Protein-tyrosine sulfotransferase 1 (TPST1)

Protein-tyrosine sulfotransferase 1 (TPST1) is an enzyme located in the trans-Golgi network of human cells that catalyzes the transfer of a sulfate group from 3′-phosphoadenylyl sulfate (PAPS) to the phenolic group of tyrosine residues in substrate proteins[1][3][4]. As a type II transmembrane glycoprotein, TPST1 recognizes and modifies acidic motifs, primarily in secreted and transmembrane proteins involved in extracellular interactions and signaling[1][4]. This post-translational modification (tyrosine O-sulfation) can regulate protein–protein interactions, receptor binding affinities, and cell–cell communication[3][4]. TPST1 shares significant sequence and structural homology with TPST2, displaying broad and overlapping substrate specificities, though with some distinctions in substrate recognition[1][3][4]. The biological significance of TPST1 centers on its role in protein maturation and regulation rather than any direct disease causation[1][3]. No specific drugs targeting TPST1 or approved clinical applications are noted in current literature, nor are there widely recognized safety concerns or biomarkers related to TPST1 function[1][3][4].

Other names

Tyrosylprotein sulfotransferase 1TPST1TPST-1TANGO13ATransport and Golgi organization 13 homolog A (Drosophila)

Catalyzes the transfer of a sulfonate (SO3-) group from the donor molecule 3′-phosphoadenylyl sulfate (PAPS) to tyrosine residues on substrate proteins[1][4]