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. 1998 Nov;118(3):1041–1048. doi: 10.1104/pp.118.3.1041

Table II.

Alignment of sites in various proteins involved in the interaction with 14-3-3 proteins

Protein Phospho-Ser Residue Position
−2 0 +2 +4 +6 +8 +10
Raf-1 Ser-259 R S T S T P N V H M V S T T L
Ser-621 R S A S E P S L H R A A H T E
β-Raf-1 Ser-364 R S S S A P N V H I N T I E P
Ser-728 R S A S E P S L N R A G F Q T
PKCβ Ser-241 R R L S V E I W D W D L T S R
Bcr Ser-95  A S A S R P Q P A P A D G A D
Ser-371 R S P S Q N S Q Q S F D S S P
cdc25a Ser-106 R I H S L P Q K L L G C S P A
Ser-191 R D S S E P G N F I P L F T P
cdc25b Ser-216 R P S S A P D L M C L S P D R
Tyr hyd Ser-349 R H A S S P M H S P E P D C C
Trp hyd Ser-260 R H S S D P F Y T P E P D T C
NR Ser-543 R T A S T P F M N T T S K M Y

All amino acids are coded using the standard single-letter codes. The abbreviated protein names are: Raf-1 kinase, Raf-1; β Raf-1 kinase, β-Raf-1; protein kinase C β, PKCβ; Tyr hydroxylase, Tyr hyd; and Trp hydroxylase, Trp hyd. The numbering of a residue position is relative to the phosphorylatable Ser at position 0. Ser and Thr residues that are present C terminal to the phosphorylatable Ser are shown in boldface, underlined type. Note that with one exception, all target proteins contain at least one Ser/Thr residue C terminal to the recognized binding motif (for review, see Aitken, 1996).