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.
UBCH8; also known as UBE2L6; belongs to the ubiquitin-conjugating enzyme family. The family of ubiquitin-conjugating (E2) enzymes is characterized by the presence of a highly conserved ubiquitin-conjugating (UBC) domain. These domains accommodate the ATP-activated ubiquitin (Ub) or ubiquitin-like (UBL) protein via a covalently linked thioester onto its active-site residue. E2 enzymes act via selective protein-protein interactions with the E1 and E3 enzymes and connect activation to covalent modification. By doing so; E2s differentiate effects on downstream substrates; either with a single Ub/UBL molecule or as a chain. UBCH8 is highly similar in primary structure to the enzyme encoded by the UBE2L3 gene. It catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. UBCH8 functions in the E6/E6-AP-induced ubiquitination of p53/TP53 and promotes ubiquitination and subsequent proteasomal degradation of FLT3. At protein level; it is present in natural killer cells.
UBE2M 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.
UBE2M is a member of the E2 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 protein is linked with a ubiquitin-like protein; NEDD8; which can be conjugated to cellular proteins; such as Cdc53/culin. UBE2M accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1; but not RBX2; suggests that the RBX1-UBE2M complex neddylates specific target proteins; such as CUL1; CUL2; CUL3 and CUL4. It involved in cell proliferation and is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation.
Ubiquitin-Conjugating Enzyme E2 R2 (UBE2R2) is a modification enzyme that belongs to the ubiquitin-conjugating enzyme family. UBE2R2 is involved in cell growth and transformation. It accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, UBE2R2 catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. It may be involved in degradation of katenin.
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