Fig. 4. Multiple sequence alignment of the amino acid sequences of Fundulus heteroclitus 14-3-3.a (in bold) and all seven isoforms of 14-3-3 from mammals (Mus musculus). Amino acid residues that are identical in all the 14-3-3 proteins are shown on gray background. The locations of helices 3, 5, 7 and 9 are indicated by black bars above the corresponding residues. These regions, which form the amphipathic substrate binding groove, are highly conserved in their amino acid sequence. Important domains are indicated by colored background: blue, protein kinase C phosphorylation site; purple, casein kinase II phosphorylation site; green, protein kinase A phosphorylation site; orange, tyrosine kinase phosphorylation site; yellow, Asn glycosylation site. Please note that the corresponding residues are colored in the 14-3-3ß sequence when two sites utilize the same residues in the 14-3-3.a sequence.
