Target intelligence / Profile preview

Ribosomal RNA processing protein 9 (RRP9)

Target
RRP9
Molecular classification
Other (snoRNP-specific protein, WD-repeat protein, ribosome biogenesis factor)
01

Overview

Ribosomal RNA processing protein 9 (RRP9) is a highly conserved, nucleolar, WD-repeat protein that specifically associates with U3 small nucleolar RNA (snoRNA), forming part of the U3 snoRNP complex, which is essential for eukaryotic ribosome biogenesis[1][2][4]. RRP9 plays a key role in the early steps of precursor ribosomal RNA (pre-rRNA) processing by facilitating the cleavage events necessary for the formation of the 18S rRNA—a component of the small ribosomal subunit[1][2][3][4]. Structurally, RRP9 has a WD-repeat domain, forming a β-propeller fold involved in specific RNA and protein interactions[1][2]. RRP9 functions as a molecular scaffold in the SSU (small subunit) processome, where it specifically recognizes and binds to the U3 snoRNA via conserved motifs (notably a unique B/C box)[1][2]. Its precise association with U3 snoRNA, enhanced by interaction with the Snu13 protein, is critical for correct assembly of the U3 snoRNP complex and subsequent pre-rRNA processing[1][2][3]. Mutations in RRP9 or in U3 snoRNA disrupting this interaction lead to failure in ribosome assembly and—at least in yeast—cell lethality[1][2][3]. There is currently no evidence indicating that RRP9 is a therapeutic target, nor are there known drugs or small molecules targeting this protein. Consequently, no clinical safety concerns, mechanism-of-action details, or approved biomarkers are associated with RRP9 in a therapeutic context.

Other names
U3 small nucleolar RNA-interacting protein 2RNU3IP2U3-55KU3 snoRNP-associated 55 kDa proteinU3-55K homologU3 small nucleolar ribonucleoprotein-associated 55 kDa proteinSSU processome component homolog
02

Biological functions

Ribosomal RNA processingSmall subunit ribosome assemblyNucleolar localizationRNA bindingRibosome biogenesis
03

Disease associations

Other (There is currently no direct evidence linking RRP9 to specific human diseases. Its disruption is lethal in yeast due to failed ribosome biogenesis, but human disease associations are not established.)

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