PXD057969 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | KDM3A catalysed formation of hydroxyacetyl-lysine on histone H3K9 |
| Description | Histone modifications, including N-lysine acetylation and methylation, play critical roles in eukaryotic transcription. The addition of acetyl- and methyl-groups and removal of acetyl-groups involves redox neutral reactions, whereas demethylation is O2 dependent, a reaction with potential to enable O2 availability mediated regulation, as occurs for reactions catalysed by the 2-oxoglutarate dependent hypoxia-inducible factor (HIF) hydroxylases. A screen for substrates of the HIF-regulated Jumonji-C (JmjC) lysine demethylase KDM3A led to the finding that purified recombinant KDM3A catalyses oxidation of the N-acetyl group of Lys-9 of histone H3 giving an N-hydroxyacetyl-lysine residue. Studies employing a N-hydroxyacetyl-lysine selective antibody and mass spectrometry support the cellular relevance of N-hydroxyacetyl-lysine. The combined biochemical and cellular results reveal evidence for an unanticipated O2-mediated link between histone lysine N-acetylation and JmjC catalysis. Future work can explore the biological significance of N-hydroxyacetylation, including in the hypoxic response where KDM3A plays a role in regulating HIF target genes. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-02-10 |
| AnnouncementXML | Submission_2026-02-09_16:14:09.400.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Simone Sidoli |
| SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606; |
| ModificationList | acetylated residue |
| Instrument | Orbitrap Fusion Lumos |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2024-11-17 12:00:19 | ID requested | |
| ⏵ 1 | 2026-02-09 16:14:09 | announced | |
Publication List
| Dataset with its publication pending |
Keyword List
| submitter keyword: histone demethylation / hydroxylation / acetylation / 2-oxoglutarate dependent oxygenase / JmjC KDMs / demethylases / KDM3A / KDM3B / hypoxia inducible factor / HIF prolyl hydroxylases / epigenetics |
Contact List
| Simone Sidoli |
| contact affiliation | Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA |
| contact email | simone.sidoli@einsteinmed.edu |
| lab head | |
| Simone Sidoli |
| contact affiliation | Albert Einstein College of Medicine |
| contact email | simone.sidoli@gmail.com |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD057969 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD057969
- Label: PRIDE project
- Name: KDM3A catalysed formation of hydroxyacetyl-lysine on histone H3K9