EC Number   |
Posttranslational Modification |
Reference |
|---|
    2.4.1.1 | glycoprotein |
each subunit has two distinct maltooligosaccharide binding sites: a storage site and a catalytic site |
736378 |
| 2.4.1.1 | phosphoprotein |
cyclin-dependent protein kinase Pho85p controls the phosphorylation state of phosphorylase and thus its activity |
671691 |
| 2.4.1.1 | phosphoprotein |
glycogen phosphorylase a is prepared from glycogen phosphorylase b by phosphorylation through a truncated form of the catalytic subunit of rabbit skeletal muscle phosphorylase kinase |
736109 |
| 2.4.1.1 | phosphoprotein |
phosphorylation and dephosphorylation of the enzyme regulates its activity and is catalyzed by a phosphorylase phosphatase |
658716 |
| 2.4.1.1 | phosphoprotein |
phosphorylation and dephosphorylation of the enzyme regulates its activity and is catalyzed by a phosphorylase phosphatase and protein kinase A |
660037 |
| 2.4.1.1 | phosphoprotein |
the glycogen phosphorylase dimer can exist in either in unphosphorylated glycogen phosphorylase b or phosphorylated glycogen phosphorylase a form depending on hormonal activation of kinase/phosphatase reactions |
720110 |
| 2.4.1.1 | phosphoprotein |
the muscle isoform of phosphorylase is activated by phosphorylation (GPb to GPa conversion) |
736773 |
| 2.4.1.1 | proteolytic modification |
- |
676520 |
| 2.4.1.1 | proteolytic modification |
cleavage of a 55 amino acid transit peptide |
676520 |
| 2.4.1.1 | proteolytic modification |
sequence predicts a transit peptide |
705365 |
