Table 1. Binding affinities of SH2 domains against dephospho- and phospho-ΔN-EphB6.

Proteins tested	KD of ΔN-EphB6	KD of PL-ΔN-EphB6	KD of PH-ΔN-EphB6	pY recognition sequence [65–67]	Full length-protein functions
Abl-SH2	Non-specific binding	45.4 ± 1.3	39.9 ± 1.8	Y-E/A-N(E)-P/V/L	Tyrosine kinase
Vav2-SH2*		19.3 ± 1.8	17.4 ± 2.0	Y-L-X-P	Guanine Exchange Factors (GEFs)
Vav3-SH2		32.2 ± 1.3	25.6 ± 1.0	No data, but high SH2 domain sequence similarity with Vav2-SH2
Nck1-SH2		96.7 ± 6.5	69.0 ± 4.9	Y-D/E-X-V/P	Adaptor proteins
Nck2-SH2		70.2 ± 6.6	52.0 ± 4.0	Y-D/E-X-V/P
CrkII-SH2		42.3 ± 3.4	30.0 ± 1.5	Y-X-X-P Or Y-D-L/V-P
CrkL-SH2		49.9 ± 1.6	44.3 ± 1.2	Y-X-X-P Or Y-D-L/V-P
Grb7-SH2*		26.0 ± 0.8	16.8 ± 0.5	P-Q-P-E-Y-N-Q-P-D
Grb10-SH2*		26.1 ± 0.9	16.6 ± 0.4	No data, but high SH2 domain sequence similarity with Grb7-SH2

Binding affinities, K_D in μM, were calculated by averaging three independent measurements. Errors represent the standard error of the mean (SEM).

^*Indicates proteins exist as dimers in solution.