TPST1 Gene: Function, Location, and Disease Associations | Biomedical SEO

The TPST1 gene encodes tyrosylprotein sulfotransferase 1, an enzyme localized to the trans-Golgi network. It catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to tyrosine residues on proteins, a post-translational modification known as tyrosine O-sulfation. This modification is critical for protein-protein interactions, receptor-ligand binding, and immune regulation. TPST1 is expressed in various tissues and is involved in multiple physiological processes, including inflammation, hemostasis, and development. Mutations or altered expression of TPST1 have been linked to several diseases, including cancer and inflammatory conditions.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Protein modification; tyrosine sulfation

• Post-translational modification: sulfation

• Glycosaminoglycan metabolism (indirect)

TPST1 is a type II transmembrane protein located in the trans-Golgi network. It consists of a short N-terminal cytoplasmic domain, a transmembrane helix, and a large luminal catalytic domain. The enzyme transfers sulfate from PAPS to tyrosine residues within acidic motifs of target proteins. TPST1 is involved in the sulfation of various proteins, including chemokine receptors, adhesion molecules, and hormones. Its activity is essential for proper protein function in immune surveillance, hemostasis, and development. Structural studies reveal a dimeric organization and substrate specificity determined by the surrounding amino acid sequence.