PXD021712-1

PXD021712 is an original dataset announced via ProteomeXchange.

Title	Hepatitis B Core Protein is Posttranslationally Modified through K29-linked Ubiquitination
Description	Hepatitis B virus (HBV) core protein (HBc) plays many roles in the HBV life cycle such as regulation of transcription, RNA encapsidation, reverse transcription and viral release. To accomplish these functions, HBc interacts with many host proteins and undergoes different posttranslational modifications (PTMs). One of the most common PTM is ubiquitination that was shown to change function, stability, and intracellular localization of different viral proteins, but the role of HBc ubiquitination in the HBV life cycle remains unknown. Here, we found that HBc protein is posttranslationally modified through K29-linked ubiquitination. We performed a series of co-immunoprecipitation experiments with wild type HBc, lysine to arginine HBc mutants and wild type ubiquitin, single lysine to arginine ubiquitin mutants or single ubiquitin-accepting lysine constructs. We observed that HBc protein could be modified by ubiquitination in transfected as well as infected hepatoma cells. In addition, ubiquitination predominantly occurred on HBc lysine 7 and the preferred ubiquitin chain linkage was through ubiquitin-K29. Mass spectrometry (MS) analyses detected UBR5 as a potential E3 ubiquitin ligase involved in K29-linked ubiquitination. These findings emphasize that ubiquitination of HBc may play an important role in HBV life cycle.
HostingRepository	PRIDE
AnnounceDate	2020-12-01
AnnouncementXML	Submission_2020-12-01_08:37:37.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD021712
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Martin Hubalek
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monohydroxylated residue
Instrument	Orbitrap Fusion Lumos; Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2020-09-28 06:02:06	ID requested
⏵ 1	2020-12-01 08:37:38	announced

Langerov, á H, Lubyov, á B, Z, á, bransk, ý A, Hub, á, lek M, Glendov, á K, Aillot L, Hodek J, Strunin D, Janovec V, Hirsch I, Weber J, Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination. Cells, 9(12):(2020) [pubmed]

submitter keyword: Hepatitis B virus

HBc

Posttranslational modifications

Ubiquitination

Ubiquitin

E3 ubiquitin-protein ligase

Martin Hubalek
contact affiliation	Institute of Organic Chemistry an Biochmeistry, CAS, Prague, The Czech Republic
contact email	hubalek@uochb.cas.cz
lab head
Martin Hubalek
contact affiliation	Institute of Organic Chemistry and Biochemistry, Czech Academy of Science
contact email	hubalek@uochb.cas.cz
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/2020/12/PXD021712

PRIDE project URI

• PRIDE
  1. PXD021712
     1. Label: PRIDE project
     2. Name: Hepatitis B Core Protein is Posttranslationally Modified through K29-linked Ubiquitination