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Protein post-translational modification (PTM) increases the functional diversity of the proteome and regulates numerous biological processes in eukaryotes. Two types of PTMs, O-linked-acetyl glucosamine modification (O-GlcNAc) and phosphorylation have been identified on the same amino acid, are cons...
ORGANISM(S): Triticum aestivum (Wheat) 
2020-12-18 | PXD008285 | Pride
Protein post-translational modification (PTM) increases the functional diversity of the proteome and regulates numerous biological processes in eukaryotes. Two types of PTMs, O-linked-acetyl glucosamine modification (O-GlcNAc) and phosphorylation have been identified on the same amino acid, are cons...
ORGANISM(S): Triticum aestivum (Wheat) 
2021-05-18 | PXD008298 | Pride
The experimental results revealed 2727 phosphorylated proteins, 5258 phosphorylated peptides and 5096 phosphorylation sites, which included 5252 quantifiable phosphorylated peptides and 5091 quantifiable phosphorylation sites on 2725 quantifiable modified proteins
ORGANISM(S): Lycium Barbarum 
2024-12-10 | PXD058720 |
Gene expression and splicing switches upon RBM4 overexpression 2 Samples
ORGANISM(S): Homo sapiens 
Comprehensive proteogenomic analysis of Microphthalmia Transcription Factor (MiT) family translocation renal cell carcinoma (tRCC) tumor and normal adjacent tissues was performed to elucidate the molecular landscape of these tumors.
ORGANISM(S): Homo Sapiens 
2022-07-20 | PXD035377 |
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