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Solution structure of a membrane-anchored ubiquitin-fold (MUB) protein from Homo sapiens. Protein Sci 2007 Jul;16(7):1479-84



Pubmed ID


Pubmed Central ID




Scopus ID

2-s2.0-34250837588   3 Citations


The protein Bc059385, whose solution structure is reported here, is the human representative of a recently identified family of membrane-anchored ubiquitin-fold (MUB) proteins. Analysis of their similarity to ubiquitin indicates that homologous amino acid residues in MUBs form a hydrophobic surface very similar to the recognition patch surrounding Ile-44 in ubiquitin. This suggests that MUBs may interact with proteins containing an alpha-helical motif similar to those of some ubiquitin binding domains. A disordered loop common to MUBs may also provide a second protein interaction site. From the available data, it is probable that this protein is prenylated and associated with the membrane. With <20% identity to ubiquitin, the MUB family further expands the sequence space that maps to the beta-grasp fold, and adds membrane localization to its list of functional roles.

Author List

de la Cruz NB, Peterson FC, Lytle BL, Volkman BF


Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin

MESH terms used to index this publication - Major topics in bold

Cell Membrane
Hydrophobic and Hydrophilic Interactions
Magnetic Resonance Spectroscopy
Membrane Proteins
Models, Molecular
Protein Binding
Protein Folding
Protein Prenylation
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46