|PROSITE documentation PDOC51203 [for PROSITE entry PS51203]|
The bipartite CS domain, which was named after CHORD-containing proteins and SGT1 , is a ~100-residue protein-protein interaction module. It is only present in eukaryota (alveolata, fungi, metazoa, and plant divisions). The CS domain can be found in stand-alone form, as well as fused with other domains, such as CHORD, SGS (see <PDOC51048>), TPR (see <PDOC50005>), cytochrome b5 (see <PDOC00170>) or b5 reductase, in multidomain proteins .
Some proteins known to contain a CS domain are listed below :
The profile we developed covers the entire CS domain.Note:
The CS domain is also known as the p23-like domain .Last update:
May 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Shirasu K. Lahaye T. Tan M.-W. Zhou F. Azevedo C. Schulze-Lefert P. disease resistance signaling in barley and development in C.|
|Title||A novel class of eukaryotic zinc-binding proteins is required for elegans.|
|2||Authors||Garcia-Ranea J.A. Mirey G. Camonis J. Valencia A.|
|Title||p23 and HSP20/alpha-crystallin proteins define a conserved sequence domain present in other eukaryotic protein families.|
|Source||FEBS Lett. 529:162-167(2002).|
|3||Authors||Lee Y.-T. Jacob J. Michowski W. Nowotny M. Kuznicki J. Chazin W.J.|
|Title||Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain.|
|Source||J. Biol. Chem. 279:16511-16517(2004).|