Phosphorylation of the high-mobility-group-like protein P1 by casein kinase-2.
The nuclear protein P1 (molecular mass 53 kDa), found in all mammalian cell types and tissues so far tested, is an excellent substrate for casein kinase-2. The number of phosphate groups on P1 is 20-30/molecule; the phosphorylation sites are distributed throughout the molecule. The phosphate is present as serine phosphate and possibly threonine phosphate. Proteolytic digestion with Staphylococcus aureus V8 protease of 32P-labelled P1 both in vivo and in vitro revealed that casein kinase-2 may be one of the kinases responsible for the phosphorylation in vivo.
Maelandsmo
G M
GM
Department of Biochemistry, University of Oslo, Norway.
Ostvold
A C
AC
Laland
S G
SG
D000596:Amino Acids / Q000032:analysis; D047388:Casein Kinases; D006609:High Mobility Group Proteins / Q000378:metabolism; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000502:physiology*; D012269:Ribosomal Proteins
D000596:Amino Acids; D006609:High Mobility Group Proteins; D010750:Phosphoproteins; D012269:Ribosomal Proteins; C035690:ribosomal phosphoprotein P1; D011494:Protein Kinases; D047388:Casein Kinases