ELM: the status of the 2010 eukaryotic linear motif resource.

ELM: the status of the 2010 eukaryotic linear motif resource.
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DOI:
10.1093/nar/gkp1016
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发表时间:
2010-01
影响因子:
14.9
通讯作者:
Gibson TJ
Gibson TJ
中科院分区:
生物学2区
文献类型:
--
作者:
Gould CM;Diella F;Via A;Puntervoll P;Gemünd C;Chabanis-Davidson S;Michael S;Sayadi A;Bryne JC;Chica C;Seiler M;Davey NE;Haslam N;Weatheritt RJ;Budd A;Hughes T;Pas J;Rychlewski L;Travé G;Aasland R;Helmer-Citterich M;Linding R;Gibson TJ

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线性基序是多结构域蛋白质的短片段,其提供独立于蛋白质三级结构的调节功能。许多细胞内信号通过线性基序的蛋白质修饰传递。现在已经报道了成千上万的线性基序实例,最显著的是磷酸化位点。尽管线性基序显然非常丰富,但由于难以获得稳健的统计评估,因此难以从头预测蛋白质序列中的线性基序。http://elm.eu.org/上的ELM资源提供了一个不断扩展的知识库,目前涵盖了146个已知的基序,其中注释包括>1300个实验报告的实例。ELM也是一个探索性的工具,建议新的候选人的已知线性基序的蛋白质的兴趣。关于蛋白质结构域、蛋白质结构和天然紊乱、细胞和分类学背景的信息用于减少或反对假阳性匹配。结果以“条形码”格式以图形方式显示,该格式还通过基于PHI-BLAST的新型“实例映射器”协议显示同源蛋白的已知实例。ELM服务器输出提供了到ELM注释以及许多远程资源的链接。使用这些链接,研究人员可以探索基序,蛋白质,复杂结构和相关文献,以评估候选基序是否值得进行实验研究。
Linear motifs are short segments of multidomain proteins that provide regulatory functions independently of protein tertiary structure. Much of intracellular signalling passes through protein modifications at linear motifs. Many thousands of linear motif instances, most notably phosphorylation sites, have now been reported. Although clearly very abundant, linear motifs are difficult to predict de novo in protein sequences due to the difficulty of obtaining robust statistical assessments. The ELM resource at http://elm.eu.org/ provides an expanding knowledge base, currently covering 146 known motifs, with annotation that includes >1300 experimentally reported instances. ELM is also an exploratory tool for suggesting new candidates of known linear motifs in proteins of interest. Information about protein domains, protein structure and native disorder, cellular and taxonomic contexts is used to reduce or deprecate false positive matches. Results are graphically displayed in a ‘Bar Code’ format, which also displays known instances from homologous proteins through a novel ‘Instance Mapper’ protocol based on PHI-BLAST. ELM server output provides links to the ELM annotation as well as to a number of remote resources. Using the links, researchers can explore the motifs, proteins, complex structures and associated literature to evaluate whether candidate motifs might be worth experimental investigation.
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