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SF1 Phosphorylation Enhances Specific Binding to U2AF(65) and Reduces Binding to 3'-Splice-Site RNA
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A novel function of SF1 in the initial recruitment of the U2 snRNP through direct interactions with two U2 snRNP-associated proteins.
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Data suggest that post-translational processing of SF1 (phosphorylation of Ser20) down-regulates nuclear import of SF1 via alterations in kinetic interaction of SF1 nuclear localization signal (NLS) with NLS receptor isoforms.
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We demonstrated that PRPF40B interacts directly with SF1 and associates with U2AF(65
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Gomafu indirectly modulates the function of the splicing factors SF1 and Celf3 by sequestering these proteins into separate nuclear bodies.
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The conserved SPSP motif phosphorylation and the SF1/U2AF interface are essential in vivo.
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Findings suggest that Zinc finger motif-1 (ZFM1) is an important factor for the stabilization of a contractile SMC phenotype under basal or mildly activating conditions.
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central ;mystery' domain of SF1 crystals belonged to space group C2 and have most probable solvent contents of 64, 52 or 39% with three, four or five molecules per asymmetric unit, respectively
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SF1 silencing affected alternative splicing of endogenous transcripts, establishing a previously unexpected role for SF1 and branch site-like sequences in splice site selection.
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the conformational changes that are induced by assembly of the SF1/U2AF(65)/RNA complex serve to position the pre-mRNA splice site optimally for subsequent stages of splicing.
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SF3a60, 66, and 120, but not SF1, are essential for pre-mRNA splicing
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SF1 was essential for the induction of alternative mRNA splicing by the beta-catenin/TCF4 complex.
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SF1 and U2AF form extraspliceosomal complexes before and after taking part in the assembly of catalytic spliceosomes.
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Puf60-UHM binds to ULM sequences in the splicing factors SF1, U2AF65, and SF3b155.
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The KH-QUA2 region of SF1 defines an enlarged KH (hn RNP K) fold which is necessary and sufficient for intron branched point sequence (BPS) binding.