PXD041525-3

PXD041525 is an original dataset announced via ProteomeXchange.

Title	A chemistry-based orthogonal enzyme-substrate design strategy for discovery of substrates of protein palmitoyltransferases
Description	Attachment of lipids to proteins is a key form of protein modification which intersects with all areas of cellular physiology 1 . Of these, the most pervasive form of protein lipidation is protein S-acylation, also commonly known as protein palmitoylation. Protein palmitoylation is a post-translational modification whereby long chain fatty acids, most typically the 16-carbon palmitic acid, is attached to a cytosol-facing cysteine through a thioester linkage. More than 10% of the proteome is targeted by this modification2, which is catalyzed by members of the zDHHC family of integral membrane enzymes. In humans, there are 23 members of the zDHHC family localized at a variety of organellar membranes as well as the plasma membrane that catalyze protein palmitoylation. Despite having been discovered more than twenty years ago 3 4 the chemistry and biology of many of the zDHHC members remain poorly understood and for several members, few substrates have been characterized. Intriguingly, there are no primary sequence determinants that dictate sites of protein palmitoylation. Cysteines that are proximal to the membrane have a high propensity of being palmitoylated.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:04:58.177.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Shelby Auger
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	palmitoylated residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2023-04-13 12:34:36	ID requested
1	2023-10-04 09:15:04	announced
2	2023-11-14 09:05:51	announced	2023-11-14: Updated project metadata.
⏵ 3	2024-10-22 06:04:59	announced	2024-10-22: Updated project metadata.

10.1021/jacs.3c04359;

Puthenveetil R, Auger SA, G, ó, mez-Navarro N, Rana MS, Das R, Healy LB, Suazo KF, Shi ZD, Swenson RE, Distefano MD, Banerjee A, Orthogonal Enzyme-Substrate Design Strategy for Discovery of Human Protein Palmitoyltransferase Substrates. J Am Chem Soc, 145(41):22287-22292(2023) [pubmed]

submitter keyword: Palmitoylation, palmitoyltransferases, Bump-Hole

Mark, D.
contact affiliation	Chemistry Department, University of Minnesota
contact email	diste001@umn.edu
lab head
Shelby Auger
contact affiliation	University of Minnesota
contact email	auger054@umn.edu
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/2023/10/PXD041525

PRIDE project URI

• PRIDE
  1. PXD041525
     1. Label: PRIDE project
     2. Name: A chemistry-based orthogonal enzyme-substrate design strategy for discovery of substrates of protein palmitoyltransferases