The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes an additional conjugation factor, E4, which is involved in multiubiquitin chain assembly. This gene is also the strongest candidate in the neuroblastoma tumor suppressor genes. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene.
E4; HDNB1; homologous to yeast UFD2; Homozygously deleted in neuroblastoma 1; homozygously deleted in neuroblastoma-1; RING-type E3 ubiquitin transferase E4 B; Ubiquitin conjugation factor E4 B; Ubiquitin fusion degradation protein 2; ubiquitin-fusion degradation protein 2; ubiquitination factor E4B (homologous to yeast UFD2); ubiquitination factor E4B (UFD2 homolog; ubiquitination factor E4B (UFD2 homolog, yeast); ubiquitination factor E4B, UFD2 homolog; UBOX3; UFD2; UFD2A; UFD2A-III/UBE4B-III splice isoform; yeast)