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The implications of alternative splicing in the ENCODE protein complement

MPG-Autoren
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Albrecht,  Mario
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;

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Assenov,  Yassen
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;
International Max Planck Research School, MPI for Informatics, Max Planck Society;

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Blankenburg,  Hagen
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;
International Max Planck Research School, MPI for Informatics, Max Planck Society;

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Huthmacher,  Carola
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;

Ramírez,  Fidel
Max Planck Society;

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Schlicker,  Andreas
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;

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Lengauer,  Thomas
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;

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Zitation

Tress, M. L., Martelli, P. L., Frankish, A., Reeves, G. A., Wesselink, J. J., Yeats, C., et al. (2007). The implications of alternative splicing in the ENCODE protein complement. Proceedings of the National Academy of Sciences, 104(13), 5495-5500. doi:10.1073/pnas.0700800104.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-000F-20FF-5
Zusammenfassung
Alternative premessenger RNA splicing enables genes to generate more than one gene product. Splicing events that occur within protein coding regions have the potential to alter the biological function of the expressed protein and even to create new protein functions. Alternative splicing has been suggested as one explanation for the discrepancy between the number of human genes and functional complexity. Here, we carry out a detailed study of the alternatively spliced gene products annotated in the ENCODE pilot project. We find that alternative splicing in human genes is more frequent than has commonly been suggested, and we demonstrate that many of the potential alternative gene products will have markedly different structure and function from their constitutively spliced counterparts. For the vast majority of these alternative isoforms, little evidence exists to suggest they have a role as functional proteins, and it seems unlikely that the spectrum of conventional enzymatic or structural functions can be substantially extended through alternative splicing .