Nucleophosmin/Npm1 Protein, Mouse (His-SUMO)

Nucleophosmin/Npm1 is a multifunctional protein engaged in various cellular processes, including ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and the regulation of tumor suppressors such as p53/TP53 and ARF. Its involvement in driving ribosome nuclear export is associated with its binding to ribosomes, while it forms complexes with nucleolar ribonucleoprotein structures and binds single-stranded nucleic acids. Acting as a chaperonin for core histones H3, H2B, and H4, Npm1 stimulates APEX1 endonuclease activity on double-stranded DNA but inhibits it on single-stranded RNA. Additionally, it plays a role in controlling APEX1 endonuclease activity within nucleoli, contributing to the repair of apurinic/apyrimidinic sites on rDNA and the removal of oxidized rRNA molecules. Npm1 is implicated in centrosome and centriole duplication, negatively regulating EIF2AK2/PKR activation to suppress apoptosis. Furthermore, it interacts with various proteins, such as MYC, NSUN2, SENP3, and NEK2, highlighting its diverse molecular partnerships and functional versatility. The protein forms a decamer with disulfide-linked dimers under specific conditions and participates in complexes like the SWAP complex, emphasizing its dynamic engagement in cellular processes.