PXD006767

PXD006767 is an original dataset announced via ProteomeXchange.

Title	Characterisation of protein methyltransferases Rkm1, Rkm4, Efm4, Efm7, Set5 and Hmt1 reveals extensive post-translational modification
Description	Protein methylation is one of the major post-translational modifications (PTMs) in the cell. In Saccharomyces cerevisiae, over twenty protein methyltransferases (MTases) and their respective substrates have been identified. However, the way in which these MTases are modified, and potentially subject to regulation, remains poorly understood. Here, we investigated six S. cerevisiae protein MTases (Rkm1, Rkm4, Efm4, Efm7, Set5 and Hmt1) to identify PTMs of potential functional relevance. We identified 51 PTM sites across the six MTases, including phosphorylation, acetylation and methylation. 45 sites are novel. We contextualised the PTM sites in structural models of the MTases and revealed that many fell in catalytic pockets or enzyme-substrate interfaces. These may regulate MTase activity. Finally, we compared PTMs on Hmt1 with those on its human homologs PRMT1, PRMT3, CARM1, PRMT6 and PRMT8. This revealed that several PTMs are conserved from yeast to human, whereas others are only found in Hmt1.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:39:05.141.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Daniel Winter
SpeciesList	scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	monomethylated residue; trimethylated residue; phosphorylated residue; monohydroxylated residue; acetylated residue; dimethylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive; LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2017-06-21 02:01:11	ID requested
1	2017-12-18 01:42:03	announced
⏵ 2	2024-10-22 04:39:13	announced	2024-10-22: Updated project metadata.

Winter DL, Hart-Smith G, Wilkins MR, Characterization of Protein Methyltransferases Rkm1, Rkm4, Efm4, Efm7, Set5 and Hmt1 Reveals Extensive Post-Translational Modification. J Mol Biol, 430(1):102-118(2018) [pubmed]

10.1016/j.jmb.2017.11.009;

curator keyword: Biological

submitter keyword: Metyltransferases,Post-translational modifications, Rkm1, Hmt1, Efm7, Rkm4, Set5, Efm4

Marc R. Wilkins
contact affiliation	UNSW Sydney
contact email	m.wilkins@unsw.edu.au
lab head
Daniel Winter
contact affiliation	UNSW
contact email	d.l.winter@unsw.edu.au
dataset submitter

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/2017/12/PXD006767

PRIDE project URI

• PRIDE
  1. PXD006767
     1. Label: PRIDE project
     2. Name: Characterisation of protein methyltransferases Rkm1, Rkm4, Efm4, Efm7, Set5 and Hmt1 reveals extensive post-translational modification