SH2 domain-containing adaptor protein B (SHB)

SH2 domain-containing adaptor protein B (SHB) is an adapter protein that regulates multiple cellular signal transduction pathways by linking activated receptors to downstream signaling effectors[1][2][5]. It possesses a carboxy-terminal SH2 (Src Homology 2) domain for binding phosphotyrosine motifs on activated membrane receptors, a central PTB (phosphotyrosine binding) domain, and N-terminal proline-rich motifs facilitating interactions with a range of signaling proteins[1]. SHB is involved in pathways regulating angiogenesis, particularly through modulating FGFR1, VEGFR2, and PDGFR signaling, as well as T-cell receptor and interleukin-2 signaling, neuronal differentiation, and apoptosis[2][5]. It plays a pivotal role in the phosphorylation and activation of downstream effectors such as FRS2, Shp-2, and the Ras/MEK/MAPK pathway, which are critical for cellular proliferation, survival, and differentiation[1]. While SHB interacts functionally with multiple signal pathways relevant to disease—especially cancer and immune system function—there is no current evidence of clinically approved drugs that directly target SHB, nor is it considered a direct therapeutic target or biomarker at present[2][5].

Other names

SHBbA3J10.2SHB (Src homology 2 domain containing) adaptor protein BSHB adaptor proteinSrc homology 2 domain containing adaptor protein B