{'fraction_non_alphanumeric': 0.02112676056338028, 'fraction_numerical': 0.02112676056338028, 'mean_word_length': 5.1419753086419755, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Human ribosomal protein L18a interacts with hnRNP E1

Abstract Heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) is one of the primary pre‐mRNA binding proteins in human cells. It consists of 356 amino acid residues and harbors three hnRNP K homology (KH) domains that mediate RNA‐binding. The hnRNP E1 protein was shown to play important roles in mRNA stabilization and translational control. In order to enhance our understanding of the cellular functions of hnRNP E1, we searched for interacting proteins through a yeast two‐hybrid screening while using HeLa cDNA library as target. One of the cDNA clones was found to be human ribosomal protein L18a cDNA (GenBank accession number BC071920). We demonstrated in this study that human ribosomal protein L18a, a constituent of ribosomal protein large subunit, interacts specifically with hnRNP E1 in the yeast two‐hybrid system. Such an interaction was observed for the first time in this study, and was also verified by biochemical assay.