DNA transposase THAP9 (THAP9)

DNA transposase THAP9 (THAP9) is a human enzyme that belongs to the THAP family of proteins, characterized by an N-terminal THAP domain (a C2CH zinc finger motif) responsible for sequence-specific DNA binding[1][3]. THAP9 contains additional structural domains, including a P-element transposase domain (homologous to Drosophila P-element transposase), a leucine-rich region (predicted to mediate oligomerization), and an RNase H-like catalytic domain essential for its DNA excision and integration functions[1][6]. THAP9 is capable of mobilizing transposable elements, exhibiting “cut and paste” activity to excise and insert DNA, though its physiological substrates in humans are not fully identified[2][4][6]. Unlike many transposases, THAP9 is considered to be “domesticated,” meaning its catalytic activity persists even within the human genome but it is not known to mobilize endogenous human transposons frequently[2][6]. Its broader biological functions, disease involvement, and pharmaceutical targeting remain largely uncharacterized, making THAP9 a candidate for further research in genome stability and potential therapeutic interventions.

Other names

THAP domain-containing protein 9hTh9FLJ34093DNA transposase THAP9THAP9

Not applicable for approved or investigational drugs, since no drug is known to target THAP9. Hypothetically, an inhibitor would block DNA excision/integration activity via the RNase-H fold (DDE/D motif), preventing transposon movement.