Home News About DMDM Database Statistics Research Publications Contact  

 
Click for a Larger Image
  Domain Name: cpn60
cpn60 chaperonin family. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings. Archaeal cpn60 (thermosome), together with TF55 from thermophilic bacteria and the eukaryotic cytosol chaperonin (CTT), belong to the type II group of chaperonins. Cpn60 consists of two stacked octameric rings, which are composed of one or two different subunits. Their common function is to sequester nonnative proteins inside their central cavity and promote folding by using energy derived from ATP hydrolysis.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 22
Total Disease Mutations Found: 12
This domain occurred 11 times on human genes (17 proteins).



  BARDET-BIEDL SYNDROME 1, MODIFIER OF
  BARDET-BIEDL SYNDROME 6
  BARDET-BIEDL SYNDROME 6, INCLUDED
  LEUKODYSTROPHY, HYPOMYELINATING, 4
  MCKUSICK-KAUFMAN SYNDROME
  SPASTIC PARAPLEGIA 13


Tips:
 If you've navigated here from a protein, hovering over a position on the weblogo will display the corresponding protein position for that domain position.

 The histograms below the weblogo indicate mutations found on the domain. Red is for disease (OMIM) and blue is for SNPs.

 Functional Features are displayed as orange boxes under the histograms. You can choose which features are displayed in the box below.



Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
ATP/Mg binding site
ring oligomerisation inte
stacking interactions





















Weblogos are Copyright (c) 2002 Regents of the University of California




Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

   |   1000 Hilltop Circle, Baltimore, MD 21250   |   Department of Biological Sciences   |   Phone: 410-455-2258