EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.3.2.23 | more |
isoform Pex4 can form a disulfide bond between the cysteine residues at positions 105 and 146. Mutating the disulfide forming cysteine residues to serines does not disturb the secondary structure of the protein but does reduce the in vitro activity of Pex4. Structure of mutant C105S/C146S in complex with the soluble domain of peroxisomal membrane protein Pex22 shows a narrowing of the active site cleft, caused by loss of the disulfide bond. This modification of the active site microenvironment is likely to restrict access of ubiquitin to the active site cysteine, modulating Pex4 activity |
735257 |
| 2.3.2.23 | more |
ubiquitination is involved in myriad cell and disease pathways. The ubiquitin-conjugating E2 is the central player in the ubiquitin-transfer pathway |
723874 |
| 2.3.2.23 | sumoylation |
conjugation of the small ubiquitin-like modifier (SUMO) to protein substrates is an important disease-associated posttranslational modification. The E2 enzyme Ubc9 is sumoylated |
758642 |
| 2.3.2.23 | sumoylation |
SUMO modification of an E2 occurs on the polyUb chain-building E2, Ube2K. Like Ube2I, the site of modification is on helix alpha1, but on a residue in the E1 and E3 binding interface, consistent with the decreased activity observed in vitro |
759030 |
