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ProteomicsProMetheus: a database of hmSILAC-validated protein methylation sites
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 fro...
ORGANISM(S): Homo sapiens (Human) 
2022-06-02 | PXD027949 | Pride
Heavy methyl silac Silac Methylation 
ProteomicsDetermining the Mitochondrial Methyl Proteome in Saccharomyces cerevisiae using Heavy Methyl SILAC
"Determining the Mitochondrial Methyl Proteome in Saccharomyces cerevisiae using Heavy Methyl SILAC" Heavy Methyl SILAC proteomics toward characterization and validation of mitochondrial, methylated proteins.
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2016-08-31 | MSV000080107 | MassIVE
UnknownDetermining the Mitochondrial Methyl Proteome in Saccharomyces cerevisiae using Heavy Methyl SILAC.
Not available
S-EPMC5148652 | biostudies-literature
ProteomicsHeavy-methyl SILAC of ribosomal proteins
Methylation on ribosome subunits and ribosime-associating proteins were compared in a low- and high-SAM conditions using heavy-methyl SILAC. Ribosome proteins were isolated in two ways; one was ultracentrifugation and the other was anti-FLAG immunoprecipitation using HeLa cells transfected with a FL...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2022-04-21 | MSV000089296 | MassIVE
ProteomicsA systematic analysis of methylpeptide false discovery rates
All large-scale LC-MS/MS post-translational methylation site discovery experiments require methylpeptide spectrum matches (methyl-PSMs) to be identified at acceptably low false discovery rates (FDRs). To meet estimated methyl-PSM FDRs, methyl-PSM filtering criteria are often determined using the tar...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-01-05 | PXD002857 | Pride
Arginine methylation Heavy-methyl silac Lysine methylation False discovery rates Target-decoy approach 
ProteomicsDiscovery of arginine methylation, phosphorylation and their co-occurrence in condensate-associated proteins in Saccharomyces cerevisiae
The formation of condensates in membraneless organelles is thought to be driven by protein phase separation. Arginine methylation and serine/threonine phosphorylation are important in the phase separation process, however these post-translational modifications are often present in intrinsically diso...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-09-17 | PXD022403 | Pride
Yeast Methylation Phosphorylation Crosstalk 
ProteomicsQuantitative profiling of the enzymatic activity of the protein lysine mono-methyltransferase SMYD2 using SILAC-based proteomics
The significance of non-histone lysine methylation in cell biology and human disease is an emerging area of research exploration, and small molecule inhibitors that selectively and potently target “writers” and “erasers” of methyl-lysine, such as the protein lysine mono-methyltransferase SMYD2, are ...
ORGANISM(S): Homo sapiens (Human) 
2016-01-11 | PXD002405 | Pride
Methylation Lysine methyltransferase Silac Immunoaffinity enrichment Smyd2 
ProteomicsProteomics Profiling of Arginine Methylation Defines PRMT5 Substarate Specificity
Protein arginine methyltransferases (PRMTs) catalyze arginine methylation, an abundant post-translational modification occurring on both chromatin-bound and cytoplasmic proteins. Growing evidence supports the involvement of PRMT5, the major Type II PRMT, in pro-survival and differentiation pathways,...
ORGANISM(S): Homo sapiens (Human) 
2019-04-10 | PXD009070 | Pride
Lc-ms Prmt5 Arginine methylation 
ProteomicsPhosphoproteomic profiling of the DNA damage response in MCF10A and human PBMC cells by SILAC labeling and 1D and 2D-LC-MS/MS
The DNA-damage response (DDR) is a critical network for maintaining genomic integrity, and mutations in the DDR are among the most frequently identified in tumors. Phosphorylation is a key signaling event in the DDR network. We sought to design high throughput, mass spectrometry based assays to moni...
ORGANISM(S): Homo sapiens (Human) 
2015-12-01 | PXD002363 | Pride
Human Pbmc Silac Ir Mms Mcf10a Lc-ms/ms 
ProteomicsHistone H3 tail interactome in MPC11 murine myeloma cells
We have used peptide capture in conjunction with super-SILAC quantification to carry out an unbiased high-throughput analysis of the composition of protein complexes that bind to histone H3K9/S10 and H3K27/S28 methyl-phospho modifications. We compared binding profiles of nuclear proteins from MPC11 ...
ORGANISM(S): Mus musculus (Mouse) 
2016-05-04 | PXD001273 | Pride
Lc-msms Histone modification Peptide capture Histone h3 tail interactome 
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