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Investigation of protein phosphorylation in humans has largely focussed on serine (Ser), threonine (Thr) and tyrosine (Tyr), with proven roles for these modifications in all aspects of life. However, mounting evidence suggests that phosphorylation of non-canonical amino acids, including histidine an...
ORGANISM(S): Homo sapiens (Human) 
2020-06-16 | PXD012188 | Pride
Confident identification of sites of protein phosphorylation by mass spectrometry (MS) is essential to advance understanding of phosphorylation-mediated signaling events. However, development of novel instrumentation requires that methods for MS data acquisition and its interrogation be evaluated an...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-03-31 | MSV000085203 | MassIVE
Pseudokinases, so named because they lack one or more conserved canonical amino acids that define their catalytically-active relatives, have evolved a variety of biological functions in both prokaryotic and eukaryotic organisms. Human PSKH2 is closely related to the canonical kinase PSKH1, which map...
ORGANISM(S): Homo sapiens (Human) 
2023-03-11 | PXD039306 | Pride
Protein sulfation can be crucial in regulating protein-protein interactions but remains largely underexplored. Sulfation is near-isobaric to phosphorylation, making it particularly challenging to investigate using mass spectrometry. The degree to which tyrosine sulfation (sY) is misidentified as pho...
ORGANISM(S): Homo sapiens (Human) 
2025-05-07 | PXD059650 | Pride
Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalysed by Golgi-resident Tyrosyl Protein Sul-foTransferases (TPSTs). Information on protein tyrosine sulfation is currently limited to ~50 human proteins with only a handful of those having verified sites of sulfation. The...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD043723 | Pride
Protein tyrosine sulfation (sY) is a post-translational modification (PTM) catalysed by Golgi-resident Tyrosyl Protein Sul-foTransferases (TPSTs). Information on protein tyrosine sulfation is currently limited to ~50 human proteins with only a handful of those having verified sites of sulfation. The...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD043713 | Pride
Polo-like kinase 4 (PLK4) is the master regulator of centriole duplication in metazoan organisms. Catalytic activity and protein turnover of PLK4 are tightly coupled in human cells, since changes in PLK4 concentration and catalysis have profound effects on centriole duplication and supernumerary cen...
ORGANISM(S): Homo sapiens (Human) 
2021-06-14 | PXD018704 | Pride
The ATR-CHK1 signalling pathway responds to single strand DNA breaks and is required for cancer cells to survive the high levels of DNA replication stress and genomic instability resulting from the activity of oncogenes such as MYC. For this reason, inhibitors of CHK1 have great potential as anti-c...
ORGANISM(S): Mus musculus (Mouse) 
2022-10-19 | PXD026203 | Pride
Confident identification of sites of protein phosphorylation by mass spectrometry (MS) is essential to advance understanding of phosphorylation-mediated signaling events. However, development of novel instrumentation requires that methods for MS data acquisition and its interrogation be evaluated an...
ORGANISM(S): Homo sapiens (Human) 
2019-09-27 | PXD007058 | Pride
In eukaryotes, protein kinase signaling is regulated by a diverse array of post-translational modifications (PTMs). While regulation by activation segment phosphorylation in Ser/Thr kinases is well understood, relatively little is known about how oxidation of cysteine (Cys) amino acids modulates cat...
ORGANISM(S): Homo sapiens (Human) 
2025-04-01 | PXD044990 | Pride
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