Table 3.

Protein SH2 or PTB domains interacting with pTyr sites in ERBB3 with high affinity (dissociation constants <1000 nm*, <500 nm**, <100 nm***)

Domain source	pY868	pY1054	pY1197	pY1222	pY1260	pY1260–62	pY1276	pY1289	pY1328
PI3KR1 N		*	*		**		*	**
PI3KR1 C		*						***
PI3KR1 NC		**	**	**	***	*	***	***
PI3KR2 N		*	**		**	**	**	***
PI3KR2 C							*
PI3KR2 NC		***	**	**	***	*	***	***
PI3KR3 N		*	**	*	**		**	***
PI3KR3 C		**		**	**		**	***
PI3KR3 NC		***	*	***	**	***	***	***
ABL1								*
ABL2	***	**		**	**		**	***	*
RASA1N	*		*	*	*		*
GRB7			***		*		*
SYK NC	*			*			*
HCK							*	**
PLCG1 C							*	**
PLCG1 NC							*	**
SHC1							*	*
SHC3							*	**
CRK							**
NCK1							**
NCK2							*
CRKL							**
JAK2							*
VAV2							**
VAV1								**
SRC								*
TENS1								*
DAPP1								*
FER								**
ITK								**
LYN								**
PTK6							**
TENC1				*
SHC1-PTB									**

Data summarized from Jones et al.,¹³³ Supplementary Table 4. Lower affinity interactions detected in the study may also be seen in this Table. For proteins with two SH2 domains, these were tested separately (N, C) or together (NC).