RT Journal
A1 Semple, Colin A.M.
A1 RIKEN GER Group
A1 GSL Members
T1 The Comparative Proteomics of Ubiquitination in Mouse
JF Genome Research 
JO Genome Research 
YR 2003 
FD June 01 
VO 13 
IS 6b 
SP 1389 
OP 1394 
DO 10.1101/gr.980303 
UL http://genome.cshlp.org/content/13/6b/1389.abstract 
AB Ubiquitination is a common posttranslational modification in eukaryotic  cells, influencing many fundamental cellular processes. Defects in  ubiquitination and the processes it mediates are involved in many human  disease states. The ubiquitination of a substrate involves four classes of  enzymes:a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme  (E2), a ubiquitin protein ligase (E3), and a de-ubiquitinating enzyme (DUB). A  substantial number of E1s (four), E2s (13), E3s (97), and DUBs (six) that were  previously unknown in the mouse are included in the FANTOM2 Representative  Transcript and Protein Set (RTPS). Many of the genes encoding these proteins  will constitute promising candidates for involvement in disease. In addition,  the RTPS provides the basis for the most comprehensive survey of  ubiquitination-associated proteins across eukaryotes undertaken to date.  Comparisons of these proteins across human and other organisms suggest that  eukaryotic evolution has been associated with an increase in the number and  diversity of E3s (possessing either zinc-finger RING, F-box, or HECT domains)  and DUBs (containing the ubiquitin thiolesterase family 2 domain). These  increases in numbers are too large to be accounted for by the presence of  fragmentary proteins in the data sets examined. Much of this innovation  appears to have been associated with the emergence of multicellular organisms,  and subsequently of vertebrates, increasing the opportunity for complex  regulation of ubiquitination-mediated cellular and developmental  processes.