O00204 (ST2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	365 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 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.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Cytoplasm Endoplasmic reticulum Microsome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome steroid metabolic process Inferred from direct assay Ref.4Ref.1. Source: UniProtKB sulfate assimilation Inferred from electronic annotation. Source: Compara xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alcohol sulfotransferase activity Traceable author statement. Source: Reactome steroid sulfotransferase activity Inferred from direct assay Ref.4Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ALS2CR12	Q96Q35	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 365

365

Sulfotransferase family cytosolic 2B member 1

PRO_0000085149

Regions

Nucleotide binding

70 – 75

6

PAPS

Nucleotide binding

244 – 249

6

PAPS

Nucleotide binding

274 – 276

3

PAPS

Compositional bias

305 – 365

61

Pro/Ser-rich

Sites

Active site

125

1

Proton acceptor

Binding site

98

1

Substrate

Binding site

103

1

Substrate

Binding site

125

1

Substrate

Binding site

147

1

PAPS

Binding site

155

1

PAPS

Binding site

210

1

PAPS

Amino acid modifications

Modified residue

348

1

Phosphoserine Ref.6

Natural variations

Alternative sequence

1 – 23

23

MDGPA…DISEI → MASPPPFH in isoform 2.

VSP_012510

Natural variant

51

1

L → S.
Corresponds to variant rs16982149 [ dbSNP | Ensembl ].

VAR_020887

Natural variant

240

1

V → I.
Corresponds to variant rs2302947 [ dbSNP | Ensembl ].

VAR_021988

Natural variant

345

1

P → L.
Corresponds to variant rs17842463 [ dbSNP | Ensembl ].

VAR_020888

Experimental info

Mutagenesis

1 – 23

23

Missing: Loss of the cholesterol sulfotransferase activity. Ref.4

Mutagenesis

1 – 18

18

Missing: Increases the cholesterol sulfotransferase activity. Ref.4

Mutagenesis

19

1

D → A: Increases the cholesterol sulfotransferase activity. Ref.4

Mutagenesis

20

1

I → A: Loss of the cholesterol sulfotransferase activity. Ref.4

Mutagenesis

21

1

S → A: Increases the cholesterol sulfotransferase activity. Ref.4

Mutagenesis

22

1

E → A: Increases the cholesterol sulfotransferase activity. Ref.4

Mutagenesis

23

1

I → A: Loss of the cholesterol sulfotransferase activity. Ref.4

Mutagenesis

347

1

S → A: No change in subcellular localization. Ref.6

Mutagenesis

348

1

S → 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

Mutagenesis

348

1

S → G: Abolishes nuclear localization. Ref.6

Mutagenesis

352

1

S → G: No change in subcellular localization. Ref.6

Mutagenesis

357

1

S → G: No change in subcellular localization. Ref.6

Sequence conflict

350

1

S → N in AAC78498. Ref.1

Secondary structure

1

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365

Helix Strand Turn

Details...

Helix

19 – 25

7

Beta strand

31 – 34

4

Beta strand

37 – 41

5

Helix

46 – 54

9

Beta strand

63 – 68

6

Helix

73 – 84

12

Turn

85 – 87

3

Helix

90 – 94

5

Helix

97 – 100

4

Beta strand

103 – 106

4

Helix

110 – 112

3

Beta strand

121 – 124

4

Turn

128 – 130

3

Helix

133 – 135

3

Beta strand

141 – 146

6

Helix

149 – 162

14

Beta strand

163 – 166

4

Helix

172 – 180

9

Helix

189 – 196

8

Helix

197 – 199

3

Beta strand

205 – 209

5

Helix

210 – 215

6

Helix

217 – 228

12

Helix

234 – 244

11

Helix

246 – 250

5

Turn

253 – 255

3

Turn

256 – 259

4

Turn

262 – 264

3

Turn

267 – 269

3

Helix

280 – 283

4

Helix

287 – 300

14

Turn

301 – 303

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SULT2B1b) (B) [UniParc]. Last modified January 4, 2005. Version 2. Checksum: 13E95248DD40DF91	FASTA	365	41,308
	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
	Isoform 2 (SULT2B1a) (A) [UniParc]. Checksum: CE5BAA8F8874E3A4	FASTA	350	39,599
	10 20 30 40 50 60 MASPPPFHSQ KLPGEYFRYK GVPFPVGLYS LESISLAENT QDVRDDDIFI ITYPKSGTTW 70 80 90 100 110 120 MIEIICLILK EGDPSWIRSV PIWERAPWCE TIVGAFSLPD QYSPRLMSSH LPIQIFTKAF 130 140 150 160 170 180 FSSKAKVIYM GRNPRDVVVS LYHYSKIAGQ LKDPGTPDQF LRDFLKGEVQ FGSWFDHIKG 190 200 210 220 230 240 WLRMKGKDNF LFITYEELQQ DLQGSVERIC GFLGRPLGKE ALGSVVAHST FSAMKANTMS 250 260 270 280 290 300 NYTLLPPSLL DHRRGAFLRK GVCGDWKNHF TVAQSEAFDR AYRKQMRGMP TFPWDEDPEE 310 320 330 340 350 DGSPDPEPSP EPEPKPSLEP NTSLEREPRP NSSPSPSPGQ ASETPHPRPS

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.

IPI

IPI00008179.
IPI00328142.

RefSeq

NP_004596.2. NM_004605.2.
NP_814444.1. NM_177973.1.

UniGene

Hs.369331.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q1Q	X-ray	2.91	A	24-365	[»]
1Q1Z	X-ray	2.40	A	19-312	[»]
1Q20	X-ray	2.30	A	19-312	[»]
1Q22	X-ray	2.50	A	19-312	[»]

DisProt

DP00404.

ProteinModelPortal

O00204.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00204. 2 interactions.

MINT

MINT-1440870.

STRING

9606.ENSP00000201586.

PTM databases

PhosphoSite

O00204.

Proteomic databases

PaxDb

O00204.

PRIDE

O00204.

Protocols and materials databases

DNASU

6820.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000201586; ENSP00000201586; ENSG00000088002.
ENST00000323090; ENSP00000312880; ENSG00000088002.

GeneID

6820.

KEGG

hsa:6820.

UCSC

uc002pjl.3. human.
uc002pjm.3. human.

Organism-specific databases

CTD

6820.

GeneCards

GC19P049055.

HGNC

HGNC:11459. SULT2B1.

HPA

CAB033013.

MIM

604125. gene.

neXtProt

NX_O00204.

PharmGKB

PA36249.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG296990.

HOGENOM

HOG000037209.

HOVERGEN

HBG001195.

InParanoid

O00204.

KO

K01015.

OMA

HYSKIAR.

OrthoDB

EOG4NS3CD.

PhylomeDB

O00204.

Enzyme and pathway databases

BRENDA

2.8.2.2. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

O00204.

CleanEx

HS_SULT2B1.

Genevestigator

O00204.

GermOnline

ENSG00000088002. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL1743297.

EvolutionaryTrace

O00204.

GenomeRNAi

6820.

NextBio

26633.

SOURCE

Search...

Entry information

Entry name

ST2B1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 115 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.