Sandbox Reserved 1656: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 12: Line 12:
==== Families ====
==== Families ====


Deubiquitinases belong to the protease family. This family is divided into five classes, according to the nature of the amino acid composition of their active site carrying out the catalysis: serine protease, cysteine proteases, acid proteases, metalloproteases, threonine proteases. DUBs belong to only two of these families: metalloproteases and cysteine proteases.  
Deubiquitinases belong to the protease family. This family is divided into five classes, according to the nature of the amino acid composition of their active site carrying out the catalysis: serine protease, [https://fr.wikipedia.org/wiki/Prot%C3%A9ase_%C3%A0_cyst%C3%A9ine cysteine proteases], acid proteases, metalloproteases, threonine proteases. DUBs belong to only two of these families: metalloproteases and cysteine proteases.  
Among the cysteine proteins, four subfamilies can be described according to their catalytic domains: ubiquitin-specific proteases (USP), les Ubiquitin C-terminal hydrolases (UCH), Otubain proteases (OTU) and Machado-joseph disease proteases (MJD). The deubiquitinases belonging to the family of metalloproteases all have a JAMM catalytic domain (JAB1/MPN/Mov34 metalloenzyme).  
Among the cysteine proteins, four subfamilies can be described according to their catalytic domains: ubiquitin-specific proteases (USP), les Ubiquitin C-terminal hydrolases (UCH), Otubain proteases (OTU) and Machado-joseph disease proteases (MJD). The deubiquitinases belonging to the family of metalloproteases all have a JAMM catalytic domain (JAB1/MPN/Mov34 metalloenzyme).  
Within these two families, DUBs are classified into subfamilies according to the differences in their amino acid sequences surrounding the catalytically active amino acid residues. <ref>PMID:15571815</ref>
Within these two families, DUBs are classified into subfamilies according to the differences in their amino acid sequences surrounding the catalytically active amino acid residues. <ref>PMID:15571815</ref>
Line 66: Line 66:


<ref>https://fr.wikipedia.org/wiki/Ubiquitination</ref> Ubiquitination https://fr.wikipedia.org/wiki/Ubiquitination
<ref>https://fr.wikipedia.org/wiki/Ubiquitination</ref> Ubiquitination https://fr.wikipedia.org/wiki/Ubiquitination
<ref>https://fr.wikipedia.org/wiki/Prot%C3%A9ase_%C3%A0_cyst%C3%A9ine</ref> Cysteine protease https://fr.wikipedia.org/wiki/Prot%C3%A9ase_%C3%A0_cyst%C3%A9ine
<ref>hhttps://fr.wikipedia.org/wiki/Microtubule</ref> Microtubule https://fr.wikipedia.org/wiki/Microtubule