This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Ubiquitin Structure & Function
From Proteopedia
Ubiquitin is a single 8565 Mr polypeptide consisting of 76 amino acid residues. Ub is highly known for its role in ATP-dependant protein degradation.
| |||||||||
| 1ubq, resolution 1.80Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Introduction
Ubiquitin is one of the most highly conserved eukaryotic proteins. Primary structures found throughout ubiquitin are identical in all bovine, insects and human ubiquitin. The only difference observed amongst these species is seen in the terminal Gly-Gly residues. Yeast and oat ubiquitin only differ in three of the 76 residues when compared to ubiquitin found in higher eukaryotes. Ubiquitin can not only be found in the nucleus, but in the cytoplasm and cell-surface membrane as well. Put structure in with intro...
Function
At first, ubiquitin was believed to be a hormone involed in inducing the differentiation of lymphocytes and activating adenylate cyclase [1].
Proteopedia Page Contributors and Editors (what is this?)
Jaclyn Gordon, Joel L. Sussman, Michal Harel, David Canner, Andrea Gorrell, Alexander Berchansky, Karsten Theis
