Takio K, Smith S B, Walsh K A, Krebs E G, Titani K
J Biol Chem. 1983 May 10;258(9):5531-6.
An exposed "hinge" region of cGMP-dependent protein kinase is known to be susceptible to both limited proteolysis and autophosphorylation. A 91-residue fragment has been isolated from this region and its amino acid sequence has been compared with the analogous regions of the cAMP-dependent protein kinases. Although a resemblance among these sequences is not striking, the phosphorylation sites are in corresponding regions toward the NH2 termini, and there are indications of homology in the vicinity of their autophosphorylation sites. As in the cAMP-dependent protein kinase, the site of autophosphorylation and the site of susceptibility to limited proteolysis are very near each other in the primary structure. The actual site of autophosphorylation (the underlined threonine residue in Pro-Arg-Thr-Thr-Arg) is quite different from those in the regulatory subunit of Type II cAMP-dependent kinase or the site in Type I regulatory subunit that can be phosphorylated by the cGMP-dependent protein kinase.
已知环磷酸鸟苷依赖性蛋白激酶的一个暴露“铰链”区域易受有限蛋白酶解和自身磷酸化作用的影响。已从该区域分离出一个91个残基的片段，并将其氨基酸序列与环磷酸腺苷依赖性蛋白激酶的类似区域进行了比较。尽管这些序列之间的相似性并不显著，但磷酸化位点位于靠近氨基末端的相应区域，并且在其自身磷酸化位点附近有同源性的迹象。与环磷酸腺苷依赖性蛋白激酶一样，自身磷酸化位点和对有限蛋白酶解敏感的位点在一级结构中彼此非常接近。自身磷酸化的实际位点（脯氨酸 - 精氨酸 - 苏氨酸 - 苏氨酸 - 精氨酸中带下划线的苏氨酸残基）与II型环磷酸腺苷依赖性激酶调节亚基中的位点或I型调节亚基中可被环磷酸鸟苷依赖性蛋白激酶磷酸化的位点有很大不同。
