SH2 domain-containing adapter protein E (SHE)

SH2 domain-containing adapter protein E (SHE) is an intracellular adapter protein characterized by the presence of an SH2 (Src homology 2) domain, which enables it to bind to phosphorylated tyrosine residues on partner proteins. SHE was initially identified through its interaction with Abelson (ABL) tyrosine kinase. In zebrafish and human endothelial cell studies, SHE functions as a conserved negative regulator of ABL kinase signaling and plays a critical role in controlling blood vessel and lumen size by regulating endothelial cell proliferation. Loss of SHE leads to enlarged vessel lumens, increased cell numbers, and defects in vascular integrity. While essential for vascular development, there is currently no evidence supporting SHE as a direct therapeutic drug target or as a biomarker in clinical practice[5][7].

Other names

Src homology 2 domain containing ESheSHESH2 domain protein E

Not applicable (no drugs targeting SHE; its biological function is as an endogenous inhibitor/negative regulator of ABL kinase signaling)