Molecules that are experimentally shown to be associated potentially by sharing just one interactor. Often associated molecules are co-purified by a pull-down or coimmunoprecipitation and share the same bait molecule.
This class of approaches is characterised by the use of affinity resins as tools to purify molecule of interest (baits) and their binding partners. The baits can be captured by a variety of high affinity ligands linked to a resin - for example, antibodies specific for the bait itself, antibodies for specific tags engineered to be expressed as part of the bait or other high affinity binders such as glutathione resins for GST fusion proteins, metal resins for histidine-tagged proteins.
Robert T. Morris, Kelly A. Doroshenk, Andrew J. Crofts, Nicholas Lewis, Thomas W. Okita, and John J. Wyrick
contact-email
rtmorris@wsu.edu
submitted
2010-7-27: Robert T. Morris; Wyrick lab, Washington State University, USA
data-processing
Where possible the identifiers in the publication were mapped to UniProt KB entries from the locus identifiers provided by the authors. The duplicate in the submission table were removed. Where mapping was not possible the locus identifiers were used to obtian the protein sequence and IntAct protein entries were constructed.
url
http://www.bioinformatics2.wsu.edu/RiceRBP
Attributes (3)
Attributes
3 attribute(s)
comment
Imported from IntAct, European Bioinformatics Institute, release date 2010-09-03.
EBI-2900369
MI:0914
4342697
39947
Q84ZP1
IPR000630
GO:0005840
NP_001059160.1
q84zp1_orysj
19685898