NPM1 (Nucleophosmin 1, B23, nutramin, NO38) is a ubiquitously expressed phosphoprotein involved in ribosome assembly/transport, cytoplasmic/nuclear trafficking, regulation of DNA polymerase alpha activity, centrosome duplication, and regulation of p53. NPM1 continuously shuttles between the nucleus, cytoplasm, nucleolus and chaperoning core histones from the nucleus to the cytoplasm. NPM1 has been shown to bind nucleic acid, prevent protein aggregation via its chaperon activities, protect enzymes during thermal denaturation, and facilitate renaturation of chemically denatured proteins. In its cellular structure role, there is evidence suggesting NPM1 is associated with the centrosome, and is the substrate of CDK2/cyclin E during duplication of centrosomes (cellular division). Due to the NPM1 gene interaction with several tumor-associated chromosome translocations, NPM1 is thought to be a portion of several fusion proteins: NPM-ALK, NPM-RAR, and NPM-MLF1. While it is not thought to be part of the transforming potential of these fusion proteins, NPM1 is believed to act as the interface for oligomerization and oncogenic conversion of these tumor promoting fusion proteins. Further, NPM1 is also known to sequester the tumor suppressor RF in the nucleolus, protecting it from degradation until it is necessary. Dysfunction of the NPM1 protein is associated with diseases such as acute myeloid leukemia and lymphomatoid papulosis.
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Protein Aliases: B23; B23NP; NO38; NPM; Nucleolar phosphoprotein B23; nucleolar protein B23.1; Nucleolar protein NO38; Nucleophosmin; nucleophosmin (nucleolar phosphoprotein B23, numatrin); nucleophosmin 1; nucleophosmin/nucleoplasmin family, member 1; Numatrin; testicular tissue protein Li 128
Gene Aliases: B23; B23NP; NO38; NPM; NPM1