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Mutations in the TMEM260 gene cause structural heart defects and renal anomalies syndrome (SHDRA), but the function of the encoded protein remains unknown. We report that TMEM260 is an ER-located protein O-mannosyltransferase that selectively glycosylates defined extracellular immunoglobulin, plexin...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-05-05 | PXD032328 | Pride
Protein O-linked mannose (O-Man) glycosylation is an evolutionary conserved post-translational modification, whose biosynthesis is initiated by three non-redundant enzyme families, POMT1/POMT2, TMTC1-4 and TMEM260. In this study, we applied a targeted workflow for membrane glycoproteomics to five hu...
ORGANISM(S): Homo sapiens (Human) 
2024-06-10 | PXD045597 | Pride
C-mannosylated peptides are easily detected by mass spectrometry (MS) from purified proteins but not from complex biological samples. Enrichment of specific glycopeptides by lectin affinity prior to MS analysis has been widely applied to support glycopeptide identification, but was up till now not a...
ORGANISM(S): Homo sapiens (Human) 
2022-05-13 | PXD031355 | Pride
Microalgae are a renewable and promising biomass for large-20 scale biofuel, food and nutrient production. However, their efficient exploitation depends on our knowledge of the cell wall composition and organization as it can limit access to high-value molecules. Here we provide an atomic-level mode...
ORGANISM(S): Homo sapiens (Human) 
2024-01-09 | PXD048024 | Pride
Protein O-mannosylation is initiated by the ER-resident enzymes POMT1 and POMT2, both of which carry multiple N-glycans essential for proper folding and activity. Although congenital disorders of glycosylation type I (CDG-I) disrupt the early N-glycosylation process, their impact on POMT biogenesis ...
ORGANISM(S): Homo sapiens (Human) 
2026-08-02 | PXD073937 | Pride
O-Mannosylation in h9 mouse neuronal stem cells (mNSC) explored by differential O-Man glycoproteomics and BC2L-A lectin affinity chomatography
ORGANISM(S): Mus musculus (Mouse) 
2026-08-02 | PXD062030 | Pride
Dynamic cycling of N-Acetylglucosamine (GlcNAc) on serine (Ser) and threonine (Thr) residues (O-GlcNAcylation) is an essential process in all eukaryotic cells except yeast, e.g Saccharomyces cerevisiae. O-GlcNAcylation modulates signaling and cellular processes in an intricate interplay with protein...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) Schizosaccharomyces pombe 
2015-12-08 | PXD002924 | Pride
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes,...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2021-04-26 | PXD025344 | Pride
O-Mannosylation is a vital protein modification conserved from fungi to humans. In an essential step towards the full understanding of O-mannosylation we mapped the O mannose glycoproteome in baker´s yeast.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-01-18 | PXD003238 | Pride
Protein O-mannosylation is found in yeast and metazoans and a family of conserved orthologous polypeptide O-mannosyltransferases is believed to initiate this important posttranslational modification. We recently discovered that the large families of cadherins and protocadherins carry highly conserve...
ORGANISM(S): Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 
2017-05-18 | PXD004341 | Pride
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