Both shc and grb2 contain that bind to the cytoplasmic domain of phosphorylated igf-1r.
a. gtpase domains
b. gip-exchange factors (gefs)
c. gtpase activators
d. sh2 domains
e. raf interaction domains

d. SH2 domains

Explanation:

SHC and GRB2 both play an important role in receptor tyrosine kinase signaling (RTK), the signaling which is related to insulin hormone. SHC and GRB2 are known to contain SH2 domain. Proteins/enzymes which have SH2 domain have very high affinity towards phosphorylated tyrosine residues.

As soon as ligand like insulin binds the insulin-like growth factor 1 receptor (IGF-1R), the receptor forms a dimer and undergoes auto phosphorylation on tyrosine residue. Not only this but also it trans phosphorylates tyrosine residues of other receptors. This hyper phosphorylated receptor then interacts with SH2 domain of SHC and SHC further interacts with SH2 domain of GRB2. Down stream GRB2 activates Ras/Raf to cause gene expression.

true, i don't really know what you're asking but from the info you provided im guessing the answer is true.