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SCIMP protein : ウィキペディア英語版 | SCIMP protein thumbnail == Preface, Structure and interactions ==
SLP65/SLP76, Csk-interacting membrane protein, termed SCIMP, belongs to family of transmembrane adaptor proteins (TRAP) which do not directly associate with a receptor, such as LAT, NTAL, LIME or LAX. SCIMP is expressed in antigen presenting cells (APC), namely B cells, bone marrow derived dendritic cells and macrophages. Like other TRAPs, SCIMP has negligible extracellular domain and transmembrane domain followed by intracellular domain, containing several tyrosines and one proline rich region (PRR). Upon phosphorylation, these tyrosines serve as docking domains for SH2 domains containing proteins. In a contrast to phospho-tyrosines, proline rich regions are generally less susceptible to post-translation modifications and they are rather targets of constitutive interactions with SH3 domains containing proteins. It has been shown that SCIMP interact via SH2 domains with Csk kinase, negative regulator of Src family kinases, but also with Slp65/76 and Grb2 adaptors, which are key pro-signalling soluble adaptor proteins in lymphocyte signalling network. SCIMP is constitutively associated with Lyn kinase via SH3 domain.
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