PXD022869 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Structural basis of chaperone regulation by a post-translational modification |
Description | The Hsp70 chaperone BiP is covalently modified with adenosine monophosphate (referred to as AMPylation) in order to adapt its activity to the fluctuating folding load within the endoplasmic reticulum. This modification is catalyzed by the only human representative of the family of filamentation induced by cyclic adenosine monophosphate (Fic) enzymes HYPE/FICD. The structural basis for BiP binding and AMPylation has remained elusive due to the low affinity of enzyme substrate complexes. |
HostingRepository | PRIDE |
AnnounceDate | 2021-04-28 |
AnnouncementXML | Submission_2021-04-28_01:12:28.535.xml |
DigitalObjectIdentifier | https://dx.doi.org/10.6019/PXD022869 |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Christoph Krisp |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | O-(phospho-5'-adenosine)-L-threonine |
Instrument | Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-12-02 08:03:50 | ID requested | |
⏵ 1 | 2021-04-28 01:12:29 | announced | |
2 | 2021-04-28 01:17:08 | announced | 2021-04-28: Updated project metadata. |
Publication List
10.1038/S41467-021-22596-0; |
Fauser J, Gulen B, Pogenberg V, Pett C, Pourjafar-Dehkordi D, Krisp C, H, ö, pfner D, K, ö, nig G, Schl, ü, ter H, Feige MJ, Zacharias M, Hedberg C, Itzen A, Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD. Nat Commun, 12(1):2426(2021) [pubmed] |
Keyword List
submitter keyword: HYPE, AMPylation, Hsp70 chaperone BiP |
Contact List
Prof. Dr. Aymelt Itzen |
contact affiliation | University Medical Center Hamburg-Eppendorf Institute of Biochemistry and Signal Transduction Hamburg, Germany |
contact email | a.itzen@uke.de |
lab head | |
Christoph Krisp |
contact affiliation | University Medical Center Hamburg-Eppendorf Institute of Clinical Chemistry and Laboratory Medicine Mass Spectrometric Proteomics |
contact email | c.krisp@uke.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD022869
- Label: PRIDE project
- Name: Structural basis of chaperone regulation by a post-translational modification