RNA polymerase II-associated protein 3 (RPAP3)

RNA polymerase II-associated protein 3 (RPAP3) is a human protein that acts as a scaffold and co-chaperone within the R2TP complex, interfacing between RNA polymerase II and the HSP90 chaperone system[1][7]. RPAP3’s structure contains tetratricopeptide repeat (TPR) domains and a C-terminal domain that enable it to recruit and stabilize client proteins—including RNA polymerase II—by facilitating their assembly and proper folding through interactions with RUVBL1, RUVBL2, PIH1D1, and HSP90[1][2][4][5]. It is essential for the biogenesis and cellular stability of several large multi-subunit complexes, particularly RNA polymerase II, and may play broader roles in the assembly of protein complexes involved in transcription, cellular stress response, and potentially apoptosis[6][7]. RPAP3 is not, however, an established therapeutic target in current drug discovery or pharmacology.

Other names

FLJ21908SPAGhSpaghTah1RNA polymerase II associated protein 3RPAP3