Annual Scientific Report 2015

Molecular Interactions
The Molecular Interactions Team provides public-domain interaction data, the
use of which ranges from network analysis of large-scale datasets to obtaining
a detailed understanding of specific protein-binding interfaces. The team also
produces the Complex Portal, a reference resource for macromolecular complexes.
The Molecular Interactions Team, created in April
2015, was previously part of the Proteomics Services
team. We have responsibility for the long-established
IntAct molecular interaction database, and for the
more recent Complex Portal. Our team will continue to
support the molecular interaction community standards
published by the HUPO Proteomics Standards
Initiative, and contribute to their further development.
We actively encourage the direct deposition of data
by data producers as part of the publication process,
as this provides the best opportunities to ensure the
information is represented accurately in the database.
IntAct is the major deposition database for groups
generating high-throughput, two-hybrid and affinitypurified
Mass Spectrometry data. We curate small-scale
data from the scientific literature, with strict qualitycontrol
procedures to ensure we provide the highest
quality reference datasets.
The Complex Portal has increased in content
and coverage since its launch in 2014. Successful
collaborations with groups such as the Saccharomyces
Genome Database have led to a shared curation effort
and broadened community access to domain-specific
expertise.
Major achievements
A To meet the changing demands that arise from
the ever-growing complexity of interaction data, we
updated the standard format for molecular interaction
data (PSI-MI XML3.0). The format now allows for the
description of allosteric interactions, dynamic data
and protein-complex data abstracted from multiple
publications. It also offers improved representation of
the effect of a mutant or variant on an interaction.
We are major contributors to the IMEx Consortium of
interaction databases, which manages curation efforts
over multiple resources. As of December 2015, IntAct
database made almost 600,000 binary interaction
evidences publicly available. Its database
infrastructure is shared as a curation platform by 12
external collaborators.
The Complex Portal contained over 1400 manually
curated complexes at the end of 2015. We launched
an innovative graphical tool in the Complex Portal,
which enables users to visualise complex topology and
stoichiometry. This tool, originally developed by the
Rapsilber group at the University of Edinburgh, was
adapted by our developers to work with a new Java
library (JAMI).
The Shelterin (Telosome) complex is
a DNA-binding protein complex that
associates with the telomeres that cap
the ends of eukaryotic chromosomes and
distinguishes them from sites of DNA
damage thus sheltering chromosome ends
from being inappropriately processed by
the DNA repair machinery. Consequently
it plays an essential role in maintaining
telomere structure and integrity. Three
subunits can interact directly either
with single-stranded (POT1) or doublestranded
telomeric DNA (TERF1 &
TERF2).
www.ebi.ac.uk/intact/complex/
details/EBI-10887677
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2015 EMBL-EBI Annual Scientific Report