PXD002299

PXD002299 is an original dataset announced via ProteomeXchange.

Title	Protein ubiquitination in Aspergillus nidulans
Description	Protein ubiquitination, an evolutionarily conserved post-translational modification process in eukaryotes, and plays an important role in many biological processes. Aspergillus nidulans, a model filamentous fungus, contributes to our understanding of cellular physiology, metabolism and genetics, but its ubiquitination remains widely unknown. In this study, the ubiquitination sites in the proteome of A. nidulans were identified using a highly sensitive mass spectrometry combined with immuno-affinity enrichment of ubiquitinated peptides. The 4816 ubiquitination sites were identified in 1913 ubiquitinated proteins, accounting for 18.1% of total proteins in A. nidulans. Bioinformatic analysis suggested that the ubiquitinated proteins are associated with a number of biological functions and display various sub-cellular localizations. Meanwhile, seven motifs were revealed from the ubiquitinated peptides, and significantly over-presented in different pathways. This study presents a first proteome-wide view of ubiquitination in filamentous fungi, and provides an initial framework for exploring the physiological role of lysine ubiquitination in filamentous fungi.
HostingRepository	PRIDE
AnnounceDate	2015-09-10
AnnouncementXML	Submission_2015-09-10_06:16:17.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD002299
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Sheng-hua Ying
SpeciesList	scientific name: Aspergillus; NCBI TaxID: 5052;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; ubiquitination signature dipeptidyl lysine
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2015-06-03 07:21:24	ID requested
⏵ 1	2015-09-10 06:16:18	announced

Chu XL, Feng MG, Ying SH, Qualitative ubiquitome unveils the potential significances of protein lysine ubiquitination in hyphal growth of Aspergillus nidulans. Curr Genet, 62(1):191-201(2016) [pubmed]

curator keyword: Biological

submitter keyword: Aspergillus nidulans, mycelial dvelopment, ubiquitination, LC-MSMS

Sheng-hua Ying
contact affiliation	College of Life Sciences, Zhejiang University, China
contact email	yingsh@zju.edu.cn
lab head
Sheng-hua Ying
contact affiliation	Zhejiang University
contact email	yingsh@zju.edu.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002299
     1. Label: PRIDE project
     2. Name: Protein ubiquitination in Aspergillus nidulans