HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by the serine-threonine kinase CK2.
The HIRIP3 protein had been identified from its interaction with the HIRA histone chaperone. Experiments using anti-peptide antisera indicated that this 556-aa protein is nuclear throughout the cell cycle and excluded from condensed chromatin during mitosis. Based on its electrophoretic migration and sensitivity to phosphatase treatment, endogenous HIRIP3 was found ... to be heavily phosphorylated. HIRIP3 can be phosphorylated in vitro by a recombinant form of the serine-threonine kinase CK2. Moreover, HIRIP3 protein was found to co-purify with a CK2 activity. Together, these data prompt us to propose HIRIP3 as a new member of the growing list of CK2 substrates with a possible role in chromatin metabolism.
Mesh Terms:
Amino Acid Sequence, Animals, Carrier Proteins, Casein Kinase II, DNA, Complementary, Hela Cells, Humans, K562 Cells, Molecular Sequence Data, Nuclear Proteins, Phosphorylation, Protein Interaction Mapping, Rabbits, Two-Hybrid System Techniques
Amino Acid Sequence, Animals, Carrier Proteins, Casein Kinase II, DNA, Complementary, Hela Cells, Humans, K562 Cells, Molecular Sequence Data, Nuclear Proteins, Phosphorylation, Protein Interaction Mapping, Rabbits, Two-Hybrid System Techniques
Biol. Chem.
Date: Apr. 01, 2007
PubMed ID: 17391060
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