EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.11.11 | lipoprotein |
irreversible covalent N-myristylation of PKA or occupancy of the myristyl binding pocket may serve as a site for allosteric regulation in the catalytic C-subunit. And N-myristylation enhances the thermal stability of the enzyme, the myristylated C-subunit has a higher affinity for membranes alone. PKA cannot be myristylated if Asn2 is mutated to Asp |
722989 |
| 2.7.11.11 | lipoprotein |
isozyme C1 cotains a consensus sequence for N-myristoylation |
675873 |
| 2.7.11.11 | more |
the C-subunit of PKA may be regulated by irreversible deamidation of Asn2. With PKA that is purified from tissues, irreversible deamidation of Asn2 to Asp or isoAsp occurs in about 1/3 of the total C-subunit protein. Also, the deamidated form of the protein has a higher cytosolic-to-nuclear ratio than the non-deamidated protein |
722989 |
| 2.7.11.11 | more |
unmyristylated Calpha2 may be essential for fertility in the male |
490981 |
| 2.7.11.11 | phosphoprotein |
activation loop phosphorylation at Thr197 regulates the enzyme's catalytic activity, molecular mechanism, classical molecular dynamics simulations and ab initio QM/MM calculations are carried out on the wild-type PKA-Mg2+- ATP-substrate complex and its dephosphorylated mutant, T197A, overview |
677019 |
| 2.7.11.11 | phosphoprotein |
analysis of in vivo phosphorylation sites on PKA-R reveals the presence of several differentially phosphorylated PKA-R isoforms, using semiquantitative mass spectrometry, overview |
-, 675671 |
| 2.7.11.11 | phosphoprotein |
autophosphorylation at Ser10, Ser139, Thr197, and Ser338 |
661759 |
| 2.7.11.11 | phosphoprotein |
autophosphorylation at Thr197 required for activation |
490800 |
| 2.7.11.11 | phosphoprotein |
autophosphorylation of PKA catalytic subunit is necessary for its enzymatic activation and interaction with PKA regulatory subunits |
723534 |
| 2.7.11.11 | phosphoprotein |
phosphate groups at Thr196 and Ser337 |
490958 |
