Dataset Information

ProMetheus: a database of hmSILAC-validated protein methylation sites

ABSTRACT: Protein arginine (R) methylation is a post-translational modification that has been shown to play a role in various biological processes, such as RNA splicing, DNA repair, immune response, signal transduction and tumor development. Here, we present a dataset of high-quality methylations obtained from several different heavy methyl SILAC (hmSILAC) experiments analyzed with a machine learning model that was trained to recognize hmSILAC doublets and show that this model allows for improved high-confidence identification of methyl-peptides. The results of our analysis of the interactions between R-methylated proteins further support the idea that this modification plays a role in modulating protein:protein interactions and suggest a potential new role of R methylation in immunity and macrophage metabolism. Moreover, we intersect the methyl-site dataset with a phosphosite dataset to investigate the cross-talk between R methylation and phosphorylation. Finally, we explore the application of hmSILAC to identify unconventional methylated residues on both histone and non-histone proteins.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

DISEASE(S): Osteosarcoma,Acute Leukemia,Cervix Carcinoma,Malignant Neoplasm Of Ovary

SUBMITTER: Enrico Massignani

LAB HEAD: Tiziana Bonaldi

PROVIDER: PXD027949 | Pride | 2022-06-02

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20120612_EXQ3_AC_SA_IPcyt_0101.raw	Raw
	20120612_EXQ3_AC_SA_IPcyt_0201.raw	Raw
	20120612_EXQ3_AC_SA_IPcyt_0301.raw	Raw
	20120612_EXQ3_AC_SA_IPcyt_0401.raw	Raw
	20120612_EXQ3_AC_SA_IPcyt_0501.raw	Raw

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Publications

Proteomics profiling of arginine methylation defines PRMT5 substrate specificity.

Musiani Daniele D Bok Jabez J Massignani Enrico E Wu Liling L Tabaglio Tommaso T Ippolito Marica Rosaria MR Cuomo Alessandro A Ozbek Umut U Zorgati Habiba H Ghoshdastider Umesh U Robinson Robert C RC Guccione Ernesto E Bonaldi Tiziana T

Science signaling 20190402 575

Protein arginine methyltransferases (PRMTs) catalyze arginine methylation on both chromatin-bound and cytoplasmic proteins. Accumulating evidence supports the involvement of PRMT5, the major type II PRMT, in cell survival and differentiation pathways that are important during development and in tumorigenesis. PRMT5 is an attractive drug target in various cancers, and inhibitors are currently in oncological clinical trials. Nonetheless, given the complex biology of PRMT5 and its multiple nonhisto ...[more]

PMID: 30940768

Publication: 1/5

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