Evidence for a highly specific protein kinase phosphorylating two strongly acidic proteins of yeast 60 S ribosomal subunit.
Two distinct, cyclic AMP-independent protein kinase (ATP : protein photransferase, EC 2.7.1.37) from yeast have been isolated and highly purified. The first of the enzymes, protein kinase 1 A, phosphorylates casein and phosvitin, and its cellular protein substrate is unknown. The second enzyme, protein kinase 1 B, phosphorylates two strongly acidic proteins, L44 and L45, of the 60 S ribosomal subunit.
D000255:Adenosine Triphosphate / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D010766:Phosphorylation; D011494:Protein Kinases / Q000145:classification / Q000378:metabolism*; D000090822:Ribosomal Protein L3; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D013379:Substrate Specificity
D000090822:Ribosomal Protein L3; D012269:Ribosomal Proteins; C029466:ribosomal protein L2; D000255:Adenosine Triphosphate; D011494:Protein Kinases; D008274:Magnesium