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Cloning and sequencing of the human snRNP E protein revealed a 92 amino acid basic protein with regions of similarity to a eukaryotic ribosomal protein.
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The snRNP E protein is one of four "core" proteins associated with the snRNAs of the U family (U1,U2,U4,U5, and U6). Screening of a human teratoma cDNA library with a partial cDNA for a human autoimmune antigen resulted in the isolation of a cDNA clone containing the entire coding region of this snRNP core protein. Comparison of the 5' end of this cDNA with the sequences of two processed pseudogenes and primer extension data suggest that the cDNA is nearly full length. The longest open reading frame in this clone codes for a basic 92 amino acid protein which is in perfect agreement with amino acid sequence data obtained from purified E protein. The predicted sequence of this protein reveals no extensive similarity to other snRNP proteins, but contains regions of similarity to a eukaryotic ribosomal protein.
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Stanford et al. (1988) studied this question. Cloning and sequencing of the human snRNP E protein revealed a 92 amino acid basic protein with regions of similarity to a eukaryotic ribosomal protein.
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