<<< Full experiment listing

PXD001085

PXD001085 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitlePHD3 and FIH substrates cluster in distinct signalling pathways
DescriptionAmino acid hydroxylation is a common post-translational modification which regulates intra and inter-molecular protein-protein interactions. The modifications are regulated by a family of 2-oxoglutarate (2OG) dependent enzymes and although the biochemistry is well understood, until now only a few substrates have been described for these enzymes. We present here a sensitive method which specifically enriches and identifies hydroxylase substrates. We screened for substrates of PHD3 and FIH, a proline and asparagine hydroxylase respectively which regulate the HIF-mediated hypoxic response and were able to confirm known substrates as well as identifying hundreds of potential novel ones. Enrichment analysis revealed that the substrates of both hydroxylases cluster in the same pathways but frequently modify different nodes of these networks. We confirm that two proteins identified in this screen, MAPK6 and RIPK4, are indeed hydroxylated in a FIH or PHD3 dependent mechanism and explore the biological consequences of the hydroxylation.
HostingRepositoryPRIDE
AnnounceDate2016-03-31
AnnouncementXMLSubmission_2016-03-31_05:37:29.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAlex von kriegsheim
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListcarbamoylated residue; monohydroxylated residue; acetylated residue
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02014-06-24 07:42:53ID requested
12016-03-31 05:37:31announced
Publication List
Rodriguez J, Pilkington R, Garcia Munoz A, Nguyen LK, Rauch N, Kennedy S, Monsefi N, Herrero A, Taylor CT, von Kriegsheim A, Substrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling Pathways. Cell Rep, 14(11):2745-60(2016) [pubmed]
Keyword List
curator keyword: Biomedical
submitter keyword: Hypoxia, Hydroxylases, DMOG, RIPK4, ERK3, MAPK6
Contact List
Alex von Kriegsheim
contact affiliationsystems biology Ireland, UCD
contact emailAlex.vonkriegsheim@ucd.ie
lab head
Alex von kriegsheim
contact affiliationSystems Biology
contact emailalex.vonkriegsheim@ucd.ie
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/2016/03/PXD001085
PRIDE project URI
Repository Record List
[ + ]