{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Juntao Yang"],"species":["Mus Musculus"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0001791000"],"submitter_email":["yangjt@pumc.edu.cn"],"submitter_affiliation":["Peking Union Medical College"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["Lysine crotonylation (Kcr) is a recently discovered post-translational modification that potentially regulates multiple biological processes. With an objective to expand the available crotonylation datasets, LC-MS/MS is performed using mouse liver samples under normal physiological conditions to obtain in vivo crotonylome. A label-free strategy is used and 10 034 Class I (localization probabilities > 0.75) crotonylated sites are identified in 2245 proteins. The KcrE, KcrD, and EKcr motifs are significantly enriched in the crotonylated peptides. The identified crotonylated proteins are mostly enzymes and primarily located in the cytoplasm and nucleus. Functional enrichment analysis based on Gene Ontology and Kyoto Encyclopedia of Genes and Genomes shows that the crotonylated proteins are closely related to the purine-containing compound metabolic process, ribose phosphate metabolic process, carbon metabolism pathway, ribosome pathway, and a series of metabolism-associated biological processes. To the best of the authors' knowledge, this research provides the first report on the mouse liver crotonylome. Furthermore, it offers additional evidence that crotonylation exists in non-histone proteins, and is likely involved in various biological processes. The mass spectrometry proteomics data have been deposited in the ProteomeXchange Consortium with the dataset identifiers PXD019145."],"pubmed_title":["Global Lysine Crotonylation Profiling of Mouse Liver."],"pubmed_authors":["Liu Jiang-Feng JF, Wu Song-Feng SF, Liu Shu S, Sun Xin X, Wang Xiao-Man XM, Xu Ping P, Chen Hou-Zao HZ, Yang Jun-Tao JT"],"additional_accession":[]},"is_claimable":false,"name":"Global lysine crotonylation profiling in the livers of mice","description":"Crotonylation (Cr) is a novel post-transcriptional modification with the potential to regulate multiple biological processes. In order to improve the crotonylation dataset for further study, we performed LC-MS/MS with mouse liver samples to obtain the in vivo crotonylome. Totally, we identified 4607 unique crotonylated peptides in 1322 proteins. The motifs KcrE, KcrD and EKcr were significantly enriched with the crotonylated peptides whose localization probability was over 0.75. The identified crotonylated proteins were mostly located in cytoplasm and nucleus, and most crotonylated proteins were enzymes. Functional enrichment analysis based on GO and KEGG pathway showed that, crotonylated proteins were closely related to small molecule catabolic process, purine-containing compound metabolic process, carbon metabolism pathway, ribosome pathway and a series of metabolism associated biological processes. In conclusion, this research provided the largest in vivo dataset of crotonylome and the first crotonylome of mouse liver. We offered another evidence that crotonylation widely existed in non-histone proteins and was probably involved in various biological processes.","dates":{"publication":"Sun Jan 19 00:00:00 GMT 2020"},"accession":"PXD015645","cross_references":{"TAXONOMY":["10090"],"pubmed":["32864800"]}}