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.
Ubiquitin-Conjugating Enzyme E2 Variant 2 (UBE2V2) is an enzyme that belongs to the ubiquitin-conjugating enzyme family. UBE2V2 can be detected in the placenta, colon, liver, and skin. It forms a heterodimer with UBE2N. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains and which leads to protein degradation by the proteasome. UBE2V2 mediates transcriptional activation of target genes. It plays a role in the control of progress through the cell cycle and differentiation. It also plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage.
Ubiquitin-conjugating enzymes, also known as UBE2W, E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step of protein ubiquitination. The modification of protein 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. UBE2W is a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is required for post-replicative DNA damage repair. It accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. It also catalyzes monoubiquitination and "Lys-11"-linked polyubiquitination. UBE2W is also considered to regulate FANCD2 monoubiquitination. UBE2W exhibits ubiquitin conjugating enzyme activity and catalyzes the monoubiquitination of PHD domain of Fanconi anemia complementation group L (FANCL). Over-expression of UBE2W in cells promotes the monoubiquitination of FANCD2 and down-regulated UBE2W markedly reduces the UV irradiation-induced but not MMC-induced FANCD2 monoubiquitination.
Ubiquitin-Conjugating Enzyme E2 Z (ZUBE2Z) is a member of the E2 ubiquitin-conjugating enzyme family. ZUBE2Z is widely expressed in many tissues, with high expression found in the placenta, pancreas, spleen, and testis. It is ubiquitinates proteins that catalyze the covalent attachment of ubiquitin to other proteins. It has shown that ZUBE2Z participate in signaling pathways, and may be involved in apoptosis regulation.
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