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ProteomicsWidespread hydroxylation of unstructured lysine-rich protein domains by JMJD6
The Jumonji domaining-containing protein JMJD6 is a 2-oxoglutarate dependent dioxygenase that has been implicated in a broad range of biological functions. Cellular studies have implicated the enzyme in chromatin biology, transcription, DNA repair, mRNA splicing and co-transcriptional processing. Al...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2022-08-02 | PXD031221 | Pride
Human Lc-msms Hydroxylation Jmjd6 Lysine derivatisation 
ProteomicsSystem-wide profiling of lysine 5-hydroxylation
Lysine 5-hydroxylation (5-Hyl) has been well recognized as an essential protein post-translational modification regulating cellular structural stability, RNA alternative splicing and epigenetic gene expression. System-wide enrichment and quantification of 5-Hyl targets have been challenging due to i...
ORGANISM(S): Homo sapiens (Human) 
2025-04-04 | PXD054608 | Pride
Chemical proteomics Lysine hydroxylation 
ProteomicsAnalysis of proline and lysine post-translational modifications of collagen from prolyl 3-hydroxylase 3 and lysyl hydroxylase 1 null mice
We performed shotgun proteomic analysis of type V collagens purified from wild-type mice and prolyl 3-hydroxylase 3 or lysyl hydroxylase 1 null mice by LC-MS after trypsin digestion for identification of lysine glycosylation sites.
ORGANISM(S): Mus Musculus (mouse) 
2021-02-19 | PXD019748 | JPOST Repository
ProteomicsJMJD6 interactome screen from "Widespread hydroxylation of unstructured lysine-rich protein domains by JMJD6"
The Jumonji domaining-containing protein JMJD6 is a 2-oxoglutarate dependent dioxygenase that has been implicated in a broad range of biological functions. Cellular studies have implicated the enzyme in chromatin biology, transcription, DNA repair, mRNA splicing and co-transcriptional processing. Al...
ORGANISM(S): Homo sapiens (Human) 
2022-08-02 | PXD031155 | Pride
Lc-msms Dia Human Hela Interactome Orbitrap fusion lumos Jmjd6 
ProteomicsDown-regulation of collagen hydroxylation in colorectal liver metastasis
Collagen, a major component of the extracellular matrix, is significantly upregulated in colorectal liver metastasis (CRLM) compared to liver tissue. Expression levels of specific collagen types in CRLM resemble those in colorectal cancer (CRC) and colon tissue. We investigated whether the collagen ...
ORGANISM(S): Homo sapiens (Human) 
2020-09-16 | PXD015015 | Pride
Crlm Liver Human Ptm Crc Collagen Colon Orbitrap fusion 
UnknownWidespread hydroxylation of unstructured lysine-rich protein domains by JMJD6.
Not available
S-EPMC9371714 | biostudies-literature
UnknownEGLN1 prolyl hydroxylation of hypoxia-induced transcription factor HIF1α is repressed by SET7-catalyzed lysine methylation.
Not available
S-EPMC9123262 | biostudies-literature
UnknownEngineering Pseudomonas taiwanensis VLB120 for regio- and stereospecific hydroxylation of L-lysine fueled by the Weimberg pathway.
Not available
S-EPMC12930750 | biostudies-literature
UnknownBiochemical investigations using mass spectrometry to monitor JMJD6-catalysed hydroxylation of multi-lysine containing bromodomain-derived substrates.
Not available
S-EPMC11878239 | biostudies-literature
Proteomics(3S)-Lysyl hydroxylation of TRAFAC GTPases is catalyzed by the 1 Jumonji-C oxygenase JMJD7
Biochemical, structural, and cellular studies reveal Jumonji-C (JmjC) domain-containing (JMJD7) as a 2-oxoglutarate (2OG)-dependent oxygenase catalyzing a previously unreported type of post translational modification, (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 as more closely r...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2018-03-20 | MSV000082185 | MassIVE
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