PXD030037 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Identification of phosphorylation sites of transcription factor after reaction with protein kinase |
Description | In previous study, we reported that MdERF17 contributes to Chl degradation in apple fruit peels. Here, we demonstrated that MdERF17 and MdMPK4 interact with each other in vitro and in vivo and raised the possibility that MdMPK4 may contribute to fruit degreening via post-transcriptional regulation of MdERF17. So an in vitro kinase assay was conducted and LC-MS/MS was used to examine the phosphorylation sites. |
HostingRepository | PRIDE |
AnnounceDate | 2022-05-20 |
AnnouncementXML | Submission_2022-05-20_01:50:49.297.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Luping Zheng |
SpeciesList | scientific name: Malus domestica; NCBI TaxID: 3750; |
ModificationList | phosphorylated residue; acetylated residue; monohydroxylated residue |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-11-29 03:10:54 | ID requested | |
⏵ 1 | 2022-05-20 01:50:50 | announced | |
Publication List
Wang S, Wang T, Li Q, Xu C, Tian J, Wang Y, Zhang X, Xu X, Han Z, Wu T, Phosphorylation of MdERF17 by MdMPK4 promotes apple fruit peel degreening during light/dark transitions. Plant Cell, 34(5):1980-2000(2022) [pubmed] |
Keyword List
submitter keyword: phosphorylation,in vitro kinase assay,LC-MS/MS |
Contact List
Shuai Wang |
contact affiliation | China Agricultural University |
contact email | 757294336@qq.com |
lab head | |
Luping Zheng |
contact affiliation | Shenzhen Institute of Advanced Technology,Chinese Academy of Sciences |
contact email | lp.zheng@siat.ac.cn |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
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[ - ]
- PRIDE
- PXD030037
- Label: PRIDE project
- Name: Identification of phosphorylation sites of transcription factor after reaction with protein kinase