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ProteomicsIdentification of PRMT5 phosphorylation sites in Hey cells LC-MS
Previous studies have shown that PRMT5 undergoes various PTMs, including phosphorylation and arginine methylation. In our investigation of PRMT5's PTMs, we detected elevated phospho-Ser/Thr levels of PRMT5 in CDDP-resistant ovarian cancer cells Hey compared to their parental counterparts by co-imm...
ORGANISM(S): Homo sapiens (Human) 
2025-03-06 | PXD061400 | Pride
Prmt5 phosphorylation sites 
UnknownLKB1 regulates PRMT5 activity in breast cancer.
Not available
S-EPMC6294691 | biostudies-literature
UnknownPRMT5: A novel regulator of Hepatitis B virus replication and an arginine methylase of HBV core.
Not available
S-EPMC5655436 | biostudies-literature
UnknownLate cornified envelope 1C (LCE1C), a transcriptional target of TAp63 phosphorylated at T46/T281, interacts with PRMT5.
Not available
S-EPMC5861035 | biostudies-literature
UnknownPhosphorylation of pICln by the autophagy activating kinase ULK1 regulates snRNP biogenesis and splice activity of the cell.
Not available
S-EPMC10034211 | biostudies-literature
ProteomicsHuman Arginine Methylome
Identification of arginine methylation sites in human HEK293 cells, yielding a total of >8.000 high-confident modification sites on >3.300 proteins
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080836 | MassIVE
UnknownA New Insight into MYC Action: Control of RNA Polymerase II Methylation and Transcription Termination.
Not available
S-EPMC9952900 | biostudies-literature
ProteomicsMitochondrial VHL rewires cell metabolism in hypoxia
Under normoxia, von Hippel-Lindau (VHL) protein targets the oxygen-induced, hydroxylated form of hypoxia-inducible factors for degradation to orchestrate mammalian oxygen sensing. However, whether VHL plays non-canonical roles in hypoxia, when protein hydroxylation is attenuated, remains elusive. He...
ORGANISM(S): Homo sapiens (Human) 
2025-08-26 | PXD056376 | Pride
Mitochondrial vhl hypoxia metabolism 
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 
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