Proteins are major functional molecules that physically and functionally interact to carry out cellular processes. The physical interactions are generally mediated by domain-level interactions. Thus, novel protein-protein interactions can be predicted using various computational methods based on domain-domain interactions, using resolved structures of protein complexes. Functional protein interactions can be inferred based on shared domains between proteins, since proteins involved in the same biological processes tend to harbor common domains. We recently developed a method of inferring functional interactions between proteins using associations between their domain compositions, which can be represented as domain profiles. Since the method requires only protein domain annotations, it can be easily applied to any species with a sequenced genome. Here, we describe in detail the method of generating domain profiles for proteins and measuring the association between them to infer functional interactions between proteins. We also demonstrate that domain profile association can be used to successfully construct a large-scale functional network of human proteins.
|Title of host publication||Methods in Molecular Biology|
|Publisher||Humana Press Inc.|
|Number of pages||10|
|Publication status||Published - 2020|
|Name||Methods in Molecular Biology|
Bibliographical noteFunding Information:
This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korean Government (MSIT) (NRF-2018M3C9A5064709, NRF-2018R1A5A2025079) to I.L.
© Springer Science+Business Media, LLC, part of Springer Nature 2020.
All Science Journal Classification (ASJC) codes
- Molecular Biology