The major phosphorylation site of nucleophosmin (B23) is phosphorylated by a nuclear kinase II

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Abstract
Nucleophosmin (B23) was phosphorylated in vitro with [gamma-32P]ATP and a nuclear kinase (type II) purified from HeLa cells. The phosphorylation was inhibited by heparin and by 2,3-diphosphoglycerate. Peptide mapping analysis indicated that the phosphorylation site in vitro was identical to that in vivo. Purified nucleoli have a similar kinase that phosphorylated nucleophosmin at the same site. These results indicated that nucleophosmin is phosphorylated in vivo by a nucleolar kinase (type II).