High impact information on Ube2h

• Ubc8 gene expression is induced by both VPA and TSA, whereas only TSA simultaneously reduces RLIM protein levels and therefore fails to induce HDAC2 degradation [1].
• In contrast to most proteins induced in reticulocytes, E2-20K and E2-230K enzymes are present at strongly reduced levels in erythrocytes and thus decline in abundance as reticulocyte maturation is completed [2].
• Induction of the E2-20K and E2-230K genes is specific, as transcript levels for at least two other ubiquitinating enzymes fall during erythroblast differentiation [2].
• Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation [3].
• Ubc8 clearly mediates protein ISGylation in transfection assays [3].

Anatomical context of Ube2h

• The reduction of Ubc8 expression by small interfering RNA causes a decrease in protein ISGylation in HeLa cells upon interferon treatment [3].

Regulatory relationships of Ube2h

• The 20-kDa ubiquitin-conjugating enzyme E2-20K is induced specifically during a late stage of erythroid differentiation [4].

Other interactions of Ube2h

• E2-20K and E2-230K, which are abundant in reticulocytes, were low or absent in undifferentiated and differentiated MEL cells [5].

References