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Fig. 1 | Thrombosis Journal

Fig. 1

From: The adaptor protein Disabled-2: new insights into platelet biology and integrin signaling

Fig. 1

Schematic illustration for the primary protein structure of Dab2. The primary structures for both Dab2 isoforms p82 (p96) and p59 (p67) are shown. The p59 (p67) isoform of Dab2 lacks the ninth coding exon corresponding to the amino acid residues of 230–447 and results in the deletion of several binding sites for endocytic proteins. The N-terminus of Dab2 contains an actin-binding motif (25KKEK28), two sulfatide binding sites (amino acid residues 24–32 and 49–54), an RGD motif (64RGD66), one thrombin cleavage site (64R) and the PTB domain (amino acid residues 45–196). Dab2-PTB is the binding sites for PI(4,5)P2 and the tails of a subset of non-tyrosine-phosphorylated NPXY-containing receptors. The clathrin type I (236LVDLN240) and type II (363PWPFS367) box sequences, and the two DPF motifs (293DPFRDDPF300) are located at the middle region of Dab2 protein. The DPF motifs bind to the α-adaptin subunit of the clathrin adaptor protein AP-2. The five asparagine-proline-phenylalanine (NPF) motifs spanning the middle and C-terminus of Dab2 possibly bind proteins containing Eps homology domain. The C-terminus of Dab2 contains the myosin VI binding domain and the PRD for the binding of proteins containing SH3 domain

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