Ubiquitin-Conjugating Enzyme E2 G2 (UBE2G2) is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation, which belong to the ubiquitin-conjugating enzyme family. It shares 60% and 100% sequence identity with S.cerevisiae Ubc7 and mouse respectively. The UBE2G2 enzyme and the GP78 E3 ligase are active components of endoplasmic reticulum-associated degradation pathway which is essential for the degradation of misfolded ER proteins. The mechanism of K48-linked poly-ubiquitination by UBE2G2/GP78 appears to involve the transfer of preassembled Ub chains from UBE2G2 to lysine residues in a substrate. The E2 and E3 enzymes form a large hetero-oligomer which brings multiple UBE2G2 molecules into close proximity which allows for Ub transfer between neighboring E2s.
UBE2H 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.
Ubiquitin-Conjugating Enzyme E2 H (UBE2H) belongs to the E2 Ubiquitin-Conjugating Enzyme family. 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. It has been shown to conjugate ubiquitin to histone H2A in an E3 dependent manner in vitro. UBE2H is the human homolog to the yeast DNA repair gene RAD6; which is induced by DNA damaging reagents. UBE2H has been associated with cancer-induced cachexia and with the regulation of sepsis-induced muscle proteolysis.
UBE2I 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.
SUMO-Conjugating Enzyme UBC9 (UBC9) belongs to the ubiquitin-conjugating enzyme family. UBC9 is homologous to ubiquitin-conjugating enzymes (E2s). However; instead of conjugating ubiquitin; UBC9 conjugates a ubiquitin homologue; Small Ubiquitin-Like Modifier 1 (SUMO-1). The conjugation of ubiquitin requires the activities of ubiquitin-activating (E1) and conjugating (E2) enzymes. It is suggested that UBC9 might play a role in DNA repair and perhaps even in aging.
Ubiquitin-Conjugating Enzyme E2 J2 (UBE2J2) belongs to the ubiquitin-conjugating enzyme family. UBE2J2 is involved in the ubiquitiantion. UBE2J2 located in the membrane of the endoplasmic reticulum, catalyzes the covalent attachment of ubiquitin to other proteins. UBE2J2 may play a important role in the selective degradation of misfolded membrane protein from the endoplasmic reticulum.
Ubiquitin/ISG15-Conjugating Enzyme E2 L6 (UBE2L6) is an enzyme member of the E2 ubiquitin-conjugating enzyme family. UBE2L6 plays a same function as UBE2D; it catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. UBE2L6 promotes ubiquitination and subsequent proteasomal degradation of FLT3. It has functions in the E6/E6-AP-induced ubiquitination of p53/TP53.
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