Sandbox Reserved 1656

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Generalities

Function

Deubiquitinases or Deubiquitinating enzymes (DUBs) are key enzymes belonging to the vast group of proteases, allowing the degradation of ubiquitin of proteins. These enzymes are thus implicated in the regulation of protein degradation. Indeed, when a protein is going to be degraded, an enzymatic cascade will add a poly-ubiquitin fragment to the protein. This mechanism is called ubiquitination.[1] Following this step, mono or poly-ubiquitin is removed from the protein which has been degraded, by deubiquitinase. ^[3]

Families

So far, six structural families of DUBs have been discovered. Of these, five belong to the protease family and the last is a family of zinc-dependent metallo-proteases. These enzymes do not play the same role during post-translational modifications : most families allow the removal of one of their substrates, ubiquitin, from the protein (USPs, OTUs, UCHs, Josephins, MINDYs, JAMMs, ULPs). While the Ub cascade family allows ubiquitin to be added to proteins and the UBDs family allow reading and therefore protein-ubiquitin recognition.

Localization

Structure

Biological role

Disease

The involvement of deubiquitinases in diseases is still poorly understood. However, it is known that they play a role in various physiological processes, particularly in the case of cancers. ^[4]

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.