P50225 (ST1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfotransferase 1A1
Short name=ST1A1
EC=2.8.2.1

Alternative name(s):
Aryl sulfotransferase 1
HAST1/HAST2
Phenol sulfotransferase 1
Phenol-sulfating phenol sulfotransferase 1
Short name=P-PST 1
ST1A3
Thermostable phenol sulfotransferase
Short name=Ts-PST

Gene names

Name:	SULT1A1
Synonyms:	STP, STP1
ORF Names:	OK/SW-cl.88

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	295 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 catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk. Ref.20 Ref.21
Catalytic activity	3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate. Ref.20 Ref.21 Ref.23 Ref.24
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Tissue specificity	Liver, lung, adrenal, brain, platelets and skin.
Sequence similarities	Belongs to the sulfotransferase 1 family.

Ontologies

Keywords
Biological process	Catecholamine metabolism Lipid metabolism Steroid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome amine metabolic process Traceable author statement PubMed 8661000. Source: ProtInc catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW estrogen metabolic process Inferred from direct assay Ref.21. Source: UniProtKB flavonoid metabolic process Inferred from direct assay PubMed 20056724. Source: BHF-UCL sulfation Inferred from direct assay PubMed 20056724. Source: BHF-UCL xenobiotic metabolic process Inferred from direct assay Ref.20. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	aryl sulfotransferase activity Inferred from direct assay Ref.20. Source: UniProtKB flavonol 3-sulfotransferase activity Inferred from direct assay PubMed 20056724. Source: BHF-UCL steroid sulfotransferase activity Inferred from direct assay Ref.21. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P50225-1)

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: P50225-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: MELIQDTSRP...PQTLLDQKVK → MLAKLLCDQV...LKQKFWNTYM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 295

295

Sulfotransferase 1A1

PRO_0000085127

Regions

Nucleotide binding

48 – 53

6

PAPS

Nucleotide binding

227 – 232

6

PAPS

Nucleotide binding

255 – 259

5

PAPS

Region

106 – 108

3

Substrate binding

Sites

Active site

108

1

Proton acceptor By similarity

Binding site

130

1

PAPS

Binding site

138

1

PAPS

Binding site

193

1

PAPS

Natural variations

Alternative sequence

1 – 124

124

MELIQ…DQKVK → MLAKLLCDQVVGAPIAVSAF YAGMSILQGKDDIFLDLKQK FWNTYM in isoform 2.

VSP_040101

Natural variant

37

1

R → Q. Ref.25

VAR_009302

Natural variant

151

1

E → D.
Corresponds to variant rs1042014 [ dbSNP | Ensembl ].

VAR_028721

Natural variant

151

1

E → Q.
Corresponds to variant rs1042011 [ dbSNP | Ensembl ].

VAR_057339

Natural variant

213

1

R → H in allele SULT1A1*2; common polymorphism; has a lower activity. Ref.12 Ref.13 Ref.25 Ref.26
Corresponds to variant rs9282861 [ dbSNP | Ensembl ].

VAR_007425

Natural variant

223

1

V → M. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.16 Ref.25 Ref.27
Corresponds to variant rs1801030 [ dbSNP | Ensembl ].

VAR_009303

Natural variant

235

1

N → T.
Corresponds to variant rs35728980 [ dbSNP | Ensembl ].

VAR_014889

Natural variant

282

1

E → K. Ref.3 Ref.9
Corresponds to variant rs36043491 [ dbSNP | Ensembl ].

VAR_061886

Experimental info

Mutagenesis

70

1

C → S: Increased sensitivity of enzyme activity to heat inactivation. Ref.19

Sequence conflict

90

1

P → L in AAA67895. Ref.3

Sequence conflict

146

1

A → T in CAA59147. Ref.5

Sequence conflict

181

1

E → G in CAA59147. Ref.5

Sequence conflict

243

1

V → A in AAA67895. Ref.3

Sequence conflict

290

1

S → T in AAA99892. Ref.3

Sequence conflict

290

1

S → T in AAC50480. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

295

Helix Strand Turn

Details...

Beta strand

13 – 15

3

Beta strand

18 – 20

3

Helix

22 – 31

10

Beta strand

41 – 46

6

Helix

51 – 62

12

Turn

63 – 65

3

Helix

67 – 70

4

Helix

75 – 78

4

Beta strand

87 – 89

3

Helix

92 – 97

6

Beta strand

104 – 107

4

Turn

111 – 113

3

Helix

116 – 120

5

Beta strand

124 – 129

6

Helix

132 – 145

14

Helix

155 – 164

10

Helix

172 – 182

11

Turn

183 – 185

3

Beta strand

188 – 192

5

Helix

193 – 198

6

Helix

200 – 211

12

Helix

217 – 226

10

Helix

229 – 234

6

Turn

236 – 238

3

Turn

245 – 247

3

Turn

250 – 252

3

Helix

263 – 266

4

Helix

270 – 283

14

Turn

284 – 286

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: 7D4362A603A29176	FASTA	295	34,165
	10 20 30 40 50 60 MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG TTWVSQILDM 70 80 90 100 110 120 IYQGGDLEKC HRAPIFMRVP FLEFKAPGIP SGMETLKDTP APRLLKTHLP LALLPQTLLD 130 140 150 160 170 180 QKVKVVYVAR NAKDVAVSYY HFYHMAKVHP EPGTWDSFLE KFMVGEVSYG SWYQHVQEWW 190 200 210 220 230 240 ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETV DFVVQHTSFK EMKKNPMTNY 250 260 270 280 290 TTVPQEFMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL
	Isoform 2 [UniParc]. Checksum: 8A6A935E4DD11A6D	FASTA	217	25,388
	10 20 30 40 50 60 MLAKLLCDQV VGAPIAVSAF YAGMSILQGK DDIFLDLKQK FWNTYMVVYV ARNAKDVAVS 70 80 90 100 110 120 YYHFYHMAKV HPEPGTWDSF LEKFMVGEVS YGSWYQHVQE WWELSRTHPV LYLFYEDMKE 130 140 150 160 170 180 NPKREIQKIL EFVGRSLPEE TVDFVVQHTS FKEMKKNPMT NYTTVPQEFM DHSISPFMRK 190 200 210 GMAGDWKTTF TVAQNERFDA DYAEKMAGCS LSFRSEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of two human brain aryl sulfotransferase cDNAs." Zhu X., Veronese M.E., Bernard C.C., Sansom L.N., McManus M.E. Biochem. Biophys. Res. Commun. 195:120-127(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223. Tissue: Brain.
[2]	"Molecular characterisation of a human aryl sulfotransferase cDNA." Zhu X., Veronese M.E., Sansom L.N., McManus M.E. Biochem. Biophys. Res. Commun. 192:671-676(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223. Tissue: Liver.
[3]	"Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase." Wilborn T.W., Comer K.A., Dooley T.P., Reardon I.M., Heinrikson R.L., Falany C.N. Mol. Pharmacol. 43:70-77(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANTS MET-223 AND LYS-282. Tissue: Liver.
[4]	"Structural similarity and diversity of sulfotransferases." Yamazoe Y., Nagata K., Ozawa S., Kato R. Chem. Biol. Interact. 92:107-117(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
[5]	"Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus." Hwang S.-R., Kohn A.B., Hook V.Y.H. Biochem. Biophys. Res. Commun. 207:701-707(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223. Tissue: Hippocampus.
[6]	"Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form." Jones A.L., Hagen M., Coughtrie M.W.H., Roberts R.C., Glatt H. Biochem. Biophys. Res. Commun. 208:855-862(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223. Tissue: Blood.
[7]	"Primary structures and properties of two related forms of aryl sulfotransferases in human liver." Ozawa S., Nagata K., Shimada M., Ueda M., Tsuzuki T., Yamazoe Y., Kato R. Pharmacogenetics 5:S135-S140(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223. Tissue: Liver.
[8]	"Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16." Dooley T.P., Huang Z. Biochem. Biophys. Res. Commun. 228:134-140(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT MET-223.
[9]	"Human phenol sulfotransferase gene contains two alternative promoters: structure and expression of the gene." Bernier F., Soucy P., Luu-The V. DNA Cell Biol. 15:367-375(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS MET-223 AND LYS-282.
[10]	"A single amino acid, Glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3." Dajani R., Hood A.M., Coughtrie M.W. Mol. Pharmacol. 54:942-948(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223. Tissue: Liver.
[11]	Raftogianis R.B., Her C., Weinshilboum R.M. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT MET-223.
[12]	"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients." Shichijo S., Itoh K. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS HIS-213 AND MET-223. Tissue: Colon adenocarcinoma.
[13]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-213.
[14]	"Full-length cDNA libraries and normalization." Li W.B., Gruber C., Jessee J., Polayes D. Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[15]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[16]	"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), VARIANT MET-223. Tissue: Colon and Placenta.
[17]	"Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7." Dooley T.P., Obermoeller R.D., Leiter E.H., Chapman H.D., Falany C.N., Deng Z., Siciliano M.J. Genomics 18:440-443(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107 (ISOFORM 1).
[18]	"Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies." Veronese M.E., Burgess W., Zhu X., McManus M.E. Biochem. J. 302:497-502(1994) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[19]	"Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability." Falany C.N., Zhuang W., Falany J.L. Chem. Biol. Interact. 92:57-66(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF CYS-70.
[20]	"Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition." Gamage N.U., Duggleby R.G., Barnett A.C., Tresillian M., Latham C.F., Liyou N.E., McManus M.E., Martin J.L. J. Biol. Chem. 278:7655-7662(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE (PAP) AND P-NITROPHENOL, CATALYTIC ACTIVITY, FUNCTION.
[21]	"The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates." Gamage N.U., Tsvetanov S., Duggleby R.G., McManus M.E., Martin J.L. J. Biol. Chem. 280:41482-41486(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE AND ESTRADIOL, CATALYTIC ACTIVITY, FUNCTION.
[22]	"Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2." Lu J., Li H., Zhang J., Li M., Liu M.Y., An X., Liu M.C., Chang W. Biochem. Biophys. Res. Commun. 396:429-434(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE.
[23]	"Directed evolution of sulfotransferases and paraoxonases by ancestral libraries." Alcolombri U., Elias M., Tawfik D.S. J. Mol. Biol. 411:837-853(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH ADENOSINE-3'-5'-DIPHOSPHATE AND P-NITROPHENOL, CATALYTIC ACTIVITY.
[24]	"The molecular basis for the broad substrate specificity of human sulfotransferase 1A1." Berger I., Guttman C., Amar D., Zarivach R., Aharoni A. PLoS ONE 6:E26794-E26794(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH ADENOSINE-3'-5'-DIPHOSPHATE AND P-NITROPHENOL, CATALYTIC ACTIVITY.
[25]	"Phenol sulfotransferase pharmacogenetics in humans: association of common SULT1A1 alleles with TS PST phenotype." Raftogianis R.B., Wood T.C., Otterness D.M., Van Loon J.A., Weinshilboum R.M. Biochem. Biophys. Res. Commun. 239:298-304(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GLN-37; HIS-213 AND MET-223.
[26]	"Association between functional genetic polymorphisms of human sulfotransferases 1A1 and 1A2." Engelke C.E., Meinl W., Boeing H., Glatt H. Pharmacogenetics 10:163-169(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-213.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-223, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U09031 mRNA. Translation: AAA18613.1.
L19955 mRNA. Translation: AAA02935.1.
L10819 mRNA. Translation: AAA35562.1.
L19999 mRNA. Translation: AAA99892.1.
U26309 mRNA. Translation: AAA67895.1.
X84654 mRNA. Translation: CAA59147.1.
X78283 mRNA. Translation: CAA55089.1.
U71086 Genomic DNA. Translation: AAB09597.1.
U54701 Genomic DNA. Translation: AAC50480.1.
AJ007418 mRNA. Translation: CAA07495.1.
U52852 Genomic DNA. Translation: AAC51816.1.
AB062428 mRNA. Translation: BAB93491.1.
BT007324 mRNA. Translation: AAP35988.1.
CR608214 mRNA. No translation available.
AC020765 Genomic DNA. No translation available.
BC000923 mRNA. Translation: AAH00923.1.
BC110887 mRNA. Translation: AAI10888.1.
L15346 Genomic DNA. Translation: AAA60595.1.

IPI

IPI00300026.
IPI00654711.

PIR

I57945.
JC2523.
JC5248.
S52399.
S52794.

RefSeq

NP_001046.2. NM_001055.3.
NP_803565.1. NM_177529.2.
NP_803566.1. NM_177530.2.
NP_803878.1. NM_177534.2.
NP_803880.1. NM_177536.3.

UniGene

Hs.567342.
Hs.736805.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LS6	X-ray	1.90	A	1-295	[»]
1Z28	X-ray	2.30	A	1-295	[»]
2D06	X-ray	2.30	A/B	1-295	[»]
3QVU	X-ray	2.50	A/B	1-295	[»]
3QVV	X-ray	2.35	A/B	1-295	[»]
3U3J	X-ray	2.70	A/B	1-294	[»]
3U3K	X-ray	2.36	A/B	1-295	[»]
3U3M	X-ray	2.30	A	1-295	[»]
3U3O	X-ray	2.00	A	1-295	[»]
3U3R	X-ray	2.36	A	1-295	[»]
4GRA	X-ray	2.56	A/B	1-295	[»]

ProteinModelPortal

P50225.

SMR

P50225. Positions 7-295.

ModBase

Search...

Protein-protein interaction databases

IntAct

P50225. 3 interactions.

STRING

9606.ENSP00000321988.

PTM databases

PhosphoSite

P50225.

Polymorphism databases

DMDM

9087220.

2D gel databases

OGP

P50225.

Proteomic databases

PaxDb

P50225.

PRIDE

P50225.

Protocols and materials databases

DNASU

6817.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314752; ENSP00000321988; ENSG00000196502.
ENST00000350842; ENSP00000329399; ENSG00000196502.
ENST00000395607; ENSP00000378971; ENSG00000196502.
ENST00000395609; ENSP00000378972; ENSG00000196502.
ENST00000569554; ENSP00000457912; ENSG00000196502.

GeneID

6817.

KEGG

hsa:6817.

UCSC

uc002dqi.3. human.
uc002dqm.3. human.

Organism-specific databases

CTD

6817.

GeneCards

GC16M028616.

H-InvDB

HIX0017846.

HGNC

HGNC:11453. SULT1A1.

MIM

171150. gene.

neXtProt

NX_P50225.

PharmGKB

PA343.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG260792.

HOGENOM

HOG000037209.

HOVERGEN

HBG001195.

InParanoid

P50225.

KO

K01014.

OMA

ISAPPKC.

OrthoDB

EOG4255T9.

Enzyme and pathway databases

BioCyc

MetaCyc:HS09898-MONOMER.

BRENDA

2.8.2.1. 2681.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P50225.

Gene expression databases

ArrayExpress

P50225.

Bgee

P50225.

CleanEx

HS_SULT1A1.

Genevestigator

P50225.

GermOnline

ENSG00000196502. Homo sapiens.

Family and domain databases

InterPro

IPR000863. Sulfotransferase_dom.
[Graphical view]

Pfam

PF00685. Sulfotransfer_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1743291.

EvolutionaryTrace

P50225.

GenomeRNAi

6817.

NextBio

26605.

SOURCE

Search...

Entry information

Entry name

ST1A1_HUMAN

Accession

Primary (citable) accession number: P50225
Secondary accession number(s): Q2NL71 , Q86U58, Q92818, Q9BVU6, Q9UGG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 30, 2010
Last modified:	April 3, 2013
This is version 135 of the entry and version 3 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.