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Biochem. Biophys. Res. Commun. Jan (2001); 280(2):535-40
Molecular cloning of a novel ubiquitin-like protein, UBIN, that binds to ER targeting signal sequences.
Matsuda M, Koide T, Yorihuzi T, Hosokawa N, Nagata K
Department of Molecular and Cellular Biology, Kyoto University, Sakyo-ku, Kyoto, 606-8397, Japan.
Abstract: To identify proteins that interact with HSP47, an endoplasmic reticulum (ER)-resident molecular chaperone, a yeast two-hybrid screening was performed using mouse full-length HSP47 including an N-terminal signal sequence as a bait. Analysis of several positive clones led to the identification and cloning of a novel gene, ubin, encoding a ubiquitin-like protein. Unlike other ubiquitin-like proteins, UBIN was shown to interact with signal sequences of various secretory and ER-luminal proteins, including HSP47, but not interact with signal sequences of mitochondrial targeting in two-hybrid system. The possible function of UBIN will be discussed with regards to novel characteristics of binding to signal sequences for ER targeting.
[PUBMED: 11162551] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.