UniProt functional annotation for P50225



	UniProt functional annotation for P50225

UniProt code: P50225.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin (PubMed:16221673, PubMed:12471039, PubMed:22069470, PubMed:21723874, PubMed:10199779, PubMed:7834621). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:7834621). {ECO:0000250|UniProtKB:P17988, ECO:0000269|PubMed:10199779, ECO:0000269|PubMed:12471039, ECO:0000269|PubMed:16221673, ECO:0000269|PubMed:21723874, ECO:0000269|PubMed:22069470, ECO:0000269|PubMed:7834621}.

Catalytic activity: Reaction=3'-phosphoadenylyl sulfate + a phenol = a phenyl sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269|PubMed:10199779, ECO:0000269|PubMed:12471039, ECO:0000269|PubMed:16221673, ECO:0000269|PubMed:21723874, ECO:0000269|PubMed:22069470, ECO:0000269|PubMed:7834621}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165; Evidence={ECO:0000305|PubMed:16221673};

Catalytic activity: Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta- estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582; Evidence={ECO:0000269|PubMed:16221673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373; Evidence={ECO:0000305|PubMed:16221673};

Biophysicochemical properties: Kinetic parameters: KM=0.12 uM for 3,3'-diiodothyronin {ECO:0000269|PubMed:10199779}; Vmax=465 umol/min/mg enzyme with 3,3'-diiodothyronin as substrate {ECO:0000269|PubMed:10199779};

Subunit: Homodimer. {ECO:0000269|PubMed:12471039, ECO:0000269|PubMed:16221673, ECO:0000269|PubMed:20417180}.

Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P17988}.

Tissue specificity: Liver, lung, adrenal, brain, platelets and skin.

Polymorphism: There are several alleles. The sequence shown is that of allele SULT1A1*3. {ECO:0000305|PubMed:10762004, ECO:0000305|PubMed:9345314}.

Similarity: Belongs to the sulfotransferase 1 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones and 3,3'-diiodothyronin (PubMed:16221673, PubMed:12471039, PubMed:22069470, PubMed:21723874, PubMed:10199779, PubMed:7834621). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:7834621). {ECO:0000250\|UniProtKB:P17988, ECO:0000269\|PubMed:10199779, ECO:0000269\|PubMed:12471039, ECO:0000269\|PubMed:16221673, ECO:0000269\|PubMed:21723874, ECO:0000269\|PubMed:22069470, ECO:0000269\|PubMed:7834621}.


Catalytic activity:		Reaction=3'-phosphoadenylyl sulfate + a phenol = a phenyl sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:12164, ChEBI:CHEBI:15378, ChEBI:CHEBI:33853, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:140317; EC=2.8.2.1; Evidence={ECO:0000269\|PubMed:10199779, ECO:0000269\|PubMed:12471039, ECO:0000269\|PubMed:16221673, ECO:0000269\|PubMed:21723874, ECO:0000269\|PubMed:22069470, ECO:0000269\|PubMed:7834621}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12165; Evidence={ECO:0000305\|PubMed:16221673};
Catalytic activity:		Reaction=17beta-estradiol + 3'-phosphoadenylyl sulfate = 17beta- estradiol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:52372, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136582; Evidence={ECO:0000269\|PubMed:16221673}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52373; Evidence={ECO:0000305\|PubMed:16221673};
Biophysicochemical properties:		Kinetic parameters: KM=0.12 uM for 3,3'-diiodothyronin {ECO:0000269\|PubMed:10199779}; Vmax=465 umol/min/mg enzyme with 3,3'-diiodothyronin as substrate {ECO:0000269\|PubMed:10199779};
Subunit:		Homodimer. {ECO:0000269\|PubMed:12471039, ECO:0000269\|PubMed:16221673, ECO:0000269\|PubMed:20417180}.
Subcellular location:		Cytoplasm {ECO:0000250\|UniProtKB:P17988}.
Tissue specificity:		Liver, lung, adrenal, brain, platelets and skin.
Polymorphism:		There are several alleles. The sequence shown is that of allele SULT1A1*3. {ECO:0000305\|PubMed:10762004, ECO:0000305\|PubMed:9345314}.
Similarity:		Belongs to the sulfotransferase 1 family. {ECO:0000305}.