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The kinship of NPM3 and NO29 is supported by recent GenBank screens with the NPM3 amino acid sequence as a TBLASTN query against the entire nonredundant GenBank database, which resulted in NO29 sequences as the best non-NPM3 match, and vice versa.
Multiple phosphorylation sites and nuclear localization signals, or the ability to bind proteins with such signals, are also characteristics of nucleophosmin and nucleoplasmin [ 16 27 28 29 ] . When the functions of NPM3 are elucidated, it will be of interest to determine the contribution of phosphorylation to these activities, since the functions of both nucleoplasmin and nucleophosmin are regulated by phosphorylation, which is extensive in both proteins [ 7 17 ] ).
The striking similarities in amino acid sequence and domain structure between NPM3 and its chaperone relatives, nucleophosmin and nucleoplasmin, together with abundant expression levels and nuclear localization, strongly suggests that NPM3 shares fundamental nuclear chaperone functions with these proteins.
Supporting this notion, the in vitro transcription/translation of a plasmid encoding the closely related NO29 protein produces a product, presumably unmodified, with slow mobility that is similar to the mobility of NO29 extracted from cells [ 43 ] . The smaller-sized polypeptide of the NPM3 doublet is probably a degradation product, as is observed in analyses of the NO29 protein [ 43 ] . This subcellular localization of NPM3, together with the other results here, suggests that this protein is a molecular chaperone with functions in the nucleus.
Although other genomic and functional studies would be required to prove an orthologous relationship between NPM3 and NO29, they appear by several analyses to share a relatively close evolutionary history and as such could be considered candidate orthologs.
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