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P50224 (ST1A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sulfotransferase 1A3/1A4

Short name=ST1A3/ST1A4
EC=2.8.2.1
Alternative name(s):
Aryl sulfotransferase 1A3/1A4
Catecholamine-sulfating phenol sulfotransferase
HAST3
M-PST
Monoamine-sulfating phenol sulfotransferase
Placental estrogen sulfotransferase
Sulfotransferase, monoamine-preferring
Thermolabile phenol sulfotransferase
Short name=TL-PST
Gene names
Name:SULT1A3
Synonyms:STM
AND
Name:SULT1A4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length295 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 phenolic monoamines (neurotransmitters such as dopamine, norepinephrine and serotonin) and phenolic and catechol drugs.

Catalytic activity

3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Liver, colon, kidney, lung, brain, spleen, small intestine, placenta and leukocyte.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the sulfotransferase 1 family.

Sequence caution

Isoform 2: The sequence BAC85507.1 differs from that shown. Reason: Frameshift at position 101.

Ontologies

Keywords
   Biological processCatecholamine metabolism
Lipid metabolism
Steroid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process3'-phosphoadenosine 5'-phosphosulfate metabolic process

Traceable author statement. Source: Reactome

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

catecholamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

flavonoid metabolic process

Inferred from direct assay PubMed 20056724. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

sulfation

Inferred from direct assay PubMed 20056724. Source: BHF-UCL

xenobiotic metabolic process

Inferred from direct assay PubMed 20056724. Source: BHF-UCL

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionaryl sulfotransferase activity

Traceable author statement. Source: Reactome

sulfotransferase activity

Inferred from direct assay PubMed 20056724. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P50224-1)

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: P50224-2)

The sequence of this isoform differs from the canonical sequence as follows:
     167-295: VSYGSWYQHV...GCSLSFRSEL → GGLDWRKEGVKPRGGGYNVQQPCVGAPCPLL
Note: No experimental confirmation available.
Isoform 3 (identifier: P50224-3)

The sequence of this isoform differs from the canonical sequence as follows:
     198-198: E → EEPSAAQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Sulfotransferase 1A3/1A4
PRO_0000085159

Regions

Nucleotide binding48 – 536PAPS
Nucleotide binding227 – 2326PAPS
Nucleotide binding257 – 2593PAPS
Region106 – 1083Substrate binding

Sites

Active site1081Proton acceptor By similarity
Binding site861Substrate
Binding site1301PAPS
Binding site1381PAPS
Binding site1461Substrate
Binding site1931PAPS

Natural variations

Alternative sequence167 – 295129VSYGS…FRSEL → GGLDWRKEGVKPRGGGYNVQ QPCVGAPCPLL in isoform 2.
VSP_012326
Alternative sequence1981E → EEPSAAQ in isoform 3.
VSP_047771

Experimental info

Sequence conflict220 – 2256MDFMVQ → VDLMVE in AAC99987. Ref.8
Sequence conflict2351N → T in AAC99987. Ref.8
Sequence conflict244 – 2452PQ → RR in AAC99987. Ref.8
Sequence conflict2901S → T in AAC99987. Ref.8

Secondary structure

..................................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: ECDDEC03DBE30D46

FASTA29534,196
        10         20         30         40         50         60 
MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLINTYPKSG TTWVSQILDM 

        70         80         90        100        110        120 
IYQGGDLEKC NRAPIYVRVP FLEVNDPGEP SGLETLKDTP PPRLIKSHLP LALLPQTLLD 

       130        140        150        160        170        180 
QKVKVVYVAR NPKDVAVSYY HFHRMEKAHP EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW 

       190        200        210        220        230        240 
ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETM DFMVQHTSFK EMKKNPMTNY 

       250        260        270        280        290 
TTVPQELMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL 

« Hide

Isoform 2 [UniParc].

Checksum: 44C5F13EDA71BC1D
Show »

FASTA19722,069
Isoform 3 [UniParc].

Checksum: 7018229AD3F67542
Show »

FASTA30134,780

References

« Hide '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).
Tissue: Brain.
[2]"Cloning and expression of cDNA encoding human placental estrogen sulfotransferase."
Bernier F., Lopez-Solache I., Labrie F., Luu-The V.
Mol. Cell. Endocrinol. 99:R11-R15(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[3]"Genomic organization and DNA sequence of the human catecholamine-sulfating phenol sulfotransferase gene (STM)."
Dooley T.P., Probst P., Munroe P.B., Mole S.E., Liu Z., Doggett N.A.
Biochem. Biophys. Res. Commun. 205:1325-1332(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[4]"Human liver thermolabile phenol sulfotransferase: cDNA cloning, expression and characterization."
Wood T.C., Aksoy I.A., Aksoy S., Weinshilboum R.M.
Biochem. Biophys. Res. Commun. 198:1119-1127(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 84-101.
Tissue: Liver.
[5]"Human thermolabile phenol sulfotransferase gene (STM): molecular cloning and structural characterization."
Aksoy I.A., Weinshilboum R.M.
Biochem. Biophys. Res. Commun. 208:786-795(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Platelet.
[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).
Tissue: Blood.
[7]"Structure of human estrogen and aryl sulfotransferase gene. Two mRNA species issued from a single gene."
Bernier F., Leblanc G., Labrie F., Luu-The V.
J. Biol. Chem. 269:28200-28205(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Leukocyte.
[8]Gaedigk A., Grant D.M.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[9]"Isolation of seven variants of catecholamine sulfotransferase cDNAs from human kidney."
Terazawa R., Shimada M., Nagata K., Yamazoe Y.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Kidney.
[10]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lung.
[11]"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. expand/collapse author list , 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].
[12]"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: Lung and Pancreas.
[13]"Thermolabile phenol sulfotransferase gene (STM): localization to human chromosome 16p11.2."
Aksoy I.A., Callen D.F., Apostolou S., Her C., Weinshilboum R.M.
Genomics 23:275-277(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 139-198.
Tissue: Lymphocyte.
[14]"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.
[15]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Crystal structure of human catecholamine sulfotransferase."
Bidwell L.M., McManus M.E., Gaedigk A., Kakuta Y., Negishi M., Pedersen L., Martin J.L.
J. Mol. Biol. 293:521-530(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Tissue: Brain.
[17]"Crystal structure of human sulfotransferase SULT1A3 in complex with dopamine and 3'-phosphoadenosine 5'-phosphate."
Lu J.H., Li H.T., Liu M.C., Zhang J.P., Li M., An X.M., Chang W.R.
Biochem. Biophys. Res. Commun. 335:417-423(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE AND L-DOPAMINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19956 mRNA. Translation: AAA02943.1.
L25275 mRNA. Translation: AAA36523.1.
U08032 mRNA. Translation: AAA17723.1.
U20499 Genomic DNA. Translation: AAA64490.1.
X84653 mRNA. Translation: CAA59146.1.
L34160 Genomic DNA. No translation available.
U37686 Genomic DNA. Translation: AAA86536.1.
U34199 mRNA. Translation: AAC99987.1.
AK122733 mRNA. Translation: BAC85507.1. Frameshift.
AK298073 mRNA. Translation: BAG60362.1.
AC106782 Genomic DNA. No translation available.
AC133555 Genomic DNA. No translation available.
AB111094 mRNA. Translation: BAE94928.1.
BC014471 mRNA. Translation: AAH14471.1.
BC078144 mRNA. Translation: AAH78144.1.
U08099 Genomic DNA. Translation: AAA82126.1.
CCDSCCDS10674.1. [P50224-1]
CCDS32427.1. [P50224-1]
PIRA55451.
RefSeqNP_001017390.1. NM_001017390.2. [P50224-1]
NP_808220.1. NM_177552.3. [P50224-1]
XP_005276563.1. XM_005276506.2. [P50224-1]
XP_005276564.1. XM_005276507.2. [P50224-1]
XP_006726684.1. XM_006726621.1. [P50224-1]
UniGeneHs.460558.
Hs.744871.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CJMX-ray2.40A1-295[»]
2A3RX-ray2.60A/B1-295[»]
DisProtDP00011.
ProteinModelPortalP50224.
SMRP50224. Positions 9-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112687. 4 interactions.
138644. 4 interactions.
IntActP50224. 2 interactions.
STRING9606.ENSP00000339221.

Chemistry

ChEMBLCHEMBL1743293.

PTM databases

PhosphoSiteP50224.

Polymorphism databases

DMDM1711609.

2D gel databases

OGPP50224.

Proteomic databases

MaxQBP50224.
PRIDEP50224.

Protocols and materials databases

DNASU445329.
6818.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338971; ENSP00000343645; ENSG00000261052. [P50224-1]
ENST00000344620; ENSP00000339221; ENSG00000213648. [P50224-1]
ENST00000354723; ENSP00000346760; ENSG00000261052. [P50224-1]
ENST00000355544; ENSP00000347739; ENSG00000261052. [P50224-1]
ENST00000360423; ENSP00000353600; ENSG00000213648. [P50224-1]
ENST00000395137; ENSP00000378569; ENSG00000261052. [P50224-1]
ENST00000395138; ENSP00000378570; ENSG00000261052. [P50224-1]
ENST00000395400; ENSP00000378796; ENSG00000213648. [P50224-1]
ENST00000563322; ENSP00000454518; ENSG00000261052. [P50224-3]
ENST00000565290; ENSP00000456834; ENSG00000213648. [P50224-3]
GeneID101929857.
445329.
6818.
KEGGhsa:101929857.
hsa:445329.
hsa:6818.
UCSCuc002dsw.3. human. [P50224-1]
uc010vdp.2. human. [P50224-2]

Organism-specific databases

CTD445329.
6818.
GeneCardsGC16P029479.
GC16P030213.
HGNCHGNC:11455. SULT1A3.
HGNC:30004. SULT1A4.
HPAHPA049500.
HPA051051.
MIM600641. gene.
neXtProtNX_P50224.
PharmGKBPA344.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000037209.
HOVERGENHBG001195.
KOK01014.
OMAPPRLIKS.
PhylomeDBP50224.
TreeFamTF321745.

Enzyme and pathway databases

BioCycMetaCyc:HS05608-MONOMER.
BRENDA2.8.2.1. 2681.
ReactomeREACT_111217. Metabolism.
REACT_17015. Metabolism of proteins.
SABIO-RKP50224.

Gene expression databases

BgeeP50224.
CleanExHS_SULT1A3.
HS_SULT1A4.
GenevestigatorP50224.

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

EvolutionaryTraceP50224.
GeneWikiSULT1A3.
NextBio111370.
PROP50224.
SOURCESearch...

Entry information

Entry nameST1A3_HUMAN
AccessionPrimary (citable) accession number: P50224
Secondary accession number(s): B4DNV0 expand/collapse secondary AC list , O95603, Q1ET66, Q6ZWJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 147 of the entry and version 1 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 16

Human chromosome 16: entries, gene names and cross-references to MIM