PXD022869

PXD022869 is an original dataset announced via ProteomeXchange.

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_01:17:07.536.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

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.

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]

submitter keyword: HYPE, AMPylation, Hsp70 chaperone BiP

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

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/2021/04/PXD022869

PRIDE project URI

• PRIDE
  1. PXD022869
     1. Label: PRIDE project
     2. Name: Structural basis of chaperone regulation by a post-translational modification