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. 1990 Sep 1;270(2):549–552. doi: 10.1042/bj2700549

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

P K Chan 1, Q R Liu 1, E Durban 1
PMCID: PMC1131759  PMID: 2400401

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).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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