PXD008400

PXD008400 is an original dataset announced via ProteomeXchange.

Title	Direct analysis of IFITM3 S-fatty-acylation, part 1
Description	Given our laboratory interest in IFITM3 S-fatty-acylation and antiviral activity, we sought to directly characterize fatty acids that are covalently attached to the Cys residues of IFITM3. IFITM3 comprises two S-fatty-acylation sites (C71 and C72) in proximity of a intramembrane domain, and another site adjacent to a transmembrane domain (C105). We directly identified the S-fatty-acylation sites of IFITM3 and further demonstrated that the highly conserved Cys residues are primarily modified by palmitic acid.
HostingRepository	PRIDE
AnnounceDate	2018-03-28
AnnouncementXML	Submission_2018-03-28_00:03:33.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Emmanuelle Thinon
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	palmitoylated residue
Instrument	LTQ Orbitrap

Revision	Datetime	Status	ChangeLog Entry
0	2017-12-11 01:30:37	ID requested
⏵ 1	2018-03-28 00:03:34	announced

Thinon E, Fernandez JP, Molina H, Hang HC, Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res, 17(5):1907-1922(2018) [pubmed]

curator keyword: Biological

submitter keyword: post translational modifications, S-fatty-acylation, S-palmitoylation, IFITM3, modification site identification

Howard C Hang
contact affiliation	Laboratory of chemical biology and microbial pathogenesis, The Rockefeller University, New York, USA
contact email	hhang@mail.rockefeller.edu
lab head
Emmanuelle Thinon
contact affiliation	The Francis Crick Institute
contact email	emmanuellethinon@gmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD008400
     1. Label: PRIDE project
     2. Name: Direct analysis of IFITM3 S-fatty-acylation, part 1