cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme

Cytogenet Cell Genet. 1997;78(2):107-11. doi: 10.1159/000134639.

Abstract

A cDNA encoding a human ubiquitin-conjugating enzyme (E2) with N-terminal extension (UBE2E2/UbcH8) was isolated. Amino acid sequence within the UBC domain of UBE2E2 shares over 90% identity with human UbcH6, mouse UbcM2, and Drosophila UbcD2, whereas the N-terminal region shows little amino acid sequence similarity with known proteins. The UBE2E2 gene is transcribed in various tissues as a 1.9-kb transcript. The UBE2E2 protein formed a thioester bond with ubiquitin in an E1-dependent manner, indicating that the gene product is a functional E2 enzyme. The UBE2E2 gene was assigned to human chromosome 3p24.2 by fluorescence in situ hybridization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Chromosome Mapping
  • Chromosomes, Human, Pair 3*
  • Cloning, Molecular
  • DNA, Complementary
  • Humans
  • In Situ Hybridization, Fluorescence
  • Ligases / genetics*
  • Molecular Sequence Data
  • Ubiquitin-Conjugating Enzymes

Substances

  • DNA, Complementary
  • UBE2E2 protein, human
  • Ubiquitin-Conjugating Enzymes
  • Ligases

Associated data

  • GENBANK/D88519