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SH2 domain-containing adapter protein F (SHF) is an adaptor protein with a Src homology 2 (SH2) domain. It is involved in modulating signal transduction pathways, particularly those initiated by receptor tyrosine kinases such as ALK (anaplastic lymphoma kinase). SHF contains four putative tyrosine phosphorylation sites and plays a negative regulatory role in pathways such as those driven by ALK in neuroblastoma, as well as in platelet-derived growth factor (PDGF) signaling[1][4][5]. Overexpression of SHF is linked to decreased apoptosis and reduced tumor invasiveness, while downregulation promotes cell growth and mobility in neuroblastoma, suggesting its function as a tumor suppressor or negative regulator in certain cancer contexts[1]. SHF does not have direct known drug interactors and is not currently an established therapeutic target. It is classified as a scaffold/adaptor molecule rather than a receptor, enzyme, or channel[1][4][5].
Not applicable (no drug interactions documented)
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