PXD038392-1

PXD038392 is an original dataset announced via ProteomeXchange.

Title	Identification of N-terminal SUMOylation of mouse cofilin-1 by IP-MS
Description	Small ubiquitin-like modifier (SUMO) typically conjugates to target proteins through isopeptide linkage to the ε-amino group of lysine residues. This posttranslational modification (PTM) plays pivotal roles in modulating protein function. As a key regulator of actin cytoskeleton dynamics, cofilins (CFLs) are well-known to undergo several different kinds of PTMs. Using mass spectrometry, our study identified the N-terminal α-amino group, rather than any of the ε-amino groups of the internal lysines, as the sole SUMO-conjugation site of cofilin-1 (CFL1).
HostingRepository	PRIDE
AnnounceDate	2023-10-24
AnnouncementXML	Submission_2023-10-24_11:25:06.321.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD038392
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	WeijiWeng
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	sumoylated lysine; acetylated residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2022-11-26 04:04:25	ID requested
⏵ 1	2023-10-24 11:25:07	announced
2	2023-11-14 09:07:41	announced	2023-11-14: Updated project metadata.
3	2024-10-22 06:08:59	announced	2024-10-22: Updated project metadata.

Weng W, Gu X, Yang Y, Zhang Q, Deng Q, Zhou J, Cheng J, Zhu MX, Feng J, Huang O, Li Y, -amino SUMOylation of cofilin-1 is critical for its regulation of actin depolymerization. Nat Commun, 14(1):5688(2023) [pubmed]

10.6019/PXD038392;

submitter keyword: Mouse, cofilin-1, IP-MS, N-terminal SUMOylation

YongLi
contact affiliation	Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine
contact email	liyong68@shsmu.edu.cn
lab head
WeijiWeng
contact affiliation	Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation, Shanghai Jiao Tong University School of Medicine
contact email	wengweiji@alumni.sjtu.edu.cn
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/PXD038392

PRIDE project URI

• PRIDE
  1. PXD038392
     1. Label: PRIDE project
     2. Name: Identification of N-terminal SUMOylation of mouse cofilin-1 by IP-MS