PXD029747 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Whole-cell abundance profiling and interaction analysis of UBQLN2 |
Description | To address whether expression of ALS/FTD-associated UBQLN2 mutant variants changes the cellular proteome, we performed label-free quantification-based global protein abundance profiling of patient-derived LCLs and CRISPR engineered HeLa cells. UBQLN2 mutant in both cell lines carried the mutation T487I or P497S both of which were reported to cause ALS (Deng et al., 2011; Williams et al, 2012). In addition, HeLa cells stably expressing HA-tagged MAP1B (HA-MAP1B) were subjected to HA immunoprecipitation (IP) followed by mass spectrometry to identify MAP1B interacting proteins. |
HostingRepository | PRIDE |
AnnounceDate | 2022-06-24 |
AnnouncementXML | Submission_2022-06-24_02:44:54.176.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Christian Behrends |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | carbamoylated residue; monohydroxylated residue |
Instrument | Q Exactive HF |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-11-15 06:38:18 | ID requested | |
⏵ 1 | 2022-06-24 02:44:54 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: UBQLN2, whole proteome, HA-IP, HeLa, LCL, ALS/FTD |
Contact List
Christian Behrends |
contact affiliation | Munich Cluster of Systems Neurology, LMU Munich, Germany |
contact email | christian.behrends@mail03.med.uni-muenchen.de |
lab head | |
Christian Behrends |
contact affiliation | SyNergy, LMU München |
contact email | christian.behrends@mail03.med.uni-muenchen.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD029747
- Label: PRIDE project
- Name: Whole-cell abundance profiling and interaction analysis of UBQLN2