BCR activation is highly regulated and coreceptors like CD22 (SIGLEC2) set a signalling threshold to prevent aberrant immune response and autoimmune disease (Cyster et al. 1997, Han et al. 2005). CD22 is a glycoprotein found on the surface of B cells during restricted stages of development. CD22 is a member of the receptors of the sialic acid-binding Ig-like lectin (Siglec) family which binds specifically to the terminal sequence N-acetylneuraminic acid alpha(2-6) galactose (NeuAc-alpha(2-6)-Gal) present on many B-cell glycoproteins (Powell et al. 1993, Sgroi et al. 1993). CD22 has seven immunoglobulin (Ig)-like extracellular domains and a cytoplasmic tail containing six tyrosines, three of which belong to the inhibitory immunoreceptor tyrosine-based inhibition motifs (ITIMs) sequences. Upon BCR cross-linking CD22 is rapidly tyrosine phosphorylated by the tyrosine kinase Lyn, thereby recruiting and activating tyrosine phosphatase, SHP-1 and inhibiting calcium signalling

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CD22 , CD79A , CD79B , IGLC1 , IGLC6 , LYN , PTPN6 , IGKV3D-11 , IGKV5-2 , IGKV4-1 , MIR5196 ,