title: Increase of functional diversity by alternative splicing.
abstract: A large-scale analysis of protein isoforms arising from alternative splicing shows that alternative splicing tends to insert or delete complete protein domains more frequently than expected by chance, whereas disruption of domains and other structural modules is less frequent. If domain regions are disrupted, the functional effect, as predicted from 3D structure, is frequently equivalent to removal of the entire domain. Also, short alternative splicing events within domains, which might preserve folded structure, target functional residues more frequently than expected. Thus, it seems that positive selection has had a major role in the evolution of alternative splicing.
authors.affiliation: European Bioinformatics Institute (EMBL-EBI), Hinxton Wellcome Trust Genome Campus, Hinxton, Cambridge, UK CB10 1SD.
authors.forename: Evgenia V
authors.initials: EV
authors.lastname: Kriventseva
authors.forename: Ina
authors.initials: I
authors.lastname: Koch
authors.forename: Rolf
authors.initials: R
authors.lastname: Apweiler
authors.forename: Martin
authors.initials: M
authors.lastname: Vingron
authors.forename: Peer
authors.initials: P
authors.lastname: Bork
authors.forename: Mikhail S
authors.initials: MS
authors.lastname: Gelfand
authors.forename: Shamil
authors.initials: S
authors.lastname: Sunyaev
mesh_terms: D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D019295:Computational Biology; D030562:Databases, Protein; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D020033:Protein Isoforms / Q000032:analysis* / Q000737:chemistry; D017434:Protein Structure, Tertiary; D012641:Selection, Genetic
chemical_list: D000596:Amino Acids; D008024:Ligands; D020033:Protein Isoforms