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CPLA 1.0: an integrated database of protein lysine acetylation

Author:
Liu, Zexian, Cao, Jun, Gao, Xinjiao, Zhou, Yanhong, Wen, Longping, Yang, Xiangjiao, Yao, Xuebiao, Ren, Jian, Xue, Yu
Source:
Nucleic acids research 2011 v.39 no.suppl_1 pp. D1029
ISSN:
0305-1048
Subject:
acetylation, acetyltransferases, computer software, gene ontology, histone deacetylase, histones, humans, lysine, nucleic acids, phosphorylation, post-translational modification, protein-protein interactions, transcription (genetics)
Abstract:
As a reversible post-translational modification (PTM) discovered decades ago, protein lysine acetylation was known for its regulation of transcription through the modification of histones. Recent studies discovered that lysine acetylation targets broad substrates and especially plays an essential role in cellular metabolic regulation. Although acetylation is comparable with other major PTMs such as phosphorylation, an integrated resource still remains to be developed. In this work, we presented the compendium of protein lysine acetylation (CPLA) database for lysine acetylated substrates with their sites. From the scientific literature, we manually collected 7151 experimentally identified acetylation sites in 3311 targets. We statistically studied the regulatory roles of lysine acetylation by analyzing the Gene Ontology (GO) and InterPro annotations. Combined with protein-protein interaction information, we systematically discovered a potential human lysine acetylation network (HLAN) among histone acetyltransferases (HATs), substrates and histone deacetylases (HDACs). In particular, there are 1862 triplet relationships of HAT-substrate-HDAC retrieved from the HLAN, at least 13 of which were previously experimentally verified. The online services of CPLA database was implemented in PHP + MySQL + JavaScript, while the local packages were developed in JAVA 1.5 (J2SE 5.0). The CPLA database is freely available for all users at: http://cpla.biocuckoo.org.
Agid:
2294751