PXD015437

PXD015437 is an original dataset announced via ProteomeXchange.

Title	TULIP2: an improved method for the identification of ubiquitin E3-specific targets
Description	Protein modification by Ubiquitin or Ubiquitin-like modifiers is mediated by an enzyme cascade composed of E1s, E2s and E3s enzymes. E1, or ubiquitin-activating enzymes, perform the ubiquitin activation. Next, ubiquitin is transferred to ubiquitin-conjugating enzymes or E2s. Finally, ubiquitin ligases or E3s catalyze the transfer of ubiquitin to the acceptor proteins. E3 enzymes are responsible of determining the substrate specificity. Determining which E3 enzyme maps to which substrate is a major challenge that is greatly facilitated by the TULIP2 methodology. TULIP2 methodology is fast, precise and cost-effective. Compared to previous TULIP methodology protocol, TULIP2 methodology achieves a more than 50-fold improvement in the purification yield and two orders of magnitude improvement in the signal-to-background ratio after label free quantification by mass spectrometry analysis. The method includes the generation of TULIP2 cell lines, subsequent purification of TULIP2 conjugates, preparation and analysis of samples by mass spectrometry
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:58:39.751.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Román González-Prieto
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-09-12 08:50:05	ID requested
1	2019-11-15 05:39:55	announced
2	2020-01-02 07:56:37	announced	2020-01-02: Updated publication reference for PubMed record(s): 31850303.
⏵ 3	2024-10-22 04:58:41	announced	2024-10-22: Updated project metadata.

Salas-Lloret D, Agabitini G, Gonz, á, lez-Prieto R, TULIP2: An Improved Method for the Identification of Ubiquitin E3-Specific Targets. Front Chem, 7():802(2019) [pubmed]

10.3389/fchem.2019.00802;

submitter keyword: Ubiquitin, E3 enzymes, Mass Spectrometry, Post-translational modifications, Proteomics

Román González-Prieto
contact affiliation	González-Prieto laboratory, Department of Cell and Chemical Biology, Leiden University Medical Center (LUMC), Leiden, The Netherlands.
contact email	R.Gonzalez_Prieto@lumc.nl
lab head
Román González-Prieto
contact affiliation	Andalusian Center for Regenerative Medicine and Cell Biology, CABIMER, University of Seville
contact email	R.Gonzalez_Prieto@lumc.nl
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/2019/11/PXD015437

PRIDE project URI

• PRIDE
  1. PXD015437
     1. Label: PRIDE project
     2. Name: TULIP2: an improved method for the identification of ubiquitin E3-specific targets