PXD001281

PXD001281 is an original dataset announced via ProteomeXchange.

Title	Proteome-wide identification of SUMO2 modification sites
Description	Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated substrates, methods to identify the modified lysines on a proteome-wide scale are lacking. We developed a method that enabled large-scale identification of sumoylated lysines and involved the expression of polyhistidine (6His)–tagged SUMO2 with Thr90 mutated to Lys. Digestion of 6His-SUMO2(T90K)–modified proteins with an endoproteinase Lys-C produces a diGly remnant on SUMO2(T90K)-conjugated lysines, enabling a specific immunoprecipitation of modified peptides with diGly-Lys-specific antibody and producing a unique mass-to-charge signature. Mass spectrometry analysis of SUMO2-enriched peptides from human cell lysates revealed more than 1000 sumoylated lysines in 539 proteins, including many functionally related proteins involved in cell cycle, transcription, and DNA repair. Not only can this strategy be used to study the dynamics of sumoylation and other potentially similar posttranslational modifications, but also, these data provide an unprecedented resource for future research on the role of sumoylation in cellular physiology and disease.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:04:15.925.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Triin Tammsalu
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	ubiquitination signature dipeptidyl lysine; phosphorylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2014-09-03 02:28:02	ID requested
1	2014-10-15 02:11:00	announced
⏵ 2	2024-10-22 04:04:24	announced	2024-10-22: Updated project metadata.

Tammsalu T, Matic I, Jaffray EG, Ibrahim AFM, Tatham MH, Hay RT, Proteome-wide identification of SUMO2 modification sites. Sci Signal, 7(323):rs2(2014) [pubmed]

10.1126/scisignal.2005146;

curator keyword: Biological

submitter keyword: heat-shock,SUMO modification sites, HEK293

Ronald T. Hay
contact affiliation	University of Dundee
contact email	R.T.Hay@dundee.ac.uk
lab head
Triin Tammsalu
contact affiliation	University of Dundee
contact email	t.tammsalu@dundee.ac.uk
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/2014/10/PXD001281

PRIDE project URI

• PRIDE
  1. PXD001281
     1. Label: PRIDE project
     2. Name: Proteome-wide identification of SUMO2 modification sites