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ProteomicsFIH regulates cellular metabolism through hydroxylation of the deubiquitinase OTUB1.
The asparagine hydroxylase, factor inhibiting HIF (FIH) confers oxygen-dependence upon the hypoxia-inducible factor (HIF), a master regulator of the cellular adaptive response to hypoxia. Studies investigating whether asparagine hydroxylation is a general regulatory oxygen-dependent modification hav...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080695 | MassIVE
ProteomicsProlyl hydroxylation regulates protein degradation, synthesis and splicing in human induced pluripotent stem cell-derived cardiomyocytes
Protein hydroxylases are oxygen and alpha-ketoglutarate-dependent enzymes that catalyze hydroxylation of amino acids such as proline, thus linking oxygen and metabolism to enzymatic activity. Prolyl hydroxylation is a dynamic post-translational modification that regulates protein stability and prote...
ORGANISM(S): Homo sapiens (Human) 
2016-05-06 | PXD003621 | Pride
Lc-ms/ms Amino acid labeling Prolyl hydroxylation Ipsc-derived cardiomyocytes 
GenomicsHydroxylation of 5-methylcytosine by TET2 maintains the active state of the mammalian HOXA cluster
This SuperSeries is composed of the following subset Series: GSE32362: Hydroxylation of 5-methylcytosine by TET2 maintains the active state of the mammalian HOXA cluster (Illumina HumanMethylation450 BeadChip) GSE33129: Hydroxylation of 5-methylcytosine by TET2 maintains the active state of the mamm...
ORGANISM(S): Homo sapiens 
2012-05-02 | E-GEOD-33130 | biostudies-arrayexpress
ProteomicsDetermining the hydroxylation status of NAA10-Trp38
NAA10 is the major human N-terminal acetyltransferase (NAT). The KAT activity of NAA10 towards hypoxia-inducible factor 1α (HIF-1α) was recently reported to depend on the hydroxylation at Trp38 of NAA10 by factor inhibiting HIF-1α (FIH). As a consequence, Trp38 hydroxylation status was proposed to a...
ORGANISM(S): Homo sapiens (Human) 
2022-02-16 | PXD023655 | Pride
Hydroxylation Asp-oh Asn-oh Naa10 Trp-oh Nat 
ProteomicsAsparagine hydroxylation of the UBA domain in Cezanne (OTUD7B)
by DUBs need to be tightly controlled. Here, we identify asparagine hydroxylation as a novel posttranslational modification involved in the regulation of Cezanne (OTUD7B), a DUB that controls key cellular functions and signaling pathways. We demonstrate that Cezanne is a substrate for FIH1- and oxyg...
ORGANISM(S): Homo sapiens (Human) 
2020-01-24 | PXD015216 | Pride
Otu7b Deubiquitinases Hydroxylation Cezanne 
ProteomicsProline hydroxylation of ChREBP
This project investigated proline hydroxylation of ChREBP. Proline hydroxylation was investigated in flag-IP enriched protein extracts from ChREBP-flag overexpressing HEK293 cells (A) and in ChREBP-IP enriched mouse liver protein (male, C57BL6/J) (B).
ORGANISM(S): Mus musculus (Mouse) 
2020-10-19 | PXD019137 | Pride
Hek293 Mouse liver Proline hydroxylation 
ProteomicsAsparagine hydroxylation is likely to be a reversible post-translational modification
Amino acid hydroxylation is a common post-translational modification, which generally regulates protein interactions or adds a functional group that can be further modified. Such hydroxylation is currently considered irreversible, necessitating the degradation and re-synthesis of the entire protein ...
ORGANISM(S): Hordeum vulgare (Barley) 
2020-03-23 | PXD013116 | Pride
Lc-ms/ms Hydroxylation Hypoxia Ptm 
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): Homo sapiens (Human) Mus musculus (Mouse) 
2022-08-02 | PXD031221 | Pride
Human Lc-msms Hydroxylation Jmjd6 Lysine derivatisation 
ProteomicsSystematic characterization of site-specific proline hydroxylation using hydrophilic interaction chromatography and mass spectrometry (RCC4)
To improve understanding of the role of site-specific proline hydroxylation in controlling protein function, we have developed a robust workflow for the identification of proline hydroxylation sites in proteins using a combination of hydrophilic interaction chromatography (HILIC) enrichment and high...
ORGANISM(S): Homo sapiens (Human) 
2025-11-28 | PXD044783 | Pride
Hilic Proteomics Hydroxylation Mass spectrometry Proline 
ProteomicsSystematic characterization of site-specific proline hydroxylation using hydrophilic interaction chromatography and mass spectrometry (HEK293)
To improve understanding of the role of site-specific proline hydroxylation in controlling protein function, we have developed a robust workflow for the identification of proline hydroxylation sites in proteins using a combination of hydrophilic interaction chromatography (HILIC) enrichment and high...
ORGANISM(S): Homo sapiens (Human) 
2025-11-28 | PXD044663 | Pride
Hilic Proteomics Hydroxylation Mass spectrometry Proline 
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