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ABCMdb: A database for the comparative analysis of protein mutations in ABC transporters, and a potential framework for a general application
Author(s) -
Gyimesi Gergely,
Borsodi Dávid,
Sarankó Hajnalka,
Tordai Hedvig,
Sarkadi Balázs,
Hegedűs Tamás
Publication year - 2012
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.22138
Subject(s) - biology , genetics , atp binding cassette transporter , computational biology , uniprot , hum , mutation , omim : online mendelian inheritance in man , mutant , database , gene , phenotype , transporter , computer science , art , performance art , art history
To overcome the pathological phenomena caused by altered function of ABC (ATP Binding Cassette) proteins, their mechanisms of action are extensively investigated, often involving the design of mutant constructs for experiments. Designing mutagenetic constructs, interpreting the result of mutagenetic experiments, and finding individual genetic variants require an extensive knowledge of previously published mutations. To aid the recapitulation of mutations described in the literature, we set up a database of ABC protein mutations (ABCMdb) extracted from full‐text papers using an automatic mining approach. We have also developed a Web application interface to compare mutations in different ABC proteins using sequence alignments and to interactively map the mutations to 3D structural models. Currently our database contains protein mutations published for ABCB1, ABCB11, ABCC1, ABCC6, ABCC7, and the proteins of the ABCG subfamily. The database will be extended to include other members and subfamilies, and to provide information on whether or not a mutation is disease causing, represents a high‐incidence polymorphism, or was generated only in vitro. The ABCMdb database should already help to compare the effects of mutations at homologous positions in different ABC proteins, and its interactive tools aim to advance the design of experiments for a wider range of proteins. Hum Mutat 33:1547–1556, 2012. © 2012 Wiley Periodicals, Inc.