If you have physical interactions to curate, please read the Directionality section carefully.
We recommend that you only annotate interactions that you think are biologically meaningful. For example, don't include known or suspected contaminants from mass spectrometry results (e.g. ribosomal proteins, translation factors, 'sticky' proteins).
When you choose 'Physical interaction', a popup appears with two pulldown menus and a text field for optional comments.
Choose an evidence type from the first pulldown menu. Some evidence types have a brief description that indicates the directionality. Further information on evidence supporting physical interactions, including examples of experiment types in each category, is available an the BioGRID help wiki and in the Directionality section below.
Choose the interacting gene from the second pulldown menu. Click 'OK' to finish the annotation and close the popup.
Note that only pairwise genetic interactions can be annotated in Canto.
Some experiments that detect physical interactions have an inherent directionality. For example, in a typical two-hybrid experiment one protein (A) is fused to a DNA binding domain and a second (B) is fused to a transcription activation domain. The reciprocal experiment, with A fused to the activation domain and B fused to the DNA binding domain, may or may not have been done.
For such "asymmetric" interactions, Canto allows you to curate in only one direction starting from the gene you select first, as indicated in the interaction type selector.
If the evidence description looks the wrong way around, you will have to change genes and start again. (You can finish and then delete an interaction annotation if you find that you have started with the wrong gene.)
|Evidence||Relationship between Interactor A (bait) and Interactor B (prey)|
|Affinity Capture-Luminescence||affinity captures|
|Affinity Capture-MS||affinity captures|
|Affinity Capture-RNA||affinity captures|
|Affinity Capture-Western||affinity captures|
|FRET (fluorescence resonance energy transfer)||fluorescence resonance energy donor to|
|Protein-peptide||binds to peptide|
|Protein-RNA||binds to RNA|
|Two-hybrid||binds activation domain construct with|
|Evidence||Relationship between gene A and gene B products|
|Co-crystal Structure||co-crystallizes with|
|Reconstituted Complex||forms complex with|
|PCA* (protein-fragment complementation assay)||interacts with|