Ubiquitin-Conjugating Enzyme E2 B (UBE2B) is a member of the ubiquitin-conjugating enzyme family. UBE2B accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. It is shown that UBE2B interacts with RAD18; UBR2; and WAC. UBE2B is required for post-replicative DNA damage repair. Additional; UBE2B plays a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.
Ubiquitin-conjugating enzyme E2 D1（UBE2D1）belongs to the ubiquitin-conjugating enzyme family. 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 enzyme is closely related to a stimulator of iron transport (SFT); and is up-regulated in hereditary hemochromatosis. It also functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.
Ubiquitin-conjugating enzyme E2 D1 (UBE2D1); a member of human E2 ubiquitin-conjugating enzymes; is closely related to SFT; which is short for stimulator of iron (Fe) transport. In other words; UbcH5A is significantly up-regulated in the liver of iron-overloaded patients with hereditary hemochromatosis; as previously published for SFT. Moreover; a complex of UBE2D1 is critical in maintaining KRAS protein stability and propose that targeting such complex may be a unique strategy to degrade mutant KRAS to kill cancer cells.
UBE2D3 is an enzyme that belongs to the ubiquitin-conjugating enzyme family. 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 enzyme functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase.
Ubiquitin-Conjugating Enzyme E2 D4 (UBE2D4) is a ligase that belongs to the Ubiquitin-Conjugating Enzyme family. UBE2D4 has been proposed to participate in Ubl conjugation pathway. UBE2D4 takes part in post-translational protein modification; protein K6-linked ubiquitination; protein K11-linked ubiquitination; protein K27-linked ubiquitination; protein K29-linked ubiquitination; protein K48-linked ubiquitination; and protein K63-linked ubiquitination. UBE2D4 regulate of protein metabolic process. UBE2D4 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro; UBE2D4 able to promote polyubiquitination using all 7 ubiquitin Lys residues; but may prefer 'Lys-11' and 'Lys-48'-linked poly-ubiquitination.
UBE2D4 is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation; ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction; and thereby the fate of the substrate; is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space; a highly sophisticated conjugation machinery has been developed. In a sequential manner; ubiquitin becomes activated by an ubiquitin-activating enzyme (E1); which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next; ubiquitin-loaded E2s are interacting with ubiquitin protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system; wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans. It has been identified the UBE2D family (UBE2D1-4) as E2 partners for IDOL that support both autoubiquitination and IDOL-dependent ubiquitination of the LDLR in a cell-free system.
UBE2F is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by an ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.
UBE2G1 is a member of the ubiquitin-conjugating E2 family whose members perform the second step in the ubiquitination reaction. Initially identified as the main process for protein degradation, ubiquitination is believed nowadays to be crucial for a wider range of cellular processes. The outcome of the ubiquitin-conjugation reaction, and thereby the fate of the substrate, is heavily dependent on the number of ubiquitin molecules attached and how these ubiquitin molecules are inter-connected. To deal with this complexity and to allow adequate ubiquitination in time and space, a highly sophisticated conjugation machinery has been developed. In a sequential manner, ubiquitin becomes activated by an ubiquitin-activating enzyme (E1), which then transfers the ubiquitin to a group of ubiquitin-conjugating enzymes (E2s). Next, ubiquitin-loaded E2s are interacting with ubiquitin protein ligases (E3s) and ubiquitin is conjugated to substrates on recruitment by the E3. These three key enzymes are operating in a hierarchical system, wherein two E1s and 35 E2s have been found and hundreds of E3s have been identified in humans.
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