CPLM

Other names: Compendium of protein lysine acetylation (CPLA), cpla

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 CPLA (Compendium of Protein Lysine Acetylation, http://cpla.biocuckoo.org) database for lysine acetylated substrates with their sites. From the scientific literature, we manually collected 7,151 experimentally identified acetylation sites in 3,311 targets. Combined with protein-protein interaction (PPI) information, we systematically discovered a potential human lysine acetylation network (HLAN) among histone acetyltransferases (HATs), substrates and histone deacetylases (HDACs). In particular, there are 1,862 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).

Webpage:
http://cplm.biocuckoo.cn/

Publications:

Tags:

proteomics resources proteins protein modifications epigenetics protein interaction

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