30397019
2019
01
23
2160-1836
9
1
2019
01
09
G3 (Bethesda, Md.)
G3 (Bethesda)
iProteinDB: An Integrative Database of Drosophila Post-translational Modifications.
1-11
10.1534/g3.118.200637
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 Drosophila 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 Drosophila At iProteinDB, scientists can view the PTM landscape for any Drosophila protein and identify predicted functional phosphosites based on a comparative analysis of data from closely-related Drosophila species. Further, iProteinDB enables comparison of PTM data from Drosophila to that of orthologous proteins from other model organisms, including human, mouse, rat, Xenopus tropicalis, Danio rerio, and Caenorhabditis elegans.
Copyright © 2019 Hu et al.
Hu
Yanhui
Y
0000-0003-1494-1402
Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Sopko
Richelle
R
Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Chung
Verena
V
Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Foos
Marianna
M
Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Studer
Romain A
RA
European Molecular Biology Laboratory (EMBL), European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
Landry
Sean D
SD
Department of Bioinformatics, Cell Signaling Technology Inc., 3 Trask Lane, Danvers, MA 01923.
Liu
Daniel
D
Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Rabinow
Leonard
L
Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Gnad
Florian
F
Department of Bioinformatics, Cell Signaling Technology Inc., 3 Trask Lane, Danvers, MA 01923.
Beltrao
Pedro
P
European Molecular Biology Laboratory (EMBL), European Bioinformatics Institute, Wellcome Genome Campus, Hinxton, Cambridge CB10 1SD, UK.
Perrimon
Norbert
N
0000-0001-7542-472X
Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115 perrimon@receptor.med.harvard.edu.
Drosophila RNAi Screening Center, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115.
Howard Hughes Medical Institute, 77 Avenue Louis Pasteur, Boston, MA 02115.
eng
figshare
10.25387/g3.6986945
R01 DK088718
DK
NIDDK NIH HHS
United States
R01 GM067761
GM
NIGMS NIH HHS
United States
P01 CA120964
CA
NCI NIH HHS
United States
R01 GM084947
GM
NIGMS NIH HHS
United States
R01 GM067761
GM
NIGMS NIH HHS
United States
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
2019
01
09
United States
G3 (Bethesda)
101566598
2160-1836
Drosophila
phosphoproteomics
post-translational modification
2018
11
7
6
0
2018
11
7
6
0
2018
11
7
6
0
epublish
30397019
g3.118.200637
10.1534/g3.118.200637
PMC6325894