O43704 (ST1B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Cytoplasm
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome cellular biogenic amine metabolic process Traceable author statement Ref.1. Source: ProtInc flavonoid metabolic process Inferred from direct assay PubMed 20056724. Source: BHF-UCL steroid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW sulfation Inferred from direct assay PubMed 20056724. Source: BHF-UCL thyroid hormone metabolic process Inferred from direct assay Ref.1. Source: UniProtKB xenobiotic metabolic process Inferred from direct assay PubMed 20056724. Source: BHF-UCL
Cellular_component	cytosol Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	aryl sulfotransferase activity Inferred from electronic annotation. Source: Compara sulfotransferase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

Sulfotransferase family cytosolic 1B member 1

PRO_0000085161

Regions

Nucleotide binding

48 – 53

6

PAPS

Nucleotide binding

228 – 233

6

PAPS

Nucleotide binding

258 – 260

3

PAPS

Region

107 – 109

3

Substrate binding By similarity

Sites

Active site

109

1

Proton acceptor By similarity

Binding site

131

1

PAPS

Binding site

139

1

PAPS

Binding site

194

1

PAPS

Experimental info

Sequence conflict

183

1

K → R in AAH10895. Ref.3

Sequence conflict

186

1

E → G in BAA24547. Ref.1

Secondary structure

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296

Helix Strand Turn

Details...

Turn

5 – 9

5

Beta strand

13 – 15

3

Beta strand

18 – 20

3

Helix

22 – 25

4

Helix

29 – 32

4

Beta strand

41 – 46

6

Helix

51 – 62

12

Turn

63 – 65

3

Helix

67 – 70

4

Helix

75 – 78

4

Turn

87 – 89

3

Helix

93 – 99

7

Beta strand

105 – 108

4

Turn

112 – 114

3

Helix

117 – 121

5

Beta strand

125 – 130

6

Helix

133 – 146

14

Helix

156 – 165

10

Helix

173 – 182

10

Turn

183 – 186

4

Beta strand

189 – 193

5

Helix

194 – 199

6

Helix

201 – 211

11

Helix

218 – 227

10

Helix

230 – 234

5

Turn

237 – 239

3

Turn

246 – 248

3

Turn

251 – 253

3

Helix

264 – 267

4

Helix

271 – 285

15

Sequences

	Sequence		Length	Mass (Da)
	O43704 [UniParc]. Last modified January 4, 2005. Version 2. Checksum: AFEB61B21DBD782C	FASTA	296	34,899
	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

References

	« Hide 'large scale' referencesShow '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.

IPI

IPI00102581.

PIR

JC5885.

RefSeq

NP_055280.2. NM_014465.3.

UniGene

Hs.129742.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z5F	X-ray	2.10	A/B	1-296	[»]
3CKL	X-ray	2.00	A/B	1-296	[»]

ProteinModelPortal

O43704.

ModBase

Search...

PTM databases

PhosphoSite

O43704.

Proteomic databases

PaxDb

O43704.

PRIDE

O43704.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310613; ENSP00000308770; ENSG00000173597.

GeneID

27284.

KEGG

hsa:27284.

UCSC

uc003hen.3. human.

Organism-specific databases

CTD

27284.

GeneCards

GC04M070641.

HGNC

HGNC:17845. SULT1B1.

HPA

HPA002107.

MIM

608436. gene.

neXtProt

NX_O43704.

PharmGKB

PA415.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG260792.

HOGENOM

HOG000037209.

HOVERGEN

HBG001195.

InParanoid

O43704.

KO

K01025.

OMA

KNLKMVH.

OrthoDB

EOG40P47H.

PhylomeDB

O43704.

Enzyme and pathway databases

BRENDA

2.8.2.1. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

O43704.

Bgee

O43704.

CleanEx

HS_SULT1B1.

Genevestigator

O43704.

GermOnline

ENSG00000173597. Homo sapiens.

Family and domain databases

InterPro

IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1743294.

EvolutionaryTrace

O43704.

GenomeRNAi

27284.

NextBio

50216.

SOURCE

Search...

Entry information

Entry name

ST1B1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.