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P50225 (ST1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 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
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 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Sulfotransferase 1A1
PRO_0000085127

Regions

Nucleotide binding48 – 536PAPS
Nucleotide binding227 – 2326PAPS
Nucleotide binding255 – 2595PAPS
Region106 – 1083Substrate binding

Sites

Active site1081Proton acceptor By similarity
Binding site1301PAPS
Binding site1381PAPS
Binding site1931PAPS

Natural variations

Alternative sequence1 – 124124MELIQ…DQKVK → MLAKLLCDQVVGAPIAVSAF YAGMSILQGKDDIFLDLKQK FWNTYM in isoform 2.
VSP_040101
Natural variant371R → Q. Ref.25
VAR_009302
Natural variant1511E → D.
Corresponds to variant rs1042014 [ dbSNP | Ensembl ].
VAR_028721
Natural variant1511E → Q.
Corresponds to variant rs1042011 [ dbSNP | Ensembl ].
VAR_057339
Natural variant2131R → 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 variant2231V → 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 variant2351N → T.
Corresponds to variant rs35728980 [ dbSNP | Ensembl ].
VAR_014889
Natural variant2821E → K. Ref.3 Ref.9
Corresponds to variant rs36043491 [ dbSNP | Ensembl ].
VAR_061886

Experimental info

Mutagenesis701C → S: Increased sensitivity of enzyme activity to heat inactivation. Ref.19
Sequence conflict901P → L in AAA67895. Ref.3
Sequence conflict1461A → T in CAA59147. Ref.5
Sequence conflict1811E → G in CAA59147. Ref.5
Sequence conflict2431V → A in AAA67895. Ref.3
Sequence conflict2901S → T in AAA99892. Ref.3
Sequence conflict2901S → T in AAC50480. Ref.9

Secondary structure

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

Details...

Sequences

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

Last modified November 30, 2010. Version 3.
Checksum: 7D4362A603A29176

FASTA29534,165
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8A6A935E4DD11A6D
Show »

FASTA21725,388

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), 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. 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].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS10637.1. [P50225-2]
CCDS32420.1. [P50225-1]
PIRI57945.
JC2523.
JC5248.
S52399.
S52794.
RefSeqNP_001046.2. NM_001055.3. [P50225-1]
NP_803565.1. NM_177529.2. [P50225-1]
NP_803566.1. NM_177530.2. [P50225-1]
NP_803878.1. NM_177534.2. [P50225-1]
NP_803880.1. NM_177536.3. [P50225-2]
XP_005255579.1. XM_005255522.1. [P50225-1]
UniGeneHs.567342.
Hs.736805.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LS6X-ray1.90A1-295[»]
1Z28X-ray2.30A1-295[»]
2D06X-ray2.30A/B1-295[»]
3QVUX-ray2.50A/B1-295[»]
3QVVX-ray2.35A/B1-295[»]
3U3JX-ray2.70A/B1-294[»]
3U3KX-ray2.36A/B1-295[»]
3U3MX-ray2.30A1-295[»]
3U3OX-ray2.00A1-295[»]
3U3RX-ray2.36A1-295[»]
4GRAX-ray2.56A/B1-295[»]
ProteinModelPortalP50225.
SMRP50225. Positions 7-295.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112686. 35 interactions.
IntActP50225. 3 interactions.
STRING9606.ENSP00000321988.

Chemistry

ChEMBLCHEMBL1743291.

PTM databases

PhosphoSiteP50225.

Polymorphism databases

DMDM313104286.

2D gel databases

OGPP50225.

Proteomic databases

MaxQBP50225.
PaxDbP50225.
PRIDEP50225.

Protocols and materials databases

DNASU6817.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314752; ENSP00000321988; ENSG00000196502. [P50225-1]
ENST00000350842; ENSP00000329399; ENSG00000196502. [P50225-2]
ENST00000395607; ENSP00000378971; ENSG00000196502. [P50225-1]
ENST00000395609; ENSP00000378972; ENSG00000196502. [P50225-1]
ENST00000569554; ENSP00000457912; ENSG00000196502. [P50225-1]
GeneID6817.
KEGGhsa:6817.
UCSCuc002dqi.3. human. [P50225-1]
uc002dqm.3. human. [P50225-2]

Organism-specific databases

CTD6817.
GeneCardsGC16M028616.
H-InvDBHIX0017846.
HGNCHGNC:11453. SULT1A1.
MIM171150. gene.
neXtProtNX_P50225.
PharmGKBPA343.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260792.
HOGENOMHOG000037209.
HOVERGENHBG001195.
InParanoidP50225.
KOK01014.
OMAVGLPINI.
OrthoDBEOG7V49ZK.
PhylomeDBP50225.
TreeFamTF321745.

Enzyme and pathway databases

BioCycMetaCyc:HS09898-MONOMER.
BRENDA2.8.2.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP50225.

Gene expression databases

ArrayExpressP50225.
BgeeP50225.
CleanExHS_SULT1A1.
GenevestigatorP50225.

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

EvolutionaryTraceP50225.
GeneWikiSULT1A1.
GenomeRNAi6817.
NextBio26605.
PROP50225.
SOURCESearch...

Entry information

Entry nameST1A1_HUMAN
AccessionPrimary (citable) accession number: P50225
Secondary accession number(s): Q2NL71 expand/collapse secondary AC list , Q86U58, Q92818, Q9BVU6, Q9UGG7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 30, 2010
Last modified: July 9, 2014
This is version 146 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

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