|PROSITE documentation PDOC50957 [for PROSITE entry PS50957]|
The Josephin domain is an eukaryotic protein module of about 180 residues, which occurs in stand-alone form in Josephin-like proteins, and as an amino-terminal domain associated with two or three copies of the ubiquitin-interacting motif (UIM) (see <PDOC50330>) in ataxin 3-like proteins. Although it has originally been proposed that the Josephin domain could be an all-α helical domain distantly related to ENTH (see <PDOC50942>) and VHS (see <PDOC50179>) domains involved in membrane trafficking and regulatory adaptor function , it is now believed that it is a mainly α helical cysteine-protease domain predicted to be active against ubiquitin chains or related substrates [2,3].
Some proteins known to contain a Josephin domain are listed below:
The profile we developed spans the entire Josephin domain.Last update:
January 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Albrecht M. Hoffmann D. Evert B.O. Schmitt I. Wuellner U. Lengauer T.|
|Title||Structural modeling of ataxin-3 reveals distant homology to adaptins.|
|2||Authors||Scheel H. Tomiuk S. Hofmann K.|
|Title||Elucidation of ataxin-3 and ataxin-7 function by integrative bioinformatics.|
|Source||Hum. Mol. Genet. 12:2845-2852(2003).|
|3||Authors||Burnett B. Li F. Pittman R.N.|
|Title||The polyglutamine neurodegenerative protein ataxin-3 binds polyubiquitylated proteins and has ubiquitin protease activity.|
|Source||Hum. Mol. Genet. 12:3195-3205(2003).|