The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part.
C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins. This subsection of the PTM / Processing section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.
Although P-CIP2 interacts with stathmin, it does not phosphorylate stathmin. Site-directed mutagenesis, phosphoamino acid analysis, and use of synthetic peptides demonstrate that PAM-Ser949 is the major site phosphorylated by P-CIP2. Although P-CIP2 interacts with stathmin, it does not phosphorylate stathmin.