Biology Reference
In-Depth Information
Information on PTMs can be obtained by
using results of published low- or high-throughput proteomics
studies;
using some specific high-quality prediction tools (e.g. for signal
sequence, transit peptide, N-glycosylation, etc.); or
propagation from already annotated orthologous proteins. This
process must be carried out with the utmost care, since it is impor-
tant to avoid propagating species- or phylum-specific PTMs outside
of their realm.
Figure 4 provides an example of entry with a predicted PTM feature.
It is also of paramount importance to correctly and fully represent
the domain structure of proteins as well as to report relevant sites and
motifs.
Annotation of topological domains (transmembrane, extracellular
regions, etc.) is made on the basis of
published experimental topological data;
transmembrane prediction tools;
results of some PTM prediction tools that offer insight into the
topology of the protein, such as GPI-anchor prediction, signal
or transit peptide prediction, etc.; or
similarity to close orthologs, complemented by a high-level
manual check to carefully estimate the specific biological context
of some topological information.
Annotation of specific validated domains and important sites
(active sites, metal-binding sites, etc.) is made on the basis of
information derived from three-dimensional (3D) structures
through software-assisted data mining of the relevant Protein
Data Bank (PDB) 9 entries;
InterPro 10 and ProRule, 11 a domain annotation rule system that
we developed to help in the annotation of important sequence
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