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PXD053474-1

PXD053474 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleGlobal Profiling of Protein Lactylation Across Subcellular Fractionation Methods in HCT-116
DescriptionProtein lactylation is a novel post-translational modification (PTM) involved in many important physiological processes such as macrophage polarization, immune regulation and tumour cell growth. However, most studies to date have focused on the function of lactylation on histones, and little is known about the distribution of lactylation on subcellular proteins. Here, we utilized subcellular fractionation methods to perform the global profiling of lactylation in human colon carcinoma HCT116 cells. This approach detected more unique lactylated proteins compared to the standard method when the amount of antibody and cells was equal. In total, 899 lysine lactylation sites were detected on 441 proteins, including 291 newly discovered lactylation sites and 63 newly lactylated proteins reported under the DDA and DIA acquisition modes. Functional enrichment analysis revealed that the majority of these proteins are involved in nucleosome assembly and slicesome function. For each subcellular fraction, the newly discovered lactylated proteins account for 10% to 20%. Notably, XPC not only has four new lactylation modification sites, but also one of which has been shown to be essential for the nucleotide excision repair process. Additionally, one of the newly discovered lactylation sites in scaffold attachment factor B1 (SAFB1) was found to be very important for the negative regulation of transcriptional activity. In conclusion, we describe a novel method that provides for understanding the characterization of subcellular lactylated proteins.
HostingRepositoryPRIDE
AnnounceDate2024-12-15
AnnouncementXMLSubmission_2024-12-14_21:37:37.278.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterBao qiuyu
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListlactic acid; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Eclipse
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-06-27 21:44:55ID requested
12024-12-14 21:37:37announced
Publication List
10.1021/JASMS.4C00366;
Keyword List
submitter keyword: Post-translation modification, subcellular fractionation method,Lactylation
Contact List
qiuyu Bao
contact affiliationSchool of Pharmacy, China Pharmaceutical University.
contact email3120010077@stu.cpu.edu.cn
lab head
Bao qiuyu
contact affiliationChina pharmaceutical university
contact email3120010077@stu.cpu.edu.cn
dataset submitter
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Dataset FTP location
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PRIDE project URI
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