Casein kinase
Casein kinase
Casein kinase (pronounced: kay-seen kai-nase) is a type of protein kinase that phosphorylates serine and threonine residues in proteins. It is named after its initial discovery as an enzyme that phosphorylates the milk protein casein.
Etymology
The term "casein kinase" is derived from the protein it was first discovered to phosphorylate, casein. "Casein" comes from the Latin caseus, meaning "cheese", as it is a major component of cheese. "Kinase" is derived from the Greek kinēsis, meaning "movement", referring to the enzyme's ability to transfer phosphate groups.
Function
Casein kinase is involved in a wide range of cellular processes, including cell division, protein synthesis, and signal transduction. It is known to phosphorylate a variety of target proteins, including transcription factors, structural proteins, and enzymes.
Types
There are two main types of casein kinase: Casein kinase 1 (CK1) and Casein kinase 2 (CK2). CK1 is a monomeric enzyme that is involved in cellular differentiation, circadian rhythm, and other processes. CK2 is a tetrameric enzyme that is involved in cell proliferation, cell cycle progression, and apoptosis.
Related Terms
- Phosphorylation: The process by which a phosphate group is added to a molecule, often a protein. Casein kinase is an enzyme that carries out this process.
- Protein kinase: A type of enzyme that modifies other proteins by chemically adding phosphate groups to them. Casein kinase is a type of protein kinase.
- Serine and Threonine: Amino acids that are often the target of phosphorylation by casein kinase.
External links
- Medical encyclopedia article on Casein kinase
- Wikipedia's article - Casein kinase
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