棕榈酰化
蛋白质组
人类蛋白质组计划
计算生物学
生物
翻译后修饰
串扰
基因亚型
蛋白质组学
半胱氨酸
生物信息学
生物化学
基因
光学
物理
酶
作者
Mathieu Blanc,Fabrice David,Laurence Abrami,Daniel Migliozzi,Florence Armand,Jérôme Bürgi,Gijs R. van den Brink
出处
期刊:F1000Research
[Faculty of 1000]
日期:2015-07-16
卷期号:4: 261-261
被引量:237
标识
DOI:10.12688/f1000research.6464.1
摘要
Protein S-palmitoylation is a reversible post-translational modification that regulates many key biological processes, although the full extent and functions of protein S-palmitoylation remain largely unexplored. Recent developments of new chemical methods have allowed the establishment of palmitoyl-proteomes of a variety of cell lines and tissues from different species. As the amount of information generated by these high-throughput studies is increasing, the field requires centralization and comparison of this information. Here we present SwissPalm ( http://swisspalm.epfl.ch), our open, comprehensive, manually curated resource to study protein S-palmitoylation. It currently encompasses more than 5000 S-palmitoylated protein hits from seven species, and contains more than 500 specific sites of S-palmitoylation. SwissPalm also provides curated information and filters that increase the confidence in true positive hits, and integrates predictions of S-palmitoylated cysteine scores, orthologs and isoform multiple alignments. Systems analysis of the palmitoyl-proteome screens indicate that 10% or more of the human proteome is susceptible to S-palmitoylation. Moreover, ontology and pathway analyses of the human palmitoyl-proteome reveal that key biological functions involve this reversible lipid modification. Comparative analysis finally shows a strong crosstalk between S-palmitoylation and other post-translational modifications. Through the compilation of data and continuous updates, SwissPalm will provide a powerful tool to unravel the global importance of protein S-palmitoylation.
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