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.
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.
Ubiquitin-Conjugating Enzyme E2 S (UBE2S) is a member of the Ubiquitin-Conjugating Enzyme family. UBE2S interacts with CDC20, FZR1/CDH1 and VHL. UBE2S can form a thiol ester linkage with Ubiquitin in an Ubiquitin Activating Enzyme-Dependent manner, a characteristic property of Ubiquitin Carrier Proteins. UBE2S acts as an essential factor of the Anaphase Promoting Complex/Cyclosome, a cell cycle-regulated Ubiquitin ligase that controls progression through mitosis. UBE2S is also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A.
Ubiquitin-Conjugating Enzyme E2 T (UBE2T) is a ligase that belongs to the Ubiquitin-Conjugating Enzyme family. UBE2T accepts the ATP-dependent ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro; UBE2T is able to catalyze polyubiquitination using all 7 ubiquitin Lys residues; but may prefer 'Lys-11'-; 'Lys-27'-; 'Lys-48'- and 'Lys-63'-linked polyubiquitination. UBE2T is an important factor of the Faconi anemia pathway of DNA damage repair and; upon self-inactivation; may negatively regulate the Faconi pathway.
Ube2T is the E2 ubiquitin-conjugating enzyme of the Fanconi anemia DNA repair pathway and it is overexpressed in several cancers; representing an attractive target for the development of inhibitors. Notably; UBE2T locates at 1q32.1; and the gain of 1q is frequently observed in a variety of cancers. For instance; UBE2T serves an important role in the growth of bladder cancer cells; and may be considered as a potential biomarker and therapeutic target for bladder cancer.
Ubiquitin-Conjugating Enzyme Variant 1a (UBE2V1) is a member of the Ubiquitin-conjugating (E2) enzyme family. The E2 catalytic core domain of UBE2V1 lacks an active site cysteine residue, rendering it catalytically inactive on its own. However, in the cytoplasm UBE2V1 is able to form a catalytically active complex with UBE2N/Ubc13, which mediates the synthesis Lys63-linked Ubiquitin chains and is required for NF-kappa B activation. UBE2V1 is required for UBE2N (Ubc13)/UBE2V1 Complex-dependent Lys63-linked Ubiquitin chain formation. More specifically, UBE2V1 orients the Ubiquitin molecule to favor linkage at Lys63 via a non-covalent interaction with the Ubiquitin molecule. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. UBE2V1 plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6, and TRAF2. It mediates transcriptional activation of target genes. UBE2V1 also controls the progress through the cell cycle and differentiation, the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.
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