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. 2009 Jul 29;284(42):29193–29204. doi: 10.1074/jbc.M109.036632

FIGURE 2.

FIGURE 2.

Blom7α-specific C terminus and self-interaction domain of SNEVPrp19-Pso4 are necessary for interaction. A, C-terminal half of amino acid 347–614 were isolated from the human aorta cDNA library. B, Blom7α deletion mutants identify the α-specific C terminus as necessary for the interaction, whereas on the side of SNEVPrp19-Pso4. C, the self-interaction domain is necessary as determined by directed yeast two-hybrid analyses under high stringent conditions. U-box, UFD2-like motif with E3 ligase activity. SID, self-interaction domain; LCR, low complexity region; CC, coiled-coil domain, GL2, globular domain; LCR1, low complexity region APG-rich; KH1, -2, KH domain (RNA binding domain); LCR2, low complexity region PS-rich; α, α-specific C terminus; β, β-specific C terminus; γ, γ-specific C terminus.