cDNA cloning, characterization, and chromosome mapping of UBE2E2 encoding a human ubiquitin-conjugating E2 enzyme.
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.
Kimura
M
M
Department of Molecular Pathobiochemistry, Gifu University School of Medicine, Japan.
Hattori
T
T
Matsuda
Y
Y
Yoshioka
T
T
Sumi
N
N
Umeda
Y
Y
Nakashima
S
S
Okano
Y
Y
D000595:Amino Acid Sequence; D001483:Base Sequence; D002874:Chromosome Mapping; D002893:Chromosomes, Human, Pair 3; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006801:Humans; D017404:In Situ Hybridization, Fluorescence; D008025:Ligases / Q000235:genetics*; D008969:Molecular Sequence Data; D044763:Ubiquitin-Conjugating Enzymes
D018076:DNA, Complementary; C106347:UBE2E2 protein, human; D044763:Ubiquitin-Conjugating Enzymes; D008025:Ligases