ERK (Extracellular Signal Regulated Kinase) or MAP kinase is an intracellular signaling molecule. ERK is involved in regulation of various functions i.e. cell proliferation, cell migrations, cell survival and many more. It gets activated in response of various stimuli like growth factors, cytokines, virus, second messengers, transforming agents and carcinogens. While transferring signals from cell surface receptors to cell nucleus, ERK interacts with a numbers of proteins. Physiochemical and functional characterization of these proteins is little known. Thus, we attempted to study physiochemical and functional properties of ERK interacting proteins using bio-computational tools. ExPASy and SOSUI server suggested 22 ERK interacting proteins. Physical and chemical parameters of these ERK interacting partners indicated higher percentage of hydrophobic amino acid and leucine as major constituent. Moreover, the instability index indicated that four proteins are stable in over wide range temperature in vitro, and remaining eighteen proteins were found unstable. In addition, SOSUI server showed that fifteen proteins were soluble and six are trans-membrane in nature.
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