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Gene Review:

ccnh - cyclin H

Xenopus laevis

Devault, A. et al., Martinez, A.M. et al.

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High impact information on ccnh-A

By mutational analysis, we demonstrate that in addition to its role in promotion of cyclin H binding, S170 phosphorylation plays a direct role in the control of CAK activity [1].

Anatomical context of ccnh-A

The kinase responsible for Thr161-Thr160 phosphorylation and activation of cdc2/cdk2 (CAK:cdk-activating kinase) has been shown previously to comprise at least two subunits, cdk7 and cyclin H. An additional protein co-purified with CAK in starfish oocytes, but its sequencing did not reveal any similarity with any known protein [2].

References

Dual phosphorylation of the T-loop in cdk7: its role in controlling cyclin H binding and CAK activity. Martinez, A.M., Afshar, M., Martin, F., Cavadore, J.C., Labbé, J.C., Dorée, M. EMBO J. (1997) [Pubmed]
MAT1 ('menage à trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK. Devault, A., Martinez, A.M., Fesquet, D., Labbé, J.C., Morin, N., Tassan, J.P., Nigg, E.A., Cavadore, J.C., Dorée, M. EMBO J. (1995) [Pubmed]

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