iProteinDB Edit

Citations: 1

z-index: 1

Basic information
Short name iProteinDB
Full name INTEGRATED PROTEIN DATABASE OF PTM FOR DROSOPHILA GENES
Description an online integrated protein database and resource tool for providing information on post-translational modifications (PTMs) in Drosophila species.
URL https://www.flyrnai.org/tools/iproteindb
Year founded 2017
Last update & version 2018 v1.0.1
Accessibility Accessible
Contact information

The contact information is provided to facilitate update of database information, and it is curated based on the contact details in the database or the related publications. To ensure effective contact with database constructors, we give priority to the contact details in the database.

University/Institution Harvard Medical School
Address New Research Building Perrimon Lab 77 Avenue Louis Pasteur Boston, MA
City Boston
Province/State
Country/Region United States
Contact name (PI/Team) Yanhui Hu
Contact email (PI/Helpdesk) claire_hu@genetics.med.harvard.edu
Data information
Data object
Data type
Database category
Major organism
Keyword
Publications
  • iProteinDB: An Integrative Database of Post-translational Modifications. [PMID: 30397019]
    Yanhui Hu, Richelle Sopko, Verena Chung, Marianna Foos, Romain A Studer, Sean D Landry, Daniel Liu, Leonard Rabinow, Florian Gnad, Pedro Beltrao, Norbert Perrimon

    Post-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing their stability, interactions, activity and localization, and is critical in many signaling pathways. The best characterized PTM is phosphorylation, whereby a phosphate is added to an acceptor residue, most commonly serine, threonine and tyrosine in metazoans. As proteins are often phosphorylated at multiple sites, identifying those sites that are important for function is a challenging problem. Considering that any given phosphorylation site might be non-functional, prioritizing evolutionarily conserved phosphosites provides a general strategy to identify the putative functional sites. To facilitate the identification of conserved phosphosites, we generated a large-scale phosphoproteomics dataset from embryos collected from six closely-related species. We built iProteinDB (https://www.flyrnai.org/tools/iproteindb/), a resource integrating these data with other high-throughput PTM datasets, including vertebrates, and manually curated information for At iProteinDB, scientists can view the PTM landscape for any protein and identify predicted functional phosphosites based on a comparative analysis of data from closely-related species. Further, iProteinDB enables comparison of PTM data from to that of orthologous proteins from other model organisms, including human, mouse, rat, , and

    G3 (Bethesda) 2019:9(1)

    1 Citations (from Europe PMC, 2019-06-08)

Rank

  • Ranking in all databases: No. 3203
  • Ranking in category/categories:
    • Modification: No. 131
The box plots depict Z-index distribution for all databases in Database Commons and for specific database category/categories. The red line indicates log2(Z-index) of iProteinDB.

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Record metadata

  • Created on: 2019-01-04
    • ***d@***c.cn [2019-01-11]
    • ***d@***c.cn [2019-01-11]
    • ***d@***c.cn [2019-01-04]

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