Ubiquitin Structure & Function

Ubiquitin is a single 8565 M_r polypeptide consisting of 76 amino acid residues. Ub is highly known for its role in ATP-dependant protein degradation.

spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D load='1ubq' size='350' frame='false' scene=
1ubq, resolution 1.80Å (default scene)
Structural annotation: Resources: CATH : 1Ubqa00 InterPro : Ipr000626, Ipr019954, Ipr019955, Ipr019956 SCOP : d1ubqa_
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
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.

Proteopedia Page Contributors and Editors (what is this?)

Jaclyn Gordon, Joel L. Sussman, Karsten Theis, Andrea Gorrell, Michal Harel, Alexander Berchansky, David Canner