The HumanHNRPDLocus Maps to 4q21 and Encodes a Highly Conserved Protein |
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Authors: | Laurie A. Dempsey Ming-jie Li Angela DePace Patricia Bray-Ward Nancy Maizels |
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Affiliation: | aDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 266 Whitney Avenue, New Haven, Connecticut, 06520-8114;bDepartment of Genetics, Yale University School of Medicine, 266 Whitney Avenue, New Haven, Connecticut, 06520-8114 |
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Abstract: | The hnRNP D protein interacts with nucleic acids bothin vivoandin vitro.Like many other proteins that interact with RNA, it contains RBD (or “RRM”) domains and arg-gly-gly (RGG) motifs. We have examined the organization and localization of the human and murine genes that encode the hnRNP D protein. Comparison of the predicted sequences of the hnRNP D proteins in human and mouse shows that they are 96.9% identical (98.9% similar). This very high level of conservation suggests a critical function for hnRNP D. Sequence analysis of the humanHNRPDgene shows that the protein is encoded by eight exons and that two additional exons specify sequences in the 3′ UTR. Use of two of the coding exons is determined by alternative splicing of theHNRPDmRNA. The humanHNRPDgene maps to 4q21. The mouseHnrpdgene maps to the F region of chromosome 3, which is syntenic with the human 4q21 region. |
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