VPTMdb: a viral posttranslational modification database. Issue 4 (22nd October 2020)
- Record Type:
- Journal Article
- Title:
- VPTMdb: a viral posttranslational modification database. Issue 4 (22nd October 2020)
- Main Title:
- VPTMdb: a viral posttranslational modification database
- Authors:
- Xiang, Yujia
Zou, Quan
Zhao, Lilin - Abstract:
- Abstract: In viruses, posttranslational modifications (PTMs) are essential for their life cycle. Recognizing viral PTMs is very important for a better understanding of the mechanism of viral infections and finding potential drug targets. However, few studies have investigated the roles of viral PTMs in virus–human interactions using comprehensive viral PTM datasets. To fill this gap, we developed the first comprehensive viral posttranslational modification database (VPTMdb) for collecting systematic information of PTMs in human viruses and infected host cells. The VPTMdb contains 1240 unique viral PTM sites with 8 modification types from 43 viruses (818 experimentally verified PTM sites manually extracted from 150 publications and 422 PTMs extracted from SwissProt) as well as 13 650 infected cells' PTMs extracted from seven global proteomics experiments in six human viruses. The investigation of viral PTM sequences motifs showed that most viral PTMs have the consensus motifs with human proteins in phosphorylation and five cellular kinase families phosphorylate more than 10 viral species. The analysis of protein disordered regions presented that more than 50% glycosylation sites of double-strand DNA viruses are in the disordered regions, whereas single-strand RNA and retroviruses prefer ordered regions. Domain–domain interaction analysis indicating potential roles of viral PTMs play in infections. The findings should make an important contribution to the field of virus–humanAbstract: In viruses, posttranslational modifications (PTMs) are essential for their life cycle. Recognizing viral PTMs is very important for a better understanding of the mechanism of viral infections and finding potential drug targets. However, few studies have investigated the roles of viral PTMs in virus–human interactions using comprehensive viral PTM datasets. To fill this gap, we developed the first comprehensive viral posttranslational modification database (VPTMdb) for collecting systematic information of PTMs in human viruses and infected host cells. The VPTMdb contains 1240 unique viral PTM sites with 8 modification types from 43 viruses (818 experimentally verified PTM sites manually extracted from 150 publications and 422 PTMs extracted from SwissProt) as well as 13 650 infected cells' PTMs extracted from seven global proteomics experiments in six human viruses. The investigation of viral PTM sequences motifs showed that most viral PTMs have the consensus motifs with human proteins in phosphorylation and five cellular kinase families phosphorylate more than 10 viral species. The analysis of protein disordered regions presented that more than 50% glycosylation sites of double-strand DNA viruses are in the disordered regions, whereas single-strand RNA and retroviruses prefer ordered regions. Domain–domain interaction analysis indicating potential roles of viral PTMs play in infections. The findings should make an important contribution to the field of virus–human interaction. Moreover, we created a novel sequence-based classifier named VPTMpre to help users predict viral protein phosphorylation sites. VPTMdb online web server (http://vptmdb.com:8787/VPTMdb/ ) was implemented for users to download viral PTM data and predict phosphorylation sites of interest. … (more)
- Is Part Of:
- Briefings in bioinformatics. Volume 22:Issue 4(2021)
- Journal:
- Briefings in bioinformatics
- Issue:
- Volume 22:Issue 4(2021)
- Issue Display:
- Volume 22, Issue 4 (2021)
- Year:
- 2021
- Volume:
- 22
- Issue:
- 4
- Issue Sort Value:
- 2021-0022-0004-0000
- Page Start:
- Page End:
- Publication Date:
- 2020-10-22
- Subjects:
- virus -- posttranslational modifications -- database -- bioinformatics
Genetics -- Data processing -- Periodicals
Molecular biology -- Data processing -- Periodicals
Genomes -- Data processing -- Periodicals
572.80285 - Journal URLs:
- http://bib.oxfordjournals.org ↗
http://www.oxfordjournals.org/content?genre=journal&issn=1477-4054 ↗
http://ukcatalogue.oup.com/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1093/bib/bbaa251 ↗
- Languages:
- English
- ISSNs:
- 1467-5463
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2283.958363
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 24948.xml