|PROSITE documentation PDOC00633 [for PROSITE entry PS00796]|
The 14-3-3 proteins [1,2,3] are a family of closely related acidic homodimeric proteins of about 30 Kd which were first identified as being very abundant in mammalian brain tissues and located preferentially in neurons. The 14-3-3 proteins seem to have multiple biological activities and play a key role in signal transduction pathways and the cell cycle. They interacts with kinases such as PKC or Raf-1; they seem to also function as protein-kinase dependent activators of tyrosine and tryptophan hydroxylases and in plants they are associated with a complex that binds to the G-box promoter elements.
The 14-3-3 family of proteins are ubiquitously found in all eukaryotic species studied and have been sequenced in fungi (yeast BMH1 and BMH2, fission yeast rad24 and rad25), plants, Drosophila, and vertebrates. The sequences of the 14-3-3 proteins are extremely well conserved. As signature patterns we have selected two highly conserved regions: the first is a peptide of 11 residues located in the N-terminal section; the second, a 20 amino acid region located in the C-terminal section.Expert(s) to contact by email:
December 2004 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|Title||14-3-3 proteins on the MAP.|
|Source||Trends Biochem. Sci. 20:95-97(1995).|
|Title||14-3-3: modulators of signaling proteins?|
|3||Authors||Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., Gamblin S.J.|
|Title||Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways.|