Differential phosphorylation of high mobility group protein hmg 14 from calf thymus and avian erythrocytes by a cyclic gmp-dependent protein kinase.
Phosphorylation of HMG 14 proteins from calf thymus and avian erythrocytes was studied using a cyclic GMP-dependent protein kinase from bovine lung. HMG 14 from calf thymus was a good substrate for the enzyme, but HMG 14 from avian erythrocytes was not phosphorylated. Of the potential phosphorylation sites, the one in the amino terminal sequence Pro-Lys-Arg-Lys-Val-Ser-Ser-Ala-Glu (residues 1-9) is present in HMG 14 from calf thymus but not in HMG 14 from avian erythrocytes suggesting that the phosphorylated amino acid residue in HMG 14 from calf thymus is Ser-6 (and possibly Ser-7).
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002645:Chickens; D002845:Chromatography / Q000379:methods; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D006152:Cyclic GMP / Q000494:pharmacology*; D004912:Erythrocytes / Q000378:metabolism*; D006609:High Mobility Group Proteins; D066298:In Vitro Techniques; D008297:Male; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013950:Thymus Gland / Q000378:metabolism*
D002868:Chromosomal Proteins, Non-Histone; D006609:High Mobility Group Proteins; D011494:Protein Kinases; D006152:Cyclic GMP