Characterization of the Regulation Mechanism of Protein Kinase CK2 by IP6 and Nopp140, an Intrinsically Disordered Protein
β Scribed by Lee, Won-Kyu; Hyeon Son, Sang; Na, Jung-Hyun; Kim, Soo-Youl; Ho Lee, Hyung; Gyu Yu, Yeon
- Book ID
- 123192032
- Publisher
- Biophysical Society
- Year
- 2013
- Tongue
- English
- Weight
- 36 KB
- Volume
- 104
- Category
- Article
- ISSN
- 0006-3495
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π SIMILAR VOLUMES
Protein kinase CK2 is a ubiquitous eukaryotic ser/thr protein kinase. The active holoenzyme is a heterotetrameric protein composed of catalytic (β£ and β£Π) and regulatory (β€) subunits that phosphorylates many different protein substrates and appears to be involved in the regulation of cell division.
We characterized a 54-kDa human protein kinase recognized by an antiserum raised against the human myotonin protein kinase. This protein kinase displays a serine/threonine kinase activity in the heart and a tyrosine kinase activity in the skeletal muscle. Both kinase activities were attributed to th