Journal
JOURNAL OF PROTEOME RESEARCH
Volume 3, Issue 1, Pages 76-83Publisher
AMER CHEMICAL SOC
DOI: 10.1021/pr034064v
Keywords
alternative splicing; human proteome; protein interaction domains; bioinformatics
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Funding
- NATIONAL INSTITUTE OF MENTAL HEALTH [P20MH065166] Funding Source: NIH RePORTER
- NIMH NIH HHS [MH65166] Funding Source: Medline
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We have constructed a database of alternatively spliced protein forms (ASP), consisting of 13 384 protein isoform sequences of 4422 human genes (www.bioinformatics.ucla.edu/ASP). We identified fifty protein domain types that were selectively removed by alternative splicing at much higher frequencies than average (p-value < 0.01). These include many well-known protein-interaction domains (e.g., KRAB; ankyrin repeats; Kelch) including some that have been previously shown to be regulated functionally by alternative splicing (e.g., collagen domain). We present a number of novel examples (Kruppel transcription factors; Pbx2; Enc1) from the ASP database, illustrating how this pattern of alternative splicing changes the structure of a biological pathway, by redirecting protein interaction networks at key switch points. Our bioinformatics analysis indicates that a major impact of alternative splicing is removal of protein-protein interaction domains that mediate key linkages in protein interaction networks. ASP expands the available dataset of human alternatively spliced protein forms from 1989 human genes (SwissProt release 42) to 5413 (nonredundant set, ASP + SwissProt), a nearly 3-fold increase. ASP will enhance the existing pool of protein sequences that are searched by mass spectroscopy software during the identification of peptide fragments.
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