DNA sequences encoding human TcAK1 kinase

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid

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4352401, 4353201, 536 231, 536 235, 536 2431, 935 2, 935 6, 935 77, 935 78, C12Q 168, C07H 2104, C12N 1585

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058637290

ABSTRACT:
Entry into mitosis requires the activity of the Cdc25C phosphatase which functions to activate Cdc2/Cyclin B. In asychronously growing cells, Cdc25C is stoichiometrically phosphorylated on serine 216. Levels of serine 216 phosphorylation remain constant throughout the G1-, S- and G2-phases of the cell cycle. A human kinase, denoted TcAK1 (for Twenty-five C Associated protein Kinase) that phosphorylates Cdc25C on serine 216 has been cloned and sequenced. A method is also provided for measuring levels of TcAK1 in RNA or of TcAK1 protein in cells. Phosphorylation of Cdc25C on serine 216 with TCAK1 creates a 14-3-3 recognition motif. The interaction between Cdc25C and 14-3-3 proceeds in a phosphorylation-specific manner. TcAK1 functions to mediate interaction between 14-3-3 proteins and other cellular proteins associated with oncogenesis or key signalling events.

REFERENCES:
Ogg et al. (1994), "Purification of a Serine Kinase That Associates with and Phosphorylates Human Cdc25C on Serine 216," J. Biol. Chem. 269:30461-30469.
Ford et al. (1994), "14-3-3 Protein Homologs Required for the DNA Damage Checkpoint in Fission Yeast," Science 265:533-535.
Morrison (1994), "14-3-3: Modulators of Signaling Proteins?" Science 266:56-57.
Aitken (1995), "14-3-3 Proteins on the MAP," TIBS 20:3pp.
Muslin et al. (1996), "Interaction of 14-3-3 with Signaling Proteins is Mediated by the Recognition of Phosphoserine," Cell 84:889-897.
Accession M80359.
A Usubel et al Editors of Short Protocols In Molecular Biology. John Wiley & Sons, New York (1989) pp. 75-79, 106-116, and 158-159.
Sequence Alignment of p78 and Seq. ID Nos. 1 & 2.

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