|Kretzschmar et al. (1994):||Functional deletion analyses revealed a bipartite structure of p15 comprising an amino-terminal regulatory domain and a carboxy-terminal cryptic DNA-binding domain. We provide evidence that activity of p15 is controlled by protein kinases that target the regulatory domain. Structural and functional similarities, including sequence homology to domains essential for cofactor function, cofactor activity, promiscuity with respect to transcriptional activators, and interactions with components of the basal transcription machinery, relate this novel cellular cofactor to viral immediate-early transcriptional regulators.|
|Kretzschmar, M; Kaiser, K; Lottspeich, F; Meisterernst, M. 1994. A novel mediator of class II gene transcription with homology to viral immediate-early transcriptional regulators. Cell 78(3):525-34 PubMed|
|Number of species containing the TAP:||123|
|Number of available proteins:||306|
The colour code corresponds to the rules for the domains:
should not be contained
(Domain names are clickable)
Phylogenetic tree for Archeaplastida:
No tree was calculated yet.
The following table shows the distribution of Coactivator p15 over all species included in TAPscan. The values for e.g. a specific kingdom are shown in the tree below if you expand the tree for that kingdom.