Scop3P: A Comprehensive Resource of Human Phosphosites
within Their Full Context
Posted on 2020-06-18 - 11:03
Protein
phosphorylation is a key post-translational modification
in many biological processes and is associated to human diseases such
as cancer and metabolic disorders. The accurate identification, annotation,
and functional analysis of phosphosites are therefore crucial to understand
their various roles. Phosphosites are mainly analyzed through phosphoproteomics,
which has led to increasing amounts of publicly available phosphoproteomics
data. Several resources have been built around the resulting phosphosite
information, but these are usually restricted to the protein sequence
and basic site metadata. What is often missing from these resources,
however, is context, including protein structure mapping, experimental
provenance information, and biophysical predictions. We therefore
developed Scop3P: a comprehensive database of human phosphosites within
their full context. Scop3P integrates sequences (UniProtKB/Swiss-Prot),
structures (PDB), and uniformly reprocessed phosphoproteomics data
(PRIDE) to annotate all known human phosphosites. Furthermore, these
sites are put into biophysical context by annotating each phosphoprotein
with per-residue structural propensity, solvent accessibility, disordered
probability, and early folding information. Scop3P, available at https://iomics.ugent.be/scop3p, presents a unique resource for visualization and analysis of phosphosites
and for understanding of phosphosite structure–function relationships.
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Ramasamy, Pathmanaban; Turan, Demet; Tichshenko, Natalia; Hulstaert, Niels; Vandermarliere, Elien; Vranken, Wim; et al. (2020). Scop3P: A Comprehensive Resource of Human Phosphosites
within Their Full Context. ACS Publications. Collection. https://doi.org/10.1021/acs.jproteome.0c00306
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AUTHORS (7)
PR
Pathmanaban Ramasamy
DT
Demet Turan
NT
Natalia Tichshenko
NH
Niels Hulstaert
EV
Elien Vandermarliere
WV
Wim Vranken
LM
Lennart Martens