Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/8512
Title: The construction of a bioactive peptide database in Metazoa
Authors: LIU, Feng 
Baggerman, G.
Schoofs, L.
WETS, Geert 
Issue Date: 2008
Publisher: AMER CHEMICAL SOC
Source: JOURNAL OF PROTEOME RESEARCH, 7(9). p. 4119-4131
Abstract: Bioactive peptides play critical roles in regulating most biological processes in animals, and have considerable biological, medical and industrial importance. A number of peptides have been discovered usually based on their biological activities in vitro or based on their sequence similarities in silico. Through searches in Swiss-Prot and Trembl protein databases using BLAST alignment tools and other in silico methods, all currently known bioactive peptides and their precursor proteins are extracted. In addition, 132 recently discovered putative peptide genes in Drosophila as well as their orthologs in other species are collected. In total, 20 027 bioactive peptides from 19 438 precursor proteins covering 2820 metazoan species are retained, and they, respectively, make up a peptide and a peptide precursor database. The peptides and peptide precursor proteins are further classified into 373 families, 178 of which are represented by Prosite Pfam or Smart motifs, or by typical peptide motifs that have been constructed recently. The remaining 195 families are novel peptide families. The motifs characterizing the 178 peptide families are saved into a peptide motif database. The peptide, peptide precursor and peptide motif databases (version 1.0) are the most complete peptide, precursor and peptide motif collection in Metazoa so far. They are available on the WWW at http://www.peptides.be/.
Notes: Katholieke Univ Leuven, ProMeta, Interfac Ctr Prote & Metab, B-3000 Louvain, Belgium. Hasselt Univ, Data Anal & Modeling Grp, Transportat Res Inst, B-3590 Diepenbeek, Belgium. Lab Funct Genom & Prote, Louvain, Belgium.
Keywords: peptide; peptide precursor; motif; Prosite; Pfam; Smart; BLAST
Document URI: http://hdl.handle.net/1942/8512
ISSN: 1535-3893
e-ISSN: 1535-3907
ISI #: 000259015500047
Category: A1
Type: Journal Contribution
Validations: ecoom 2009
Appears in Collections:Research publications

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