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Literature summary extracted from

  • Idris, M.; Mitchell, D.J.; Gordon, R.; Sidharthan, N.P.; Butcher, N.J.; Minchin, R.F.
    Interaction of the brain-selective sulfotransferase SULT4A1 with other cytosolic sulfotransferases effects on protein expression and function (2020), Drug Metab. Dispos., 48, 337-344 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.2.1 expression in HeLa cell, SKN-MC cell, and SH-SY5Y cell Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.8.2.1 additional information mutation of isoforms SULT1A1 and SULT1A3 to the sequence found in mouse Sult1e1, which does not form homodimers (T269P, V270E). Mutants bind neither to SULT4A1 nor to each other Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.8.2.1 Homo sapiens P0DMM9 isoform SULT1A3
-
2.8.2.1 Homo sapiens P50225 isoform SULT1A1
-
2.8.2.1 Homo sapiens Q9BR01 isoform SULT4A1
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.8.2.1 neuron isoforms SULT4A1 and SULT1A1/3 colocalize in brain neurons Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.2.1 3'-phosphoadenylyl sulfate + dopamine
-
Homo sapiens adenosine 3',5'-bisphosphate + dopamine sulfate
-
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Subunits

EC Number Subunits Comment Organism
2.8.2.1 More isoforms SULT4A1, SULT1A1, and SULT1A3 form homodimers and heterodimers that require the sulfotransferase dimerization motif Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.8.2.1 SULT1A1
-
Homo sapiens
2.8.2.1 SULT1A3
-
Homo sapiens

General Information

EC Number General Information Comment Organism
2.8.2.1 metabolism isoform SULT4A1 interacts with both SULT1A1 and SULT1A3 when expressed in human cells. SULT4A1, SULT1A1, and SULT1A3 proteins form homodimers and heterodimers that require the sulfotransferase dimerization motif. A loss in SULT1A1/3 protein but an increase in SULT4A1 protein is observed during differentiation of neuronal SH-SY5Y cells, resulting in an increase in the toxicity of substrate dopamine Homo sapiens