Pub. Date : 1996 Oct 11
PMID : 8898866
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The annexin II-p11 interaction is mediated through the unique N-terminal domain of annexin II and is inhibited by protein kinase C phosphorylation of a serine residue in annexin II. | Serine | annexin A2 | Homo sapiens |
| 2 | To map this regulatory serine phosphorylation site we developed a baculovirus-mediated expression system for wild-type annexin II and for a series of annexin II mutants which contained substitutions in one or more serine residues present in the N-terminal domain. | Serine | annexin A2 | Homo sapiens |
| 3 | To map this regulatory serine phosphorylation site we developed a baculovirus-mediated expression system for wild-type annexin II and for a series of annexin II mutants which contained substitutions in one or more serine residues present in the N-terminal domain. | Serine | annexin A2 | Homo sapiens |
| 4 | However, significant differences in phosphate incorporation were observed when the individual serine mutants were subjected to phosphorylation by protein kinase C. A comparison of the phosphorylation patterns obtained identified Ser-II as the protein kinase C site responsible for regulating the annexin II-p11 interaction. | Serine | annexin A2 | Homo sapiens |
| 5 | Ser-II lies within the sequence mediating p11 binding, i.e. amino-acid residues 1 to 14 of annexin II, and phosphorylation at this site most likely leads to a direct spatial interference with p11 binding. | Serine | annexin A2 | Homo sapiens |