title: Possible relationship between coding recognition amino acid sequence motif or residue(s) and post-translational chemical modification of proteins.
abstract: 1. The "code-sequence" of N-glycosylation site(s), the amino acids located around O-glycosylation site(s), the sequence motifs of several kinases, the sequence motifs of--sulfation, amidation, isoprenylation, myristoylation, palmitoylation and N-acetylation, Aspartic and Asparagine hydroxylation-site, gamma-carboxyglutamate domain, phosphopantetheine attachment site etc. are extensively listed, compared to those reported by "PROSITE" Computer Screen Center and discussed. 2. The structural aspects of protein-DNA recognition are quoted as discussion and conclusion.
authors.affiliation: Unité INSERM N. 16, Lille, France.
authors.forename: K K
authors.initials: KK
authors.lastname: Han
authors.forename: A
authors.initials: A
authors.lastname: Martinage
mesh_terms: D000107:Acetylation; D000215:Acylation; D000595:Amino Acid Sequence; D000818:Animals; D006031:Glycosylation; D006801:Humans; D006900:Hydroxylation; D008969:Molecular Sequence Data; D010204:Pantetheine / Q000031:analogs & derivatives / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D010204:Pantetheine; D011494:Protein Kinases; C003129:4'-phosphopantetheine