Literature summary for 2.8.2.1 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 .

Search for more literature for 2.8.2.1

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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

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

Source Tissue

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
SULT1A1	-	Homo sapiens
SULT1A3	-	Homo sapiens

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)