The 53-aa peptide competitively binds to the arginine residue in the RGG motif of the splicing factor hnRNPA1 and blocks the binding of hnRNPA1 to the PKM pre-mRNA, thereby inhibiting the cleavage of PKM exon 9, resulting in the reduced synthesis of PKM2, an isoenzyme of glycolytic pyruvate kinase, thereby inhibiting the reprogramming of glucose metabolism and ultimately inhibiting the growth of CRC [52] (Fig. 4a). This evidence concerns the gene HNRNPA1 and colorectal carcinoma.