Molecular cloning of a novel ubiquitin-like protein, ubin, that binds to er targeting signal sequences

Miho Matsuda, Takaki Koide, Tetuya Yorihuzi, Nobuko Hosokawa, Kazuhiro Nagata

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15 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)535-540
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2001 Jan 1



  • Endoplasmic reticulum
  • Signal peptide
  • Two-hybrid system
  • Ubiquitin-like protein

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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