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NHP2-like protein 1 (SNU13) is a highly conserved nuclear protein and core component of the [U4/U6.U5] tri-snRNP and box C/D small nucleolar ribonucleoprotein (snoRNP) complexes[1][2][3]. It specifically recognizes and binds a conserved RNA kink-turn motif found in the 5′ stem-loop of U4 small nuclear RNA (snRNA) and box C/D snoRNAs[1][2]. SNU13 acts as a molecular bridge, providing a platform for the association of other core sn/snoRNP proteins including NOP56, NOP58, and fibrillarin, and is critical for assembly of mature snRNPs and snoRNPs[1][2][3]. These complexes are essential for pre-mRNA splicing (especially in spliceosome function) and for site-specific modifications of ribosomal RNA during ribosome biogenesis[1][2][3]. SNU13 interacts with multiple assembly factors and chaperones (like NUFIP1, TIP48, TIP49), which help ensure correct complex formation and stability[1][4]. Structural studies have revealed that SNU13 is well-folded, with conformational flexibility important for precise RNA recognition and nucleation of ribonucleoprotein assemblies[1][2][3]. There are no direct reports of SNU13 being directly implicated as a therapeutic drug target or as a biomarker in human disease.
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