260792.
HOGENOMHOG000037209.
HOVERGENHBG001195.
InParanoidO43704.
KOK01025.
OMAKNLKMVH.
OrthoDBEOG7V49ZK.
PhylomeDBO43704.
TreeFamTF321745.

Enzyme and pathway databases

BRENDA2.8.2.1. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressO43704.
BgeeO43704.
CleanExHS_SULT1B1.
GenevestigatorO43704.

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

EvolutionaryTraceO43704.
GeneWikiSULT1B1.
GenomeRNAi27284.
NextBio50216.
PROO43704.
SOURCESearch...

Entry information

Entry nameST1B1_HUMAN
AccessionPrimary (citable) accession number: O43704
Secondary accession number(s): O15497, Q96FI1, Q9UK34
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 115 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 chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM