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Investigating protein isoforms via proteomics: A feasibility study by Paul Blakeley; Jennifer A. Siepen; Craig Lawless; Simon J. Hubbard is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Alternative splicing (AS) and processing of pre‐messenger RNAs explains the discrepancy between the number of genes and proteome complexity in multicellular eukaryotic organisms. However, relatively few alternative protein isoforms have been experimentally identified, particularly at the protein level. In this study, we assess the ability of proteomics to inform on differently spliced protein isoforms in human and four other model eukaryotes. The number of Ensembl‐annotated genes for which proteomic data exists that informs on AS exceeds 33% of the alternately spliced genes in the human and worm genomes. Examining AS in chicken __via__ proteomics for the first time, we find support for over 600 AS genes. However, although peptide identifications support only a small fraction of alternative protein isoforms that are annotated in Ensembl, many more variants are amenable to proteomic identification. There remains a sizeable gap between these existing identifications (10–52% of AS genes) and those that are theoretically feasible (90–99%). We also compare annotations between Swiss‐Prot and Ensembl, recommending use of both to maximize coverage of AS. We propose that targeted

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It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Paul Blakeley; Jennifer A. Siepen; Craig Lawless; Simon J. Hubbard
Publisher
John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley; Research Square (ISSN 1615-9853)
Published
2010
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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