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The spliceosome is a complex piece of machinery responsible for catalyzing the removal of pre-mRNA introns before the material is shipped out of the nucleus to be translated into protein. This large catalytic complex is composed of 5 snRNAs (U1, U2, U4, U5 and U6) and many other protein factors including Prp8. Prp8 is the only know protein of the spliceosome that makes contact with all its critical catalytic components (U5 and U6 snRNAs, 5’-ss, 3’-ss, and BP)<ref name="Galej5">Galej, Wojciech P, Andrew J. Newman, Thi Hoang Duong Nguyen, Nagai Kiyoshi. "Structural Studies of the Spliceosome: Zooming into the Heart of the Machine." Current Opinion In Structural Biology 25.Theory and simulation / Macromolecular</ref>. Studies have show that through these cross-links, Prp8 is able to regulate the equilibrium between two important catalytic steps of the splicing process<ref name="Yang2008">Yang, Kui, Annie Xeroux, Lingdi Zhang, Rui Zhao, and Tao Xu. "Crystal Structure of the β-Finger Domain of Prp8 Reveals Analogy to Ribosomal Proteins." Proceedings of the National Academy of Sciences of the United States of America 2008: 13817. JSTOR Journals. Web. 13 Apr. 2015. </ref>. This function is carried out by the B-finger domain, which resembles many features of ribosomal stabilizing structures and RNase H folds in DNA repair enzymes<ref name="Yang2008" />.  

The human Prp8 protein is 2,335 residues in length and yeast Prp8 is 2,413 residues<ref name="Yang2008" />. These two proteins share 61 percent of their amino acid sequence, emphasizing the evolutionary conservation of the Prp8 protein throughout many species<ref name="Galej5" />. Mutations throughout the structure of the Prp8 have shown the importance of the protein, which is found throughout all tissue types, but at higher levels in cardiac and skeletal muscles<ref name="Galej5" />.