Phosphopeptides identified harboring minimal 14-3-3 binding motifs Phosphopeptides identified harboring minimal 14-3-3 binding motifs. 14-3-3 proteins employ two modes of binding to phosphoproteins based on primary amino acid sequence surrounding a phosphoserine residue. Phosphopeptides identified harboring minimal 14-3-3 binding motifs. 14-3-3 proteins employ two modes of binding to phosphoproteins based on primary amino acid sequence surrounding a phosphoserine residue. A, phosphopeptides identified containing minimal binding motifs for 14-3-3 family members. B and D, potential 14-3-3 binding sites found in CrkL, Epsin 2 and UBPY show different degrees of conservation relative to surrounding amino acids found in orthologous proteins from other members of the animal kingdom. Similar alignments for all other potential 14-3-3 binding sites identified are presented in Supplemental Fig. 2. Motif residues are in bold with the identified phosphorylated serine residue in lowercase. Asterisks indicate the sequence was identified from the translated EST database. Bryan A. Ballif et al. Mol Cell Proteomics 2004;3:1093-1101 © 2004 The American Society for Biochemistry and Molecular Biology